Unnamed: 0
int64 9
557k
| Entry
stringlengths 6
10
| Sequence
stringlengths 20
934
| Protein names
stringlengths 7
327
| Organism
stringlengths 16
143
| Organism (ID)
int64 1.43k
1.84M
| Length
int64 20
934
| Mass
int64 2.19k
106k
| Keywords
stringlengths 9
380
⌀ | Gene Ontology IDs
stringlengths 10
178
⌀ | Protein existence
stringclasses 5
values | Annotation
float64 1
5
| Subcellular location [CC]
stringlengths 31
1.53k
⌀ | Signal peptide
stringclasses 65
values | Transmembrane
stringclasses 37
values | Pfam
stringlengths 8
40
⌀ | InterPro
stringlengths 10
150
⌀ | PDB
stringlengths 5
2.36k
⌀ | Taxonomic lineage
stringlengths 189
688
| Gene Names
stringlengths 3
51
⌀ | Toxin
bool 2
classes | species
stringclasses 66
values | cdhit_cluster
int64 0
4.38k
| cdhit_rep
stringlengths 5
10
| cdhit_rep_is_ref
bool 1
class | cdhit_pct_id
float64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
5,661 |
D0Z6T1
|
MNKVKCYVLFTALLSSLCAYGAPQSITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGATFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMEN
|
Heat-labile enterotoxin B chain (LT-B, human) (LTH-B)
|
Escherichia coli O78:H11 (strain H10407 / ETEC)
| 316,401 | 124 | 14,028 |
Disulfide bond;Enterotoxin;Plasmid;Signal;Toxin;Virulence
|
GO:0005576; GO:0090729
|
Inferred from homology
| 2 | null |
SIGNAL 1..21; /evidence="ECO:0000250"
| null |
PF01376;
|
IPR008992;IPR001835;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
|
eltB ltpB ETEC_p666_0650
| true |
Escherichia coli
| 7 |
row_5420
| false | null |
239 |
P0A968
|
MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPVEVEAAVA
|
Cold shock-like protein CspD (CSP-D)
|
Escherichia coli (strain K12)
| 83,333 | 74 | 7,969 |
Cytoplasm;Direct protein sequencing;DNA replication inhibitor;DNA-binding;Reference proteome;RNA-binding;Toxin
|
GO:0003676; GO:0003697; GO:0003723; GO:0005829; GO:0006355; GO:0008156; GO:0010468; GO:0042594; GO:0042803; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null |
PF00313;
|
IPR012156;IPR050181;IPR011129;IPR019844;IPR002059;IPR012751;IPR012340;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
|
cspD cspH ybjA b0880 JW0864
| true |
Escherichia coli
| 8 |
row_223
| false | null |
6,825 |
P64454
|
MSLYQHMLVFYAVMAAIAFLITWFLSHDKKRIRFLSAFLVGATWPMSFPVALLFSLF
|
Orphan toxin OrtT
|
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
| 199,310 | 57 | 6,646 |
Cell inner membrane;Cell membrane;Membrane;Reference proteome;Stress response;Toxin;Transmembrane;Transmembrane helix
|
GO:0005886; GO:0090729
|
Inferred from homology
| 2 |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P64453}; Multi-pass membrane protein {ECO:0000305}.
| null |
TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 34..54; /note="Helical"; /evidence="ECO:0000255"
|
PF10753;
|
IPR019689;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
|
ortT c1870
| true |
Escherichia coli
| 9 |
row_6572
| false | null |
4,597 |
Q4JHE3
|
MNVFFMFSLLFLAALESCADVRRNPLEECFREADYEEFLEIARNGLKKTSNPKHVVVVGAGMAGLSAAYVLAGAGHKVTLLEASERVGGRVHTYRNEKEGWYVNLGPMRLPERHRIIREYIRKFGLKLNEFFQENENAWYFIRNIRKRVWEVKKDPGVFKYPVKPSEEGKSASQLYRESLKKVIEELKRTNCSYILNKYDTYSTKEYLIKEGNLSRGAVDMIGDLLNEDSSYYLSFIESLKSDDLFSYEKRFDEIVGGFDQLPISMYQAIAEMVHLNAQVIKIQHNAEKVRVAYQTPAKTLSYVTADYVIVCSSSRAARRIYFEPPLPPKKAHALRSIHYKSGTKIFLTCSKKFWEADGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIVAYTISDDADFFQSLDIKTSADIVINDLSLIHQLPKKEIQALCYPSMIKKWSLDKYAMGSITSFAPYQFQDFIERVAAPVGRIYFAGEYTARVHGWLDSTIKSGLTAARDVNRASQKPSRRQLSNDNEL
|
L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 517 | 59,070 |
Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Oxidoreductase;Secreted;Signal;Toxin
|
GO:0001716; GO:0005576; GO:0006915; GO:0009063; GO:0031640; GO:0042742; GO:0090729
|
Evidence at transcript level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16261251}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF01593;
|
IPR002937;IPR036188;IPR001613;IPR050281;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 0 |
row_4375
| false | null |
2,031 |
Q3I5F4
|
MSMLCYTLIIVFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAQTHEGLKTSRNTDQRHPAPKKAEDQELGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNEDTLNRNIRAKRETHPVHNLGEYSVCDSISVWVANKTEAMDIKGKPVTVMVDVNLNNHVFKQYFFETKCRNPNPVPSGCRGIDSGHWNSYCTTTQTFVRALTMEGNQASWRFIRIDTACVCVISRKTENF
|
Venom nerve growth factor (v-NGF) (vNGF)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 243 | 27,382 |
Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
|
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008191; GO:0008289; GO:0021675; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21801740}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF00243;
|
IPR029034;IPR020408;IPR002072;IPR020425;IPR019846;IPR020433;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 1 |
row_1950
| false | null |
7,078 |
Q3SB07
|
MIAFTVLLSLAAVLQQSSGTVDFASESSNKKDYRKEIVDKHNDLRRSVKPTARNMLQMKWNSRAAQNAKRWANRCTFAHSPPYTRTVGKLRCGENIFMSSQPFAWSGVVQAWYDEVKKFVYGIGAKPPSSVIGHYTQVVWYKSHLLGCASAKCSSTKYLYVCQYCPAGNIIGSIATPYKSGPPCGDCPSACDNGLCTNPCKHNNDFSNCKALAKKSKCQTEWIKSKCPATCFCRTEII
|
Cysteine-rich venom protein pseudechetoxin-like (CRVP)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 238 | 26,410 |
Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Signal;Toxin
|
GO:0005576; GO:0090729; GO:0099106
|
Evidence at transcript level
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
SIGNAL 1..19; /evidence="ECO:0000250"
| null |
PF00188;PF08562;
|
IPR018244;IPR014044;IPR035940;IPR042076;IPR001283;IPR013871;IPR034117;IPR003582;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 2 |
row_6800
| false | null |
635 |
Q45Z47
|
MHPAHLLVLLAVCVSLLGASDIPPLPLNLAQFGFMIRCANGGSRSPLDYTDYGCYCGKGGRGTPVDDLDRCCQVHDECYGEAEKRLGCSPFVTLYSWKCYGKAPSCNTKTDCQRFVCNCDAKAAECFARSPYQKKNWNINTKARCK
|
Phospholipase A2 OS2 (PLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 146 | 16,104 |
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Neurotoxin;Presynaptic neurotoxin;Secreted;Signal;Toxin
|
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted.
|
SIGNAL 1..27; /evidence="ECO:0000255"
| null |
PF00068;
|
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 3 |
row_594
| false | null |
174 |
P00614
|
NLLQFGFMIRCANRRSRPVWHYMDYGCYCGKGGSGTPVDDLDRCCQVHDECYGEAVRRFGCAPYWTLYSWKCYGKAPTCNTKTRCQRFVCRCDAKAAECFARSPYQNSNWNINTKARCR
|
Basic phospholipase A2 taipoxin alpha chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 119 | 13,829 |
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Presynaptic neurotoxin;Secreted;Toxin
|
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted.
| null | null |
PF00068;
|
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 4 |
row_161
| false | null |
1,856 |
P83228
|
MVGLSRLAGGGLLLLLLLALLPLALDGKPAPLPQALPEALAGGTTALRRDVTEEQQQQLVAEESSGPAAGRSDPKIGDGCFGLPLDHIGSVSGLGCNRPVQNRPKQIPGGS
|
Natriuretic peptide TNP-b (Taipan natriuretic peptide) (Venom natriuretic peptide OxsSNPb)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 111 | 11,252 |
Direct protein sequencing;Disulfide bond;Hypotensive agent;Secreted;Signal;Toxin;Vasoactive;Vasodilator
|
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15652496}.
|
SIGNAL 1..27; /evidence="ECO:0000255"
| null |
PF00212;
|
IPR000663;IPR030480;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 5 |
row_1781
| false | null |
5,208 |
A8HDK9
|
MKTLLLTLVVVTIVCLDLGYTRRCFTTPSVRSERCPPGQEVCYTKTWTDGHGGSRGKRVDLGCAATCPTPKKKDIKIICCSTDNCNTFPKWP
|
Long neurotoxin 1 (LNTX-1)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 92 | 10,183 |
3D-structure;Acetylcholine receptor inhibiting toxin;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin
|
GO:0005576; GO:0030550; GO:0090729; GO:0099106
|
Evidence at protein level
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
SIGNAL 1..21; /evidence="ECO:0000250"
| null |
PF21947;
|
IPR003571;IPR045860;IPR018354;IPR054131;
|
8D9Y;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 6 |
row_4975
| false | null |
69 |
B7S4N9
|
MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCHLPPKPGPCRAAIPRFYYNPHSKQCEKFIYGGCHGNANSFKTPDECNYTCLGVSLPK
|
Kunitz-type serine protease inhibitor taicotoxin (Taicatoxin, serine protease inhibitor component) (TCX) (TSPI) (Venom protease inhibitor 1) (Venom protease inhibitor 2)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 88 | 9,711 |
Blood coagulation cascade inhibiting toxin;Calcium channel impairing toxin;Calcium-activated potassium channel impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Ion channel impairing toxin;Neurotoxin;Potassium channel impairing toxin;Protease inhibitor;Secreted;Serine protease inhibitor;Signal;Toxin;Voltage-gated calcium channel impairing toxin
|
GO:0004867; GO:0005246; GO:0005615; GO:0015459; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1485334}.
|
SIGNAL 1..24; /evidence="ECO:0000269|PubMed:1485334, ECO:0000269|PubMed:21843588"
| null |
PF00014;
|
IPR002223;IPR036880;IPR020901;IPR050098;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 7 |
row_63
| false | null |
2,036 |
Q45Z11
|
MKTLLLTLVVVTIVCLDLGYTMTCYNQQSSEAKTTTTCSGGVSSCYKKTWSDGRGTIIERGCGCPSVKKGIERICCRTDKCNN
|
Short neurotoxin 1 (SNTX-1) (Toxin 3)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 83 | 9,025 |
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin
|
GO:0005576; GO:0030550; GO:0090729; GO:0099106
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8672493}.
|
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:8672493"
| null |
PF21947;
|
IPR003571;IPR045860;IPR018354;IPR054131;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 8 |
row_1954
| false | null |
5,203 |
A8HDK2
|
MKTLLLTLVVMTIVCLDLGYTLTCYMNPSGTMVCKEHETMCYQLIVWTFQYRVLYLKGCTSSCPGGNNRACCSTDLCNN
|
Short neurotoxin 3 (SNTX-3) (Three-finger toxin) (3FTx)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 79 | 8,877 |
Disulfide bond;Secreted;Signal;Toxin
|
GO:0005576; GO:0090729
|
Inferred from homology
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
SIGNAL 1..23; /evidence="ECO:0000250"
| null |
PF21947;
|
IPR003571;IPR045860;IPR054131;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 9 |
row_4970
| false | null |
3,333 |
P0CB06
|
MTCYNQQSSEAKTTTTCSGGVSSCYKKTWSDIRGTIIERGCGCPSVKKGIERICCRTDKCNN
|
Short neurotoxin 2 (SNTX-2)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 62 | 6,790 |
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
|
GO:0005576; GO:0030550; GO:0090729; GO:0099106
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8672493}.
| null | null |
PF21947;
|
IPR003571;IPR045860;IPR018354;IPR054131;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 10 |
row_3215
| false | null |
7,073 |
Q3SAX8
|
PAAGLSDPKIGNGCFGFPIDRIGSVSGLGCNRLVQNPPKPISGES
|
Natriuretic peptide OsNP-d
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 45 | 4,524 |
Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
|
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
|
Evidence at transcript level
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16261251}.
| null | null |
PF00212;
|
IPR000663;IPR030480;IPR002408;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 11 |
row_6795
| false | null |
4,266 |
P83231
|
SDSKIGNGCFGFPLDRIGSVSGLGCNRIMQNPPKKFSGE
|
Natriuretic peptide TNP-c (Taipan natriuretic peptide) (Venom natriuretic peptide OxsSNPc)
|
Oxyuranus scutellatus canni (Papuan taipan)
| 183,720 | 39 | 4,115 |
Direct protein sequencing;Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
|
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15652496}.
| null | null |
PF00212;
|
IPR000663;IPR030480;IPR002408;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 12 |
row_4099
| false | null |
4,262 |
P83225
|
SDSKIGDGCFGLPLDHIGSVSGLGCNRPVQNRPKK
|
Natriuretic peptide TNP-a (Taipan natriuretic peptide) (Venom natriuretic peptide OxsSNPa)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 35 | 3,653 |
Direct protein sequencing;Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
|
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15652496}.
| null | null |
PF00212;
|
IPR000663;IPR030480;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 13 |
row_4095
| false | null |
2,116 |
Q7LZG2
|
NLAQFGFMIRCANGGSRSALDYADYGC
|
Phospholipase A2 taicatoxin (TCX) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
| 8,667 | 27 | 2,901 |
Calcium;Calcium-activated potassium channel impairing toxin;Direct protein sequencing;Disulfide bond;Hydrolase;Ion channel impairing toxin;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Potassium channel impairing toxin;Secreted;Toxin
|
GO:0004623; GO:0005576; GO:0006644; GO:0015459; GO:0016042; GO:0046872; GO:0050482; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1373076, ECO:0000269|PubMed:1485334}.
| null | null | null |
IPR036444;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 14 |
row_2032
| false | null |
1,506 |
P0DKT7
|
NLLQFGYMIRCANGRSRPVW
|
Basic phospholipase A2 cannitoxin alpha chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
|
Oxyuranus scutellatus canni (Papuan taipan)
| 183,720 | 20 | 2,382 |
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Presynaptic neurotoxin;Secreted;Toxin
|
GO:0004623; GO:0005576; GO:0016042; GO:0046872; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Oxyuranus (genus), Oxyuranus scutellatus (species)
| null | true |
Oxyuranus scutellatus
| 15 |
row_1443
| false | null |
140 |
I1C083
|
MYFEEGRLFFIKSQFNGRVLDVEDGSTEDDANIIVYTQKYEDCLNQLWRYENGYFINAKSAKVLDIRGGEMQPESQIIQYAQKMVEEAANQRWAIDEDGYIFCEARPDLVLDIQGAEDEDCVPVILYERREGEVSANQRWELVPFEG
|
Mucoricin (EC 3.2.2.22) (Ricin-like toxin) (rRNA N-glycosidase)
|
Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
| 246,409 | 147 | 17,138 |
Hydrolase;Protein synthesis inhibitor;Reference proteome;Secreted;Toxin;Virulence
|
GO:0005576; GO:0017148; GO:0019057; GO:0030598; GO:0045007; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33462434}.
| null | null |
PF00652;
|
IPR035992;IPR000772;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Fungi incertae sedis (no rank), Mucoromycota (phylum), Mucoromycotina (subphylum), Mucoromycetes (class), Mucorales (order), Mucorineae (suborder), Rhizopodaceae (family), Rhizopus (genus), Rhizopus delemar (species)
|
RLT1 RO3G_06568
| true |
Rhizopus delemar
| 0 |
row_130
| false | null |
155 |
O05442
|
MAPLAVDPAALDSAGGAVVAAGAGLGAVISSLTAALAGCAGMAGDDPAGAVFGRSYDGSAAALVQAMSVARNGLCNLGDGVRMSAHNYSLAEAMSDVAGRAAPLPAPPPSGCVGVGAPPSAVGGGGGAPKGWGWVAPYIGMIWPNGDSTKLRAAAVAWRSAGTQFALTEIQSTAGPMGVIRAQQLPEAGLIESAFADAYASTTAVVGQCHQLAAQLDAYAARIDAVHAAVLDLLARICDPLTGIKEVWEFLTDQDEDEIQRIAHDIAVVVDQFSGEVDALAAEITAVVSHAEAVITAMADHAGKQWDRFLHSNPVGVVIDGTGQQLKGFGEEAFGMAKDSWDLGPLRASIDPFGWYRSWEEMLTGMAPLAGLGGENAPGVVESWKQFGKSLIHWDEWTTNPNEALGKTVFDAATLALPGGPLSKLGSKGRDILAGVRGLKERLEPTTPHLEPPATPPRPGPQPPRIEPPESGHPAPAPAAKPAPVPANGPLPHSPTESKPPPVDRPAEPVAPSSASAGQPRVSAATTPGTHVPHGLPQPGEHVPAQAPPATTLLGGPPVESAPATAHQPQWATTPAAPAAAPHSTPGGVHSTESGPHGRSLSAHGSEPTHDGASHGSGHGSGSEPPGLHAPHREQQLAMHSNEPAGEGWHRLSDEAVDPQYGEPLSRHWDFTDNPADRSRINPVVAQLMEDPNAPFGRDPQGQPYTQERYQERFNSVGPWGQQYSNFPPNNGAVPGTRIAYTNLEKFLSDYGPQLDRIGGDQGKYLAIMEHGRPASWEQRALHVTSLRDPYHAYTIDWLPEGWFIEVSEVAPGCGQPGGSIQVRIFDHQNEMRKVEELIRRGVLRQ
|
Outer membrane channel protein CpnT (Channel protein with necrosis-inducing toxin) [Cleaved into: N-terminal channel domain; Tuberculosis necrotizing toxin (TNT) (NAD(+) glycohydrolase) (EC 3.2.2.5)]
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
| 83,332 | 846 | 88,335 |
3D-structure;Cell outer membrane;Host cytoplasm;Hydrolase;Ion transport;Membrane;NAD;Porin;Reference proteome;Secreted;Toxin;Transmembrane;Transmembrane beta strand;Transport;Virulence
|
GO:0001907; GO:0003953; GO:0005576; GO:0005829; GO:0006811; GO:0009274; GO:0009279; GO:0009986; GO:0015288; GO:0044164; GO:0046930; GO:0050135; GO:0061809; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: [N-terminal channel domain]: Cell outer membrane {ECO:0000269|PubMed:24753609}.; SUBCELLULAR LOCATION: [Tuberculosis necrotizing toxin]: Secreted {ECO:0000269|PubMed:24753609}. Cell surface {ECO:0000269|PubMed:24753609}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:26237511}. Note=Secreted into the cytosol of infected macrophages while the bacteria are still confined to the phagosome. Access to the macrophage cytosol depends on the ESX-1 / type VII secretion system (T7SS). {ECO:0000269|PubMed:26237511}.
| null | null |
PF14021;
|
IPR025331;
|
4QLP;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Mycobacteriales (order), Mycobacteriaceae (family), Mycobacterium (genus), Mycobacterium tuberculosis complex (no rank), Mycobacterium tuberculosis (species)
|
cpnT Rv3903c
| true |
Mycobacterium tuberculosis
| 0 |
row_142
| false | null |
577 |
P9WJ63
|
MARRARVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSERAWVSRGAHKLVGALEAFAIAVAGRRCLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLPALVGCASRDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYFLWLRTQTDRALSAKGLEDAVHRAISEGP
|
16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA (EC 2.1.1.226) (EC 2.1.1.227) (16S rRNA (cytidine1409-2'-O)-methyltransferase) (23S rRNA (cytidine1920-2'-O)-methyltransferase) (Hemolysin TlyA)
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
| 83,332 | 268 | 28,074 |
3D-structure;Cell wall;Cytolysis;Cytoplasm;Hemolysis;Host cell membrane;Host membrane;Membrane;Methyltransferase;Reference proteome;Ribosome biogenesis;RNA-binding;rRNA processing;S-adenosyl-L-methionine;Secreted;Toxin;Transferase;Virulence
|
GO:0001897; GO:0003723; GO:0005576; GO:0005737; GO:0008649; GO:0016020; GO:0020002; GO:0031167; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20854656}. Secreted, cell wall {ECO:0000269|PubMed:26347855}. Host cell membrane {ECO:0000269|PubMed:20854656}. Note=Can bind to target membranes such as macrophage phagosomal membranes (PubMed:20854656). In native and recombinant hosts (M.smegmatis and E.coli), M.tuberculosis TlyA can reach the bacterial surface in functional form and colocalizes with the HBHA protein which is known to be part of cell-wall (PubMed:26347855). TlyA does not seem to depend on either Tat or Sec pathways for translocation to cell-wall (PubMed:26347855). Appears to be capable of reaching the extra-cellular milieu using a vesicle mediated transport (PubMed:26347855). {ECO:0000269|PubMed:20854656, ECO:0000269|PubMed:26347855}.
| null | null |
PF01728;PF01479;
|
IPR004538;IPR002877;IPR002942;IPR036986;IPR029063;IPR047048;
|
5KS2;5KYG;7S0S;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Mycobacteriales (order), Mycobacteriaceae (family), Mycobacterium (genus), Mycobacterium tuberculosis complex (no rank), Mycobacterium tuberculosis (species)
|
tlyA Rv1694
| true |
Mycobacterium tuberculosis
| 1 |
row_541
| false | null |
1,953 |
P9WJ62
|
MARRARVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSERAWVSRGAHKLVGALEAFAIAVAGRRCLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLPALVGCASRDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYFLWLRTQTDRALSAKGLEDAVHRAISEGP
|
16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA (EC 2.1.1.226) (EC 2.1.1.227) (16S rRNA (cytidine1409-2'-O)-methyltransferase) (23S rRNA (cytidine1920-2'-O)-methyltransferase) (Hemolysin TlyA)
|
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
| 83,331 | 268 | 28,074 |
3D-structure;Cell wall;Cytolysis;Cytoplasm;Hemolysis;Host cell membrane;Host membrane;Membrane;Methyltransferase;Reference proteome;Ribosome biogenesis;RNA-binding;rRNA processing;S-adenosyl-L-methionine;Secreted;Toxin;Transferase;Virulence
|
GO:0003723; GO:0005576; GO:0005737; GO:0006364; GO:0008168; GO:0016020; GO:0020002; GO:0031640; GO:0032259; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WJ63}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WJ63}. Host cell membrane {ECO:0000250|UniProtKB:P9WJ63}. Note=Can bind to target membranes such as macrophage phagosomal membranes. In native and recombinant hosts (M.smegmatis and E.coli), M.tuberculosis TlyA can reach the bacterial surface in functional form and colocalizes with the HBHA protein which is known to be part of cell-wall. TlyA does not seem to depend on either Tat or Sec pathways for translocation to cell-wall. Appears to be capable of reaching the extra-cellular milieu using a vesicle mediated transport. {ECO:0000250|UniProtKB:P9WJ63}.
| null | null |
PF01728;PF01479;
|
IPR004538;IPR002877;IPR002942;IPR036986;IPR029063;IPR047048;
|
5EOV;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Mycobacteriales (order), Mycobacteriaceae (family), Mycobacterium (genus), Mycobacterium tuberculosis complex (no rank), Mycobacterium tuberculosis (species)
|
tlyA MT1733
| true |
Mycobacterium tuberculosis
| 2 |
row_1874
| false | null |
1,296 |
O31506
|
MKVFEAKTLLSEATDRAKEYKELRTQMVNLRKALKGVADLSDSEFSGKGASNIKAFYHDHVGVADQWIDYIDMKIAFFNSIAGAAEDKGLSDAYIEESFLEHELANANKKSKSIMSEQKKAMKDILNDIDDILPLDLFSTETFKDELADANDKRKKTLEKLDALDEDLKTEYALSEPNEQFIKSDFQKLQEATGKGKNATPIHYNAKAYRESDIHKKKGDIEKRTEAYLKIKKEEAKEREIEKLKERLKNYDYADADEFYEMAKTIGYENLTAEQQRYFTQIENTRELEAGFKGVAVGLYDSGKDAVVGLWDMVTDPGGTVEAITGAMAHPIKTYEAISAAIEESYQKDMVNGDTYSRARWVSYAVGTVVTSIVGTKGVGAVSKTGTAAKVTTKVKTAASKSATAQKAITVSKQTVDHIKQKVNTGIEVSKKHVKTKLNQIGDLTLADILPYHPRHDLVPAGVPYNAVNGVTLKEGLQKFAKVILPKPYGTSSSGRRTPAPHVPPVTVKYGEHFARWSRKKVLKPNIIYKTKEGYTYTTDNYGRITSVKADLQLGEAKRNQYAQTNAGKPQDRKPDDDGGHLIATQFKGSGQFDNIVPMNSQINRSGGKWYEMEQEWAKALSKKPPKKVAVQIEPVYSGDSLRPSYFDVTYKIGSRKEISVSIKNQPGG
|
Toxin YeeF (DNase YeeF)
|
Bacillus subtilis (strain 168)
| 224,308 | 669 | 74,488 |
Cell membrane;Coiled coil;DNA-binding;Hydrolase;Membrane;Nuclease;Reference proteome;Toxin
|
GO:0003677; GO:0004518; GO:0005886; GO:0045121; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210}. Membrane raft {ECO:0000269|PubMed:22882210}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:22882210). Delivery to target cells requires the type VII secretion system (T7SS) and YukE (PubMed:34280190). {ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:34280190}.
| null | null |
PF13930;PF04740;
|
IPR051768;IPR044929;IPR044927;IPR006829;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
yeeF BSU06810
| true |
Bacillus subtilis
| 0 |
row_1237
| false | null |
1,297 |
O34330
|
MKVFEADSLLFEADKRTKEYKELRSQMVKLKKAFKEVANLDDSEFSGKGADNIKAFYHGHVGVTDQWIDLIDMKIAFLSSMSATLEDAKMSDAYIEESFLEHELANAYAKSKSIMSEQKKAMKDILNNINDILPLEIFSTEDFKDKLSSADDKREKTIDKLNKLDEDLKTEYAETEPNEQFIQQDFKKLQESTGKGKNATPIHYNAKAYRESDIHKKKGDIEKHSEAYLSVKKEEAKEREIKELKKKLNDGVSDPDEYLEIAKKVGYENLEPTQVQLAVQIEQAKQLEGAGEITWDIVKGVGVGLYDVGKDTVTGIWDFITDPGETLSALGNAAMHPVKTYDAISAAIEESYQKDMVNGDAYSRSRWVTYAIGSVAVAVVGTKGAGAINKADAAGKVINKASQAGKKIKDVKIPDLLPYNPKYKLALADNVPYNVVDSQNLKNELLTNAKKIPDGTRKPFTGQKKSPPWLNKEKYDAYEIEGKVKAKGKVKDVSRRVYTMKDIDINQKTEFGVTNLQLMKNGNAPYAKDGTQINLHHLIQEEPGPMLEIPNSLHTKYSDVIHQLKSDGESFRNDKVLKAQYESFRKRYWKWRAKQFENEN
|
Toxin YobL (DNase YobL)
|
Bacillus subtilis (strain 168)
| 224,308 | 600 | 67,770 |
Coiled coil;Hydrolase;Nuclease;Reference proteome;Secreted;Toxin
|
GO:0004518; GO:0005576; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34280190}. Note=Delivery to target cells requires the type VII secretion system (T7SS) and YukE. {ECO:0000269|PubMed:34280190}.
| null | null |
PF14411;PF04740;
|
IPR051768;IPR026834;IPR006829;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
yobL BSU19000
| true |
Bacillus subtilis
| 1 |
row_1238
| false | null |
3,001 |
O31998
|
MKVFEADSLLSEADKRTKEYKELRSQMVKLKKAFKAVADLDDSKFSGKGADNIKAFYHDHVGVTDQWIDLIDMKIVFLSSISAKLEDAKMSDAYIEESFLEHELVNAYTKSKSIMSEQKKAMKDILNDINDILPLEIFSTEDFKDKLSSADDKREKTIDKINKLDEDLKTEYAETEQNEQFIQQDFKKLQESTGKGKNATPIHYSAKAYRESDIHKKKGDIEQHSEAYLTVKKEEAKEREIKELKKKLNDGVSDPDEYLEIAKKVGYENLEPAQVQLAVQIEQAKQLEGAGEITWDIVKGVGVGLYDVGKDTVTGLWDFITDPGETLSALGNAVIHPVKTYDAISAAIEESYQKDMVNGDAYSRSRWVTYAIGSVAAAVIGTKGAGAINKADAAGKVINKASQAGKKIKDVKIPDLLPYNPKYDLAMAGDVPYNVVDGENLKNQLMSFAKGSDKEVKPFDVVDYRPSNSPLENHHGVMDVWAKHNVPNYVSRGSNTPTVALTKEQHNATKKVYREWLFEKTGKKVGGKVNWKEVSPREIQELTEKMFDAANVPKEARQQYYNAFNQYNFRK
|
Toxin YokI (DNase YokL) (SPbeta prophage-derived protein YokI)
|
Bacillus subtilis (strain 168)
| 224,308 | 571 | 64,261 |
Coiled coil;Hydrolase;Nuclease;Reference proteome;Secreted;Toxin
|
GO:0004518; GO:0005576; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34280190}. Note=Delivery to target cells requires the type VII secretion system (T7SS) and YukE. {ECO:0000269|PubMed:34280190}.
| null | null |
PF04740;PF15652;
|
IPR051768;IPR006829;IPR028900;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
yokI BSU21580
| true |
Bacillus subtilis
| 2 |
row_2902
| false | null |
3,989 |
P42296
|
MKTLDVHALHEGIQHTIEKLDKQKQQLEKLEKSVEHLAGMKDALKGKGGDAIRTFYEECHKPFLLFFGIFIDEYKKVLKQTQHAISSVESNSHGMIAEAFLSHDARHGVKHAREVTEQLTDAVNRQTSAIDHIVSLPTVNDSFFRMETEQAERLISDTLNKLFQFDGQQTQALEAAKSDFQTMKKYIDQLETMYTGPKIEITGYKSGSILKSQEEENINQIFGAINPQMKQADDSPMEMMLKKLAENEKSKVDSVVKTGDSKKVSKNIIVINGKVYNTSEHREHIKTDFSNAEVKQVVYNDTLYNVYISGNDMKLEPVVSLSDIKVDENGYVKILETAVELTGVYDLFKAATGRDPVSGEKVTGKDRVVASINSVPFAKIAKLEKLIDINKLINNGKKAKKASEVKNVAKDKGKIANDVSGSANKINSDLIKKYARDIEQRTGRELPKNQIDKLKEALRNKEYKKMSPIETAKHRTKFDKVKNKVIKEWEENTGQKWPVYKENVVSEKTGKIIRKKGDKYDAHHIIENTFGGEHEWWNMHPAKFPNEHQAGIHGTGSPANELFKGGKKK
|
Toxin YxiD (DNase YxiD)
|
Bacillus subtilis (strain 168)
| 224,308 | 569 | 64,326 |
Coiled coil;Hydrolase;Nuclease;Reference proteome;Secreted;Toxin
|
GO:0004518; GO:0005576; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34280190}. Note=Delivery to target cells requires the type VII secretion system (T7SS) and YukE. {ECO:0000269|PubMed:34280190}.
| null | null |
PF04740;PF14449;
|
IPR003615;IPR006829;IPR027797;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
yxiD J3D BSU39300
| true |
Bacillus subtilis
| 3 |
row_3832
| false | null |
1,716 |
P45942
|
MKVFEAKTLLTEAEKRAQEYKDLKSKMVKLKKAFKAVADLDDSEFSGKGANNIKSFYEDQAGIADQWIDLIEMKISFLTSIPGFLEDANLSDAYIEETFLAHELANAYTKSKSIMSEQKKAMKDILNDINDILPLDLFSTETFKNELSSAEKKRKEAIEKMDEVDQNLTSEYGLSEANEQMIQADYQALMNATAKGKSASPIHYNAKAYRDSEIHKMTEDVKKQSTDYISFKDQQAEQRRIAKEQEELANRPWYEKSWDAVCNFTGEVSGYYDYKRAADGVDPVTGEKLTAGQRVAAGAMAAAGYIPIVGWAGKLAKGGKAVYSTSKALYRADKALDVYKTPKTFHALQNSSKGLYGLASANGFSEAITGRDMFGNKVSKERQEQSLSGAMAMLVPFGARGINKKLNAKSSSRVSEASTNTSKKPKVPKTYKRPTYFRKGVRDKVWENAKDSTGSVKDPLTKQVMKKDEPWDMGHKPGYEFRKHQQSAMERNISRKQFLDEHNNPDHYQPELPSSNRSHKGEDMTDDYFGD
|
Toxin YqcG (DNase YqcG)
|
Bacillus subtilis (strain 168)
| 224,308 | 531 | 59,669 |
Coiled coil;Hydrolase;Nuclease;Reference proteome;Secreted;Toxin
|
GO:0004518; GO:0005576; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34280190}. Note=Delivery to target cells requires the type VII secretion system (T7SS) and YukE. {ECO:0000269|PubMed:34280190}.
| null | null |
PF14410;PF04740;PF14449;
|
IPR051768;IPR006829;IPR027797;IPR026835;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
yqcG BSU25860
| true |
Bacillus subtilis
| 4 |
row_1645
| false | null |
159 |
O34344
|
MKSKLLRLLIVSMVTILVFSLVGLSKESSTSAKENHTFSGEDYFRGLLFGQGEVGKLISNDLDPKLVKEANSTEGKKLVNDVVKFIKKDQPQYMDELKQSIDSKDPKKLIENMTKADQLIQKYAKKNENVKYSSNKVTPSCGLYAVCVAAGYLYVVGVNAVALQTAAAVTTAVWKYVAKYSSSASNNSDLEAAAAKTLKLIHQ
|
Sporulation delaying protein C (SdpC) (Cannibalism toxin SDP) (Killing factor SdpC) (Toxic peptide SdpC) [Cleaved into: Sporulation delaying protein (SDP)]
|
Bacillus subtilis (strain 168)
| 224,308 | 203 | 22,221 |
Antibiotic;Antimicrobial;Bacteriocin;Direct protein sequencing;Disulfide bond;Reference proteome;Secreted;Signal;Toxin;Virulence
|
GO:0001906; GO:0005576; GO:0031640; GO:0042742; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:14568161, ECO:0000269|PubMed:23687264}. Note=Produces a secreted protein originating from this gene (PubMed:12817086), secreted by the general secretory pathway (PubMed:14568161).
|
SIGNAL 1..32; /evidence="ECO:0000269|PubMed:10816431"
| null | null |
IPR023888;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
sdpC yvaY BSU33770
| true |
Bacillus subtilis
| 5 |
row_146
| false | null |
6,965 |
P96723
|
MENEYDMKSIKEKGVDFEDLWFSSVSDEILDNPEDENGQPFTGLAYELYPNGQIIYFTKYKNGLAHGLTCEFYENGNKKSEKEYRYGQLHGISIIWFENGRKKSEQQYEHSILISEKNWDEEGNLLNKYEIDTDSPHFEILESRRETHINLGRE
|
Immunity protein YwqK
|
Bacillus subtilis (strain 168)
| 224,308 | 154 | 18,217 |
Cytoplasm;Reference proteome;Toxin
|
GO:0005737; GO:0090729
|
Evidence at protein level
| 2 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null |
PF07661;
|
IPR011652;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus subtilis (species), Bacillus subtilis subsp. subtilis (subspecies)
|
ywqK BSU36180
| true |
Bacillus subtilis
| 6 |
row_6687
| false | null |
1,305 |
O74486
|
MKNKYYPLRSSMDELSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSENINLKDPKQMGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFAVWCASCLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVTSISLAKCVKLTAVFLAQCVKVTAVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILEGAGRAIRGANDNNDIPLGEMEVESEV
|
Meiotic driver wtf19
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
| 284,812 | 393 | 43,945 |
Alternative initiation;Cytoplasm;Endoplasmic reticulum;Membrane;Reference proteome;Toxin;Transmembrane;Transmembrane helix;Vacuole
|
GO:0005737; GO:0005774; GO:0005789; GO:0005794; GO:0072324; GO:0110134
|
Evidence at transcript level
| 4 |
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
| null |
TRANSMEM 104..124; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 137..157; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 167..187; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 208..228; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 233..253; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 269..289; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 296..316; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 332..352; /note="Helical"; /evidence="ECO:0000255"
|
PF03303;
|
IPR004982;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), Taphrinomycotina (subphylum), Schizosaccharomycetes (class), Schizosaccharomycetales (order), Schizosaccharomycetaceae (family), Schizosaccharomyces (genus), Schizosaccharomyces pombe (species)
|
wtf19 SPCC1906.03
| true |
Schizosaccharomyces pombe
| 0 |
row_1246
| false | null |
166 |
O74420
|
MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
|
Meiotic driver wtf13
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
| 284,812 | 388 | 42,607 |
Alternative initiation;Cytoplasm;Endoplasmic reticulum;Membrane;Reference proteome;Toxin;Transmembrane;Transmembrane helix;Vacuole
|
GO:0005737; GO:0005774; GO:0005789; GO:0072324; GO:0110134
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000255, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000269|PubMed:30475921}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000255, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
| null |
TRANSMEM 89..109; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 119..139; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 152..172; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 182..202; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 207..227; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 243..263; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 267..287; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 297..317; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 331..351; /note="Helical"; /evidence="ECO:0000255"
|
PF03303;
|
IPR004982;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), Taphrinomycotina (subphylum), Schizosaccharomycetes (class), Schizosaccharomycetales (order), Schizosaccharomycetaceae (family), Schizosaccharomyces (genus), Schizosaccharomyces pombe (species)
|
wtf13 wtf12 SPCC162.04c
| true |
Schizosaccharomyces pombe
| 1 |
row_153
| false | null |
3,031 |
O94409
|
MKNKYYPLRSSMDELSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSENINLKDPKQMGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFGVWCAICLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILGGIGNAMMGLANAFRGGNDNNNNIPLGEMDVEGEV
|
Meiotic driver wtf23
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
| 284,812 | 368 | 41,197 |
Alternative initiation;Cytoplasm;Endoplasmic reticulum;Membrane;Reference proteome;Toxin;Transmembrane;Transmembrane helix;Vacuole
|
GO:0005774; GO:0005789; GO:0005794; GO:0072324; GO:0110134
|
Inferred from homology
| 3 |
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
| null |
TRANSMEM 105..124; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 139..158; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 170..192; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 202..221; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 234..256; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 266..283; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 328..350; /note="Helical"; /evidence="ECO:0000255"
|
PF03303;
|
IPR004982;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), Taphrinomycotina (subphylum), Schizosaccharomycetes (class), Schizosaccharomycetales (order), Schizosaccharomycetaceae (family), Schizosaccharomyces (genus), Schizosaccharomyces pombe (species)
|
wtf23 wtf10 SPCC1620.02
| true |
Schizosaccharomyces pombe
| 2 |
row_2930
| false | null |
779 |
Q9P3V0
|
MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIVIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
|
Meiotic driver wtf4
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
| 284,812 | 366 | 40,360 |
Alternative initiation;Cytoplasm;Endoplasmic reticulum;Membrane;Reference proteome;Toxin;Transmembrane;Transmembrane helix;Vacuole
|
GO:0000324; GO:0005737; GO:0005774; GO:0005789; GO:0072324; GO:0110134
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
| null |
TRANSMEM 89..109; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 119..139; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 149..169; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 185..205; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 221..241; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 245..265; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 275..295; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 309..329; /note="Helical"; /evidence="ECO:0000255"
|
PF03303;
|
IPR004982;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), Taphrinomycotina (subphylum), Schizosaccharomycetes (class), Schizosaccharomycetales (order), Schizosaccharomycetaceae (family), Schizosaccharomyces (genus), Schizosaccharomyces pombe (species)
|
wtf4 wtf13 SPCC548.03c
| true |
Schizosaccharomyces pombe
| 3 |
row_729
| false | null |
167 |
O84616
|
MMEVFMNFLDQLDLIIQNKHMLEHTFYVKWSKGELTKEQLQAYAKDYYLHIKAFPKYLSAIHSRCDDLEARKLLLDNLMDEENGYPNHIDLWKQFVFALGVTPEELEAHEPSEAAKAKVATFMRWCTGDSLAAGVAALYSYESQIPRIAREKIRGLTEYFGFSNPEDYAYFTEHEEADVRHAREEKALIEMLLKDDADKVLEASQEVTQSLYGFLDSFLDPGTCCSCHQSY
|
4-aminobenzoate synthase (EC 1.3.3.-) (Chlamydia protein associating with death domains) (CADD) (para-aminobenzoate synthase) (PABA synthase)
|
Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
| 272,561 | 231 | 26,734 |
3D-structure;Host cytoplasm;Iron;Metal-binding;Oxidoreductase;Reference proteome;Secreted;Toxin;Virulence
|
GO:0005576; GO:0006790; GO:0016491; GO:0030430; GO:0044281; GO:0046872; GO:0090729; GO:0141072
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11805081}. Host cytoplasm {ECO:0000269|PubMed:11805081}. Note=Secreted into the host cytoplasm, where it co-localizes with Fas in the proximity of the inclusion body. {ECO:0000269|PubMed:11805081}.
| null | null |
PF03070;
|
IPR027572;IPR016084;IPR039068;IPR004305;
|
1RCW;8VA9;8VAB;8VAG;8VAI;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), PVC group (clade), Chlamydiota (phylum), Chlamydiia (class), Chlamydiales (order), Chlamydiaceae (family), Chlamydia/Chlamydophila group (no rank), Chlamydia (genus), Chlamydia trachomatis (species)
|
CT_610
| true |
Chlamydia trachomatis
| 0 |
row_154
| false | null |
4,596 |
Q4JHE2
|
MNVFFMFSLLFLAALESCADDRRRPLEECFQEADYEEFLEIARNGLNETSNPKHVVVVGAGMAGLSAAYVLAGAGHNVTLLEASERVGGRVNTYRNETEGWYVNLGPMRLPERHRIIREYIRKFGLKLNEFLQENENAWYFIRNIRKRVWEVKKDPGVFKYPVEPSEEGKSASQLYRESLEKVIEELKRTNCSYILNKYDTYSTKEYLIKEGNLSRGAVDMIGKLPNEDSSYYLSFIESLKSDDLFSYEKRFDEIVGGFDQLPISMYQAIAEMVHLNAQVIKIQHNAEEVRVAYQTPAKTLSYVTADYVIVCSTSRAARRIYFEPPLPPKKAHALRSIHYRSGTKIFLTCTRKFWEADGIHGGKSTTDLPSRFIYYPNHNFTSDVGVIVAYTLADDADFFQALDIKTSADIVINDLSLIHQLPKEEIQALCYPSMIKKWSLDKYAMGAITSFTPYQFQDFIETVAAPVGRIYFAGEYTARVHGWLDSTIKSGLTAARDVNRASQKPSRRQLSNDNEL
|
L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 517 | 59,058 |
Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Oxidoreductase;Secreted;Signal;Toxin
|
GO:0001716; GO:0005576; GO:0006915; GO:0009063; GO:0031640; GO:0042742; GO:0090729
|
Evidence at transcript level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16261251}.
|
SIGNAL 1..18; /evidence="ECO:0000250|UniProtKB:P81382"
| null |
PF01593;
|
IPR002937;IPR036188;IPR001613;IPR050281;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 0 |
row_4374
| false | null |
513 |
P82807
|
MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRSNSLFEEIRPGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLPNYEGKNCEKVLYQSCRVDNGNCWHFCKRVQSETQCSCAESYRLGVDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKATLLKKSDNPSPDIRIVNGMDCKLGECPWQAVLINEKGEVFCGGTILSPIHVLTAAHCINQTKSVSVIVGEIDISRKETRRLLSVDKIYVHTKFVPPNYYYVHQNFDRVAYDYDIAIIRMKTPIQFSENVVPACLPTADFANEVLMKQDSGIVSGFGRIRFKEPTSNTLKVITVPYVDRHTCMLSSDFRITQNMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIISWGEGCARKGKYGVYTKVSRFIPWIKKIMSLK
|
Venom prothrombin activator notecarin-D1 (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Notecarin-D1 light chain; Notecarin-D1 heavy chain]
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 455 | 51,464 |
Blood coagulation cascade activating toxin;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Repeat;Secreted;Signal;Toxin
|
GO:0004252; GO:0005509; GO:0005576; GO:0005615; GO:0006508; GO:0007596; GO:0016504; GO:0035807; GO:0044469; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10779512, ECO:0000269|PubMed:12403650}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
| null |
PF00008;PF14670;PF00594;PF00089;
|
IPR017857;IPR001881;IPR000742;IPR000152;IPR018097;IPR035972;IPR000294;IPR012224;IPR050442;IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 1 |
row_477
| false | null |
2,024 |
Q3HXY5
|
MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAQTHEGLKTSRNTDQRHPAPKKAEDQELGSVANIIVDPKLFQKRRFQSSRVLFSTQPPPLSRDEQSVEFLDNEDTLNRNIRAKRENHPVHNQGEHSVCDSVSDWVIKTTATDIRGNMVTVMVDINRDNEVYKQYFFETKCRNPNPNPVQSECRGIDSRLWNSYCTTTRTFVRALTMEGNQASWRFIRIDTACVCVIIRKTDNF
|
Venom nerve growth factor 3 (v-NGF-3) (vNGF-3)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 244 | 27,789 |
Cleavage on pair of basic residues;Disulfide bond;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
|
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008191; GO:0008289; GO:0021675; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
|
Evidence at transcript level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61898}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF00243;
|
IPR029034;IPR020408;IPR002072;IPR020425;IPR019846;IPR020433;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 2 |
row_1943
| false | null |
2,025 |
Q3HXY6
|
MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAQTHEGLKTSRNTDQRHPAPKKAEDQELGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNEDTLNRNIRAKRENHPVHNQGEHSVCDSVSDWVIKTTATDIRGNMVTVMVDINRNNEVYKQYFFETKCRNPNPNPVQSERRGIDSRLWNSYCTTTQTFVRALTMEGNQASWRFIRIDTACVCVIIRKTDNF
|
Venom nerve growth factor 2 (v-NGF-2) (vNGF-2)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 244 | 27,795 |
Cleavage on pair of basic residues;Disulfide bond;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
|
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008191; GO:0008289; GO:0021675; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
|
Evidence at transcript level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61898}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF00243;
|
IPR029034;IPR020408;IPR002072;IPR020425;IPR020433;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 3 |
row_1944
| false | null |
7,075 |
Q3SB04
|
MIAFIVLLSLAAVLQQSSGTVDFASESSNKKDYQKEIVDKHNALRRSVKPTARNMLRMEWNSHAAQNAKRWADRCTFAHSPPHTRTVGKLRCGENIFMSSQPFAWSGVVQAWYDEVKKFVYGIGAKPPGSVIGHYTQVVWYKSHLLGCASAKCSSTKYLYVCQYCPAGNIRGSIATPYKSGPTCGDCPSACVNGLCTNPCKYEDDFSNCKALAKNSKCQTEWIKSKCPAACFCHNKII
|
Cysteine-rich venom protein pseudechetoxin-like (CRVP)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 238 | 26,327 |
Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Signal;Toxin
|
GO:0005576; GO:0090729; GO:0099106
|
Evidence at transcript level
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
SIGNAL 1..19; /evidence="ECO:0000250"
| null |
PF00188;PF08562;
|
IPR018244;IPR014044;IPR035940;IPR042076;IPR001283;IPR013871;IPR034117;IPR003582;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 4 |
row_6797
| false | null |
2,265 |
Q9PSN5
|
NLYQFGNMIQCANHGRRPTRHYMDYGCYCGKGGSGTPVDELDRCCQTHDDCYGEAEKLPACNYMMSGPYYNTYSYECNEGELTCKDNNDECKAFICNCDRTAAICFARAPYNDANWNIDTKTRCQ
|
Acidic phospholipase A2 HTe (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 125 | 14,262 |
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Neurotoxin;Secreted;Toxin
|
GO:0005102; GO:0005509; GO:0005543; GO:0005576; GO:0006633; GO:0006644; GO:0016042; GO:0047498; GO:0048146; GO:0050482; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted.
| null | null |
PF00068;
|
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 5 |
row_2181
| false | null |
173 |
P00608
|
NLVQFSYLIQCANHGKRPTWHYMDYGCYCGAGGSGTPVDELDRCCKIHDDCYDEAGKKGCFPKMSAYDYYCGENGPYCRNIKKKCLRFVCDCDVEAAFCFAKAPYNNANWNIDTKKRCQ
|
Basic phospholipase A2 notexin (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 119 | 13,593 |
3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Neurotoxin;Presynaptic neurotoxin;Secreted;Toxin
|
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted.
| null | null |
PF00068;
|
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
|
1AE7;4E4C;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 6 |
row_160
| false | null |
3,038 |
P01384
|
MKTLLLTLVVVTIVCLDLGDSLICYMGPKTPRTCPRGQNLCYTKTWCDAFCSSRGKVVELGCAATCPIAKSYEDVTCCSTDNCNPFPVRPRPHP
|
Alpha-elapitoxin-Nss2a (Alpha-EPTX-Nss2a) (Long neurotoxin 1) (LNTX-1) (Notechis III-4)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 94 | 10,289 |
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin
|
GO:0005576; GO:0030550; GO:0090729; GO:0099106
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:497256}.
|
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:497256"
| null |
PF21947;
|
IPR003571;IPR045860;IPR018354;IPR054131;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 7 |
row_2936
| false | null |
5,201 |
A8HDK0
|
MKTLLLTLVVVTIVFLDLGYTMTCCNQQSSQPKTTTTCAESSCYKKTWRDHRGTITERGCGCPNVKPGVQINCCKTDECNN
|
Short neurotoxin 1 (SNTX-1)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 81 | 8,982 |
Acetylcholine receptor inhibiting toxin;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin
|
GO:0005576; GO:0030550; GO:0090729; GO:0099106
|
Inferred from homology
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
SIGNAL 1..21; /evidence="ECO:0000250"
| null |
PF21947;
|
IPR003571;IPR045860;IPR018354;IPR054131;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 8 |
row_4968
| false | null |
7,065 |
Q3SAE7
|
SGSKTAKIGDGCFGLPLDRIGSTSGMGCGSVPKPTPGGS
|
Natriuretic peptide NsNP-b
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 39 | 3,681 |
Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
|
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
|
Evidence at transcript level
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16908092}.
| null | null |
PF00212;
|
IPR000663;IPR030480;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 9 |
row_6787
| false | null |
7,066 |
Q3SAE8
|
SGSEVAKIGDGCFGLPLDRIGSASGMGCRSVPKPTPGGS
|
Natriuretic peptide NsNP-a
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 39 | 3,749 |
Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
|
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
|
Evidence at transcript level
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16908092}.
| null | null |
PF00212;
|
IPR000663;IPR030480;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 10 |
row_6788
| false | null |
6,357 |
P0DL19
|
SNKKDYQKEIVDKHNALRRSVK
|
Cysteine-rich venom protein notescatin (CRVP) (Notescatin-a) (Notescatin-b)
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
| 70,142 | 22 | 2,657 |
Direct protein sequencing;Disulfide bond;Secreted;Toxin
|
GO:0005576; GO:0090729
|
Evidence at protein level
| 2 |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 11 |
row_6109
| false | null |
1,468 |
P0CY52
|
SNSLFEEVRPIVNGMDCKLG
|
Venom prothrombin activator notanarin-D (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Notanarin-D light chain; Notanarin-D heavy chain]
|
Notechis scutatus niger (Peninsula tiger snake) (Notechis ater niger)
| 1,027,870 | 20 | 2,209 |
Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Secreted;Toxin
|
GO:0004252; GO:0005576; GO:0006508; GO:0016504; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12403650}.
| null | null | null | null | null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
| null | true |
Notechis scutatus
| 12 |
row_1407
| false | null |
232 |
P09545
|
MPKLNRCAIAIFTILSAISSPTLLANINEPSGEAADIISQVADSHAIKYYNAADWQAEDNALPSLAELRDLVINQQKRVLVDFSQISDAEGQAEMQAQFRKAYGVGFANQFIVITEHKGELLFTPFDQAEEVDPQLLEAPRTARLLARSGFASPAPANSETNTLPHVAFYISVNRAISDEECTFNNSWLWKNEKGSRPFCKDANISLIYRVNLERSLQYGIVGSATPDAKIVRISLDDDSTGAGIHLNDQLGYRQFGASYTTLDAYFREWSTDAIAQDYRFVFNASNNKAQILKTFPVDNINEKFERKEVSGFELGVTGGVEVSGDGPKAKLEARASYTQSRWLTYNTQDYRIERNAKNAQAVSFTWNRQQYATAESLLNRSTDALWVNTYPVDVNRISPLSYASFVPKMDVIYKASATETGSTDFIIDSSVNIRPIYNGAYKHYYVVGAHQSYHGFEDTPRRRITKSASFTVDWDHPVFTGGRPVNLQLASFNNRCIQVDAQGRLAANTCDSQQSAQSFIYDQLGRYVSASNTKLCLDGEALDALQPCNQNLTQRWEWRKGTDELTNVYSGESLGHDKQTGELGLYASSNDAVSLRTITAYTDVFNAQESSPILGYTQGKMNQQRVGQDHRLYVRAGAAIDALGSASDLLVGGNGGSLSSVDLSGVKSITATSGDFQYGGQQLVALTFTYQDGRQQTVGSKAYVTNAHEDRFDLPAAAKITQLKIWSDDWLVKGVQFDLN
|
Hemolysin
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
| 243,277 | 741 | 81,962 |
3D-structure;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Host cell membrane;Host membrane;Lectin;Membrane;Reference proteome;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Virulence
|
GO:0005576; GO:0016020; GO:0020002; GO:0030246; GO:0042802; GO:0051715; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15978620}. Host cell membrane {ECO:0000269|PubMed:15978620}; Multi-pass membrane protein {ECO:0000269|PubMed:15978620}. Note=In the hemolytic biotype El Tor the 80 kDa hemolysin precursor is secreted as monomer. After binding to target membranes the protein assembles into a heptameric prepore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation.
|
SIGNAL 1..25; /evidence="ECO:0000269|PubMed:2174833"
| null |
PF16458;PF12563;PF07968;
|
IPR032496;IPR022220;IPR043080;IPR044883;IPR036404;IPR016183;IPR036435;IPR035992;IPR000772;
|
1XEZ;3O44;4GX7;7YL9;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
|
hlyA VC_A0219
| true |
Vibrio cholerae
| 0 |
row_217
| false | null |
6,755 |
P38442
|
MSIFIHHGAPGSYKTSGALWLRLLPAIKSGRHIITNVRGLNLERMAKYLKMDVSDISIEFIDTDHPDGRLTMARFWHWARKDAFLFIDECGRIWPPRLTVTNLKALDTPPDLVAEDRPESFEVAFDMHRHHGWDICLTTPNIAKVHNMIREAAEIGYRHFNRATVGLGAKFTLTTHDAANSGQMDSHALTRQVKKIPSPIFKMYASTTTGKARDTMAGTALWKDRKILFLFGMVFLMFSYSFYGLHDNPIFTGGNDATIESEQSEPQSKATVGNAVGSKAVAPASFGFCIGRLCVQDGFVTVGDERYRLVDNLDIPYRGLWATGHHIYKDTLTVFFETESGSVPTELFASSYRYKVLPLPDFNHFVVFDTFAAQALWVEVKRGLPIKTENDKKGLNSIF
|
Zona occludens toxin (Zonular occludens toxin) (Zot)
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
| 243,277 | 399 | 44,903 |
Enterotoxin;Reference proteome;Toxin;Virulence
|
GO:0090729
|
Evidence at protein level
| 2 | null | null | null |
PF05707;
|
IPR027417;IPR008900;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
|
zot VC_1458
| true |
Vibrio cholerae
| 1 |
row_6503
| false | null |
207 |
P01555
|
MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL
|
Cholera enterotoxin subunit A (Cholera enterotoxin, A chain) [Cleaved into: Cholera enterotoxin subunit A1 (EC 2.4.2.-) (Cholera enterotoxin A1 chain) (Cholera enterotoxin alpha chain) (NAD(+)--diphthamide ADP-ribosyltransferase); Cholera enterotoxin subunit A2 (Cholera enterotoxin A2 chain) (Cholera enterotoxin gamma chain)]
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
| 243,277 | 258 | 29,336 |
3D-structure;Direct protein sequencing;Disulfide bond;Enterotoxin;Glycosyltransferase;NAD;Nucleotidyltransferase;Reference proteome;Signal;Toxin;Transferase;Virulence
|
GO:0005534; GO:0005615; GO:0008289; GO:0016757; GO:0016779; GO:0042531; GO:0042597; GO:0090729; GO:0141104; GO:1902494
|
Evidence at protein level
| 5 | null |
SIGNAL 1..18; /evidence="ECO:0000269|PubMed:7238869, ECO:0000269|PubMed:955672"
| null |
PF01375;
|
IPR001144;
|
1S5B;1S5C;1S5D;1S5E;1S5F;1XTC;2A5D;2A5F;2A5G;8OXS;8Q6I;8QRE;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
|
ctxA toxA VC_1457
| true |
Vibrio cholerae
| 2 |
row_194
| false | null |
208 |
P01556
|
MIKLKFGVFFTVLLSSAYAHGTPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN
|
Cholera enterotoxin subunit B (Cholera enterotoxin B chain) (Cholera enterotoxin gamma chain) (Choleragenoid)
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
| 243,277 | 124 | 13,957 |
3D-structure;Direct protein sequencing;Disulfide bond;Enterotoxin;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence
|
GO:0005534; GO:0005576; GO:0016020; GO:0020002; GO:0042531; GO:0042597; GO:0046812; GO:0090729; GO:1902494
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
|
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:903362, ECO:0000269|PubMed:903363"
| null |
PF01376;
|
IPR008992;IPR001835;
|
1CHP;1CHQ;1CT1;1FGB;1G8Z;1JR0;1MD2;1RCV;1RD9;1RDP;1RF2;1S5B;1S5C;1S5D;1S5E;1S5F;1XTC;2CHB;3CHB;3EFX;5ELC;5ELE;5ELF;5LZG;5LZJ;6HJD;6HMW;6HMY;6HSV;7LVB;8OXS;8Q6I;8QRE;9EWF;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
|
ctxB toxB VC_1456
| true |
Vibrio cholerae
| 3 |
row_195
| false | null |
6,754 |
P38441
|
MLMMDTLYDWLIDGFTWLVIKLGIMWIESKIFVIQFFWEMSQKVIDMFTIYPLIQQAIDMLPPQYSGFLFFLGLDQALAIVLQALMTRFALRALNL
|
Accessory cholera enterotoxin (Ace)
|
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
| 243,277 | 96 | 11,347 |
Enterotoxin;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Toxin;Transmembrane;Transmembrane helix;Virulence
|
GO:0005576; GO:0016020; GO:0020002; GO:0090729
|
Predicted
| 2 |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
| null |
TRANSMEM 76..96; /note="Helical"; /evidence="ECO:0000255"
|
PF10734;
|
IPR019670;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
|
ace VC_1459
| true |
Vibrio cholerae
| 4 |
row_6502
| false | null |
212 |
P04512
|
MEKLTDLNYTLSVITLMNNTLHTILEDPGMAYFPYIASVLTGLFALNKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIYDKLTVQTTGEIDMTKEINQKNVRTLEEWESGKNPYEPREVTAAM
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain Both))
| 37,137 | 175 | 20,267 |
3D-structure;Activation of host autophagy by virus;Calcium;Direct protein sequencing;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Reference proteome;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08434, ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091, ECO:0000269|PubMed:17376898}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091, ECO:0000269|PubMed:17035333}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
|
1G1I;1G1J;2O1K;
|
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Simian rotavirus A (no rank), Simian rotavirus A/SA11 (no rank)
| null | true |
Rotavirus A
| 0 |
row_199
| false | null |
958 |
B3SRV6
|
MDKLADLNYTLSVITLMNDTLHSIIQDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVIKYCIVTIINTLLKLAGYKEQVTTKDEIEQQMDRIVKEMRRQLEMIDKLTTREIEQVELLKRIHDNLITRSVDVIDMSKEFNQKNIKTLDEWESGKNPYEPSEVTASM
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A)
| 10,957 | 175 | 20,237 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Inferred from homology
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G3 (no rank)
| null | true |
Rotavirus A
| 1 |
row_903
| false | null |
1,293 |
O11982
|
MEKLADLNYTLGVITLLNDTLHNILEEPGMVYFPYVASALTVLFTMHKASLPAMKLAMRTSQCSYRIIKRVVVTLINTLLRLGGYNDYLTDKDETEKQINRVVKELRQQLTMIEKLTTREIEQVELLKRIYDMMVVRHDREIDMSKETNQKAFNTLHDWGNDRNYDDNTDVIAPL
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (isolate RVA/Mouse/Brazil/EHP/1981/G16P[20]) (RV-A)
| 578,840 | 175 | 20,413 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Evidence at transcript level
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G16 (no rank)
| null | true |
Rotavirus A
| 2 |
row_1234
| false | null |
1,303 |
O56850
|
MEKLTDLNYTLSVITLMNDTLHTIMEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALRTSRCSYKVIKYCIVSIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIHDMLIIKPVDKIDMSQEFNQRQFKTLNEWAEGENPYEPKEVTASL
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (strain RVA/Human/Japan/AU-1/1982/G3P3[9]) (RV-A)
| 39,013 | 175 | 20,513 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Evidence at transcript level
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G3 (no rank)
| null | true |
Rotavirus A
| 3 |
row_1244
| false | null |
1,694 |
P30031
|
MEKLTVLNYTLNVITLMNSTLHTILEDPGMAYFPYIASVLTVLFTLHRASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLADYKEQITTKDEIEKQMDRVAKEMRRQLEMIDKLTTREIEQVKLLKRIYDKLMVRATDGIDMTKEINQKNVKTLEEWKSGKNPYEPKEVTAAM
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (isolate RVA/Human/United Kingdom/A64/1987/G10P11[14]) (RV-A)
| 578,827 | 175 | 20,360 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Inferred from homology
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G10 (no rank), Rotavirus G10P11 (no rank)
| null | true |
Rotavirus A
| 4 |
row_1623
| false | null |
2,034 |
Q3ZK64
|
MDKLTDLNYTLSVITLMNSTLHKILEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSRCSYKVIKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVREMRRQLEMIDKLTTREIEQVELLRRIYDRLTVQKTDEIDMSKEINQKNVRTLDEWENGKNPYEPSEVTASL
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (isolate RVA/Human/Belgium/B4106/2000/G3P11[14]) (RV-A) (Rotavirus A (isolate B4106))
| 578,843 | 175 | 20,487 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Inferred from homology
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G3 (no rank)
| null | true |
Rotavirus A
| 5 |
row_1952
| false | null |
2,280 |
Q9PYC8
|
MEKLTDLNYTLSVITLMNSTLHTILEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMERVVKEMRRHFKMIDKLTTREIEQVGLLKRIHDKLDIRAVDEIDMTKEINQKNVRTLEEWEWGKNPYEPKEVTAAM
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (isolate RVA/Cow/United States/B223/1983/G10P8[11]) (RV-A)
| 1,835,656 | 175 | 20,446 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Inferred from homology
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G10 (no rank), Rotavirus G10P11 (no rank)
| null | true |
Rotavirus A
| 6 |
row_2196
| false | null |
2,295 |
Q9WAI7
|
MDKLADLNYTLSVVTLMNDTLHSIIQDPGMAYFPYVASVLTVLFALHKASIPTMKMALKTSKCSYKVIKYCIVPIINTLFKLAGFQEPITTKDEIEQPMDGIVKEIRRPLEMIDKLTTPEIEQVELLKSLHDHLITRPVDVIDMSKEFNQKNIKTLDEWDSGKNPYEPSEVTASM
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (strain RVA/Human/Japan/MO/1982/G3P1A[8]) (RV-A)
| 10,956 | 175 | 19,905 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Inferred from homology
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G1 (no rank)
| null | true |
Rotavirus A
| 7 |
row_2211
| false | null |
2,187 |
Q8V790
|
MENATTINETLVEEVYNMTMSYFEHNVIIMKYFPFLASILTIAFTAWKMGKSTFKVTKTVAGSGFKVVRVIVITIFNCIMRLFGSKTEIVSDDRLDALASKILAQINNQVKVIEQLTKRELEQVKLLADIYEMLKFKKDEVDMSFETNKKEYEKWVKDPYQPTRAVSLD
|
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
|
Rotavirus A (strain RVA/Turkey/Ireland/Ty-1/1978/G7P[17]) (RV-A)
| 12,584 | 169 | 19,572 |
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
|
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
|
Inferred from homology
| 4 |
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
| null |
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
|
PF01452;
|
IPR002107;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Avian rotavirus A (no rank)
| null | true |
Rotavirus A
| 8 |
row_2103
| false | null |
215 |
P04977
|
MRCTRAIRQTARTGWLTWLAILAVTAPVTSPAWADDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLDHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVIGACMARQAESSEAMAAWSERAGEAMVLVYYESIAYSF
|
Pertussis toxin subunit 1 (PTX S1) (Islet-activating protein S1) (IAP S1) (NAD-dependent ADP-ribosyltransferase) (EC 2.4.2.-)
|
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
| 257,313 | 269 | 29,974 |
3D-structure;Direct protein sequencing;Disulfide bond;Glycosyltransferase;NAD;Nucleotidyltransferase;Pharmaceutical;Reference proteome;Secreted;Signal;Toxin;Transferase;Virulence;Whooping cough
|
GO:0003950; GO:0005576; GO:0016779; GO:0090729; GO:0141104
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11854200}. Note=The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secretion of assembled toxin through the outer membrane.
|
SIGNAL 1..34
| null |
PF02917;
|
IPR003898;
|
1BCP;1PRT;1PTO;6RO0;7SKI;7SKK;7SKY;7SNE;7U6Z;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
|
ptxA BP3783
| true |
Bordetella pertussis
| 0 |
row_201
| false | null |
3,124 |
P04979
|
MLINNKKLLHHILPILVLALLGMRTAQAVAPGIVIPPKALFTQQGGAYGRCPNGTRALTVAELRGNAELQTYLRQITPGWSIYGLYDGTYLGQAYGGIIKDAPPGAGFIYRETFCITTIYKTGQPAADHYYSKVTATRLLASTNSRLCAVFVRDGQSVIGACASPYEGRYRDMYDALRRLLYMIYMSGLAVRVHVSKEEQYYDYEDATFQTYALTGISLCNPAASIC
|
Pertussis toxin subunit 3 (PTX S3) (Islet-activating protein S3) (IAP S3)
|
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
| 257,313 | 227 | 24,988 |
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
|
GO:0005576; GO:0016020; GO:0020002; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
|
SIGNAL 1..28
| null |
PF03440;PF02918;
|
IPR005138;IPR037015;IPR016187;IPR008992;IPR003899;IPR020063;
|
1BCP;1PRT;1PTO;6RO0;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
|
ptxC BP3787
| true |
Bordetella pertussis
| 1 |
row_3022
| false | null |
1,355 |
P04978
|
MPIDRKTLCHLLSVLPLALLGSHVARASTPGIVIPPQEQITQHGGPYGRCANKTRALTVAELRGSGDLQEYLRHVTRGWSIFALYDGTYLGGEYGGVIKDGTPGGAFDLKTTFCIMTTRNTGQPATDHYYSNVTATRLLSSTNSRLCAVFVRSGQPVIGACTSPYDGKYWSMYSRLRKMLYLIYVAGISVRVHVSKEEQYYDYEDATFETYALTGISICNPGSSLC
|
Pertussis toxin subunit 2 (PTX S2) (Islet-activating protein S2) (IAP S2)
|
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
| 257,313 | 226 | 24,799 |
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
|
GO:0005576; GO:0016020; GO:0020002; GO:0090729; GO:0141071
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
|
SIGNAL 1..27
| null |
PF03440;PF02918;
|
IPR005138;IPR037015;IPR016187;IPR008992;IPR003899;IPR020063;
|
1BCP;1PRT;1PTO;6RO0;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
|
ptxB BP3784
| true |
Bordetella pertussis
| 2 |
row_1296
| false | null |
3,161 |
P0A3R5
|
MLRRFPTRTTAPGQGGARRSRVRALAWLLASGAMTHLSPALADVPYVLVKTNMVVTSVAMKPYEVTPTRMLVCGIAAKLGAAASSPDAHVPFCFGKDLKRPGSSPMEVMLRAVFMQQRPLRMFLGPKQLTFEGKPALELIRMVECSGKQDCP
|
Pertussis toxin subunit 4 (PTX S4) (Islet-activating protein S4) (IAP S4)
|
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
| 257,313 | 152 | 16,544 |
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
|
GO:0005576; GO:0016020; GO:0020002; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
|
SIGNAL 1..42
| null |
PF09275;
|
IPR008992;IPR015355;
|
1BCP;1PRT;1PTO;6RO0;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
|
ptxD BP3785
| true |
Bordetella pertussis
| 3 |
row_3048
| false | null |
3,125 |
P04981
|
MQRQAGLPLKANPMHTIASILLSVLGIYSPADVAGLPTHLYKNFTVQELALKLKGKNQEFCLTAFMSGRSLVRACLSDAGHEHDTWFDTMLGFAISAYALKSRIALTVEDSPYPGTPGDLLELQICPLNGYCE
|
Pertussis toxin subunit 5 (PTX S5) (Islet-activating protein S5) (IAP S5)
|
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
| 257,313 | 133 | 14,500 |
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
|
GO:0005576; GO:0016020; GO:0020002; GO:0090729
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
|
SIGNAL 1..34
| null |
PF09276;
|
IPR008992;IPR015356;
|
1BCP;1PRT;1PTO;6RO0;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
|
ptxE BP3786
| true |
Bordetella pertussis
| 4 |
row_3023
| false | null |
231 |
P09385
|
MKCILFKWVLCLLLGFSSVSYSREFTIDFSTQQSYVSSLNSIRTEISTPLEHISQGTTSVSVINHTPPGSYFAVDIRGLDVYQARFDHLRLIIEQNNLYVAGFVNTATNTFYRFSDFTHISVPGVTTVSMTTDSSYTTLQRVAALERSGMQISRHSLVSSYLALMEFSGNTMTRDASRAVLRFVTVTAEALRFRQIQREFRQALSETAPVYTMTPGDVDLTLNWGRISNVLPEYRGEDGVRVGRISFNNISAILGTVAVILNCHHQGARSVRAVNEESQPECQITGDRPVIKINNTLWESNTAAAFLNRKSQFLYTTGK
|
Shiga-like toxin 2 subunit A (SLT-2 A subunit) (SLT-2a) (SLT-IIa) (EC 3.2.2.22) (Verocytotoxin 2 subunit A) (Verotoxin 2 subunit A) (rRNA N-glycosidase 2)
|
Escherichia phage 933W (Bacteriophage 933W)
| 10,730 | 319 | 35,714 |
3D-structure;Disulfide bond;Hydrolase;Modulation of host virulence by virus;Protein synthesis inhibitor;Reference proteome;Secreted;Signal;Toxin;Viral exotoxin;Virulence
|
GO:0005576; GO:0017148; GO:0030598; GO:0090729; GO:0098676
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted.
|
SIGNAL 1..22; /evidence="ECO:0000255"
| null |
PF00161;
|
IPR036041;IPR001574;IPR017988;IPR016138;IPR016139;IPR016331;
|
1R4P;2GA4;7UJJ;8SZ2;
|
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
|
stxA2 stx2A L0103
| true |
Traversvirus tv933W
| 0 |
row_216
| false | null |
1,365 |
P09386
|
MKKMFMAVLFALASVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND
|
Shiga-like toxin 2 subunit B (SLT-2 B subunit) (SLT-2b) (SLT-IIb) (Verocytotoxin 2 subunit B) (Verotoxin 2 subunit B)
|
Escherichia phage 933W (Bacteriophage 933W)
| 10,730 | 89 | 9,874 |
3D-structure;Disulfide bond;Modulation of host virulence by virus;Reference proteome;Secreted;Signal;Toxin;Viral exotoxin;Virulence
|
GO:0005576; GO:0019836; GO:0090729; GO:0098676
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted.
|
SIGNAL 1..19; /evidence="ECO:0000255"
| null |
PF02258;
|
IPR008992;IPR003189;
|
1R4P;2GA4;6FE4;7UJJ;
|
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
|
stxB2 stx2B L0104
| true |
Traversvirus tv933W
| 1 |
row_1306
| false | null |
1,470 |
P0DF97
|
MSNKKTFKKYSRVAGLLTAALIIGNLVTANAESNKQNTASTETTTTNEQPKPESSELTTEKAGQKTDDMLNSNDMIKLAPKEMPLESAEKEEKKSEDKKKSEEDHTEEINDKIYSLNYNELEVLAKNGETIENFVPKEGVKKADKFIVIERKKKNINTTPVDISIIDSVTDRTYPAALQLANKGFTENKPDAVVTKRNPQKIHIDLPGMGDKATVEVNDPTYANVSTAIDNLVNQWHDNYSGGNTLPARTQYTESMVYSKSQIEAALNVNSKILDGTLGIDFKSISKGEKKVMIAAYKQIFYTVSANLPNNPADVFDKSVTFKELQRKGVSNEAPPLFVSNVAYGRTVFVKLETSSKSNDVEAAFSAALKGTDVKTNGKYSDILENSSFTAVVLGGDAAEHNKVVTKDFDVIRNVIKDNATFSRKNPAYPISYTSVFLKNNKIAGVNNRTEYVETTSTEYTSGKINLSHQGAYVAQYEILWDEINYDDKGKEVITKRRWDNNWYSKTSPFSTVIPLGANSRNIRIMARECTGLAWEWWRKVIDERDVKLSKEINVNISGSTLSPYGSITYK
|
Streptolysin O (SLO) (Thiol-activated cytolysin)
|
Streptococcus pyogenes serotype M3 (strain SSI-1)
| 193,567 | 571 | 63,638 |
3D-structure;Cytolysis;Hemolysis;Host cell membrane;Host membrane;Lipid-binding;Membrane;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Virulence
|
GO:0005576; GO:0015485; GO:0016020; GO:0020002; GO:0031640; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C2J9}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04IN8}. Note=Probably secreted as soluble protein by the accessory Sec system (By similarity). It then inserts into the host cell membrane and forms pores formed by transmembrane beta-strands (By similarity). {ECO:0000250|UniProtKB:P0C2J9, ECO:0000250|UniProtKB:Q04IN8}.
|
SIGNAL 1..33; /evidence="ECO:0000255"
|
TRANSMEM 260..273; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 280..289; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 358..367; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 375..387; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"
|
PF17440;PF01289;
|
IPR035390;IPR038700;IPR001869;IPR036363;IPR036359;
|
4HSC;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M3 (serotype)
|
slo SPs0132
| true |
Streptococcus pyogenes
| 0 |
row_1409
| false | null |
242 |
P0C0J1
|
MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP
|
Streptopain (EC 3.4.22.10) (Exotoxin type B) (Group A streptococcal cysteine protease) (Streptococcal cysteine proteinase) (SPE B) (Streptococcus peptidase A) (SPP)
|
Streptococcus pyogenes serotype M1
| 301,447 | 398 | 43,130 |
3D-structure;Autocatalytic cleavage;Direct protein sequencing;Host cytoplasm;Hydrolase;Methylation;Protease;Reference proteome;Secreted;Signal;Thiol protease;Toxin;Virulence;Zymogen
|
GO:0004197; GO:0005576; GO:0005829; GO:0006508; GO:0034050; GO:0042783; GO:0043655; GO:0044164; GO:0051604; GO:0090729; GO:0140321
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7516997}. Host extracellular space {ECO:0000269|PubMed:18160402, ECO:0000269|PubMed:7516997}. Host cytoplasm {ECO:0000269|PubMed:35545676}.
|
SIGNAL 1..27; /evidence="ECO:0000250|UniProtKB:P0C0J0"
| null |
PF13734;PF01640;
|
IPR038765;IPR000200;IPR025896;IPR044934;
|
2JTC;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species)
|
speB SPy_2039 M5005_Spy1735
| true |
Streptococcus pyogenes
| 1 |
row_226
| false | null |
293 |
P0DD38
|
MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP
|
Streptopain (EC 3.4.22.10) (Exotoxin type B) (SPE B) (Streptococcal cysteine proteinase) (Streptococcus peptidase A) (SPP)
|
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
| 198,466 | 398 | 43,174 |
Autocatalytic cleavage;Host cytoplasm;Hydrolase;Methylation;Protease;Secreted;Signal;Thiol protease;Toxin;Virulence;Zymogen
|
GO:0004197; GO:0005576; GO:0006508; GO:0034050; GO:0042783; GO:0043655; GO:0044164; GO:0090729; GO:0140321
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7516997}. Host extracellular space {ECO:0000269|PubMed:7516997}. Host cytoplasm {ECO:0000250|UniProtKB:P0C0J0}.
|
SIGNAL 1..27; /evidence="ECO:0000250|UniProtKB:P0C0J0"
| null |
PF13734;PF01640;
|
IPR038765;IPR000200;IPR025896;IPR044934;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M3 (serotype)
|
speB SpyM3_1742
| true |
Streptococcus pyogenes
| 2 |
row_277
| false | null |
6,821 |
P62561
|
MENNKKVLKKMVFFVLVTFLGLTISQEVFAQQDPDPSQLHRSSLVKNLQNIYFLYEGDPVTHENVKSVDQLLSHDLIYNVSGPNYDKLKTELKNQEMATLFKDKNVDIYGVEYYHLCYLCENAERSACIYGGVTNHEGNHLEIPKKIVVKVSIDGIQSLSFDIETNKKMVTAQELDYKVRKYLTDNKQLYTNGPSKYETGYIKFIPKNKESFWFDFFPEPEFTQSKYLMIYKDNETLDSNTSQIEVYLTTK
|
Exotoxin type A (Erythrogenic toxin) (SPE A) (Scarlet fever toxin)
|
Streptococcus pyogenes serotype M18 (strain MGAS8232)
| 186,103 | 251 | 29,246 |
3D-structure;Disulfide bond;Signal;Toxin;Virulence
|
GO:0005576; GO:0090729
|
Evidence at protein level
| 2 | null |
SIGNAL 1..30; /evidence="ECO:0000250"
| null |
PF02876;PF01123;
|
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;IPR006177;
|
1L0Y;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M18 (serotype)
|
speA spyM18_0393
| true |
Streptococcus pyogenes
| 3 |
row_6568
| false | null |
6,085 |
P0C0I7
|
MRYNCRYSHIDKKIYSMIICLSFLLYSNVVQANSYNTTNRHNLESLYKHDSNLIEADSIKNSPDIVTSHMLKYSVKDKNLSVFFEKDWISQEFKDKEVDIYALSAQEVCECPGKRYEAFGGITLTNSEKKEIKVPVNVWDKSKQQPPMFITVNKPKVTAQEVDIKVRKLLIKKYDIYNNREQKYSKGTVTLDLNSGKDIVFDLYYFGNGDFNSMLKIYSNNERIDSTQFHVDVSIS
|
Exotoxin type H (SPE H)
|
Streptococcus pyogenes serotype M1
| 301,447 | 236 | 27,485 |
Reference proteome;Secreted;Signal;Toxin;Virulence
|
GO:0005576; GO:0090729
|
Inferred from homology
| 2 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
SIGNAL 1..32; /evidence="ECO:0000255"
| null |
PF02876;PF01123;
|
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species)
|
speH SPy_1008
| true |
Streptococcus pyogenes
| 4 |
row_5843
| false | null |
4,763 |
Q8NKX2
|
MKKINIIKIVFIITVILISTISPIIKSDSKKDISNVKSDLLYAYTITPYDYKDCRVNFSTTHTLNIDTQKYRGKDYYISSEMSYEASQKFKRDDHVDVFGLFYILNSHTGEYIYGGITPAQNNKVNHKLLGNLFISGESQQNLNNKIILEKDIVTFQEIDFKIRKYLMDNYKIYDATSPYVSGRIEIGTKDGKHEQIDLFDSPNEGTRSDIFAKYKDNRIINMKNFSHFDIYLEK
|
Exotoxin type C (SPE C)
|
Streptococcus pyogenes serotype M18 (strain MGAS8232)
| 186,103 | 235 | 27,372 |
3D-structure;Direct protein sequencing;Signal;Toxin;Virulence;Zinc
|
GO:0005576; GO:0090729
|
Evidence at protein level
| 3 | null |
SIGNAL 1..27; /evidence="ECO:0000269|PubMed:3045005"
| null |
PF02876;PF01123;
|
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;IPR006177;
|
1AN8;1HQR;1KTK;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M18 (serotype)
|
speC spyM18_0778
| true |
Streptococcus pyogenes
| 5 |
row_4539
| false | null |
6,312 |
P0DG08
|
MKTNILTIIILSCVFSYGSQLAYADENLKDLKRSLRFAYNITPCDYENVEIAFVTTNSIHINTKQKRSECILYVDSIVSLGITDQFIKGDKVDVFGLPYNFSPPYVDNIYGGIVKHSNQGNKSLQFVGILNQDGKETYLPSEVVRIKKKQFTLQEFDLKIRKFLMEKYNIYDSESRYTSGSLFLATKDSKHYEVDLFNKDDKLLSRDSFFKRYKDNKIFNSEEISHFDIYLKTY
|
Exotoxin type G (Pyrogenic exotoxin G) (SPE G)
|
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
| 198,466 | 234 | 27,282 |
Signal;Toxin;Virulence
|
GO:0005576; GO:0090729
|
Inferred from homology
| 2 | null |
SIGNAL 1..24; /evidence="ECO:0000255"
| null |
PF02876;PF01123;
|
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;IPR006177;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M3 (serotype)
|
speG SpyM3_0155
| true |
Streptococcus pyogenes
| 6 |
row_6064
| false | null |
256 |
P0C2E9
|
MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN
|
Perfringolysin O (PFO) (Theta-toxin) (Thiol-activated cytolysin)
|
Clostridium perfringens (strain 13 / Type A)
| 195,102 | 500 | 55,830 |
3D-structure;Cytolysis;Direct protein sequencing;Hemolysis;Host cell membrane;Host membrane;Lipid-binding;Membrane;Reference proteome;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Virulence
|
GO:0001897; GO:0005576; GO:0015485; GO:0016020; GO:0020002; GO:0044179; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2878682}. Host cell membrane; Multi-pass membrane protein {ECO:0000305|PubMed:15851031}. Note=Secreted as soluble protein that then inserts into the host cell membrane and forms huge pores formed by transmembrane beta-strands. {ECO:0000305|PubMed:15851031}.
|
SIGNAL 1..28; /evidence="ECO:0000269|PubMed:2878682"
|
TRANSMEM 189..202; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 209..218; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 287..296; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 304..316; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"
|
PF17440;PF01289;
|
IPR035390;IPR038700;IPR001869;IPR036363;IPR036359;
|
1M3I;1M3J;1PFO;2BK1;2BK2;5DHL;5DIM;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Clostridia (class), Eubacteriales (order), Clostridiaceae (family), Clostridium (genus), Clostridium perfringens (species)
|
pfo pfoA pfoR CPE0163
| true |
Clostridium perfringens
| 0 |
row_240
| false | null |
250 |
P0C216
|
MKRKICKALICATLATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKIIANGKVVVDKDINEWISGNSTYNIK
|
Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase)
|
Clostridium perfringens (strain 13 / Type A)
| 195,102 | 398 | 45,530 |
3D-structure;Calcium;Cytolysis;Hemolysis;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal;Toxin;Virulence;Zinc
|
GO:0005576; GO:0008270; GO:0031640; GO:0034480; GO:0050429; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
|
SIGNAL 1..28; /evidence="ECO:0000250"
| null |
PF01477;PF00882;
|
IPR001024;IPR036392;IPR008947;IPR029002;IPR001531;
|
1CA1;1GYG;1QM6;1QMD;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Clostridia (class), Eubacteriales (order), Clostridiaceae (family), Clostridium (genus), Clostridium perfringens (species)
|
plc cpa CPE0036
| true |
Clostridium perfringens
| 1 |
row_234
| false | null |
1,358 |
P06200
|
MTENWKFRRRTFLKHGAQAATLAGLSGLFPETLRRALAVEPDIRTGTIQDVQHVVILMQENRSFDHYFGHLNGVRGFNDPRALKRQDGKPVWYQNYKYEFSPYHWDTKVTSAQWVSSQNHEWSAFHAIWNQGRNDKWMAVQYPEAMGYFKRGDIPYYYALADAFTLCEAYHQSMMGPTNPNRLYHMSGRAAPSGDGKDVHIGNDMGDGTIGASGTVDWTTYPERLSAAGVDWRVYQEGGYRSSSLWYLYVDAYWKYRLQEQNNYDCNALAWFRNFKNAPRDSDLWQRAMLARGVDQLRKDVQENTLPQVSWIVAPYCYCEHPWWGPSFGEYYVTRVLEALTSNPEVWARTVFILNYDEGDGFYDHASAPVPPWKDGVGLSTVSTAGEIEVSSGLPIGLGHRVPLIAISPWSKGGKVSAEVFDHTSVLRFLERRFGVVEENISPWRRAVCGDLTSLFDFQGAGDTQVAPDLTNVPQSDARKEDAYWQQFYRPSPKYWSYEPKSLPGQEKGQRPTLAVPYQLHATLALDIAAGKLRLTLGNDGMSLPGNPQGHSAAVFQVQPREVGNPRFYTVTSYPVVQESGEELGRTLNDELDDLLDANGRYAFEVHGPNGFFREFHGNLHLAAQMARPEVSVTYQRNGNLQLNIRNLGRLPCSVTVTPNPAYTREGSRRYELEPNQAISEVWLLRSSQGWYDLSVTASNTEANYLRRLAGHVETGKPSRSDPLLDIAAT
|
Hemolytic phospholipase C (EC 3.1.4.3) (Heat-labile hemolysin) (PLC-H) (Phosphatidylcholine cholinephosphohydrolase)
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
| 208,964 | 730 | 82,667 |
Cytolysis;Hemolysis;Hydrolase;Reference proteome;Signal;Toxin;Virulence
|
GO:0005615; GO:0015628; GO:0016042; GO:0016298; GO:0033188; GO:0034480; GO:0044179; GO:0090729
|
Inferred from homology
| 4 | null |
SIGNAL 1..38; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
| null |
PF04185;PF05506;
|
IPR017850;IPR017767;IPR007312;IPR008475;IPR006311;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)
|
plcH PA0844
| true |
Pseudomonas aeruginosa
| 0 |
row_1299
| false | null |
361 |
P11439
|
MHLTPHWIPLVASLGLLAGGSFASAAEEAFDLWNECAKACVLDLKDGVRSSRMSVDPAIADTNGQGVLHYSMVLEGGNDALKLAIDNALSITSDGLTIRLEGGVEPNKPVRYSYTRQARGSWSLNWLVPIGHEKPSNIKVFIHELNAGNQLSHMSPIYTIEMGDELLAKLARDATFFVRAHESNEMQPTLAISHAGVSVVMAQAQPRREKRWSEWASGKVLCLLDPLDGVYNYLAQQRCNLDDTWEGKIYRVLAGNPAKHDLDIKPTVISHRLHFPEGGSLAALTAHQACHLPLETFTRHRQPRGWEQLEQCGYPVQRLVALYLAARLSWNQVDQVIRNALASPGSGGDLGEAIREQPEQARLALTLAAAESERFVRQGTGNDEAGAASADVVSLTCPVAAGECAGPADSGDALLERNYPTGAEFLGDGGDISFSTRGTQNWTVERLLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRVYVPRSSLPGFYRTGLTLAAPEAAGEVERLIGHPLPLRLDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPRNVGGDLDPSSIPDKEQAISALPDYASQPGKPPREDLK
|
Exotoxin A (ETA) (EC 2.4.2.36) (NAD(+)--diphthamide ADP-ribosyltransferase) (Pseudomonas exotoxin) (PE)
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
| 208,964 | 638 | 69,284 |
3D-structure;Direct protein sequencing;Disulfide bond;Glycosyltransferase;NAD;Nucleotidyltransferase;Reference proteome;Signal;Toxin;Transferase;Virulence
|
GO:0001907; GO:0016779; GO:0047286; GO:0090729; GO:0141155
|
Evidence at protein level
| 5 | null |
SIGNAL 1..25; /evidence="ECO:0000269|PubMed:6201861"
| null |
PF09101;PF09009;PF09102;
|
IPR013320;IPR015185;IPR015099;IPR015186;IPR036478;
|
1AER;1DMA;1IKP;1IKQ;1XK9;1ZM2;1ZM3;1ZM4;1ZM9;2ZIT;3B78;3B82;3B8H;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)
|
eta PA1148
| true |
Pseudomonas aeruginosa
| 1 |
row_334
| false | null |
2,245 |
Q9I788
|
MHIQSSQQNPSFVAELSQAVAGRLGQVEARQVATPREAQQLAQRQEAPKGEGLLSRLGAALARPFVAIIEWLGKLLGSRAHAATQAPLSRQDAPPAASLSAAEIKQMMLQKALPLTLGGLGKASELATLTAERLAKDHTRLASGDGALRSLATALVGIRDGSRIEASRTQAARLLEQSVGGIALQQWGTAGGAASQHVLSASPEQLREIAVQLHAVMDKVALLRHAVESEVKGEPVDKALADGLVEHFGLEAEQYLGEHPDGPYSDAEVMALGLYTNGEYQHLNRSLRQGRELDAGQALIDRGMSAAFEKSGPAEQVVKTFRGTQGRDAFEAVKEGQVGHDAGYLSTSRDPGVARSFAGQGTITTLFGRSGIDVSEISIEGDEQEILYDKGTDMRVLLSAKDGQGVTRRVLEEATLGERSGHGEGLLDALDLATGTDRSGKPQEQDLRLRMRGLDLA
|
Exoenzyme T [Includes: GTPase-activating protein (GAP); ADP-ribosyltransferase (ADPRT) (EC 2.4.2.31)]
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
| 208,964 | 457 | 48,515 |
3D-structure;Glycosyltransferase;GTPase activation;Nucleotidyltransferase;Reference proteome;Secreted;Toxin;Transferase;Virulence
|
GO:0005096; GO:0005576; GO:0016779; GO:0090729; GO:0106274; GO:0141029
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24387107}. Note=Secreted via type III secretion system (T3SS) and delivered into the host cytoplasm. {ECO:0000305}.
| null | null |
PF03496;PF03545;
|
IPR003540;IPR050999;IPR003537;IPR014773;IPR037168;
|
4JMF;6GNN;6JNP;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)
|
exoT PA0044
| true |
Pseudomonas aeruginosa
| 2 |
row_2161
| false | null |
2,948 |
G3XDA1
|
MHIQSLQQSPSFAVELHQAASGRLGQIEARQVATPSEAQQLAQRQDAPKGEGLLARLGAALVRPFVAIMDWLGKLLGSHARTGPQPSQDAQPAVMSSAVVFKQMVLQQALPMTLKGLDKASELATLTPEGLAREHSRLASGDGALRSLSTALAGIRAGSQVEESRIQAGRLLERSIGGIALQQWGTTGGAASQLVLDASPELRREITDQLHQVMSEVALLRQAVESEVSRVSADKALADGLVKRFGADAEKYLGRQPGGIHSDAEVMALGLYTGIHYADLNRALRQGQELDAGQKLIDQGMSAAFEKSGQAEQVVKTFRGTRGGDAFNAVEEGKVGHDDGYLSTSLNPGVARSFGQGTISTVFGRSGIDVSGISNYKNEKEILYNKETDMRVLLSASDEQGVTRRVLEEAALGEQSGHSQGLLDALDLASKPERSGEVQEQDVRLRMRGLDLA
|
Secreted exoenzyme S [Includes: GTPase-activating protein (GAP); ADP-ribosyltransferase (ADPRT) (EC 2.4.2.31)]
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
| 208,964 | 453 | 48,302 |
3D-structure;Glycosyltransferase;GTPase activation;Nucleotidyltransferase;Reference proteome;Secreted;Toxin;Transferase;Virulence
|
GO:0005096; GO:0005576; GO:0016779; GO:0090729; GO:0106274
|
Evidence at protein level
| 3 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26090668}. Note=Secreted via type III secretion system (T3SS) and delivered into the host cytoplasm. {ECO:0000305}.
| null | null |
PF03496;PF03545;
|
IPR003540;IPR050999;IPR003537;IPR014773;IPR037168;
|
6Y7T;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)
|
exoS PA3841
| true |
Pseudomonas aeruginosa
| 3 |
row_2852
| false | null |
362 |
P13128
|
MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEVNYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNKVDNPIE
|
Listeriolysin O (LLO) (Thiol-activated cytolysin)
|
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
| 169,963 | 529 | 58,688 |
3D-structure;Cytolysis;Hemolysis;Host cell membrane;Host membrane;Lipid-binding;Membrane;Phosphoprotein;Reference proteome;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Ubl conjugation;Virulence
|
GO:0005576; GO:0015485; GO:0016020; GO:0020002; GO:0031640; GO:0042802; GO:0044658; GO:0090729; GO:0141160
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}. Host membrane {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}; Multi-pass membrane protein {ECO:0000269|PubMed:3110067}. Host cell membrane {ECO:0000269|PubMed:3110067}; Multi-pass membrane protein {ECO:0000269|PubMed:3110067}. Note=Secreted as soluble protein that then inserts into the host membrane and forms pores formed by transmembrane beta-strands. {ECO:0000305|PubMed:24751541}.
|
SIGNAL 1..24; /evidence="ECO:0000255"
|
TRANSMEM 214..227; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 234..243; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 312..321; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 329..341; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"
|
PF17440;PF01289;
|
IPR035390;IPR038700;IPR001869;IPR036363;IPR036359;
|
4CDB;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Listeriaceae (family), Listeria (genus), Listeria monocytogenes (species)
|
hly hlyA lisA lmo0202
| true |
Listeria monocytogenes
| 0 |
row_335
| false | null |
493 |
P75409
|
MPNPVRFVYRVDLRSPEEIFEHGFSTLGDVRNFFEHILSTNFGRSYFISTSETPTAAIRFFGSWLREYVPEHPRRAYLYEIRADQHFYNARATGENLLDLMRQRQVVFDSGDREMAQMGIRALRTSFAYQREWFTDGPIAAANVRSAWLVDAVPVEPGHAHHPAGRVVETTRINEPEMHNPHYQELQTQANDQPWLPTPGIATPVHLSIPQAASVADVSEGTSASLSFACPDWSPPSSNGENPLDKCIAEKIDNYNLQSLPQYASSVKELEDTPVYLRGIKTQKTFMLQADPQNNNVFLVEVNPKQKSSFPQTIFFWDVYQRICLKDLTGAQISLSLTAFTTQYAGQLKVHLSVSAVNAVNQKWKMTPQDIAITQFRVSSELLGQTENGLFWNTKSGGSQHDLYVCPLKNPPSDLEELQIIVDECTTHAQFVTMRAASTFFVDVQLGWYWRGYYYTPQLSGWSYQMKTPDGQIFYDLKTSKIFFVQDNQNVFFLHNKLNKQTGYSWDWVEWLKHDMNEDKDENFKWYFSRDDLTIPSVEGLNFRHIRCYADNQQLKVIISGSRWGGWYSTYDKVESNVEDKILVKDGFDRF
|
ADP-ribosylating toxin CARDS (EC 2.4.2.-) (ADP-ribosyltransferase CARDS) (Community-Acquired Respiratory Distress Syndrome Toxin) (CARDX TX)
|
Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
| 272,634 | 591 | 68,057 |
3D-structure;Cell membrane;Cell projection;Cytoplasm;Disulfide bond;Glycosyltransferase;Host cytoplasm;Host endoplasmic reticulum;Lipid-binding;Membrane;NAD;Nucleotidyltransferase;Reference proteome;Toxin;Transferase;Virulence
|
GO:0003950; GO:0005576; GO:0005737; GO:0005886; GO:0008289; GO:0009986; GO:0016779; GO:0033099; GO:0042995; GO:0044075; GO:0044164; GO:0044165; GO:0090729; GO:0141079
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16617115, ECO:0000269|PubMed:20199607}. Cytoplasm {ECO:0000269|PubMed:16617115, ECO:0000269|PubMed:20199607}. Cell surface {ECO:0000269|PubMed:15845487, ECO:0000269|PubMed:20199607}. Cell projection, attachment organelle {ECO:0000269|PubMed:20199607}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:25538194}. Host endoplasmic reticulum {ECO:0000269|PubMed:29362229, ECO:0000269|PubMed:34078958}. Note=In bacteria most protein is cytoplasmic, 7-10% is on cell surface, including in the tip (attachment) organelle (PubMed:20199607). In host cells is found in the cytosol and in a punctate pattern in the perinuclear region in the host ER (PubMed:25538194, PubMed:29362229, PubMed:34078958). In host cells, an isolated C-terminal fragment (residues 273-591) is detected in a larger punctate pattern (PubMed:34078958). In 10% of host cells colocalizes with the speck NLRP3 inflammasome complex (purified protein incubated with mouse macrophages) (PubMed:25538194). {ECO:0000269|PubMed:20199607, ECO:0000269|PubMed:25538194, ECO:0000269|PubMed:29362229, ECO:0000269|PubMed:34078958}.
| null | null |
PF22509;PF22346;PF02917;
|
IPR003898;IPR055043;IPR055042;
|
4TLV;4TLW;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Mycoplasmatota (phylum), Mycoplasmoidales (order), Mycoplasmoidaceae (family), Mycoplasmoides (genus), Mycoplasmoides pneumoniae (species)
|
cards MPN_372 MP464
| true |
Mycoplasmoides pneumoniae
| 0 |
row_457
| false | null |
580 |
Q04IN8
|
MANKAVNDFILAMNYDKKKLLTHQGESIENRFIKEGNQLPDEFVVIERKKRSLSTNTSDISVTATNDSRLYPGALLVVDETLLENNPTLLAVDRAPMTYSIDLPGLASSDSFLQVEDPSNSSVRGAVNDLLAKWHQDYGQVNNVPARMQYEKITAHSMEQLKVKFGSDFEKTGNSLDIDFNSVHSGEKQIQIVNFKQIYYTVSVDAVKNPGDVFQDTVTVEDLKQRGISAERPLVYISSVAYGRQVYLKLETTSKSDEVEAAFEALIKGVKVAPQTEWKQILDNTEVKAVILGGDPSSGARVVTGKVDMVEDLIQEGSRFTADHPGLPISYTTSFLRDNVVATFQNSTDYVETKVTAYRNGDLLLDHSGAYVAQYYITWDELSYDHQGKEVLTPKAWDRNGQDLTAHFTTSIPLKGNVRNLSVKIRECTGLAWEWWRTVYEKTDLPLVRKRTISIWGTTLYPQVEDKVEND
|
Pneumolysin (PLY) (Thiol-activated cytolysin)
|
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
| 373,153 | 471 | 52,899 |
3D-structure;Cytolysis;Direct protein sequencing;Hemolysis;Host cell membrane;Host membrane;Lipid-binding;Membrane;Reference proteome;Secreted;Toxin;Transmembrane;Transmembrane beta strand;Virulence
|
GO:0005576; GO:0015485; GO:0016020; GO:0020002; GO:0031640; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C2J9}. Host cell membrane {ECO:0000269|PubMed:28323617, ECO:0000305|PubMed:15851031}; Multi-pass membrane protein {ECO:0000269|PubMed:28323617}. Note=Secreted as soluble protein by the accessory Sec system (By similarity). It then inserts into the host cell membrane and forms pores formed by transmembrane beta-strands (PubMed:15851031, PubMed:28323617). {ECO:0000250|UniProtKB:P0C2J9, ECO:0000269|PubMed:15851031, ECO:0000269|PubMed:28323617}.
| null |
TRANSMEM 158..171; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:28323617, ECO:0007744|PDB:5LY6"; TRANSMEM 178..187; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:28323617, ECO:0007744|PDB:5LY6"; TRANSMEM 256..265; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:28323617, ECO:0007744|PDB:5LY6"; TRANSMEM 273..285; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:28323617, ECO:0007744|PDB:5LY6"
|
PF17440;PF01289;
|
IPR035390;IPR038700;IPR001869;IPR036363;IPR036359;
|
4ZGH;5AOD;5AOE;5AOF;5CR6;5CR8;5LY6;7T2A;7T2B;7T2C;7T2D;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)
|
ply SPD_1726
| true |
Streptococcus pneumoniae
| 0 |
row_543
| false | null |
584 |
Q07730
|
MKFSKIACATVFALSSQAAIIHHAPEFNMKRDVAPAAPAAPADQAPTVPAPQEFNTAITKRSIIGIIMGILGNIPQVIQIIMSIVKAFKGNKREDIDSVVAGIIADMPFVVRAVDTAMTSVASTKRDGANDDVANAVVRLPEIVARVATGVQQSIENAKRDGVPDVGLNLVANAPRLISNVFDGVSETVQQAKRDGLEDFLDELLQRLPQLITRSAESALKDSQPVKRDAGSVALSNLIKKSIETVGIENAAQIVSERDISSLIEEYFGKA
|
Extent of cell elongation protein 1 [Cleaved into: ECE1-I; ECE1-II; Candidalysin ECE1-III; ECE1-IV; ECE1-V; ECE1-VI; ECE1-VII; ECE1-VIII]
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
| 237,561 | 271 | 28,878 |
Cleavage on pair of basic residues;Host cell membrane;Host membrane;Membrane;Reference proteome;Repeat;Secreted;Signal;Toxin;Transmembrane;Transmembrane helix;Virulence
|
GO:0001897; GO:0005539; GO:0005576; GO:0009609; GO:0016020; GO:0020002; GO:0030446; GO:0044179; GO:0052553; GO:0090729; GO:0140912; GO:0141139
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23136884}.; SUBCELLULAR LOCATION: [Candidalysin ECE1-III]: Host cell membrane {ECO:0000269|PubMed:27027296}; Single-pass membrane protein {ECO:0000255}. Note=Candidalysin is delivered to the invasion pocket in which the hypha is tightly surrounded by the host membrane, to enable the full damage potential of during mucosal infection. {ECO:0000269|PubMed:34245079}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
|
TRANSMEM 62..82; /note="Helical"; /evidence="ECO:0000255"
| null | null | null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)
|
ECE1 CAALFM_C403470CA CaO19.10882 CaO19.3374
| true |
Candida albicans
| 0 |
row_547
| false | null |
602 |
Q1ID47
|
MSKVKESAIVSATSALQPQGPSSSYGLINSFAHQYDRGGANVNGKPSYTVDQAANYLLRDGAAWKDLNKDGTISLSYTFLTKAPSDFYSRGLGTFSQFSDLQKGQAKLAMQSWADVAKVTFTEAASGGDGHMTFGNFSASNGGAAFAYLPFDMPGSHKGESWYLINSSYQVNTTPGTGNYGRQTLTHEIGHVLGLSHPGDYNAGEGNPTYRDATYAQDTRGYSVMSYWSESNTGQNFVKAGGQYYASAPLMDDIAAIQKLYGANYATRSGDTVYGFNSNADRDFYSATSSSSKLVFSVWDGGGNDTFDFSGFTQNQKINLNETSFSDVGGMIGNVSIAKGVTIENAFGGSGNDLLIGNALANVLKGGAGNDIIYGGGGADQLWGGTGADTFVFGAISDSTKAAPDRIMDFTSGQDKIDLSAISAFAVNKLPLQFVNAFTGHAGEAVLSYDQGTNLGSLSIDFTGNSSADFLVTTVGQAAVTDIVV
|
Metalloprotease AprA (EC 3.4.24.-)
|
Pseudomonas entomophila (strain L48)
| 384,676 | 485 | 50,931 |
Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Toxin;Virulence;Zinc
|
GO:0004222; GO:0005509; GO:0005615; GO:0008233; GO:0008270; GO:0030198; GO:0030574; GO:0031638; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16789834, ECO:0000269|PubMed:21980286}. Note=Is probably secreted via the associated Type 1 transporter encoded by aprDEF. {ECO:0000305|PubMed:16789834}.
| null | null |
PF00353;PF08548;PF13583;
|
IPR018511;IPR001343;IPR024079;IPR016294;IPR013858;IPR006026;IPR034033;IPR011049;
| null |
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas entomophila (species)
|
aprA PSEEN1550
| true |
Pseudomonas entomophila
| 0 |
row_563
| false | null |
601 |
Q1I8U1
|
MTIKEELGQPQSHSIELDEVSKEAASTRAALTSNLSGRFDQYPTKKGDFAIDGYLLDYSSPKQGCWVDGITVYGDIYIGKQNWGTYTRPVFAYLQYVETISIPQNVTTTLSYQLTKGHTRSFETSVNAKYSVGANIDIVNVGSEISTGFTRSESWSTTQSFTDTTEMKGPGTFVIYQVVLVYAHNATSAGRQNANAFAYSKTQAVGSRVDLYYLSAITQRKRVIVPSSNAVTPLDWDTVQRNVLMENYNPGSNSGHFSFDWSAYNDPHRRY
|
Monalysin (beta-barrel pore-forming toxin) (beta-PFT)
|
Pseudomonas entomophila (strain L48)
| 384,676 | 271 | 30,201 |
3D-structure;Cytolysis;Direct protein sequencing;Hemolysis;Host cell membrane;Host membrane;Ion transport;Membrane;Porin;Secreted;Toxin;Transmembrane;Transmembrane beta strand;Transport;Virulence;Zymogen
|
GO:0005576; GO:0006811; GO:0015288; GO:0020002; GO:0044179; GO:0046930; GO:0051260; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21980286}. Host cell membrane {ECO:0000305|PubMed:21980286}.
| null | null |
PF18063;
|
IPR040927;
|
4MJT;4MKO;4MKQ;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas entomophila (species)
|
mnl PSEEN3174
| true |
Pseudomonas entomophila
| 1 |
row_562
| false | null |
665 |
Q63KH5
|
MLEHGVMKIPGINNVGKTGQAGGETERIPSTEPLGSSAATSPAGPLGGLPARSSSISNTNRTGENPMITPIISSNLGLKHRVTLRKATLASLMQSLSGESSNRVMWNDRYDTLLIARDPREIKNAIEKSVTDFGGLENYKELTGGADPFALMTPVCGLSANNIFKLMTEKDVPIDPTSIEYLENTSFAEHVNTLDSHKNYVVIVNDGRLGHKFLIDLPALTQGPRTAYIIQSDLGGGALPAVRVEDWISRRGSDPVSLDELNQLLSKDFSKMPDDVQTRLLASILQIDKDPHKVDIKKLHLDGKLRFASHEYDFRQFQRNAQYVAGLG
|
Protein-glutamine deamidase Cif (EC 3.5.1.44) (Cycle-inhibiting factor homolog) (CHBP)
|
Burkholderia pseudomallei (strain K96243)
| 272,560 | 328 | 35,819 |
3D-structure;Host nucleus;Hydrolase;Reference proteome;Secreted;Toxin;Virulence
|
GO:0005576; GO:0042025; GO:0044071; GO:0050568; GO:0085034; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984}. Host nucleus {ECO:0000250|UniProtKB:P0DUW5}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984}.
| null | null |
PF16374;
|
IPR032278;
|
3EIR;3EIT;3GQM;4HCN;4HCP;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Burkholderiaceae (family), Burkholderia (genus), pseudomallei group (no rank), Burkholderia pseudomallei (species)
|
cif BPSS1385
| true |
Burkholderia pseudomallei
| 0 |
row_620
| false | null |
679 |
Q6RY98
|
IWDEPVVVSARDTEEAARVPSPQKRSQPLCSCNDINDKECMYFCHQDVIWDEPVVVSVRDTEEAARVPSPQKRPQPRCSCNDMNDKECMYFCHQDVIWDEPVVVSVRDTEEAARVPSPQKRSQPRCSCNDMNDKECVYFCHLDIIWDEPVVVSVRDTEEATRVPSPQKRSQPLCSCNDINDKECMYFCHQDIIWDEPVVVSVRDTEEAARVPSPQKRSQPLCSCNDINDKECMYFCHQDIIWDEPVVVSVRDTEEAARVPSPQKRSQPLCSCNDINDKECMYFCHQDVIWDEPVVVSVQDTEEAARVPSPQKRSQPLCSCNNMSDKECLNFCNLDIIWENVDTSADPEFLG
|
Long-sarafotoxin (L-SRTX) [Cleaved into: Sarafotoxin-m (SRTX-m); Sarafotoxin-m1 (SRTX-m1); Sarafotoxin-m2 (SRTX-m2); Sarafotoxin-m3 (SRTX-m3); Sarafotoxin-m4 (SRTX-m4); Sarafotoxin-m5 (SRTX-m5)]
|
Atractaspis microlepidota microlepidota
| 172,021 | 351 | 40,341 |
3D-structure;Cardiotoxin;Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Repeat;Secreted;Toxin;Vasoactive;Vasoconstrictor
|
GO:0003100; GO:0005179; GO:0005615; GO:0006874; GO:0014826; GO:0019229; GO:0031708; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15350691}.
| null | null |
PF00322;
|
IPR020475;IPR019764;IPR001928;
|
2LDF;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Lamprophiidae (family), Atractaspidinae (subfamily), Atractaspis (genus), Atractaspis microlepidota (species)
| null | true |
Atractaspis microlepidota
| 0 |
row_634
| false | null |
693 |
Q7NWF2
|
MRVENHSPSLSKLNPPEAGSGDPTAIGRRLSGIRRAPLPHVSAGSDGEAAAAGKIGAFLRKAVAAQSYGLMFANGKLFEATGDALEKRGQYGFSALQRLDGLSRRNLAAVEARLGALDSAERGLKERIMTGAWHFRHQSNAALDDGKTAAIASNHLLARESRSSGGNTFAGDKALLSNHDFVFFGVEFSGRGKQDKPLNHKHSTMDFGANAYVVPDTLPACRHGYLTLTDHFFNRVPGGREAEHQDFVGSFPQMGAETGRWIHEGKYRQNAPIFNYRDMKAAVALHLIEFLRDSKDAAFKAYVFDQAMQSGQALDRVLNSVFQAEFHIPRLMATTDYAKHPLRPMLLKEAVDSVNLPALSGLVSSKGDAVTAMWHAIDKGKDAVAAHLLGNWRFEAGDFASAPPGFYHELNYALSEHGASVYILDQFLSRGWAAVNAPFEHVNSGETMLDNAVKYGNREMAAALIKHGADRNLLSEWNGGKLDALLA
|
Arginine ADP-riboxanase CopC (EC 4.3.99.-)
|
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)
| 243,365 | 487 | 52,911 |
3D-structure;ANK repeat;Host cytoplasm;Lyase;Reference proteome;Repeat;Secreted;Toxin;Virulence
|
GO:0005516; GO:0005576; GO:0030430; GO:0052040; GO:0090729; GO:0140740
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0H2US87}. Host cytoplasm {ECO:0000250|UniProtKB:A0A0H2US87}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:A0A0H2US87}.
| null | null |
PF13606;PF06128;
|
IPR002110;IPR036770;IPR010366;
|
7WZS;7XN4;7XN5;7XN6;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Neisseriales (order), Chromobacteriaceae (family), Chromobacterium (genus), Chromobacterium violaceum (species)
|
copC CV_2038
| true |
Chromobacterium violaceum
| 0 |
row_648
| false | null |
753 |
Q95P65
|
MKSLIGTLGLYCLFILTNNVVSSYGDDLYPLTIMHTNDFHARFEETNVKGNPCKSGEKCIGGLARVLHTIKKIIKEQEKKNIESLYINAGDNFQGTIWYNIGRWNVTSELMNIQPPDVMVLGNHEFDHGIDGLLPFLNNMDKTEIVVANMDARDEPQVAKKIKPFTIIKKKYRNIGVIGVVVEEVPDLANTGKLKFRNESEAILEAARNLKKEDPSVNIIIVVSHVGFDVDKIIAERTGSEVDIIVGGHSHTVLYTGTPPGPEKPEDNYPYVYNHPSGNKVLVVQAVCHAKYVGNLTVFFDKKGKVVTYEGAPIYMDTKVEQDKDVLEAMKPWRKLIDEKTKLVVGRTNVDLPRDICRSEECALGNLYTDSMIYAFGGKENCKSGSTWTTAPIAFVHAGAMRSSLHQGDILYSDALLLSPFTNMVVAYDLPGAQLKAALEFSAAPKNEDEKRRFLQMSGLKVTYNMSRAANNRIVDLKVRTNVCPYDQYENLDEKKTYRVVSPSFLQGGGDGFKMLRDYAKNIQNQKIDLDALVDYLKKFSPLAPKAEGRITIIH
|
5'-nucleotidase-related protein (5'Nuc) (EC 3.6.1.5)
|
Glossina morsitans morsitans (Savannah tsetse fly)
| 37,546 | 555 | 62,064 |
Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Nucleotide-binding;Platelet aggregation inhibiting toxin;Secreted;Signal;Toxin;Zinc
|
GO:0000166; GO:0000287; GO:0004050; GO:0005178; GO:0005615; GO:0005886; GO:0006196; GO:0008253; GO:0030145; GO:0035893; GO:0090729
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20351782}.
|
SIGNAL 1..25; /evidence="ECO:0000255"
| null |
PF02872;PF00149;
|
IPR008334;IPR036907;IPR006146;IPR006179;IPR004843;IPR029052;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Brachycera (suborder), Muscomorpha (infraorder), Eremoneura (clade), Cyclorrhapha (clade), Schizophora (no rank), Calyptratae (no rank), Hippoboscoidea (superfamily), Glossinidae (family), Glossina (genus), Glossina (subgenus), Glossina morsitans (species)
| null | true |
Glossina morsitans
| 0 |
row_706
| false | null |
818 |
A0A0H3B1Q8
|
MKISPNTISPSQSDPRMSTNVSQRSRVSGIGVPVSHSINNPSIQHVQDFATLSARSLRANVLLNSDDHSVPIHAKNPSELLEAIDNNISQTAQDWGVSIQEVEVILGSSKRIIEPVCGVTANTIMKLFLDNDIFSYSFEKGQSLSLSQLQERLASLPAHKNFILRVNDGGLGHAYVIDFPATTNPSRDAFLYQSDLGEGVTREVRFEDWMTQKASHPISLDDINTHFIGIAQDQIDLAHIAKLFDVDGNVKMLRADHLISHKTSEFNFQLFEYDLKNLENNMSIIKTHCN
|
Protein-glutamine deamidase Cif (EC 3.5.1.44) (Cycle-inhibiting factor homolog) (CHYP)
|
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
| 502,800 | 290 | 32,280 |
3D-structure;Host nucleus;Hydrolase;Secreted;Toxin;Virulence
|
GO:0005576; GO:0016787; GO:0042025; GO:0044071; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUW5}. Host nucleus {ECO:0000250|UniProtKB:P0DUW5}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUW5}.
| null | null |
PF16374;
|
IPR032278;
|
4F8C;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Yersiniaceae (family), Yersinia (genus), Yersinia pseudotuberculosis complex (no rank), Yersinia pseudotuberculosis (species)
|
cif YPK_1971
| true |
Yersinia pseudotuberculosis
| 0 |
row_767
| false | null |
891 |
A3UNN4
|
MNTRFLLLLCCLSFTTFSQPFDAIKQPNRSEEEVTQLAEDFKDWSKASNGWRYSFITANEKEAVEDFSISGYQTANDYLRATDTSTWGVAGADARQYIRTVKSALNKLPKYKGTAYRGTWVKLSLLNKLEEGDVLVEPAFTSTSTLPEVAKRFSVVHPNSPQRLKRVLFEVKINQGGHTIAGLSEYSKEAEVLFAPNAHFRITQIERTSNHTYIGVETVKASAVKNTQKYNLYSGEEVEASFWHSLVCT
|
Putative NAD(+)--arginine ADP-ribosyltransferase Vis (EC 2.4.2.31) (Putative mono(ADP-ribosyl)transferase) (mADPRT) (mART) (Toxin Vis)
|
Vibrio splendidus (strain 12B01)
| 314,291 | 249 | 28,087 |
3D-structure;Glycosyltransferase;NAD;NADP;Nucleotide-binding;Nucleotidyltransferase;Secreted;Signal;Toxin;Transferase;Virulence
|
GO:0000166; GO:0005576; GO:0016779; GO:0090729; GO:0106274
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF03496;
|
IPR003540;
|
4XZJ;4XZK;4Y1W;4YC0;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio splendidus (species)
|
V12B01_18061
| true |
Vibrio splendidus
| 0 |
row_838
| false | null |
905 |
A8GG78
|
MSELSAARELDEIAHTASEGWMIAGLIGGAIVGAALIAVTGGTAAVAVAAVVAGASAGGGLGEVLGSMSWAPRHVTGVLADGSPNVYINGRPAIRAHISTGECSEDGPAKKVVAQGSAKVYINDFPAARINDLLACSAEIHTGSPNVIIGGEKEQTDDIEPEIPDWVNWTLLAAGAGAAAVLATPAIAILGTLGGLGGGFAGSLIGGAFFGEGSDGQKWSMLAGGFVGGFAGGKGGAKFDAWRNTKIVEPPPRVTTKVDPISPPRMTLAEAVGQEQAKVWTQTARANAEKNNAQLSTLLTDDQIGAIYGYTTNEGYTALNPALRGQTPLTPELEAFTGHVTDGLNKLPAYNGETYRGTTLPAHILEQNQIGGTVSDGGFMSTSAKTPFDGDVSISVRGNSGKQIDFLSKYKNEAEVLYPPNTRFEVINRIEQNGTTHLLYREIP
|
NAD(+)--protein-arginine ADP-ribosyltransferase Tre1 (EC 2.4.2.31) (Effector protein Tre1) (Tre1-Sp) (Type VI secretion ADP-ribosyltransferase effector 1)
|
Serratia proteamaculans (strain 568)
| 399,741 | 444 | 45,824 |
3D-structure;Glycosyltransferase;Host cytoplasm;Nucleotidyltransferase;Secreted;Toxin;Transferase;Virulence
|
GO:0003950; GO:0005576; GO:0016779; GO:0030430; GO:0090729; GO:0106274
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Probably delivered to target cells by a type 6 secretion system (T6SS). {ECO:0000305|PubMed:30343895}.
| null | null |
PF01129;PF05488;
|
IPR050999;IPR000768;IPR008727;
|
6DRE;6DRH;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Yersiniaceae (family), Serratia (genus), Serratia proteamaculans (species)
|
tre1 Spro_3017
| true |
Serratia proteamaculans
| 0 |
row_852
| false | null |
939 |
B2AFA8
|
MSDKDRIAQLLRELEEAKAREEEAKARAEEAKARAEEAKARAEEAKAREEEAKAREAQERCERERLQLEHRNTTFLEYLHNCHRHLYNALRLTNTSRYSTGYTKVVGKYYPKRLRPWTYFANVLHPHYFDLVQSICGQRQLFEPANTTKSLGTIISDHLAGNEKAIDRFEVDAVERPVQGILKVLATHKEAGKASICPEFRFSANLRELTQKDDGSSGADDNTSDGSLERRQQAGPNKRPTSKRKYICSNRQPDGVGIRMQPGGGQTHAFIYDYKAAHKVAIEYIRSATAKEHLFHEVVARINDDKLSRDEEVQRREQAEALIAMALTQVFDYMITYGVSYGYVAAGRCLLLLYVDRDDWQTLYCHPCLPADDVGEPTNDWTDRLSHTAVAQLISFCLSSFQSEALEGQSLETALSIAKATLKTWSESYADVAYLGLEPAELSSAPSSQNTDISEYTSKAEPTGRNVALRSQSSCKPAAVLPQSNEHDDEEDHSEPGASRLRLAANKRKRGPSSGGEDGDIAMADSGPTKQYCTQACLLGLKRGKDLDEKCPNVSLHRFDGSSRHPVNAHRFTDMVEQQLLLSPYKGCRMVDFWGKRGAMGWLFKLELLPYGYTFVGKGTLEDRLSRLEHEGRVYAQLDHLQGDVVPVYLGLVRLDRGYILPGLEFVVHMMLMSWAGQTPSASMDDAETLKRESLTAIWNEGVVHGDENRANYLWNAERGRIMIIDFDRAHLSPPPKPRAVSRLSKPKRKRGDSEADAQLFGPLEINRSKHRIRT
|
Meiotic driver SPOK2 (Spore killer 2)
|
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
| 515,849 | 775 | 87,293 |
Coiled coil;Cytoplasm;Nucleus;Reference proteome;Toxin
|
GO:0004536; GO:0005634; GO:0005737; GO:0016301; GO:0090729; GO:0110134
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24830502}. Nucleus {ECO:0000269|PubMed:24830502}.
| null | null | null |
IPR011009;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Sordariomycetes (class), Sordariomycetidae (subclass), Sordariales (order), Podosporaceae (family), Podospora (genus), Podospora anserina (species)
|
SPOK2 PODANS_5_10
| true |
Podospora anserina
| 0 |
row_886
| false | null |
1,242 |
E0TU96
|
MKVLEVKTLLSEATDRAKEYKELRTQMVNLRKALKSVADLGDSEFSGKGASNIKAFYHDHVGVTDQWIDYIDMKIAFFNSIAGAAEDKGLSDAYIEESFLEHELANAHKKSKSIMSEQKKAMKDILNDIDNILPLDLFSTETFNDELADANDKRKKTLEKLDALDEDLKTEYALSEPNEQFIKSDFQKLQEATGKGKNATPIHYNAKAYRESDIHKKKGDIEKRTEAYLKIKKEEAKEREIEKLKERLKNYDYADADEFYEMAKTIGYENLTAEQQRYFTQIENTRELEAGFKGVAVGLYDSGKDAVVGLWDMVTDPGGTVEAITGAVAHPIKTYEAISAAIEESYQKDMVNGDTYSRARWVSYAVGTVVTSIVGTKGVGAVSKTGTATKVTTKVKTAASKSATAQKAITVSKQTIDHIKQKVNKGIEVSKKHVKTKLNQIGDLTLADILPYHPRHDLVPAGVPYNAVNGVTLKEGLQKFAKVILPKPYGTSSSGRRTPAPVVPPVTVKYGEHYARWSRKKVLKPNIIYKTKEGYTYTTDNYGRITSVKADLQLGEAKRNQYAQSHAGKPQDRKPDDDGGHLIATQFKGSGQFDNIVPMNSQINRSGGRWYEMEQEWAKALKEEPPQKVNVNIKAIYKGDSLRPDKFIVKFRIGDADFEKVTIKNQSGG
|
Toxin YeeF (DNase YeeF)
|
Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus subtilis subsp. spizizenii)
| 655,816 | 669 | 74,714 |
Cell membrane;DNA-binding;Hydrolase;Membrane;Nuclease;Toxin
|
GO:0003677; GO:0004518; GO:0005886; GO:0045121; GO:0090729
|
Evidence at protein level
| 4 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O31506}. Membrane raft {ECO:0000250|UniProtKB:O31506}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. Delivery to target cells requires the type VII secretion system (T7SS) and YukE. {ECO:0000250|UniProtKB:O31506}.
| null | null |
PF13930;PF04740;
|
IPR051768;IPR044929;IPR044927;IPR006829;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus subtilis group (no rank), Bacillus spizizenii (species)
|
yeeF BSUW23_03455
| true |
Bacillus spizizenii
| 0 |
row_1185
| false | null |
3,151 |
P0A369
|
MDNNPNINECIPYNCLSNPEVEVLGGERIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEADPTNPALREEMRIQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRLIGNYTDYAVRWYNTGLERVWGPDSRDWVRYNQFRRELTLTVLDIVALFSNYDSRRYPIRTVSQLTREIYTNPVLENFDGSFRGMAQRIEQNIRQPHLMDILNRITIYTDVHRGFNYWSGHQITASPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIFRTLSSPLYRRIILGSGPNNQELFVLDGTEFSFASLTTNLPSTIYRQRGTVDSLDVIPPQDNSVPPRAGFSHRLSHVTMLSQAAGAVYTLRAPTFSWQHRSAEFNNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQISTLRVNITAPLSQRYRVRIRYASTTNLQFHTSIDGRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVPAEVTFEAEYDLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKQELSEKVKHAKRLSDERNLLQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENYVTLLGTFDECYPTYLYQKIDESKLKAYTRYQLRGYIEDSQDLEIYLIRYNAKHETVNVPGTGSLWPLSAQSPIGKCGEPNRCAPHLEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHARLGNLEFLEEKPLVGEALARVKRAEKKWRDKREKLEWETNIVYKEAKESVDALFVNSQYDRLQADTNIAMIHAADKR
|
Pesticidal crystal protein Cry1Aa (133 kDa crystal protein) (Crystaline entomocidal protoxin) (Insecticidal delta-endotoxin CryIA(a))
|
Bacillus thuringiensis subsp. sotto
| 29,340 | 934 | 105,673 |
Plasmid;Sporulation;Toxin;Virulence
|
GO:0001907; GO:0005102; GO:0030435; GO:0090729
|
Evidence at transcript level
| 3 | null | null | null |
PF17997;PF03944;PF18449;PF00555;PF03945;
|
IPR041587;IPR008979;IPR038979;IPR054544;IPR005638;IPR005639;IPR036716;IPR036399;IPR001178;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus cereus group (no rank), Bacillus thuringiensis (species)
|
cry1Aa cry-1-1 cry1A(a) cryA crybns3-1 cryIA(a) icp
| true |
Bacillus thuringiensis
| 0 |
row_3044
| false | null |
4,905 |
Q9S597
|
MNPYQNKNEYEILDAKRNNCHMSNGYPRHPLANDPQMYLRNAHYKDWLSMCNKNNPVGLIPPESFEWTWLNGTVAALTIVSVIAGILVTAPVSVTAGLITVLGAGAALLAGITPLIWPATTDNTFNKITDATEVLLNKEISEFVRKTANTKIDSLQQLIYYYQNALENWKKNPNDSAARNTVSTRFQIVNAFFVEAMPALSMPGYEVVQLGAYAQAANLHLILLREGIAYADQWNLARDPMHAAGDLHYKEFLDYRNQYINHCSTWYNEGQNEANLKNNGLVYQRTMTLFVLDLIAMFSTYDPRLYTMPIKTEILTRTIYTDGVNRNEPKSIHNPGLFRRLEQMKLHIYEYQGAQFLSGHQNIFRSMNYNHPLIYGPVQGYSSSNINKITTINLGDYDKIYSINTESRNRLVQGSTTFDKINFYGAFNENWLFSVYNQNGPIIKHSNIPGIDAPSTGLNYSNYTHYLSNCIFQSNRNGGSAPDYNTQSYVFGWNHYTIDPTGNYVTDAFEVNKNLPESRYVPQISQVPAVKASDIFNPGRVVNAKVESGPYFTGGDVIVSKAQLDGSGLARTLITFPIIPKRYRASGFRVRMYYAANHTGQVSYGVANINTTGYANFQKTFDGWEYFRARHEHFKYIEFDTTFSLRNSGQLEEHLLHIYYPNTTKISGDQLLIIDKIEFIPVGIPLNQTSEGYNTYDQNTNSYNQNYNNYNQNMDTTYQPNYDNYKQNSSGMYDNPYNQNPKDSYNQNYTDTYDSGYNNSQNVGSNYNQEYNTYNQDTENMYNQSYNNYNSDNNNYNQNSDCMCSPGYNGNYECRCNQRANGNYPK
|
Pesticidal crystal protein Cry27Aa (94 kDa crystal protein) (Crystaline entomocidal protoxin) (Insecticidal delta-endotoxin CryXXVIIA(a))
|
Bacillus thuringiensis subsp. higo
| 132,266 | 826 | 94,435 |
Sporulation;Toxin;Virulence
|
GO:0001907; GO:0005102; GO:0030435; GO:0090729
|
Evidence at transcript level
| 3 | null | null | null |
PF03944;PF00555;PF03945;
|
IPR008979;IPR038979;IPR005638;IPR005639;IPR036716;IPR036399;IPR001178;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus cereus group (no rank), Bacillus thuringiensis (species)
|
cry27Aa cryXXVIIA(a)
| true |
Bacillus thuringiensis
| 1 |
row_4678
| false | null |
3,003 |
O32321
|
MNPYQNNDEIVDVPENYDNNLNRYPYANDPNVAMQNTNYKDWMNGYEEINPSSITAILASIGILNRVIALTGVLGNTQEVISIIQDALGFIRNGTGNELLIHVEQLIQQTLATQYRSAATGAIYGISRSYDNYLMFFRQWERNRTRENGQQVESAFTTINTLCINALAPQASLSRRGFETLLLPNYAMAANFHLLLLRDAVLYRNQWLSNSISTANVNLNILRAAINEYITHCTRWYQDGLNRFDRSSRANMNEWRRFNAYRRDMTLSVLDFATVFPTYDPVLFPAATNVELTRVVYTDPIVMAGGRTAIPGFTRMENLVNSASRVSFLNQMNIYTSFYFRPHNIPRYYWSGNQNFLSNGTSNLYGYRSDGRTTFNVSNIDIFRVNMTTHIGGAFTDDYRGLHRAEFIGANTQNNQRTSLLYSVEIPSSHFRFENHTVFLPGESGLEPNERNYTHRLFQMMNEVSVNPNARGRVFLHAWTHRSLRRTNGLRSDQILQIPAVKTISNGGDRAVVLNYGENIMKLDNLTTGLSYKLTAVDSEASNTRFIVRVRYASMNNNKLNLVLNGAQIASLNVEHTVQRGGSLTDLQYGNFKYATFAGNFKMGSQSILGIFKEIPNIDFVLDKIELIPSNFMSSLEQTQNYNTYNQDTIYTHNQGYDTYDQNSSGMYHQSYNNYDQNMDTTYQPSYDNYNQNASGTYDDGYNPNASDSYDQSYTNNYSQNTNSMYDQGYYNNNYDQHSGCTCNQGYDNNYLK
|
Pesticidal crystal protein Cry20Aa (86 kDa crystal protein) (Crystaline entomocidal protoxin) (Insecticidal delta-endotoxin CryXXA(a))
|
Bacillus thuringiensis subsp. fukuokaensis
| 132,265 | 753 | 86,139 |
Sporulation;Toxin;Virulence
|
GO:0001907; GO:0005102; GO:0030435; GO:0090729
|
Evidence at transcript level
| 3 | null | null | null |
PF03944;PF00555;PF03945;
|
IPR008979;IPR038979;IPR005638;IPR005639;IPR036716;IPR036399;IPR001178;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus cereus group (no rank), Bacillus thuringiensis (species)
|
cry20Aa cryXXA(a)
| true |
Bacillus thuringiensis
| 2 |
row_2904
| false | null |
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