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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
298,042
Q8Z5B2
MRVLLAPMEGVLDALVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELLHASRTPSGTPVRIQLLGQHPQWLAENAARATALGSYGVDLNCGCPSKVVNGSGGGATLLTDPELIYQGAKAMRAAVPSHLPVTVKVRLGWDSGDRKFEIADAVQQAGASELVVHGRTKAQGYRAEHIDWQAIGEIRQRLTIPVIANGEIWDWQSAQACMATSGCDAVMIGRGALNIPNLSRVVKYNEPRMPWPEVVTLLQKYTRLEKQGDTGLYHVARIKQWLGYLRKEYIEATELFQSIRALNRSSEIARVIQAIKI
tRNA-dihydrouridine(16) synthase (EC 1.3.1.-) (U16-specific dihydrouridine synthase) (U16-specific Dus) (tRNA-dihydrouridine synthase C)
Salmonella typhi
90,370
312
34,568
Flavoprotein;FMN;NADP;Oxidoreductase;RNA-binding;tRNA processing;tRNA-binding
GO:0000049; GO:0010181; GO:0050660; GO:0102262
Inferred from homology
3
null
null
null
PF01207;
IPR013785;IPR035587;IPR001269;IPR032886;IPR042270;IPR018517;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies)
dusC STY2404 t0681
false
Salmonella enterica
876
row_281939
false
null
198,569
P29848
MNTLEQTIGNTPLVKLQRLGPDNGSEIWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALAMSERGEGKLLDQFNNPDNPYAHYTTTGPEIWRQTSGRITHFVSSMGTTGTITGVSRFLREQEKPVTIVGLQPEEGSSIPGIRRWPAEYMPGIFNASLVDEVLDIHQNDAENTMRELAVREGIFCGVSSGGAVAGALRVARATPGAIVVAIICDRGDRYLSTGVFGEEHFSQGAGI
Cysteine synthase B (CSase B) (EC 2.5.1.47) (O-acetylserine (thiol)-lyase B) (OAS-TL B) (O-acetylserine sulfhydrylase B)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
99,287
303
32,645
3D-structure;Amino-acid biosynthesis;Cysteine biosynthesis;Pyridoxal phosphate;Reference proteome;Transferase
GO:0004124; GO:0005737; GO:0006535; GO:0019344
Evidence at protein level
3
null
null
null
PF00291;
IPR005856;IPR050214;IPR005858;IPR001216;IPR001926;IPR036052;
2JC3;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
cysM STM2440
false
Salmonella enterica
915
row_185168
false
null
69,190
O54297
MARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIEQAPGQHGARKPRLSDYGVQLREKQKVRRIYGVLERQFRNYYKEAARLKGNTGENLLALLEGRLDNVVYRMGFGATRAEARQLVSHKAIMVNGRVVNIASYQVSPNDVVSIREKAKKQSRVKAALELAEQREKPTWLEVDAGKMEGTYKRKPERSDLSADINEHLIVELYSK
Small ribosomal subunit protein uS4 (30S ribosomal protein S4)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
99,287
206
23,485
Antibiotic resistance;Reference proteome;Ribonucleoprotein;Ribosomal protein;RNA-binding;rRNA-binding
GO:0003735; GO:0006412; GO:0015935; GO:0019843; GO:0042274; GO:0046677
Evidence at protein level
4
null
null
null
PF00163;PF01479;
IPR022801;IPR005709;IPR018079;IPR001912;IPR002942;IPR036986;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
rpsD STM3416
false
Salmonella enterica
1,371
row_60190
false
null
179,944
E1WGG9
MAEPLTVSPELTANYAYFFDLDGTLAEIKPHPDQVVVPHKILQLLDRLAAHNAGALALISGRSMTELDALAKPFRFPLAGVHGAERRDINGKTHIVRLPEAVVREVEALLRSTLVALPGTELESKGMAFALHYRQAPEHEAALLALAQHVTQHWPQLALQLGKCVVEIKPKGTNKGEAIAAFMQEAPFAGRIPVFVGDDLTDEAGFGVVNHAGGISVKVGVGATQAAWRLESVPDVWRWLEQINYPQQEQQVMNNRRDGYESFSRSI
Trehalose-phosphate phosphatase (TPP) (EC 3.1.3.12) (Trehalose 6-phosphate phosphatase) (Trehalose-phosphatase)
Salmonella typhimurium (strain SL1344)
216,597
267
29,261
3D-structure;Hydrolase;Magnesium;Metal-binding
GO:0000287; GO:0004805; GO:0005992
Evidence at protein level
3
null
null
null
PF02358;
IPR036412;IPR006379;IPR023214;IPR044651;IPR003337;
6UPB;6UPC;6UPD;6UPE;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
otsB SL1344_1863
false
Salmonella enterica
1,084
row_167139
false
null
205,764
P58580
MIKLGIVMDPIAHINIKKDTSFAMLLEAQRRGYELHYMEMADLYLINGEARARTRTLSVEQNYDKWYEFGSEQEIKLADLDVILMRKDPPFDTEFIYATYILERAEEEGTLIVNKPQSLRDCNEKLYTAWFADLTPETLVTRNKAQLKAFWEKHGDIIMKPLDGMGGASIFRVKEGDPNIGVIAETLTELGNRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARIPQGGETRGNLAAGGRGEPRPLSESDWEIARRVGPTLKAKGLIFVGLDIIGDRLTEINVTSPTCVREIEAEYPISITGMLMDAIEARLAK
Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GSH-S) (GSHase) (Glutathione synthase)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
99,287
315
35,433
ATP-binding;Glutathione biosynthesis;Ligase;Magnesium;Manganese;Metal-binding;Nucleotide-binding;Reference proteome
GO:0004363; GO:0005524; GO:0005737; GO:0046872
Inferred from homology
3
null
null
null
PF02955;PF02951;
IPR011761;IPR013815;IPR006284;IPR004218;IPR004215;IPR016185;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
gshB STM3095
false
Salmonella enterica
856
row_192214
false
null
55,262
Q9S498
MKTFTDRWRQLEWDDIRLRINGKTAADVERALNAAHLSRDDLMALLSPAAADYLEPIAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEVDIQRECDAIRKLGFEHLLLVTGEHQAKVGMDYFRRHLPTIRRQFSSLQMEVQPLSQENYAELKTLGIDGVMVYQETYHEAIYAQHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDCYMVAEHLLWMQKHYWQSRYSVSFPRLRPCTGGVEPASVMDEKQLVQTICAFRLLAPEIELSLSTRESPWFRDHVIPLAINNVSAFSKTQPGGYADDHPELEQFSPHDARRPETVASALSAQGLQPVWKDWDSWLGRASQTR
2-iminoacetate synthase (EC 4.1.99.19) (Dehydroglycine synthase) (Tyrosine lyase)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
99,287
377
43,447
4Fe-4S;Iron;Iron-sulfur;Lyase;Metal-binding;NADP;Reference proteome;S-adenosyl-L-methionine;Thiamine biosynthesis
GO:0005506; GO:0009229; GO:0036355; GO:0051539
Evidence at protein level
5
null
null
null
PF06968;PF04055;
IPR013785;IPR010722;IPR007197;IPR012726;IPR034428;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
thiH STM4159 STMF1.38
false
Salmonella enterica
602
row_47904
false
null
298,761
Q8ZQP4
MKCGWREGNQIQLLENGDQFYPAVFEAIAQAQQKIILETFILFEDEVGKKLHTALLKAAQRGVKAEVLLDGYGSPDLSDAFVGELTSAGVIFRYYDPRPRLLGLRTNIFRRMHRKIVVIDDRIAFVGGINYSAEHMSDYGPQAKQDYAVRVEGPVVADILQFEVENLPGQSPARRWWKRHHQAEENRHPGEAQALFVWRDNEEHRDDIERHYLKMLTQAKREVIIANAYFFPGYRLLHAMRKAARRGVSVKLIVQGEPDMPIVKVGARLLYNYLVKGGVQVYEYRRRPLHGKVALMDDHWATVGSSNLDPLSLSLNLEANLIIHDRTFNQTLRDNLQGIIVNDCKQVDESMLPKRTWWNLTKSVLAFHFLRHFPALVGWLPAHTPHLAQVPPPAQPEMETQDRVDPENTGVKP
Cardiolipin synthase B (CL synthase) (EC 2.7.8.-)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
99,287
413
47,302
Cell membrane;Lipid biosynthesis;Lipid metabolism;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Reference proteome;Repeat;Transferase
GO:0005886; GO:0008808; GO:0016020; GO:0032049
Inferred from homology
3
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01917}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01917}.
null
null
PF13091;
IPR030872;IPR025202;IPR001736;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
clsB ybhO STM0812
false
Salmonella enterica
494
row_282652
false
null
354,508
A9N7X9
MKKMAIACALLSSVVASSVWADAASSLKSRLDKVSSFHATFTQKVTDGSGAAVQEGQGDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARNQASDWQQYNIKQDGDNFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSAYQLKSQQNGAVDPSKFTFTPPQGVTIDDQRK
Outer-membrane lipoprotein carrier protein
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
1,016,998
203
22,481
Chaperone;Periplasm;Protein transport;Signal;Transport
GO:0030288; GO:0042953; GO:0044874
Inferred from homology
2
SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00240}.
SIGNAL 1..21; /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
null
PF03548;
IPR029046;IPR004564;IPR018323;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella paratyphi B (no rank)
lolA SPAB_02561
false
Salmonella enterica
1,385
row_337550
false
null
423,885
P58316
MNVNYLNDSDLDFLQHCSEEQLANFARLLTHNEKGKTRLSSVLMRNELFKSMEGHPEQHRRNWQLIAGELQHFGGDSIANKLRGHGKLYRAILLDVSKRLKLKADKEMSTFEIEQQLLEQFLRNTWKKMDEEHKQEFLHAVDARVNELEELLPLLMKDKLLAKGVSHLLSSQLTRILRTHAAMSVLGHGLLRGAGLGGPVGAALNGVKAVSGSSYRVTIPAVLQIACLRRMVSATQV
UPF0174 protein YaaW
Escherichia coli O157:H7
83,334
237
26,681
Reference proteome
null
Inferred from homology
2
null
null
null
PF13099;PF03981;
IPR025217;IPR021150;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
yaaW Z0011 ECs0012
false
Escherichia coli
2,604
row_406007
false
null
25,436
P76141
MTINDSAISEQGMCEEEQVARIAWFYYHDGLTQSEISDRLGLTRLKVSRLLEKGHQSGIIRVQINSRFEGCLEYETQLRRQFSLQHVRVIPGLADADVGGRLGIGAAHMLMSLLQPQQMLAIGFGEATMNTLQRLSGFISSQQIRLVTLSGGVGSYMTGIGQLNAACSVNIIPAPLRASSADIARTLKNENCVKDVLLAAQAADVAIVGIGAVSQQDDATIIRSGYISQGEQLMIGRKGAVGDILGYFFDAKGDVVTNIKIHNELIGLPLSALKTIPVRVGVAGGENKAEAIAAAMKGGYINALVTDQDTAAAILRS
Transcriptional regulator LsrR (lsr regulator)
Escherichia coli (strain K12)
83,333
317
33,797
3D-structure;Activator;Cytoplasm;DNA-binding;Reference proteome;Repressor;Transcription;Transcription regulation
GO:0000987; GO:0005829; GO:0006351; GO:0009408; GO:0030246; GO:0042802; GO:2000142
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
null
null
PF04198;
IPR037171;IPR051054;IPR007324;IPR036388;
4GO1;4L4Y;4L4Z;4L50;4L51;4L5I;4L5J;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
lsrR ydeW b1512 JW1505
false
Escherichia coli
1,782
row_22229
false
null
191,426
P0AF63
MQLTSFTDYGLRALIYMASLPEGRMTSISEVTDVYGVSRNHMVKIINQLSRAGYVTAVRGKNGGIRLGKPASAIRIGDVVRELEPLSLVNCSSEFCHITPACRLKQALSKAVQSFLTELDNYTLADLVEENQPLYKLLLVE
HTH-type transcriptional repressor NsrR
Escherichia coli (strain K12)
83,333
141
15,593
2Fe-2S;DNA-binding;Iron;Iron-sulfur;Metal-binding;Reference proteome;Repressor;Transcription;Transcription regulation
GO:0003690; GO:0003700; GO:0005506; GO:0005829; GO:0006355; GO:0045892; GO:0051537
Inferred from homology
3
null
null
null
PF02082;
IPR030489;IPR000944;IPR023761;IPR036388;IPR036390;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
nsrR yjeB b4178 JW4136
false
Escherichia coli
3,569
row_178264
false
null
11,848
P0A7N4
MAVQQNKPTRSKRGMRRSHDALTAVTSLSVDKTSGEKHLRHHITADGYYRGRKVIAK
Large ribosomal subunit protein bL32 (50S ribosomal protein L32)
Escherichia coli (strain K12)
83,333
57
6,446
3D-structure;Direct protein sequencing;Reference proteome;Ribonucleoprotein;Ribosomal protein
GO:0000027; GO:0000302; GO:0002181; GO:0003735; GO:0005737; GO:0005829; GO:0009314; GO:0022625
Evidence at protein level
5
null
null
null
PF01783;
IPR002677;IPR044957;IPR011332;
2J28;2RDO;3BBX;3J5L;3J7Z;3J8G;3J9Y;3J9Z;3JA1;3JBU;3JBV;3JCD;3JCE;3JCJ;3JCN;4CSU;4U1U;4U1V;4U20;4U24;4U25;4U26;4U27;4UY8;4V47;4V48;4V4H;4V4Q;4V4V;4V4W;4V50;4V52;4V53;4V54;4V55;4V56;4V57;4V5B;4V5H;4V5Y;4V64;4V65;4V66;4V69;4V6C;4V6D;4V6E;4V6K;4V6L;4V6M;4V6N;4V6O;4V6P;4V6Q;4V6R;4V6S;4V6T;4V6V;4V6Y;4V6Z;4V70;4V71;4V72;4V73;4V74;4V75;4V76;4V77;4V78;4V79;4V7A;4V7B;4V7C;4V7D;4V7I;4V7S;4V7T;4V7U;4V7V;4V85;4V89;4V9C;4V9D;4V9O;4V9P;4WF1;4WOI;4WWW;4YBB;5ADY;5AFI;5AKA;5GAD;5GAE;5GAF;5GAG;5GAH;5H5U;5IQR;5IT8;5J5B;5J7L;5J88;5J8A;5J91;5JC9;5JTE;5JU8;5KCR;5KCS;5KPS;5KPV;5KPW;5KPX;5L3P;5LZA;5LZB;5LZC;5LZD;5LZE;5LZF;5MDV;5MDW;5MDY;5MDZ;5MGP;5NCO;5NP6;5NWY;5O2R;5U4I;5U9F;5U9G;5UYK;5UYL;5UYM;5UYN;5UYP;5UYQ;5WDT;5WE4;5WE6;5WF0;5WFK;5WFS;6BU8;6BY1;6C4I;6DNC;6ENF;6ENJ;6ENU;6GBZ;6GC0;6GC4;6GC6;6GC7;6GC8;6GWT;6GXM;6GXN;6GXO;6GXP;6H4N;6H58;6HRM;6I0Y;6I7V;6O9J;6O9K;6OFX;6OG7;6OGF;6OGG;6OGI;6OM6;6ORE;6ORL;6OSK;6OSQ;6OST;6OT3;6OUO;6PJ6;6Q98;6Q9A;6QDW;6QUL;6S0K;6SZS;6TBV;6TC3;6U48;6VU3;6VYQ;6VYR;6VYS;6VYT;6VYU;6VYW;6VYX;6VYY;6VYZ;6VZ2;6VZ3;6VZ5;6VZ7;6VZJ;6WD0;6WD1;6WD2;6WD3;6WD4;6WD5;6WD6;6WD7;6WD8;6WD9;6WDA;6WDB;6WDC;6WDD;6WDE;6WDF;6WDG;6WDH;6WDI;6WDJ;6WDK;6WDL;6WDM;6WNT;6WNV;6WNW;6X6T;6X7F;6X7K;6X9Q;6XDQ;6XDR;6XGF;6XII;6XIJ;6XZ7;6XZA;6XZB;6Y69;6YS3;6YSR;6YSS;6YST;6YSU;6ZTJ;6ZTL;6ZTM;6ZTN;6ZTO;6ZTP;6ZU1;7ABZ;7AC7;7ACJ;7ACR;7B5K;7BL2;7BL3;7BL4;7BL5;7BL6;7BV8;7D6Z;7D80;7JSS;7JSW;7JSZ;7JT1;7JT2;7JT3;7K00;7K50;7K51;7K52;7K53;7K54;7K55;7LV0;7LVK;7M5D;7N1P;7N2C;7N2U;7N2V;7N30;7N31;7NBU;7NWT;7O19;7O1A;7O1C;7ODE;7OIZ;7OJ0;7P3K;7PJS;7PJT;7PJU;7PJV;7PJW;7PJX;7PJY;7PJZ;7Q4K;7QG8;7QGH;7QGN;7QGR;7QQ3;7S1G;7S1H;7S1I;7S1J;7S1K;7SA4;7SS9;7SSD;7SSL;7SSN;7SSO;7SSW;7ST2;7ST6;7ST7;7TOS;7UG7;7UPH;7Y7C;7Y7D;7Y7E;7Y7F;7Y7G;7Y7H;7Z20;7ZOD;7ZP8;7ZQ5;7ZQ6;7ZTA;8A3L;8AKN;8AM9;8ANA;8AP4;8AYE;8B0X;8B7Y;8BF7;8BGE;8BGH;8BH4;8BHJ;8BHL;8BHN;8BHP;8BIL;8BIM;8C8X;8C8Y;8C8Z;8C90;8C91;8C92;8C93;8C94;8C96;8C97;8CAM;8CEU;8CGD;8CGK;8CGV;8E30;8E32;8E33;8E35;8E36;8E3L;8E3M;8E3O;8E41;8E42;8E43;8E44;8E45;8E46;8E47;8E48;8E49;8EIU;8EKC;8EMM;8FIZ;8FTO;8FZD;8FZE;8FZF;8FZG;8FZH;8FZI;8FZJ;8G2U;8G31;8G34;8G38;8G6W;8G6X;8G6Y;8G7P;8G7Q;8G7R;8G7S;8HSP;8HTZ;8HU1;8IFB;8IFC;8J1Z;8P16;8P17;8P18;8PEG;8PHJ;8PKL;8PVA;8Q4F;8QBT;8QK7;8QOA;8R6C;8R8M;8RPY;8RPZ;8RQ0;8RQ2;8SYL;8T5D;8T5H;8VS9;8VSA;8W51;8YUO;8YUP;8YUQ;8YUR;8YUS;9D89;9FBV;9GFT;9GGR;9H3S;9H3T;9H3U;9H3V;9H3W;9H3X;9H3Y;9H3Z;9HA5;9HA6;9HAI;9MOR;9MQ4;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
rpmF b1089 JW1075
false
Escherichia coli
4,372
row_10058
false
null
539,692
P0ACW4
MKKLALILFMGTLVSFYADAGRKPCSGSKGGISHCTAGGKFVCNDGSISASKKTCTN
Uncharacterized protein YdcA
Escherichia coli (strain K12)
83,333
57
5,860
Reference proteome;Signal
null
Inferred from homology
1
null
SIGNAL 1..20; /evidence="ECO:0000255"
null
null
null
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
ydcA b1419 JW1416
false
Escherichia coli
4,381
row_519981
false
null
195,241
P15006
MEQPVIPVRNIYYMLTYAWGYLQEIKQANLEAIPGNNLLDILGYVLNKGVLQLSRRGLELDYNPNTEIIPGIKGRIEFAKTIRGFHLNHGKTVSTFDMLNEDTLANRIIKSTLAILIKHEKLNSTIRDEARSLYRKLPGISTLHLTPQHFSYLNGGKNTRYYKFVISVCKFIVNNSIPGQNKGHYRFYDFERNEKEMSLLYQKFLYEFCRRELTSANTTRSYLKWDASSISDQSLNLLPRMETDITIRSSEKILIVDAKYYKSIFSRRMGTEKFHSQNLYQLMNYLWSLKPENGENIGGLLIYPHVDTAVKHRYKINGFDIGLCTVNLGQEWPCIHQELLDIFDEYLK
Type IV methyl-directed restriction enzyme EcoKMcrBC (EcoKMcrBC) (Protein McrC)
Escherichia coli (strain K12)
83,333
348
40,590
3D-structure;Direct protein sequencing;Reference proteome;Restriction system
GO:0009307; GO:0032067; GO:1905348
Evidence at protein level
3
null
null
null
PF10117;
IPR019292;IPR014407;
6HZ4;6HZ5;6HZ6;6HZ7;6HZ8;6HZ9;6UT6;7VSR;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
mcrC b4345 JW5789
false
Escherichia coli
1,498
row_181924
false
null
209,678
P77481
MAQLSLQHIQKIYDNQVHVVKDFNLEIADKEFIVFVGPSGCGKSTTLRMIAGLEEISGGDLLIDGKRMNDVPAKARNIAMVFQNYALYPHMTVYDNMAFGLKMQKIAKEVIDERVNWAAQILGLREYLKRKPGALSGGQRQRVALGRAIVREAGVFLMDEPLSNLDAKLRVQMRAEISKLHQKLNTTMIYVTHDQTEAMTMATRIVIMKDGIVQQVGAPKTVYNQPANMFVSGFIGSPAMNFIRGTIDGDKFVTETLKLTIPEEKLAVLKTQESLHKPIVMGIRPEDIHPDAQEENNISAKISVAELTGAEFMLYTTVGGHELVVRAGALNDYHAGENITIHFDMTKCHFFDAETEIAIR
Putative uncharacterized ABC transporter ATP-binding protein YcjV
Escherichia coli (strain K12)
83,333
360
40,147
ATP-binding;Nucleotide-binding;Reference proteome;Transport
GO:0005524; GO:0008643; GO:0016020; GO:0016887; GO:0055052; GO:0055085; GO:0140359
Uncertain
3
null
null
null
PF00005;PF17912;PF03459;
IPR003593;IPR003439;IPR017871;IPR015855;IPR047641;IPR008995;IPR012340;IPR040582;IPR027417;IPR005116;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
ycjV ymjB b4524 JW1311/JW5203 b1318
false
Escherichia coli
1,407
row_196071
false
null
18,533
P32695
MHGNSEMQKINQTSAMPEKTDVHWSGRFSVAPMLDWTDRHCRYFLRLLSRNTLLYTEMVTTGAIIHGKGDYLAYSEEEHPVALQLGGSDPAALAQCAKLAEARGYDEINLNVGCPSDRVQNGMFGACLMGNAQLVADCVKAMRDVVSIPVTVKTRIGIDDQDSYEFLCDFINTVSGKGECEMFIIHARKAWLSGLSPKENREIPPLDYPRVYQLKRDFPHLTMSINGGIKSLEEAKAHLQHMDGVMVGREAYQNPGILAAVDREIFGSSDTDADPVAVVRAMYPYIERELSQGTYLGHITRHMLGLFQGIPGARQWRRYLSENAHKAGADINVLEHALKLVADKR
tRNA-dihydrouridine(20/20a) synthase (EC 1.3.1.-) (EC 1.3.1.91) (U20-specific dihydrouridine synthase) (U20-specific Dus) (tRNA-dihydrouridine synthase A)
Escherichia coli (strain K12)
83,333
345
38,468
Direct protein sequencing;Flavoprotein;FMN;NADP;Oxidoreductase;Reference proteome;RNA-binding;tRNA processing;tRNA-binding
GO:0000049; GO:0005829; GO:0010181; GO:0017150; GO:0050660; GO:0102264; GO:0102266
Evidence at protein level
5
null
null
null
PF01207;
IPR013785;IPR035587;IPR001269;IPR004653;IPR018517;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
dusA yjbN b4049 JW5950
false
Escherichia coli
1,521
row_15950
false
null
17,194
P27302
MSSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQNPSWADRDRFVLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHPEVGYTAGVETTTGPLGQGIANAVGMAIAEKTLAAQFNRPGHDIVDHYTYAFMGDGCMMEGISHEVCSLAGTLKLGKLIAFYDDNGISIDGHVEGWFTDDTAMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSLLMCKTIIGFGSPNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAGQAKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQANPAKIASRKASQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAAGNYIHYGVREFGMTAIANGISLHGGFLPYTSTFLMFVEYARNAVRMAALMKQRQVMVYTHDSIGLGEDGPTHQPVEQVASLRVTPNMSTWRPCDQVESAVAWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGGYVLKDCAGQPELIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESVLPKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFTVDNVVAKAKELL
Transketolase 1 (TK 1) (EC 2.2.1.1)
Escherichia coli (strain K12)
83,333
663
72,212
3D-structure;Acetylation;Calcium;Magnesium;Metal-binding;Reference proteome;Thiamine pyrophosphate;Transferase
GO:0000287; GO:0004802; GO:0005829; GO:0006098; GO:0009052; GO:0030145; GO:0030976; GO:0042803
Evidence at protein level
5
null
null
null
PF02779;PF22613;PF00456;
IPR029061;IPR009014;IPR055152;IPR005475;IPR005478;IPR020826;IPR049557;IPR033247;IPR005474;
1QGD;2R5N;2R8O;2R8P;5HHT;6RJC;6TJ8;6TJ9;8WA7;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
tktA tkt b2935 JW5478
false
Escherichia coli
228
row_14754
false
null
14,778
P17109
MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREAPRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQVSHL
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (SEPHCHC synthase) (EC 2.2.1.9) (Menaquinone biosynthesis protein MenD)
Escherichia coli (strain K12)
83,333
556
61,367
3D-structure;Magnesium;Manganese;Menaquinone biosynthesis;Metal-binding;Reference proteome;Thiamine pyrophosphate;Transferase
GO:0000287; GO:0009234; GO:0030145; GO:0030976; GO:0042803; GO:0070204
Evidence at protein level
5
null
null
null
PF02775;PF16582;PF02776;
IPR004433;IPR032264;IPR029061;IPR012001;IPR011766;
2JLA;2JLC;3FLM;3HWW;3HWX;5EJ4;5EJ5;5EJ6;5EJ7;5EJ8;5EJ9;5EJA;5EJM;5Z2P;5Z2R;5Z2U;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
menD b2264 JW5374
false
Escherichia coli
393
row_12609
false
null
463,785
Q3SB15
MAATLTPEQITEYKGIFEMFDEEGNGLVKTDDLESLMSLIGINPTKRDLANMAKDVDKDKKGTFNCDGFLVLMGIYHEKSKNQDEELRAAFKVFDKEHKGYIEWDTLKYVLMNAGEPLNEHEAELMMKEADKDGDGTIDYEEFVAMMTGESFKLTQ
Calglandulin
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
156
17,767
Calcium;Cytoplasm;Metal-binding;Repeat
GO:0005509; GO:0005737; GO:0016460
Evidence at transcript level
2
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Not found in venom. {ECO:0000250}.
null
null
PF13499;PF13833;
IPR050230;IPR011992;IPR018247;IPR002048;
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
false
Oxyuranus scutellatus
0
row_445161
false
null
33,856
Q4VRI5
MHPAHLLVLLAVCVSLLGAARIPPLPLSLLNFANLIECANHGTRSALAYADYGCYCGKGGRGTPLDDLDRCCHVHDDCYGEAEKLPACNYLMSSPYFNSYSYKCNEGKVTCTDDNDECKAFICNCDRTAAICFAGATYNDENFMISKKRNDICQ
Phospholipase A2 OS1 (PLA2) (EC 3.1.1.4) (OS5) (Phosphatidylcholine 2-acylhydrolase)
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
154
16,898
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal
GO:0005102; GO:0005509; GO:0005543; GO:0005576; GO:0006633; GO:0006644; GO:0016042; GO:0047498; GO:0048146; GO:0050482
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..27; /evidence="ECO:0000250"
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
false
Oxyuranus scutellatus
1
row_29454
false
null
9,135
P00616
MHPAHLLVLLAVCVSLLGSSEIPQPSLDFEQFSNMIQCTIPCGESCLAYMDYGCYCGPGGSGTPIDDLDRCCKTHDECYAEAGKLSACKSVLSEPNNDTYSYECNEGQLTCNDDNDECKAFICNCDRTAVTCFAGAPYNDLNYNIGMIEHCK
Acidic phospholipase A2 homolog taipoxin gamma chain (svPLA2 homolog)
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
152
16,558
Direct protein sequencing;Disulfide bond;Glycoprotein;Secreted;Sialic acid;Signal
GO:0005102; GO:0005509; GO:0005543; GO:0005576; GO:0006633; GO:0006644; GO:0016042; GO:0047498; GO:0048146; GO:0050482
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..19; /evidence="ECO:0000269|PubMed:22776098, ECO:0000269|PubMed:563806"
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
false
Oxyuranus scutellatus
2
row_7586
false
null
9,134
P00615
MHPAHLLVLLAVCVSLLGASDIPPLPLNLVQFGKMIECAIRNRRPALDFMNYGCYCGKGGSGTPVDDLDRCCQVHDECYAEAEKHGCYPSLTTYTWECRQVGPYCNSKTQCEVFVCACDFAAAKCFAQEDYNPAHSNINTGERCK
Neutral phospholipase A2 homolog taipoxin beta chain 1 (svPLA2 homolog)
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
145
16,008
3D-structure;Direct protein sequencing;Disulfide bond;Secreted;Signal
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..27; /evidence="ECO:0000269|PubMed:22776098, ECO:0000269|PubMed:6756920"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
3VC0;
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
false
Oxyuranus scutellatus
3
row_7585
false
null
401,654
E3P6N6
MVHSQLPVAAPLRLLCALLLLPSATMIPGGLSPRSVTDPDVQKAAEFAVQEYNALSTNAYYYKQLRIVEAQSQVVAGAKYYLTMELMKTKCAKTTGKPKVYKEIQNCELPPKAQQEKLTCHFQVWSRPWLEKVELTKMSCN
Cystatin
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
141
15,849
Disulfide bond;Protease inhibitor;Secreted;Signal;Thiol protease inhibitor
GO:0004869; GO:0070062
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..26; /evidence="ECO:0000250"
null
PF00031;
IPR000010;IPR046350;IPR018073;
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
false
Oxyuranus scutellatus
4
row_384230
false
null
376,651
B5KL29
MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCELPADIGPCEDFTGAFHYSPREHECIEFIYGGCKGNANNFNTLEECESACAA
Kunitz-type serine protease inhibitor scutellin-3
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
83
9,029
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005576
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
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
false
Oxyuranus scutellatus
5
row_359387
false
null
376,652
B5KL30
MSSGGLLLLLGLLTLWAELTPVSSKDHPEFCELPADSGPCRGILHAFYYHPVHRTCLGFIYGGCYGNANNFKTIDECKRTCAA
Kunitz-type serine protease inhibitor scutellin-4
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
83
9,063
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005615
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
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
false
Oxyuranus scutellatus
6
row_359388
false
null
490,685
Q6ITB6
MSSGGLLLLLGLLTLWEVLTPVSSKDRPDFCELPADTGPCRVGFPSFYYNPDEKKCLEFIYGGCEGNANNFITKEECESTCAA
Kunitz-type serine protease inhibitor scutellin-2
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
83
9,074
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005615
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
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
false
Oxyuranus scutellatus
7
row_471564
false
null
376,679
B5L5Q3
MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFYELPADIGPCEDFTGAFHYSPREHEYIEFIYGGCEGNANNFNTLEECET
Scutellin-5
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
79
8,848
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005576
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
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
false
Oxyuranus scutellatus
8
row_359415
false
null
376,634
B5G6G8
MSSGGLLLLLGLLTLWAELTPVSGQDRPKKPGLCPPRPQKPPCVKECKNDWSCPGQQKCCSYGCIDECRDPIFVN
Scuwaprin-a
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
8,667
75
8,218
Antibiotic;Antimicrobial;Disulfide bond;Secreted;Signal
GO:0004867; GO:0005576; GO:0005615; GO:0019731; GO:0044278; GO:0045087
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18979207}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00095;
IPR036645;IPR008197;IPR050514;
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
false
Oxyuranus scutellatus
9
row_359370
false
null
73,013
P0DKT9
NLVQFGFMIECAIRNRQPALDFMNYGCYCGTVGRGTPVDD
Neutral phospholipase A2 homolog cannitoxin beta chain 2 (svPLA2 homolog)
Oxyuranus scutellatus canni (Papuan taipan)
183,720
40
4,473
Direct protein sequencing;Disulfide bond;Secreted
GO:0004623; GO:0005509; GO:0005576; GO:0006644; GO:0016042; GO:0050482
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
null
null
PF00068;
IPR001211;IPR016090;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
false
Oxyuranus scutellatus
10
row_63846
false
null
73,014
P0DKU0
SEIPQPSLDFEQFSNMIQCTIPPGEECLAY
Acidic phospholipase A2 homolog cannitoxin gamma chain (svPLA2 homolog)
Oxyuranus scutellatus canni (Papuan taipan)
183,720
30
3,388
Direct protein sequencing;Disulfide bond;Glycoprotein;Secreted
GO:0005576
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
false
Oxyuranus scutellatus
11
row_63847
false
null
4,061
I1C4E4
MKLSLTIVSSSFLVAIAHAASVQFNLIAPSATDVKVSVNGQQVALTASDPNVPYFTGSAEVGGTEESFERSLAGITNSTFNDFYNRPVTYANLPQLPWPIENDPQWTRKGKKAEIFDDNYIPSVFFHGDDSQVQDLVKNVPKDKVTGTLTFIGSNYVHSFANVSFGIHGAGKKHNNAKQSWKWTLSGTDTMGNRNHFKLRHMEEDPTQIRERLYADILHAMGTYANETTMVRLFINGQGFGTFNMLDDITEFSYINAMFYGGNPPATLGPLFDGASGADFIYHPGNLDGYSSWKPNKDNANGEGYEAFDPLCKAWNETDYTDNTAIANFEKMFDTEHFLRFMVIEYLTAHWDGYWMGQTNDGAYRDPSDNNKWYFLDQDFDATFGVNLDVPENKDFISVSYKDFPSRYPAGVMANGLLQNADKKAKFEQYLTETVRVLFNNVTLTNRVLAIHNFLSPDLEWDRSIVQQSPGTNFGWTFEQTSQNLWQGVSAPNNNGGGAEWGLVEYIAAKSQAMAKEFNITIVSEPVGPPAANGTATSTNDGGNTHTAAGESKPASSSESSGSKIASQSVSGASRSAVSTVLLGVTALVATAIF
Invasin CotH2 (Spore coat protein homolog 2)
Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
246,409
594
65,254
Cell membrane;Glycoprotein;GPI-anchor;Lipoprotein;Membrane;Reference proteome;Signal;Virulence
GO:0005886; GO:0044409; GO:0044652; GO:0046789; GO:0098552
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24355926}; Lipid-anchor, GPI-anchor {ECO:0000255}.
SIGNAL 1..19; /evidence="ECO:0000255"
null
PF08757;
IPR014867;
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)
CotH2 RO3G_08029
false
Rhizopus delemar
6
row_3214
false
null
213,235
P9WQK5
MGDLSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPDFAETNRPPETVHLQAGEVLFEQSTMGDLIYVVSEGEFEIVHELADGGEELVKVAGPGDYFGEIGVLFHLPRSATVRARSDATAVGYTVQAFRERLGVGGLRDLIEHRALAND
Uncharacterized ABC transporter ATP-binding protein Rv0073
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
83,332
330
35,801
ATP-binding;Isopeptide bond;Nucleotide-binding;Reference proteome;Transport;Ubl conjugation
GO:0005524; GO:0005886; GO:0016887; GO:0022857; GO:0055085
Evidence at protein level
3
null
null
null
PF00005;PF00027;
IPR003593;IPR003439;IPR017871;IPR015854;IPR018488;IPR000595;IPR018490;IPR017911;IPR027417;IPR014710;
null
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)
Rv0073
false
Mycobacterium tuberculosis
969
row_199433
false
null
1,313
A5U654
MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH
Polyphosphate glucokinase (Poly(P) glucokinase) (EC 2.7.1.63) (ATP-dependent glucokinase) (EC 2.7.1.2) (Polyphosphate--glucose phosphotransferase)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
419,947
265
27,429
ATP-binding;Direct protein sequencing;Kinase;Nucleotide-binding;Reference proteome;Transferase
GO:0004340; GO:0005524; GO:0047330
Evidence at protein level
5
null
null
null
PF00480;
IPR043129;IPR000600;
null
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)
ppgK MRA_2730
false
Mycobacterium tuberculosis
1,294
row_1069
false
null
26,773
P9WH11
MKARELDVPGAWEITPTIHVDSRGLFFEWLTDHGFRAFAGHSLDVRQVNCSVSSAGVLRGLHFAQLPPSQAKYVTCVSGSVFDVVVDIREGSPTFGRWDSVLLDDQDRRTIYVSEGLAHGFLALQDNSTVMYLCSAEYNPQREHTICATDPTLAVDWPLVDGAAPSLSDRDAAAPSFEDVRASGLLPRWEQTQRFIGEMRGT
dTDP-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13) (Thymidine diphospho-4-keto-rhamnose 3,5-epimerase) (dTDP-4-keto-6-deoxyglucose 3,5-epimerase) (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) (dTDP-L-rhamnose synthase)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
83,332
202
22,314
3D-structure;Carbohydrate metabolism;Isomerase;Reference proteome
GO:0000271; GO:0005829; GO:0008830; GO:0019305
Evidence at protein level
5
null
null
null
PF00908;
IPR000888;IPR014710;IPR011051;
1PM7;1UPI;2IXC;
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)
rmlC strM Rv3465
false
Mycobacterium tuberculosis
1,596
row_23419
false
null
68,729
O34426
METMGRHVISELWGCDFDKLNDMDFIEKTFVNAALKSGAEVREVAFHKFAPQGVSGVVIISESHLTIHSFPEHGYASIDVYTCGDLDPNVAADYIAEALHADTRENIEIPRGMGPVQIKQAQAKVL
S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase beta chain; S-adenosylmethionine decarboxylase alpha chain]
Bacillus subtilis (strain 168)
224,308
126
13,873
Autocatalytic cleavage;Decarboxylase;Lyase;Polyamine biosynthesis;Pyruvate;Reference proteome;S-adenosyl-L-methionine;Schiff base;Spermidine biosynthesis;Zymogen
GO:0004014; GO:0005829; GO:0008295
Evidence at protein level
4
null
null
null
PF02675;
IPR042286;IPR003826;IPR042284;IPR016067;IPR017716;
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)
speH speD ytcF BSU29010
false
Bacillus subtilis
3,282
row_59757
false
null
200,725
P39605
MNNTIETILNHRSIRSFTDQLLTAEEIDTLVKSAQAASTSSYVQAYSIIGVSDPEKKRELSVLAGNQPYVEKNGHFFVFCADLYRHQQLAEEKGEHISELLENTEMFMVSLIDAALAAQNMSIAAESMGLGICYIGGIRNELDKVTEVLQTPDHVLPLFGLAVGHPANLSGKKPRLPKQAVYHENTYNVNTDDFRHTMNTYDKTISDYYRERTNGKREETWSDQILNFMKQKPRTYLNDYVKEKGFNKN
FMN reductase (NADPH) (EC 1.5.1.38) (NADPH-dependent FMN reductase) (NADPH-dependent nitro/flavin reductase) (NADPH-dependent nitroreductase) (NADPH-dependent oxidoreductase)
Bacillus subtilis (strain 168)
224,308
249
28,320
3D-structure;Flavoprotein;FMN;NADP;Oxidoreductase;Reference proteome
GO:0052873
Evidence at protein level
3
null
null
null
PF00881;
IPR016446;IPR029479;IPR000415;
3N2S;
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)
nfrA1 nfrA ywcG BSU38110 ipa-43d
false
Bacillus subtilis
2,101
row_187273
false
null
26,384
P96645
MISKKVVLPLVFSAPFIFFFVLCIVVVMTISRENQVGDDFIGGGDGEYETVGIAPEVERFRAVFEKYARQEGVFDQVNIIMALTMQESGGRSLDIMQSSESIGLPPNSITDPERSIEVGIKHFKKVFKQAGGDVRLTLQAYNFGSGFIDYVKKNGGKYTKKLALDFSRLQAFKMGWKSYGDPSYVDHVMRYVKGSDKNVKPVKGSMDFYETVMKEALKYEGQPYAWGGSNPETGFDCSGLVQWSFAKAGITLPRTAQEQHGATKKISEKEATAGDLVFFGGTYEGKAITHVGIYVGNGRMFNSNDSGIQYSDLKSGYWRDHLVSFGRIK
Bifunctional muramidase/DL-endopeptidase CwlT (EC 3.2.1.17) (EC 3.4.-.-) (Bifunctional cell wall hydrolase CwlT) (Cell wall lytic enzyme T)
Bacillus subtilis (strain 168)
224,308
329
36,546
Cell wall biogenesis/degradation;Conjugation;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease
GO:0000270; GO:0003796; GO:0004175; GO:0005576; GO:0006508; GO:0008234; GO:0071555
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24532767}. Note=Accumulates in culture supernatant and some of it is found associated with the cell (PubMed:24532767). The putative signal sequence is required for CwlT to function in conjugation, but the putative lipid attachment site is not (PubMed:24532767). {ECO:0000269|PubMed:24532767}.
SIGNAL 1..29; /evidence="ECO:0000255, ECO:0000305|PubMed:24532767"
null
PF13702;PF00877;
IPR047194;IPR023346;IPR000064;IPR038765;IPR051202;
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)
cwlT yddH BSU04970
false
Bacillus subtilis
1,326
row_23096
false
null
34,599
Q59HN7
MPIKKKVMMCLAVTLVFGSMSFPTLTNSGGFKESTDRNTTYIDHSPYKLSDQKKALS
Phosphatase RapH inhibitor (Phosphatase regulator H)
Bacillus subtilis (strain 168)
224,308
57
6,345
Competence;Cytoplasm;Reference proteome;Secreted;Sporulation
GO:0005576; GO:0005737; GO:0030420; GO:0030435
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21908671}. Cytoplasm {ECO:0000269|PubMed:21908671}. Note=Peptides are secreted by the bacterium, and are then actively transported into the cell where they interact with intracellular receptors to regulate gene expression (Probable). Probably transported into the cell by the Opp (Spo0K) oligopeptide permease (PubMed:21908671). {ECO:0000269|PubMed:21908671, ECO:0000305|PubMed:21908671}.
null
null
null
null
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)
phrH BSU06839
false
Bacillus subtilis
3,992
row_30086
false
null
430,634
P94476
MPHDDHKGSRLSLLLFYFLAFLLLWEWLRPLDSFTETKHTGFFSVFIGLTFLLTFFRMRWFVTVPFCVIFTLISIHILFYQGSIFDLSWVSSFLQDVYLNITLIQSGQWNDMIPSFRTLLFFVLLWLLVYLLHYWVIYQRRILFFFLMTVAYITILDTFTPYDATFAVIRIVLIGFFMLGLLYLERIKLMERITLPKTSVLKWFLPLSVLVLAATGFGLAAPKSEPAWPDPVPFLKKITHQDRVSAGESKIGYGNHDESLGGPFQQDATPVFTWQGKERTYFRVETKDTYTGKGWIETDTGMSYQLSNGKVENLWFDHKVATERRTVRVKVDKHYGYNHLMYPIGAETIQPKQAVSLEMNGNTEQISPISEQAGEIRNMGNYTVTYNSPVYKLDELRKVKVRKNSEEYTFSDRYMQLPDSLPERVRTLAIKLTQDHDNMFDKVKAVEDYLGSNAFTYETENVTIPKNDEDYVDQFLFETKMGYCDNFSSAMVVLLRSAGIPARWVKGYTSGEYKEAGNKNGSIYEVTNNNAHSWVEVYFPEQGWVTFEPTKGFTNPAQFTSSDTKDSGSDSSSSPKKAKEKQKEEKKQPQKEEKQKEKREPAVSKKPSASHTNAGAGLYAALAVLAVLLVAAVLLYVFRSLWIPVFAVRKLKRRSDQHAFFEAYGALLKQLKRKGLPKRDSETLRDYAKRIDEKYDIEDMSKLTLSYERALYRNEDSSALWNDSRELWENLIKRRWS
Uncharacterized protein YebA
Bacillus subtilis (strain 168)
224,308
737
85,402
Cell membrane;Membrane;Reference proteome;Transmembrane;Transmembrane helix
GO:0005886
Predicted
2
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
TRANSMEM 11..31; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 36..56; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 60..80; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 118..138; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 142..162; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 164..184; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 200..220; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 618..638; /note="Helical"; /evidence="ECO:0000255"
PF13559;PF11992;PF01841;
IPR052901;IPR038765;IPR025403;IPR021878;IPR002931;
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)
yebA BSU06350
false
Bacillus subtilis
74
row_412396
false
null
77,216
P38424
MKVTKSEIVISAVKPEQYPEGGLPEIALAGRSNVGKSSFINSLINRKNLARTSSKPGKTQTLNFYIINDELHFVDVPGYGFAKVSKSEREAWGRMIETYITTREELKAVVQIVDLRHAPSNDDVQMYEFLKYYGIPVIVIATKADKIPKGKWDKHAKVVRQTLNIDPEDELILFSSETKKGKDEAWGAIKKMINR
Probable GTP-binding protein EngB
Bacillus subtilis (strain 168)
224,308
195
22,026
3D-structure;Cell cycle;Cell division;GTP-binding;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Septation
GO:0000917; GO:0005525; GO:0005829; GO:0046872
Evidence at protein level
4
null
null
null
PF01926;
IPR030393;IPR006073;IPR019987;IPR027417;IPR005225;
1SUL;1SVI;1SVW;
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)
engB ysxC BSU28190
false
Bacillus subtilis
2,573
row_67862
false
null
204,546
P54383
MTNKLTSFLADRKKTIENQLSVYTEKLDMPDSLKKSMLYSLQAGGKRLRPLIVLAVLNAYGKSEKDGIPVGCAVEMIHTYSLIHDDLPCMDDDDLRRGKPTNHKVFGEATAVLAGDGLLTESFKLITSHVSDEVSAEKRLRLVNELISAAGTEGMVGGQVADMEAENRQVTLEELESIHERKTAKLLGFCVIAGAILADAPEEDIETLRTFSSHIGIGFQIRDDILDLEGSEEKIGKRVGSDTTNDKSTYPSLLSLEGAKHKLDVHIKEAKRLIGGLSLQKDLLYELCDLIAARDH
Farnesyl diphosphate synthase (FPP synthase) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Geranyltranstransferase)
Bacillus subtilis (strain 168)
224,308
296
32,503
Cytoplasm;Isoprene biosynthesis;Magnesium;Metal-binding;Reference proteome;Transferase
GO:0004337; GO:0004659; GO:0005737; GO:0008299; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
null
null
PF00348;
IPR008949;IPR000092;IPR033749;IPR053378;
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)
ispA yqiD BSU24280
false
Bacillus subtilis
1,643
row_191008
false
null
56,800
Q9UST6
MSDSPIELMRSTLAGFQIAPDVKTISNIQDIRAQIQSFREKELEGSQTKFKVLSRKLEISTQAMESLKQTAESSQHAEEILSREKEKFRIAKLLNITENEIMSLESQLQKMKEQLLQLEERENTSEDICQSEENANMLKLNFYHSLGFDLETAENTGNKRVIIHTENDLQTVQISNKYSPYFYSNYFWDLLDDSKDKK
Kinetochore protein spc24
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
284,812
198
23,039
Cell cycle;Cell division;Centromere;Chromosome;Coiled coil;Cytoplasm;Cytoskeleton;Kinetochore;Meiosis;Mitosis;Nucleus;Reference proteome
GO:0000070; GO:0000775; GO:0000776; GO:0000779; GO:0005634; GO:0005816; GO:0005829; GO:0007059; GO:0008608; GO:0031134; GO:0031262; GO:0051301; GO:0051455; GO:1990571
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15728720}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15728720}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Note=Associated with kinetochores. {ECO:0000269|PubMed:15728720}.
null
null
PF08286;
IPR013252;IPR038066;
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)
spc24 SPBC336.08
false
Schizosaccharomyces pombe
3,662
row_49225
false
null
311,760
Q9US49
MSNLGNNITERIESDCISQNECRIDVYFSEKEKESTEASINMFLAELERLQLEYGKEHIWQNEELNLQRVEYQGKDCILGITNFGDCIDDEWYIVWLLREASKAVKSAFVRIIDEDGEFLLIEAALSLPKWIDEDNSDYRVWIHNGEVIILRPEDEFLKKMNRCPPLTREQAIFQISSGSNLYTSREVNDSISQRLKKFPKAANVKLRAICTVPRKIVHVLQKNKNLISSAVNAFYYRDPIDENYCDRMSKFNQNDLVTTTITFTPLLYAQLYQQRCKTFRPFHLPSDVHSLDYERAILGMKLSCGFEILYNSKENVEKRTEIDEYLQIQPLPTDEDIKKIPLIEDDTSFMNVNPDELEELLEKKLNSFCDDFGDDERSGFDNTDHDNTLVGEEEMVPGNHGGKSINEEITKNKQKQNFNESDLKNMASRIETFINDEASNNHREDFYGVKNSDTDTDSDSLADSDDEIFLNRNQGIDEVEFDETKFYDLLKGKDGKYQNQDVDEFSSGNEDEMDIPGDANMEEYMRAMDEELYGGLRGRDEGLEGIDDKDIDLNLMKNIIEGIEANPDLYGGPISTLLNSLKIQIPREK
Protein ecdysoneless homolog (Suppressor of GCR two) (sgt1)
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
284,812
590
68,157
Cytoplasm;Nucleus;Reference proteome;Transcription;Transcription regulation
GO:0005634; GO:0005829; GO:0045292; GO:0070990
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
null
null
PF07093;
IPR010770;
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)
sgt1 SPAC1002.10c
false
Schizosaccharomyces pombe
886
row_295308
false
null
520,281
Q9HDW5
MGIASSLRLFGKAPASYLFNGFRRQMKNPLMKKGVVYAGVSGTCAAAGYMFGNFVMEKHIYQVKYTEEQEKEVLEVENRLQNLKIVKDLRQNPSFRELRMPFNRSNHSLTNNLLSGPGRITVPPVIFYDKSTRQVYAIAHVGKDVGLDDDTIHPGLIATCMDEVLAICSFLSLPNKIAVTANLKLSNPTKAYTNHFYILRSHLEWTKGRKAQTHGTAYMLDNEDPSKSTCVAIADGLFVEPRFAKYLKHVIPVSLP
UPF0644 protein PB2B4.06
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
284,812
256
28,714
Membrane;Mitochondrion;Reference proteome;Transmembrane;Transmembrane helix
GO:0005739; GO:0006631; GO:0031966; GO:0047617
Inferred from homology
2
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
null
TRANSMEM 34..56; /note="Helical"; /evidence="ECO:0000255"
null
IPR029069;IPR052061;
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)
SPAPB2B4.06
false
Schizosaccharomyces pombe
3,172
row_500718
false
null
305,549
Q9HE15
MSIPLEQPENVVVLRQTMYLLSLMTILRDQQTGHSEFVRTANLIINMLMQEALSALPYKKCLIKTSSGGTYTGVQPARDICGVSILRAGESMEYGLAAACNYSVPVGKLLVQRDETTFEAKLMFCKLPKDAQDRLVLLLDPLLATGNSVILAIQTLINKGIPEENIVFVNLIACNEGITNVFAKFPKLRMVTASIDPELNANKYVVPGCGDFGDRYFGTC
Uracil phosphoribosyltransferase 2 (UPRTase 2) (EC 2.4.2.9) (UMP pyrophosphorylase 2)
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
284,812
220
24,155
Allosteric enzyme;Glycosyltransferase;GTP-binding;Nucleotide-binding;Reference proteome;Transferase
GO:0004845; GO:0005525; GO:0005634; GO:0005737; GO:0005829; GO:0008655; GO:0044206
Inferred from homology
3
null
null
null
PF14681;
IPR000836;IPR029057;
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)
SPAC1399.04c
false
Schizosaccharomyces pombe
3,458
row_289276
false
null
355,742
B0B7U3
MLLKKRSPTSILGTLALTGIVISYMIGGGIFSLPQNMAASASAGAVMLAWMLSGIGIFFIANTFKTLSIIRPDLKAGIYTYSREGFGPYVGFTIAWGYWLCQIFGNVGYAVITMDALNYFFPPYFAGGNTIPAILLGSLLIWIFNYIVLRGIRQASFVNIIGVVCTLIPLLLFILITARFFKFSIFKTDFWGTAPQHTLGSIGSQLKSTMLVTLWAFIGIEGAVVISGRAANPSSVGKATILGFSGCLLIYVLLSLLPFGSLFQYQLAKIADPSTAGVLNILVGKWGEVLMNTGLLIAVLTSWLSWTILASEIPYAAAKNGTFPECFAIENSKHAPSFSLFMTSGLMQITMLLVYFSSNAWNTMLEITGVMVLPAYLTSSLFLVKFSLSKKYPKQAAIKARIAMITGLLGSLYSLWLIYAGGLQHLFMVAILLALGIPFYVDSGIRHKQEKTFLNRKEILKMTIMALAALLAIFLFSANKIHL
Arginine/agmatine antiporter
Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
471,472
483
52,662
Amino-acid transport;Antiport;Cell inner membrane;Cell membrane;Membrane;Transmembrane;Transmembrane helix;Transport;Virulence
GO:0005886; GO:0006865; GO:0015297
Inferred from homology
2
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
null
TRANSMEM 11..33; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 48..70; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 90..112; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 127..149; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 156..178; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 209..228; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 241..263; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 293..315; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 335..357; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 367..389; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 415..435; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 458..477; /note="Helical"; /evidence="ECO:0000255"
PF13520;
IPR002293;IPR004754;IPR050367;
null
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)
aaxC arcD CTL0628
false
Chlamydia trachomatis
79
row_338771
false
null
179,150
D2YVK5
MGRFLLVTLSMLVVTFSLNEANSCCCPQDWLPKNGFCYKVFNDLKNWNDAEMFCRKFKPGCHLASIHSNADSADLAEYISDYLKSDGHVWIGLNDPRKQRTWVWSDRSSTNYLAWNQGEPNNSKNIEYCVHLWALTGYLKWNDTPCEALYHFICQCKF
C-type lectin mannose-binding isoform (CTL) (Venom C-type lectin mannose binding isoform 1)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
158
18,380
Calcium;Disulfide bond;Glycoprotein;Hemagglutinin;Lectin;Metal-binding;Secreted;Signal
GO:0005576; GO:0030246; GO:0046872
Evidence at transcript level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF00059;
IPR001304;IPR016186;IPR050111;IPR018378;IPR016187;
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
false
Notechis scutatus
0
row_166378
false
null
463,782
Q3SB12
MAATLTPEQITEYKGIFEMFDEEGNGLVKTDDLESLMSLIGINPTKRDLANMAKDVDKDKKGTFNCDGFLVLMGIYHEKSKNQDEELRAAFKVFDKEHKGYIEWDTLKYVLMNAGEPLNEHEAELMMKEADKDGDGTIDYEEFVAMMTGESFKLTQ
Calglandulin
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
156
17,767
Calcium;Cytoplasm;Metal-binding;Repeat
GO:0005509; GO:0005737; GO:0016460
Evidence at transcript level
2
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Not found in venom. {ECO:0000250}.
null
null
PF13499;PF13833;
IPR050230;IPR011992;IPR018247;IPR002048;
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
false
Notechis scutatus
1
row_445158
false
null
71,838
P08873
MYPAHLLVLLTVCVSLLEASSIPARPLNLYQFGNMIQCANHGRRPTLAYADYGCYCGAGGSGTPVDELDRCCKAHDDCYGEAGKKGCYPTLTLYSWQCIEKTPTCNSKTGCERSVCDCDATAAKCFAKAPYNKKNYNIDTEKRCQ
Basic phospholipase A2 notechis 11'2 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
145
15,903
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..19; /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), Notechis (genus), Notechis scutatus (species)
null
false
Notechis scutatus
2
row_62737
false
null
74,741
P20146
MYPAHLLVLLAVCVSLLGAASIPPLPLNVAQFDNMIECANYGSRPSWHYMEYGCYCGKEGSGTPVDELDRCCKAHDDCYTEAEKRRCHPKFSAYSWKCGSDGPTCDPETGCKRTVCDCDATAAKCFAKAPFNQANWNIDTETHCQ
Acidic phospholipase A2 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
145
16,002
Calcium;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..21; /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), Notechis (genus), Notechis scutatus (species)
null
false
Notechis scutatus
3
row_65504
false
null
401,660
E3P6P2
MVHSQLPVVALLRLLCALLLLPSATMIPGGLSPRSVTDPDVQEAAEFAVQEYNALSANAYYYKQLRIVEAQSQVVAGAKYYLTMELMKTKCAKTTGKPKVYKEIQNCELPPKAQQEKLTCRFQVWSRPWLQKIELTKMSCN
Cystatin
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
141
15,896
Disulfide bond;Protease inhibitor;Secreted;Signal;Thiol protease inhibitor
GO:0004869; GO:0070062
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..26; /evidence="ECO:0000250"
null
PF00031;
IPR000010;IPR046350;IPR018073;
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
false
Notechis scutatus
4
row_384236
false
null
188,304
P00607
NLVQFSNMIQCANHGSRPSLAYADYGCYCSAGGSGTPVDELDRCCKTHDDCYARATKSYSCTPYWTLYSWQCIEKTPTCDSKTGCQRFVCDCDATAAKCFAKAPYNKENYNIDPKKRCQ
Basic phospholipase A2 homolog 1 (svPLA2 homolog) (Notechis II-1)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
119
13,323
Direct protein sequencing;Disulfide bond;Secreted
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7007039}.
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
false
Notechis scutatus
5
row_175189
false
null
376,654
B5KL32
MSSGGLLLLLGLLTLWEILTPVSSKDRPHFCHLPHDTGPCNRNTQAFYYNPVYHTCLKFIYGGCQGNSNNFKTIDECKRTCAA
Kunitz-type serine protease inhibitor tigerin-3
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
83
9,294
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005576
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
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), Notechis (genus), Notechis scutatus (species)
null
false
Notechis scutatus
6
row_359390
false
null
376,683
B5L5R4
MSSGGLLLLLGLLTLWAELTPVSSKDRPKFCELPADSGPCRGILRAFYYHPVHRTCQMFIYGGCYGNANNFKTIDECKRTCAA
Tigerin-4
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
83
9,190
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005576
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
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), Notechis (genus), Notechis scutatus (species)
null
false
Notechis scutatus
7
row_359419
false
null
376,640
B5G6H4
MSSGGLLLLLGLLTLWAELTPVSSLDRPKKPGLCPPRPQKPPCVRECKNDWRCPGEQKCCRYGCIYECRDPIFVK
Notewaprin-a
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
75
8,462
Antibiotic;Antimicrobial;Disulfide bond;Secreted;Signal
GO:0004867; GO:0005576; GO:0005615; GO:0019731; GO:0044278; GO:0045087
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18979207}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00095;
IPR036645;IPR008197;IPR050514;
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
false
Notechis scutatus
8
row_359376
false
null
277,094
Q7LZG5
NLIQLSNMIKCAIPGSQPLF
Phospholipase A2 II-5b (svPLA2) (EC 3.1.1.4) (Notechis II-5b non-toxic venom protein) (Phosphatidylcholine 2-acylhydrolase)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
20
2,188
Calcium;Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Secreted
GO:0004623; GO:0005576; GO:0016042
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1814009}.
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
false
Notechis scutatus
9
row_261477
false
null
124,500
A5F5N9
MVRIAIAGAAGRMGRNLVKATHQNPLSELGAGSERPESSLVGVDIGELCGIGKQGIVLVDNLEQAVEQFDVIIDFTAPASTLANLALCEQHGKKLVIGTTGFTDAQRQTIEQAAKKIPIVMAPNYSVGVNLVFKLLEKAAKVMGDYCDIEIIEAHHRHKVDAPSGTAIGMGEAIAHAMGNQLSDVAVYAREGITGERSRNEIGFATIRAGDIIGEHTAMFADIGERVEITHKATDRMTFANGAVKAAIWLAEQPAGFYTMTDVLGLNDL
4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
345,073
269
28,607
Amino-acid biosynthesis;Cytoplasm;Diaminopimelate biosynthesis;Lysine biosynthesis;NAD;NADP;Oxidoreductase
GO:0005829; GO:0008839; GO:0009089; GO:0016726; GO:0019877; GO:0050661; GO:0051287
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}.
null
null
PF05173;PF01113;
IPR022663;IPR000846;IPR022664;IPR023940;IPR036291;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species)
dapB VC0395_A1970 VC395_2506
false
Vibrio cholerae
543
row_112712
false
null
334,817
A5F3G7
MNYFELFGLPIQFELDGSLLSSQFRALQKRFHPDNFATASERDRLMAVQQAAQINDAYQTLKDPLRRAEYLLSLQGIEMNAEQQTLQDPMFLMEQMELREELESVTACADPEAALVAFDTKVTAMQRHYLAQLQGQLAQSEWLAAADQIRKLKFIAKLKNEVERVEDQLLG
Co-chaperone protein HscB homolog
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
345,073
171
19,627
Chaperone
GO:0001671; GO:0006457; GO:0044571; GO:0051087; GO:0051259; GO:1990230
Inferred from homology
2
null
null
null
PF00226;PF07743;
IPR001623;IPR004640;IPR036386;IPR009073;IPR036869;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species)
hscB VC0395_A0280 VC395_0768
false
Vibrio cholerae
776
row_318039
false
null
521,859
Q9KP46
MPQLSQTVLIQNRLGLHARAAVKLVQLAQSFDAVLTVQSQDGREATADSVMGLLMLESAQGQNVVISAEGSQAEQALQAVCQLIEQKFDEDE
Phosphocarrier protein NPr (Nitrogen-related HPr)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
92
9,910
Cytoplasm;Phosphotransferase system;Reference proteome
GO:0005737; GO:0009401
Inferred from homology
2
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
null
null
PF00381;
IPR050399;IPR000032;IPR035895;IPR001020;IPR002114;
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)
npr VC_2533
false
Vibrio cholerae
936
row_502278
false
null
307,373
Q9KL34
MQTIAIQGRDLCVTYGSRQVLDHVDITLRCGEVAALLGPNGAGKSTLLKLLCGEMSGAGKLDYFGVPASQWPAEKLANHLGILPQQSSLTFPFTAQEVVELGAIPLNLPRKEVERVARHYMLKTDVLHLAASLYPSLSGGEKQRLHLARVLTQLHQAGQQRILMLDEPTSALDLAHQHNTLQLARQLADEEQCAVVVVLHDLNLAAQYSDRLILLHQGKIVCDAAPWQALTAERIEQVYGYQALVAAHPTRDFPMVYPA
Hemin import ATP-binding protein HmuV (EC 7.6.2.-)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
259
28,419
ATP-binding;Cell inner membrane;Cell membrane;Membrane;Nucleotide-binding;Reference proteome;Translocase;Transport
GO:0005524; GO:0005886; GO:0016887
Inferred from homology
3
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01718}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01718}.
null
null
PF00005;
IPR003593;IPR003439;IPR027417;
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)
hmuV hutD VC_A0915
false
Vibrio cholerae
568
row_291062
false
null
307,722
Q9KUT4
MRNVDKQDNLVRAFKALLKEERFGSQGDIVEALKNEGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTASSSLRELVLDVDYNNALVVIRTGPGAAQLIARLLDSLGKSEGILGVVAGDDTIFITPTLDVPVKELFHSVCELFEYAG
Arginine repressor
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
156
17,076
Amino-acid biosynthesis;Arginine biosynthesis;Cytoplasm;DNA-binding;Reference proteome;Repressor;Transcription;Transcription regulation
GO:0000821; GO:0000987; GO:0003700; GO:0005667; GO:0005737; GO:0006526; GO:0034618; GO:0051259; GO:1900079
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00173}.
null
null
PF01316;PF02863;
IPR001669;IPR020899;IPR036251;IPR020900;IPR036388;IPR036390;
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)
argR VC_0431
false
Vibrio cholerae
805
row_291407
false
null
116,735
A2T3M4
MATFKDACFHYRRLTALNRRLCNIGANSICMPVPDAKIKGWCLECCQIADLTHCYGCSLPHVCKWCVQNRRCFLDNEPHLLKLRTVKHPITKDKLQCIIDLYNIIFPINDKVIRKFERMIKQRKCRNQYKIEWYNHLLLPITLNAAAFKFDENNLYYVFGLYEKSVSDIYAPYRIVNFINEFDKLLLDDINFTRMSNLPIELRNHYAKKYFQLSRLPSSKLKQIYFSDFTKETVIFNTYTKTPGRSIYRNVTEFNWRDELELYSDLKNDKNKLIAAMMTSKYTRFYAHDNNFGRLKMTIFELGHHCQPNYVASNHPGNASDIQYCKWCNIKYFLSKIDWRIRDMYNLLMEFIKDCYKSNVNVGHCSSVENIYPLIKRLIWSLFTNHMDQTIEEVFNHMSPVSVEGTNVIMLILGLNISLYNEIKRTLNVDSIPMVLNLNEFSSIVKSISSKWYNVDELDKLPMSIKSTEELIEMKNSGTLTEEFELLISNSEDDNE
Non-structural protein 1 (NSP1) (NCVP2) (Non-structural RNA-binding protein 53) (NS53)
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
450,149
496
58,565
Host cytoplasm;Host cytoskeleton;Host-virus interaction;Inhibition of host innate immune response by virus;Inhibition of host IRF3 by virus;Inhibition of host IRF7 by virus;Inhibition of host RLR pathway by virus;Interferon antiviral system evasion;Metal-binding;Reference proteome;RNA-binding;Viral immunoevasion
GO:0003723; GO:0030430; GO:0039548; GO:0039557; GO:0044163; GO:0046872
Evidence at protein level
3
SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04088}.
null
null
PF00981;
IPR002148;
null
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
false
Rotavirus A
31
row_105113
false
null
284,675
Q86504
MLKMESTQQMASSIINTSFEAAVVAATSTLELMGIQYDYNEVYTRVKSKFDYVMDDSGVKNNLLGKAATIDQALNGKFGSAARNRNWMADTRTTARLDEDVNKLRMMLSSKGIDQKMRVLNACFNVKRVPGKSSSIIKCTRLMRDKIERGEVEVDDSFVEEKMEVDTIDWKSRYEQLEKRFESLKQRVNEKYTSWVQKAKKVNENMYSLQNVISQQQSQIADLQNYCNKLEVDLQNKISSLVSSVEWYLKSMELPDEIKTDIEQQLNSIDVINPINAIDDFESLIRNIILDYDRIFLMFKGLMRQCNYEYTYE
Non-structural protein 3 (NSP3) (NCVP4) (Non-structural RNA-binding protein 34) (NS34)
Rotavirus A (strain RVA/Cow/France/RF/1975/G6P6[1]) (RV-A)
10,933
313
36,347
Coiled coil;Host cytoplasm;Host-virus interaction;RNA-binding;Translation regulation
GO:0003723; GO:0006417; GO:0030430
Evidence at protein level
3
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04094}.
null
null
PF01665;
IPR042519;IPR036082;IPR002873;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Bovine rotavirus A (no rank), Bovine rotavirus A unknown G-type (no rank)
null
false
Rotavirus A
72
row_268883
false
null
71,168
P03537
MAELACFCYPHLENDSYRFIPFNSLAIKCMLTAKVDKKDQDKFYNSIIYGIAPPPQFKKRYNTSDNSRGMNYETSMFNKVAALICEALNSIKVTQSDVASVLSKIVSVRHLENLVLRRENHQDVLFHSKELLLKSVLIAIGHSKEIETTATAEGGEIVFQNAAFTMWKLTYLEHKLMPILDQNFIEYKITLNEDKPISESHVKELIAELRWQYNKFAVITHGKGHYRVVKYSSVANHADRVYATFKSNNKNGNMIEFNLLDQRIIWQNWYAFTSSMKQGNTLEICKKLLFQKMKRESNPFKGLSTDRKMDEVSQIGI
Non-structural protein 2 (NSP2) (EC 3.6.4.-) (NCVP3) (Non-structural RNA-binding protein 35) (NS35)
Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain Both))
37,137
317
36,628
ATP-binding;Host cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;RNA-binding
GO:0003723; GO:0004550; GO:0005524; GO:0017111; GO:0019079; GO:0030430; GO:0046872
Evidence at protein level
4
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}. Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}.
null
null
PF02509;PF21067;
IPR048306;IPR048573;IPR003668;IPR024076;IPR024068;
null
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
false
Rotavirus A
67
row_62085
false
null
75,094
P23045
MASLIYRQLLTNSYTVELSDEIKTIGSEKSQNVTINPGPFAQTTYAPVTWRHGEVNDSTTVEPVLDGPYQPTSFKPPNDYWILLNPINKGVVFKGTNRTDVWVAILLIEQRVPSQDRQYTLFGEVKQITVENSSDKWKFFEMFRNNANIDFQLQRPLTSDTKLAGFLTHGGRVWTFNGETPHATTDYSTTSNLPDVEVVIHTEFYIIPRSQESKCNEYINTGLPPMQNTRNVVPVALSSRSITYQRAQVNEDIIISKTSLWKEMQYNRDITIRFKFGNSIVKLGGLGYKWSEVSFKAANYQYNYLRDGEQVTAHTTCSVNGVNNFSYNGGSLPTDFSVSRYELIKENSYVYIDYWDDSQAFKNMVYVRSLAANLNSVKCSGGNYNFKIPVGAWPVMSGGAVSLHFAGVTLSTQFTNFVSLNSLRFRFSLTVEEPSFSILRTRVSGLYGLPAANPNNGNEYYEIAGRFSLILLVPSNDDYQTPIMNSVTVRQDLERQLGDLREEFNSLSQEIAMTQLIDLALLPLDMFSMFSGIKSTIDVAKSMATNVMKKFKKSGLATSISELTGSLPSAASSVSRSSSIRSNISSISVWTDVSEQIADASNSVRSISTQTSAISKRLRLREITTQTEGMNFDDISAAVLKTPLDKSTHISPDTLPDIITESSEKFIPKRAYRVLKNDEVMEADVDGKFFAYRVDTFEEVPFDVDKFVNLATASPVISAIIDFKTLKNLNDNYGITRSQALDLIRSDPRVLRDFINQNNPIIKNRIEQLILQCRL
Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
Rotavirus A (strain RVA/Pig/United States/Gottfried/1983/G4P2B[6]) (RV-A)
10,917
775
87,098
Capsid protein;Coiled coil;Disulfide bond;Hemagglutinin;Host cell membrane;Host cytoplasm;Host cytoskeleton;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Membrane;Outer capsid protein;Viral attachment to host cell;Viral penetration into host cytoplasm;Viral penetration via permeabilization of host membrane;Virion;Virus entry into host cell
GO:0016020; GO:0019062; GO:0020002; GO:0039624; GO:0039665; GO:0044163; GO:0044168; GO:0044172
Inferred from homology
4
SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04132}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04132}. Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04132}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04132}. Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. VP4 also seems to associate with lipid rafts of the host cell membrane probably for the exit of the virus from the infected cell by an alternate pathway. {ECO:0000255|HAMAP-Rule:MF_04132}.; SUBCELLULAR LOCATION: [Outer capsid protein VP8*]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Note=Outer capsid protein. {ECO:0000255|HAMAP-Rule:MF_04132}.; SUBCELLULAR LOCATION: [Outer capsid protein VP5*]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Note=Outer capsid protein. {ECO:0000255|HAMAP-Rule:MF_04132}.
null
null
PF17477;PF00426;PF17478;
IPR013320;IPR042546;IPR035330;IPR038017;IPR000416;IPR035329;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), unclassified Rotavirus A (no rank)
null
false
Rotavirus A
25
row_65840
false
null
123,467
A4ZCW6
MKVLALRRSVAQVYADTQVYTHDDTKDDYENAFLISNLTTHNILYLNYSIKTLEILNKSGIAAVEIQSLEELFTLIRCNFTYDYEDNIIYLHDYSYYTNNEIRTDQHWVTKTDIEEYLLPGWKLTYVGYNGSDTRGHYNFSFTCQNAATDDDLIIEYIYSEVLDFQNFMLKKIKERMTTSLPIARLSNRVFRDKLFPLLSKKRQRILNIGPRNESMFTFLNFPSIKQFSNGPYLVKDTIKLKQERWLGKRVSQFDIGQYKNMMNVITTVYYYYNLYQKKPTIYMVGSAPSYWIYDVKQYSDFTFETWDPFDTPYSSMHHKELFSEKDIAKLKDDSILYIDIRTDRGNIDWKEWRKIVEAQTVSNLKLAYQYLASGKSKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLLLDIWDISNVKRFIPKGVLYSFINNVITENVFIQPPFKIKTFKNDYIVALYALSNDFNDRTDVINLINNQKQSLITVRINNTFKDEPKVGFKNIYDWTFLPTDFNTTDTIITSYDGCLGIFGLSISLASKPTGNNHLFILNGTDKYYKLDQFANHTGISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNIENSVSGHVYNALIYYRYNYSFDLKRWIYLHSIEKADIEGGKYYEHAPIELIYACKSAKEFASLQDDLTVLRYANEIERYINKVYSITYADDPNYFIGIKFRHIPYKYDVKVPHLTFGVLFISDSMIPDVVKIMKNMRNELFEMDVTTSYTYMLSDGVYVANVSGVLATYFKMYNLFYKSQITFGQSRMFIPHITLSFNNNRTVRIETTKLKINSIYLRKIRGDTVFDMSE
Protein VP3 [Includes: 2',5'-phosphodiesterase (EC 3.1.4.-); mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)]
Rotavirus A (strain RVA/Human/Japan/AU-1/1982/G3P3[9]) (RV-A)
39,013
835
98,046
GTP-binding;Host-virus interaction;Hydrolase;Inhibition of host innate immune response by virus;Methyltransferase;mRNA capping;mRNA processing;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;RNA-binding;S-adenosyl-L-methionine;Transferase;Viral immunoevasion;Virion
GO:0003723; GO:0004482; GO:0004484; GO:0005525; GO:0016032; GO:0016787; GO:0019013; GO:0052170
Inferred from homology
3
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04128}. Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128}.
null
null
PF06929;
IPR011181;
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
false
Rotavirus A
4
row_111705
false
null
77,306
P39033
MASLIYRQLLSNSYVTNISDEVNEIGTKKTTNVTVNPGPFAQTGYAPVDWGHGELPDSTLVQPTLDGPYQPTSLNLPVDYWMLIAPTREGKVAEGTNTTDRWFACVLVEPNVQNTQRQYVLDGQNVQLQVSNDSSTSWKFILFIKLTPDGTYTQYSTLSTPHKLCAWMKRDNRVYWYQGATPNASESYYLTINNDNSNVSSDAEFYLIPQSQTAMCTQYINNGLPPIQNTRNIVPVNITSRQIKDIRAQINEDIVISKTSLWKEMQYNRDIIIRFKFANSIIKSGGLGYKWSEISFKPMNYQYTYTRDGEEVTAHTTCSVNGVNDFNYNGGTLPTDFAISRFEVIKENSYVYVDYWDDSQAFRNMVYVRSLAANLNDVVCSGGSYSFALPVGNHPVMSGGAVTLTSAGVTLSTQYTDYVSLNSLRFRFRLAVSEPSFSISRTRMSGIYGLPAVNPNNNAEYYEIAGRFSLISLVLTNDDYQTPIANSVTVRQDLERQLGELREEFNSLSQEIAVSQLIDLATLPLDMFSMFSGIKSTVEAVKSMTTNVMKRFKTSSLANAISDLTSNMSEAASSVRLTSVRSVGTVTLPRARVSLQVSDDLRSMQDVSTQVSNVSRNLRLKEFTTQTDTLSFDDISAAVLKTKLDKSTQISQQTMPDIIAESSEKFIPKRSYRIVDEDTAFETGIDGTFYAYKVDTFNEIPFDMERFNKLVTDSPVLSAIIDFKTLKNLNDNYGITKKQAMELLHSNPKTLKEFINNNNPIIRNRIENLISQCRL
Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
Rotavirus A (strain RVA/Human/Japan/AU-1/1982/G3P3[9]) (RV-A)
39,013
775
87,093
Capsid protein;Coiled coil;Disulfide bond;Hemagglutinin;Host cell membrane;Host cytoplasm;Host cytoskeleton;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Membrane;Outer capsid protein;Viral attachment to host cell;Viral penetration into host cytoplasm;Viral penetration via permeabilization of host membrane;Virion;Virus entry into host cell
GO:0016020; GO:0019062; GO:0020002; GO:0039624; GO:0039665; GO:0044163; GO:0044168; GO:0044172
Evidence at transcript level
4
SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04132}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04132}. Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04132}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04132}. Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. VP4 also seems to associate with lipid rafts of the host cell membrane probably for the exit of the virus from the infected cell by an alternate pathway. {ECO:0000255|HAMAP-Rule:MF_04132}.; SUBCELLULAR LOCATION: [Outer capsid protein VP8*]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Note=Outer capsid protein. {ECO:0000255|HAMAP-Rule:MF_04132}.; SUBCELLULAR LOCATION: [Outer capsid protein VP5*]: Virion {ECO:0000255|HAMAP-Rule:MF_04132}. Note=Outer capsid protein. {ECO:0000255|HAMAP-Rule:MF_04132}.
null
null
PF17477;PF00426;PF17478;
IPR013320;IPR042546;IPR035330;IPR038017;IPR000416;IPR035329;
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
false
Rotavirus A
26
row_67942
false
null
196,461
P21285
MYGIEYTTILTILISIVLLNYILKSITSMMDFIIYRFLLVFVIVLPFIKAQNYGINLPITGSMDTAYVNSTQQESFMTSTLCLYYPNSVTTEITDPDWTHTLSQLFLTKGWPTNSVYFKSYADIASFSVNPQLYCDYNIVLVQYQNSLALDVSELADLILNEWLCNPMDVTLYYYQQTDEANKWISMGDSCTVKVCPLNMQTLGIGCTTTDVATFEEVANAEKLVITDVVDGVNHKINITLNTCTIQNCKKLGPRENVAIIQVGGSDIIDITADPTTIPQTERIMRINWKKWWQVFYTVVDYINQIVQVMSKRSRSLNSAAFYYRI
Outer capsid glycoprotein VP7
Rotavirus A (strain RVA/Human/Philippines/L26/1987/G12P1B[4]) (RV-A)
10,953
326
37,176
Alternative initiation;Calcium;Capsid protein;Disulfide bond;Glycoprotein;Host endoplasmic reticulum;Host-virus interaction;Metal-binding;Outer capsid protein;Signal;T=13 icosahedral capsid protein;Virion
GO:0039621; GO:0039624; GO:0044166; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04131}.
SIGNAL 1..50; /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
null
PF00434;
IPR001963;IPR042207;IPR042210;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus A isolates (clade)
null
false
Rotavirus A
60
row_183107
false
null
295,869
Q8UZL8
MLKMESTQQMASSIINSSFEAAVVAATSTLELMGIQYDYNEVYTRVKSKFDLVMDDSGVKNNLIGKAITIDQALNGKFSSAIRNRNWMTDSRTVAKLDEDVNKLRIMLSSKGIDQKMRVLNACFSVKRIPGKSSSIVKCTRLMKDKLERGEVEVDDSFVEEKMEVDTIDWKSRYEQLEKRFESLKHRVNEKYNHWVLKARKVNENMNSLQNVISQQQAHINELQMYNNKLERDLQSKIGSVVSSIEWYLRSMELSDDVKSDIEQQLNSIDQLNPVNAIDDFESILRNLISDYDRLFIMFKGLLQQCNYTYTYE
Non-structural protein 3 (NSP3) (NCVP4) (Non-structural RNA-binding protein 34) (NS34)
Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A)
444,185
313
36,315
Coiled coil;Host cytoplasm;Host-virus interaction;RNA-binding;Translation regulation
GO:0003723; GO:0006417; GO:0030430
Evidence at protein level
3
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04094, ECO:0000269|PubMed:26063427}.
null
null
PF01665;
IPR042519;IPR036082;IPR002873;
null
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)
null
false
Rotavirus A
73
row_279804
false
null
93,401
Q6WAT6
MKVLALRHSVAQVYADTQIYIHDETKDDYENAFFISNLTTHNILYLNYSVKTLQILNKSGIAAVEIQKMDKLFTLIRCNFTYDYIDDVVYLHDYSYYTNNEIRTDQHWVTKTNIEDYLLPGWKLTYVGYNGNDTRGHYNFSFKCQNAATDDDAIIEYIYSNELDFQNFILKKIKERMTTSLPIARLSNRVFRDKLFKTLVSDHSKIVNVGPRNESMFTFLDHPSIKQFSNGPYLVKDTIKLKQERWLGKRLSQFDIGQYKNYVKCINNLISIYDMYHEKPIIYMLGSAPSYWIHDVKQYSNLKFETWDPLDTPYSDLHHKELFYISDVTKLKDNSILYIDIRTDRENADWKTWRKIVEEQTVNNLNIAYKYLSTGKAKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLIMDIWDSKNIKRFIPKGVLYSYINNIITENVFIQQPFKLKTLRNEYVVALYALSNDFNNREDVIKLINNQKNALITVRINNTFKDEPKVGFKDIYDWTFLPTDFETNESIITSYDGCLGVFGLSISLASKPTGNNHLFMLSGTNKYFNMDQFANHMSISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYSFDLKRWIYLHSTNKASIEGGRYYEHAPIELIYACRSAREFAKLQDDLTVLRYSNEIENYINKVYSITYADDPNYFIGIKFKNIPYEYDVKVPHLTFGVLNISDSMVPDVVVILKKFKSELFRMDVTTSYTYMLSDEIYVANVSGVLSTYFKLYNAFYKEQITFGQSRMFIPHITLSFSNKKVVRIDSTRLNIDFIYLRKIKGDTVFDMAE
Protein VP3 [Includes: 2',5'-phosphodiesterase (EC 3.1.4.-); mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)]
Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A)
10,934
835
98,045
GTP-binding;Host-virus interaction;Hydrolase;Inhibition of host innate immune response by virus;Methyltransferase;mRNA capping;mRNA processing;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;RNA-binding;S-adenosyl-L-methionine;Transferase;Viral immunoevasion;Virion
GO:0003723; GO:0004482; GO:0004484; GO:0005525; GO:0016032; GO:0016787; GO:0019013; GO:0052170
Evidence at protein level
4
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000269|PubMed:20122940}. Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000305}.
null
null
PF06929;
IPR011181;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Bovine rotavirus A (no rank), Bovine rotavirus G6 (no rank)
null
false
Rotavirus A
3
row_82962
false
null
418,343
P33410
MKQIPLILAMSLAFAAAAKGESAPDMQAAVNFDSAMLWGGANGADLSRFNYSNALRPGNYIVDIYANNYPLIRQQVRFVAAQTSGQGLKTAPAVACFTYGQLEAMQVRLRALDPALVADLKSSGRCEVLGKLFPDSRESFDFGENRLEVSIPQAYTINRFRRDISPDEWDSGITAFRLGYQYNYADYIGGLRAGRRLDLNLYSGFNFKGWYLRNSSTLGWGQGRFTRRSQRTSLQTDIPSWRARLVFGDVFSSGEYFAPYSMRGMLVGSDTAMLPYSERLYRPTIRGVARTRANVKVYQAGVLVFQDAVPPGPFAIDDYSPASYGGDLRVVVTEANGAVQTFTVPYASAVRLILPGQTQWSFSAGRYRNYRNDGQDRPWVTQLTGRHGVADGVNLYGGLLIAQAYQAGLAGLSWNTPWGAMAADATLSRSQLSTTGNANGSSLRFSYSKTLSGTNTAIRLATLRYSSSGFWNFADAVNAGPVETNGRNGRFGLYSLLGRERPRGDFSVTLSQPLGGYGSLYVSALRRTYWGSSRVDQQTQLGYSTQVGRVGVNLDVSRTENRRSTEHQVMLNLSIPLYGATSSGVVTGSLARTGSAPVQQSVNYSGMSGERDQYTYGLGVQRAGTSAQYALNGSWSGTYGEVSGQLTHGRSYSQYQINGSGGLVAHAGGVTFGQYQAGTIGLIQAEAAAGAKVVNTRNAAVDRSGYGLVSLTPYSLNEVELSPQDLPLDVQLESTVEQVIPRAGAVVALRFPTRHDVAAMLVAEPGSEGALVFGTEVRDGAGKVVGVAGQGASALVRGVSASGTLEVTRADGSICRATYDLKSAGQAVHGLPRIALACAPQGGGERGARAAGQAVAQPSAISISGKDHEPDIR
Outer membrane usher protein FimC
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
873
93,369
Cell outer membrane;Disulfide bond;Fimbrium biogenesis;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane beta strand;Transport
GO:0009279; GO:0009297; GO:0015473
Inferred from homology
2
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
SIGNAL 1..15; /evidence="ECO:0000255"
null
PF13953;PF13954;PF00577;
IPR000015;IPR018030;IPR042186;IPR025949;IPR043142;IPR025885;IPR037224;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
fimC fhaA BP1882
false
Bordetella pertussis
11
row_400571
false
null
280,869
Q7VVW3
MKAKVIDGSRASARIREQLKERVACLRARNIRPGLAVLLVGEDPASQVYVRNKVAACEQVGIHSVTERYPSAWTENQLLDRIASLHGDPAINGILVQLPLPPHMSAHRVIEAISPLKDVDGFHISNAGLLMTGKPQFQPCTPYGVMKLLESEGVSLRGAEAVIVGASNIVGKPMAMLLLAAGATVTICNSKTRDLAGQARRADVLIVAAGRAGIVDGSMIKPGAVVIDVGINRSPDGRLCGDVDYGSAAKVAGAITPVPGGVGPMTIAMLLANTVEAAERSAI
Bifunctional protein FolD 2 [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)]
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
283
29,529
Amino-acid biosynthesis;Histidine biosynthesis;Hydrolase;Methionine biosynthesis;Multifunctional enzyme;NADP;One-carbon metabolism;Oxidoreductase;Purine biosynthesis;Reference proteome
GO:0000105; GO:0004477; GO:0004488; GO:0005829; GO:0006164; GO:0009086; GO:0035999
Inferred from homology
3
null
null
null
PF00763;PF02882;
IPR046346;IPR036291;IPR000672;IPR020630;IPR020867;IPR020631;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
folD2 BP2522
false
Bordetella pertussis
238
row_265167
false
null
280,875
Q7VW29
MEKAMKYAKIAGSGGYLPERVVTNDDLAAELATRQISTSDEWIVERTGIRQRHLAERGVTTSQLATEAARRAMDDAGVQADEIDMIIVATSTPDYVFPSTACLVQANLGAKGGAAFDVQAVCSGFVYAMTTADNFIRAGRARCALVIGAEVFSRILDWNDRGTCVLFGDGAGAVVLKAADEPGILAAHLHADGSQTKILCAAGNVAYGDVTGDPFLRMDGQAVFKQAVTVLDRSARDVCAEAGVEVDDIDWLIPHQANVRILNFLARKLRVPTERVVITMDQHANTSAASVPLALDVARRDGRVKPGQLVLMQGVGGGFTWGSVLARM
Beta-ketoacyl-[acyl-carrier-protein] synthase III (Beta-ketoacyl-ACP synthase III) (KAS III) (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase 3) (3-oxoacyl-[acyl-carrier-protein] synthase III)
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
328
34,920
Acyltransferase;Cytoplasm;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Multifunctional enzyme;Reference proteome;Transferase
GO:0004315; GO:0005737; GO:0006633; GO:0033818; GO:0044550
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
null
null
PF08545;PF08541;
IPR013747;IPR013751;IPR004655;IPR016039;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
fabH BP2443
false
Bordetella pertussis
190
row_265173
false
null
557,192
Q7VUZ9
MPSFDVVSEVDKHELTNAVDQANRELSTRFDFKGTNASFELEGYVVTQVAPSAFQLKQMLDILRGRLSARSIDVRCMDVADPLENLGGARQKVTIKQGIEQAIAKKLIAAIKASKVKVESQINGEKLRITGKKRDDLQAVIALLRKTDVDLPLQFENFRD
Nucleotide-binding protein BP2916
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
160
17,844
Nucleotide-binding;Reference proteome
GO:0000166; GO:0005829
Inferred from homology
1
null
null
null
PF04461;
IPR007551;IPR035571;IPR035570;IPR036183;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
BP2916
false
Bordetella pertussis
400
row_537192
false
null
499,414
Q7VWM0
MGNWLLPEGLADVLPAEARRIEELRRELLDLYRTYGFELVAPPLVEYIDSLLSSTGSDLNLRTCKLVDQLSGRTLGVRADMTSQVTRIDAHLLNRAGVTRLCYCGSVLHARPADLLSSRELLQIGAEIYGHAGFEADLEIIQLVMDTLATAGVRNARLDLCHSGVMRAIFDADPQASRHAGDLCTLLREKDVPGLAELASRVDGLGEDTVRALQALATLYGGPEIIARARRELPAVPGMAQALDALQALVDAMPGVTLSVDLADVGGYGYHSGVTFAVYGEDWHDALVRGGRYDDVSCAFGRARPATGFSLDLRKLAAGLTPAEPARAVRAPWGQDPALTDAVRRLRRSGEIVVQVLPGHEQGLDEFVCDRELALQDGAWTVRTL
ATP phosphoribosyltransferase regulatory subunit
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
385
41,627
Amino-acid biosynthesis;Cytoplasm;Histidine biosynthesis;Reference proteome
GO:0000105; GO:0004821; GO:0005737; GO:0006427
Inferred from homology
2
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00125}.
null
null
PF13393;
IPR045864;IPR041715;IPR004516;IPR004517;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
hisZ BP2189
false
Bordetella pertussis
132
row_480151
false
null
526,308
Q9XJJ7
MRELKMKLCVLMLPLVVSACGSTPPAPVPCVKPPAPPAWIMQPAPDWQTPLNGIISSSERG
Spanin, outer membrane subunit (o-spanin) (Outer membrane lipoprotein Rz1)
Escherichia phage 933W (Bacteriophage 933W)
10,730
61
6,509
Cytolysis;Disulfide bond;Host cell lysis by virus;Host cell outer membrane;Host membrane;Lipoprotein;Membrane;Palmitate;Reference proteome;Signal;Viral release from host cell
GO:0016020; GO:0020002; GO:0044659
Inferred from homology
2
SUBCELLULAR LOCATION: Host cell outer membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Periplasmic side {ECO:0000250}.
SIGNAL 1..19; /evidence="ECO:0000250"
null
PF06085;
IPR010346;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
Rz1 L109
false
Traversvirus tv933W
6
row_506669
false
null
545,063
P69176
MTFTVKTIPDMLVEAYENQTEVARILNCSRNTVRKYTGDKEGKRHAIVNGVLMVHRGWGKDTDA
Protein ninH
Escherichia phage 933W (Bacteriophage 933W)
10,730
64
7,266
Reference proteome
null
Inferred from homology
1
null
null
null
PF06322;
IPR010454;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
ninH L0098
false
Traversvirus tv933W
4
row_525305
false
null
191,578
P0C0C0
MFKSGFVAILGRPNVGKSTFLNHVMGQKIAIMSDKAQTTRNKIMGIYTTETEQIVFIDTPGIHKPKTALGDFMVESAYSTLREVETVLFMVPADEKRGKGDDMIIERLKAAKIPVILVINKIDKVHPDQLLEQIDDFRSQMDFKEVVPISALEGNNVPNLIKLLTDNLEEGFQYFPEDHPERFLVSEMVREKVLHLTQQEVPH
GTPase Era
Streptococcus pyogenes serotype M49
301,452
203
23,065
Cell membrane;Cytoplasm;GTP-binding;Membrane;Nucleotide-binding;Ribosome biogenesis
GO:0000028; GO:0005525; GO:0005829; GO:0005886; GO:0019843; GO:0043024
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
null
null
PF01926;
IPR030388;IPR006073;IPR005662;IPR015946;IPR027417;IPR005225;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species)
era
false
Streptococcus pyogenes
306
row_178412
false
null
325,440
A2RGZ8
MSRYTGPSWKQSRRLGLSLTGTGKELARRNYVPGQHGPNNRSKLSEYGLQLAEKQKLRFSYGLGEKQFRNLFVQATKIKEGTLGFNFMVLLERRLDNVVYRLGLATTRRQARQFVNHGHILVDGKRVDIPSYRVDPGQVISVREKSMKVPAILEAVEATLGRPAFVSFDAEKLEGSLTRLPERDEINPEINEALVVEFYNKML
Small ribosomal subunit protein uS4 (30S ribosomal protein S4)
Streptococcus pyogenes serotype M5 (strain Manfredo)
160,491
203
23,123
Ribonucleoprotein;Ribosomal protein;RNA-binding;rRNA-binding
GO:0003735; GO:0006412; GO:0015935; GO:0019843; GO:0042274
Inferred from homology
2
null
null
null
PF00163;PF01479;
IPR022801;IPR005709;IPR018079;IPR001912;IPR002942;IPR036986;
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 M5 (serotype)
rpsD SpyM51805
false
Streptococcus pyogenes
307
row_308770
false
null
116,101
A2RCT3
MISSFHRPTVARVNLQAIKENVASVQKHIPLGVKTYAVVKADAYGHGAVQVSKALLPQVDGYCVSNLDEALQLRQAGIDKEILILGVLLPNELELAVANAITVTIASLDWIALARLEKKECQGLKVHVKVDSGMGRIGLRSSKEVNLLIDSLKELGADVEGIFTHFATADEADDTKFNQQLQFFKKLIAGLEDKPRLVHASNSATSIWHSDTIFNAVRLGIVSYGLNPSGSDLSLPFPLQEALSLESSLVHVKMISAGDTVGYGATYTAKKSEYVGTVPIGYADGWTRNMQGFSVLVDGQFCEIIGRVSMDQLTIRLSKAYPLGTKVTLIGSNQQKNISTTDIANYRNTINYEVLCLLSDRIPRIY
Alanine racemase (EC 5.1.1.1)
Streptococcus pyogenes serotype M5 (strain Manfredo)
160,491
366
39,891
Isomerase;Pyridoxal phosphate
GO:0005829; GO:0008784; GO:0009252; GO:0030170; GO:0030632
Inferred from homology
3
null
null
null
PF00842;PF01168;
IPR000821;IPR009006;IPR011079;IPR001608;IPR020622;IPR029066;
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 M5 (serotype)
alr SpyM50314
false
Streptococcus pyogenes
137
row_104493
false
null
49,156
Q9A1S2
MKLRHLLLTGAALTSFAATTVHGETVVNGAKLTVTKNLDLVNSNALIPNTDFTFKIEPDTTVNEDGNKFKGVALNTPMTKVTYTNSDKGGSNTKTAEFDFSEVTFEKPGVYYYKVTEEKIDKVPGVSYDTTSYTVQVHVLWNEEQQKPVATYIVGYKEGSKVPIQFKNSLDSTTLTVKKKVSGTGGDRSKDFNFGLTLKANQYYKASEKVMIEKTTKGGQAPVQTEASIDQLYHFTLKDGESIKVTNLPVGVDYVVTEDDYKSEKYTTNVEVSPQDGAVKNIAGNSTEQETSTDKDMTITFTNKKDFEVPTGVAMTVAPYIALGIVAVGGALYFVKKKNA
Pilin (Lancefield T antigen) (Pilus backbone structural protein)
Streptococcus pyogenes serotype M1
301,447
340
37,188
3D-structure;Cell wall;Fimbrium;Isopeptide bond;Peptidoglycan-anchor;Reference proteome;Secreted;Signal
GO:0005576; GO:0009289
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. Fimbrium. Note=Attached to the cell wall by a peptidoglycan anchor.
SIGNAL 1..23; /evidence="ECO:0000255"
null
PF24547;PF12892;
IPR055382;IPR017503;IPR022464;IPR038174;
3B2M;3GLD;3GLE;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species)
SPy_0128 M5005_Spy0109
false
Streptococcus pyogenes
155
row_42476
false
null
528,722
A2RF77
MSQEIYDYANQLERAVRALPEYQKVLEVKEAIQADASASQLFDEFVAMQEKIQGMMQSGQMPTAEEQTSIQELSQKIEANDQLKAYFEAQQALSVYMSDIERIVFAPLKDLVK
UPF0342 protein SpyM51181
Streptococcus pyogenes serotype M5 (strain Manfredo)
160,491
113
12,899
null
null
Inferred from homology
1
null
null
null
PF06133;
IPR010368;IPR023378;
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 M5 (serotype)
SpyM51181
false
Streptococcus pyogenes
413
row_509058
false
null
325,417
A2RGC9
MTVTGIIAEFNPFHNGHKYLLETVEGLKIIAMSGNFMQRGEPALIDKWIRSEMALKNGADIVVELPFFVSVQSADYFAQGAIDILCQLGIQQLAFGTEDVIDYQKLIKVYEKKSEQMTAYLSTLEDTLSYPQKTQKMWEIFAGVKFSGQTPNHILGLSYAKASAGKHIQLCPIKRQGAAYHSKDKNHLLASASAIRQHLNDWDFISHSVPNAGLLINNPHMSWDHYFSFLKYQILNHSDLTSIFQVNDELASRIKKAIKVSQNIDHLVDTVATKRYTKARVRRILIYILVNAKEPTLPKGIHILGFTSKGQAHLKKLKKSRPLITRIGAETWDEMTQKADSIYQLGHQDIPEQSFGRIPIIIKNERLN
tRNA(Met) cytidine acetate ligase (EC 6.3.4.-)
Streptococcus pyogenes serotype M5 (strain Manfredo)
160,491
368
41,687
ATP-binding;Cytoplasm;Ligase;Nucleotide-binding;RNA-binding;tRNA processing;tRNA-binding
GO:0000049; GO:0005524; GO:0005737; GO:0006400; GO:0016879
Inferred from homology
2
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01539}.
null
null
PF05636;
IPR014729;IPR008513;
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 M5 (serotype)
tmcAL SpyM51587
false
Streptococcus pyogenes
135
row_308748
false
null
528,719
A2RE19
MKTIAFDSNKYLNLQRDHILERISQFDGKLYMEFGGKMLEDYHAARVLPGYEPDNKIKLLKELKEQVEIVIAINANNIEHSKARGDLGISYDQEVFRLIDKFNTLDIYVGSVVITQYNNQPAADAFRKQLEKNGIASYLHYPIKGYPTDINHIISSEGMGKNDYIKTSRNLIVVTAPGPGSGKLATCMSQMYHDQINGVKSGYAKFETFPVWNLPLHHPVNLAYEAATADLDDVNMIDPFHLETYGKTAVNYNRDIEVFPVLNRTFERILSKSPYASPTDMGVNMVGFSIVNEEAAIEASKQEIIRRYYQTLVDFKAERVTESAVKKIELLMNDIGVTPDDRHVTVAAHQKAEQTGQPALALQLPNGQIVTGKTSELFGPTAAVIINAIKTLAKIDKTTHLIEPEYVKPIQGLKVNHLGSHNPRLHSNEILIALAITAMTSEEANLAMKELGNLKGSEAHSTVILTEEDKNVLRKLGVNITFDPVYQHHKLYRK
UPF0371 protein SpyM50764
Streptococcus pyogenes serotype M5 (strain Manfredo)
160,491
494
55,360
null
null
Inferred from homology
1
null
null
null
PF08903;PF20921;
IPR014999;IPR048441;IPR048496;
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 M5 (serotype)
SpyM50764
false
Streptococcus pyogenes
61
row_509055
false
null
296,829
Q8XJ76
MKVPFNWLKDYVDIDMTAEELGDALTLSGSKVEEVVTAGAEIENIVTCQIDKIEQHPDAEKLKICQVNIGSEMIQIVTAADNMKEHDKVPVALHGAILADGSKIKKGKLRGEVSNGMFCSEEELGIADGKEVIGLMILPEDAPIGVCIKEYLGLNKQVLDFEITSNRPDCLSVLGMARETAATTRKTYRMPNTKFEVKCDKNINDEIKVTVNDKLCNRYMARGVKNVKVAPSPTWMQERLLDAGVRPINNIVDITNFVMLELGQPMHAFDRRELKSSNIVVERAKDGDKFVTLDEIERELNSDVLCIKDGEEIVALAGIMGGLNSGVKDDTTEIVFESANFDGTNIRVNSKNLGLRTESSSRFEKDIDPNLAALALDRACALVEELGCGEIMEGTIDVYNNVKEEKTLEVSVSWINKFLGTSLEAEEMKKCLDSLDLKTTINGDTLEILVPTFRIDVDIREDVAEEVARIYGYNNIPATLISTSTEKEAKDKKQLLDEKVIDTMLASGLNQSISYSFVSPKVFDKICVPEDSSLRNVVKIKNPLGEDYSVMRTSTLPSMMESLARNYSRSNEIVRLFEIGKTYIPNSDENELPTERNILTIGIYGQCDYFDLKGIVENLLDSLGLKSASFKRMSENPSYHPGKTAELILGRTSLGVLGEIHPDVNENYGVDVPCYVAELDLDAMYNFSKTEKYYKPLPKYPAITRDIALLVDDAVLVQEIEDAIRKAGGQVVEKVELFDVYKGAQIPEGKKSIAYAIAYRDPSKTLKDKDINKVHDKILRALEYKLGAQLREQ
Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS)
Clostridium perfringens (strain 13 / Type A)
195,102
793
88,258
Aminoacyl-tRNA synthetase;ATP-binding;Cytoplasm;Ligase;Magnesium;Metal-binding;Nucleotide-binding;Protein biosynthesis;Reference proteome;RNA-binding;tRNA-binding
GO:0000049; GO:0000287; GO:0004826; GO:0005524; GO:0006432; GO:0009328; GO:0016740; GO:0140096
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
null
null
PF03483;PF03484;PF03147;PF01588;PF17759;
IPR045864;IPR005146;IPR009061;IPR005121;IPR036690;IPR012340;IPR045060;IPR004532;IPR020825;IPR041616;IPR002547;IPR033714;IPR005147;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Clostridia (class), Eubacteriales (order), Clostridiaceae (family), Clostridium (genus), Clostridium perfringens (species)
pheT CPE1885
false
Clostridium perfringens
11
row_280739
false
null
441,125
Q0TRT2
MKIIRKSILAVLVFTILCGIIYPVSTTVLAQVLFKEEANGSIIEVDGKKYGSELLGQQFTDNKYLWGRIMNINVEMFKDSNGKPLMYSSPSNLSPASEEYEKLVKERVERIRSYNKGKEEEPIPVDLVTSSGSGLDPHISVAAAKYQVDRIAKERNLSVDYVNEIIDKYTTGRFLGIFGEKTVNVLKVNLALDGILRE
Potassium-transporting ATPase KdpC subunit (ATP phosphohydrolase [potassium-transporting] C chain) (Potassium-binding and translocating subunit C) (Potassium-translocating ATPase C chain)
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
195,103
198
22,196
ATP-binding;Cell membrane;Ion transport;Membrane;Nucleotide-binding;Potassium;Potassium transport;Transmembrane;Transmembrane helix;Transport
GO:0005524; GO:0005886; GO:0008556
Inferred from homology
2
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00276}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276}.
null
TRANSMEM 8..28; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
PF02669;
IPR003820;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Clostridia (class), Eubacteriales (order), Clostridiaceae (family), Clostridium (genus), Clostridium perfringens (species)
kdpC CPF_1212
false
Clostridium perfringens
324
row_422761
false
null
306,183
Q9I0D9
MNLKPQTLMVAIQCVAARTRELDAQLQNDDPQNAAELEQLLVGYDLAADDLKNAYEQALGQYSGLPPYDRLIEEPAS
Immune protein Tsi2 (Anti-toxin protein Tsi2)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
208,964
77
8,520
3D-structure;Disulfide bond;Reference proteome
null
Evidence at protein level
3
null
null
null
PF21643;
IPR049070;IPR053756;IPR033783;
3RQ9;3STQ;3VPV;4C18;5AKO;
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)
tsi2 PA2703
false
Pseudomonas aeruginosa
1,453
row_289891
false
null
101,609
Q9I2F1
MRTLILSLLLLVDLTTQAATLGFPALPGGGLVYKQVQSIRERRFADLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLAHADPEIVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVFAVIGQGYDRGNPLLTPPEPLTARNRLDRFKPVRDAELMEFGFIQSDFF
Probable functional amyloid protease FapD (EC 3.4.22.-) (Probable fibril-associated protease FapD)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
208,964
226
25,272
ATP-binding;Hydrolase;Nucleotide-binding;Periplasm;Protease;Reference proteome;Signal;Thiol protease
GO:0005524; GO:0006508; GO:0008234; GO:0016020; GO:0042597; GO:1990000
Inferred from homology
4
SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:23504942}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF03412;
IPR005074;
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)
fapD PA1953
false
Pseudomonas aeruginosa
1,002
row_90597
false
null
201,587
P43334
MKTTQYVARQPDDNGFIHYPETEHQVWNTLITRQLKVIEGRACQEYLDGIEQLGLPHERIPQLDEINRVLQATTGWRVARVPALIPFQTFFELLASQQFPVATFIRTPEELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLKASKEERVFLARLYWMTIEFGLVETDQGKRIYGGGILSSPKETVYSLSDEPLHQAFNPLEAMRTPYRIDILQPLYFVLPDLKRLFQLAQEDIMALVHEAMRLGLHAPLFPPKQAA
Phenylalanine-4-hydroxylase (PAH) (EC 1.14.16.1) (Phe-4-monooxygenase)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
208,964
262
30,322
Iron;Metal-binding;Monooxygenase;Oxidoreductase;Phenylalanine catabolism;Reference proteome
GO:0004505; GO:0005506; GO:0006559
Inferred from homology
3
null
null
null
PF00351;
IPR001273;IPR018301;IPR036951;IPR036329;IPR019774;IPR005960;
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)
phhA PA0872
false
Pseudomonas aeruginosa
887
row_188107
false
null
101,581
Q9HZ17
MSRVLVIESSARQRGSVSRLLTAEFISHWKIAHPADRFQVRDLAREPLPHLDELLLGAWTTPCDGHSAAERRALERSNRLTEELRMADVLVLAAPMYNFAIPSSLKSWFDHVLRAGLTFRYAEQGPEGLLQGKRAFVLTARGGIYAGGGLDHQEPYLRQVLGFVGIHDVTFIHAEGMNMGPEFREKGLARARERMRQALETDTSLCVPLPTLR
FMN-dependent NADH:quinone oxidoreductase 3 (EC 1.6.5.-) (Azo-dye reductase 3) (FMN-dependent NADH-azo compound oxidoreductase 3) (FMN-dependent NADH-azoreductase 3) (EC 1.7.1.17)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
208,964
213
23,898
Flavoprotein;FMN;NAD;Oxidoreductase;Reference proteome
GO:0009055; GO:0010181; GO:0016652; GO:0016655
Evidence at protein level
4
null
null
null
PF02525;
IPR003680;IPR029039;IPR050104;IPR023048;
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)
azoR3 PA3223
false
Pseudomonas aeruginosa
1,042
row_90571
false
null
386,797
B8DFZ7
MALTQERKNEIIAEYRVHDTDTGSPEVQIAVLTAEINSLNEHVRVHKKDHHSYRGLMKMVGHRRNLLTYLRKKDVQRYRELIKRLGLRR
Small ribosomal subunit protein uS15 (30S ribosomal protein S15)
Listeria monocytogenes serotype 4a (strain HCC23)
552,536
89
10,631
Ribonucleoprotein;Ribosomal protein;RNA-binding;rRNA-binding
GO:0003735; GO:0006412; GO:0019843; GO:0022627
Inferred from homology
2
null
null
null
PF00312;
IPR000589;IPR005290;IPR009068;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Listeriaceae (family), Listeria (genus), Listeria monocytogenes (species)
rpsO LMHCC_1240
false
Listeria monocytogenes
604
row_369478
false
null
545,391
P75314
MSKINDKLTEINTVEYEVASKHSQYLFYSRFGLLDTAAYFLFLLSFFVTAVMFLVGIFHTEQFTLNDQNQGISGFYLFWNVKKPADIFNANFVYSISSFGIAILALGLFSLFLMIFLGYRWAISLFIKSQITKWERVIFSTGFYFSVVAYCFWIALMLLFLVLSDQHFFPRTTTQLKSNPNLSLFFRISHKDNVFSSRLNQLGAFATALCITLVVYELPFLGLFAFNWNKQRAKAIFCRKRKQ
Uncharacterized protein MG323.1 homolog
Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
272,634
243
28,278
Cell membrane;Membrane;Reference proteome;Transmembrane;Transmembrane helix
GO:0005886
Predicted
1
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
TRANSMEM 38..58; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 99..119; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 143..163; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 204..224; /note="Helical"; /evidence="ECO:0000255"
null
null
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Mycoplasmatota (phylum), Mycoplasmoidales (order), Mycoplasmoidaceae (family), Mycoplasmoides (genus), Mycoplasmoides pneumoniae (species)
MPN_469 MP372 P01_orf243
false
Mycoplasmoides pneumoniae
391
row_525629
false
null
360,292
B1I837
MIYKVFYQETKERSPRRETTRALYLDIDTSSELEGRITARQLVEENRPEYNIEYIELLSDKLLDYEKETGAFEITEF
DNA-directed RNA polymerase subunit epsilon (RNAP epsilon subunit) (EC 2.7.7.6) (RNA polymerase epsilon subunit) (Transcriptase subunit epsilon)
Streptococcus pneumoniae (strain Hungary19A-6)
487,214
77
9,288
DNA-directed RNA polymerase;Nucleotidyltransferase;Transcription;Transferase
GO:0000428; GO:0003677; GO:0003899; GO:0006351
Inferred from homology
2
null
null
null
PF07288;
IPR009907;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)
rpoY SPH_0238
false
Streptococcus pneumoniae
551
row_343245
false
null
254,499
Q5A644
MMLRFRSFSTTTHLLRGQNLTEKIVQKYAVGLQPSSKKVYSGDYVTIKPAHCMSHDNSWPVATKFMNLGASKVKDNRQIVCTLDHDVQNKSEQNLTKYTNIEKFAKSQGIDFYPAGRGIGHQIMIEEGYAFPLNLTVASDSHSNTYGGIGALGTPIVRTDAASIWATGQTWWQIPPVAKVELIGQLPKGVTGKDIIVALCGIFNNDEVLNHAIEFVGDDAISKLPIDYRLTIANMTTEWGALSGLFPVDETLVEFYQNRLKKLNKPDHPRINNQTIDQLINNKLTSDNDAVYAKHLQIDLSSLSPYISGPNSVKISNSLYDLSQQNIAINKAYLVSCTNSRLSDIQAAADIIKGHKVNPNVEFYVAAASSLVQKDAEQSGAWQTILDAGAKPLPAGCGPCIGLGTGLLKDGEVGISATNRNFKGRMGSKDALAYLASPEVVAASAVLGKIGGPEELNGEPVKQAPRIIKSIETESNSANEAESTSEEASGSIDILPGFPQSIEGELILCNADNINTDGIYPGKYTYQDDITKEQMAKVCMENYDSQFYSKTKPGDIIISGYNFGTGSSREQAATCILARGMKLIVAGSFGNIFSRNSINNALLTLEIPDLINKLRQQYEGNDELTIRTGWFLKWDVTKAQVTVVDGDDNLILTQKVGELGTNLQDIIVKGGLEGWVKSELKTNQ
Homoaconitase, mitochondrial (EC 4.2.1.36) (Homoaconitate hydratase)
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
237,561
684
74,456
Amino-acid biosynthesis;Iron;Iron-sulfur;Lyase;Lysine biosynthesis;Metal-binding;Mitochondrion;Reference proteome;Transit peptide
GO:0004409; GO:0005759; GO:0009085; GO:0019878; GO:0046872; GO:0051539
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
null
null
PF00330;PF00694;
IPR015931;IPR001030;IPR015928;IPR018136;IPR036008;IPR000573;IPR004418;IPR039386;IPR050067;
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)
LYS4 CAALFM_C404410CA CaO19.11327 CaO19.3846
false
Candida albicans
162
row_239563
false
null
227,078
Q1I7I9
MSAPLIELCDIRKAYGGIDSPKVEVLRGISLSIHPGEFVAIVGASGSGKSTLMNILGCLDRPTSGSYRFAGRDVAELDSDELAWLRREAFGFVFQGYHLIPSGSAQENVEMPAIYAGTPPAERHARALALLDRLGLASRTGNRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVIILITHDREVAARAQRIIEIRDGQMVSDSAASQPSPAQPEQLQANDLRQRLDRGAILKGAWKGEMIEALQAAWRVMWINRFRTALTLLGIIIGVASVVVMLAVGEGSKRQVMAQMAAFGSNILYLNGKRATAQEPGGIVTLDDVAAIGELPQVLHVMPVIGGQLMVRQGNSSQKFYVGGNNTWFPAIFNWPVVEGTFFSEADEASGAAVAVIGQKVRSKMFGEGSNPLGQYLLIGNVPFQVVGILAAKGASSGSEDSDERIVVPYSAASIRLFGSHDPEYVAIAAIDSRRVNETEAAIDRLLRQRHQGKHDFDLTNDAALIQAEARTQNSLSLMLGAIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQRDILRQFLTEAVMLSMVGGVTGIVIALLVGGGLLLADIAVAFALPAILGAFACAVITGVVFGFMPARKAARLDPVKALTSE
Pyoverdine export ATP-binding/permease protein PvdT (EC 7.6.2.-)
Pseudomonas entomophila (strain L48)
384,676
654
69,628
ATP-binding;Cell inner membrane;Cell membrane;Membrane;Nucleotide-binding;Translocase;Transmembrane;Transmembrane helix;Transport
GO:0005524; GO:0005886; GO:0016887; GO:0022857
Inferred from homology
3
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q88F88}; Multi-pass membrane protein {ECO:0000255}.
null
TRANSMEM 282..302; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 529..549; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 596..616; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 617..637; /note="Helical"; /evidence="ECO:0000255"
PF00005;PF02687;PF12704;
IPR003593;IPR003838;IPR003439;IPR017871;IPR017911;IPR025857;IPR050250;IPR027417;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas entomophila (species)
pvdT PSEEN3665
false
Pseudomonas entomophila
21
row_212921
false
null
227,192
Q1IGY7
MSDALIRLEQVGVSFAGEAVLDSIDLAVAPGQIVTLIGPNGAGKTTLVRAVLGLLKPHRGKVWRKPKLRIGYMPQKIQVDATLPLSVLRFLRLVPGVDRAAALSALQEVGAEQVIDSPIQTISGGEMQRVLLARALLREPELLVLDEPVQGVDVVGQTELYNLITRLRDRHGCGVLMVSHDLHLVMSATDQVVCLNRHVCCSGHPEQVSNDPAFVELFGQNAKSLAVYHHHHDHSHDLHGSVIAPGAHVHGEHCKHG
Zinc import ATP-binding protein ZnuC (EC 7.2.2.20)
Pseudomonas entomophila (strain L48)
384,676
257
27,811
ATP-binding;Cell inner membrane;Cell membrane;Ion transport;Membrane;Nucleotide-binding;Translocase;Transport;Zinc;Zinc transport
GO:0005524; GO:0005886; GO:0010043; GO:0015633; GO:0016887
Inferred from homology
3
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01725}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01725}.
null
null
PF00005;
IPR003593;IPR003439;IPR017871;IPR050153;IPR027417;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas entomophila (species)
znuC PSEEN0071
false
Pseudomonas entomophila
268
row_213034
false
null
118,492
A3NQ63
MEQFHGTTILSVRRGDKVALGGDGQVTLGNIVMKGGARKVRRIYNNQVLVGFAGGTADAFSLLDRFEAKLEKHQGNLTRAAVELAKDWRTDRLLRRLEAMLIAADATTTLVITGNGDVLDPEGGICAIGSGGSYAQAAARALAENTDLSPREIVEKALGIAGDMCIYTNHNRIIETIE
ATP-dependent protease subunit HslV (EC 3.4.25.2)
Burkholderia pseudomallei (strain 1106a)
357,348
178
19,053
Allosteric enzyme;Cytoplasm;Hydrolase;Metal-binding;Protease;Sodium;Threonine protease
GO:0004298; GO:0005839; GO:0009376; GO:0046872; GO:0051603
Inferred from homology
3
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}.
null
null
PF00227;
IPR022281;IPR029055;IPR001353;IPR023333;
null
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)
hslV BURPS1106A_0201
false
Burkholderia pseudomallei
386
row_106821
false
null
98,691
Q90X97
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLPLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
Actin, alpha skeletal muscle (EC 3.6.4.-) (Alpha-actin-1) [Cleaved into: Actin, alpha skeletal muscle, intermediate form]
Atractaspis microlepidota microlepidota
172,021
377
42,061
Acetylation;ATP-binding;Cytoplasm;Cytoskeleton;Hydrolase;Methylation;Muscle protein;Nucleotide-binding;Oxidation
GO:0005524; GO:0005737; GO:0005856; GO:0016787
Evidence at transcript level
4
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
null
null
PF00022;
IPR004000;IPR020902;IPR004001;IPR043129;
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), Lamprophiidae (family), Atractaspidinae (subfamily), Atractaspis (genus), Atractaspis microlepidota (species)
ACTA1
false
Atractaspis microlepidota
0
row_87850
false
null
497,409
Q7NWI9
MNMNHHDKLQRFLFDGAPVRGALVRLDGAWQQVLARRAYPQALKTVLGEMMAASVLMAANLKFDGSLILQIHGTGALKLAVVECNNDRTVRATAKWDGDLDGKPLKALLGEGGKFVLTLEPRLDKNQTWQGIVALEGDSVGQMLENYMLRSEQLDTALVLASGDEAAAGMLLQRLPEGHGEAEGWDRVQMLGRTLKAEELLGLGAEDILHRLFHEEQVRVFEQETVSFNCNCSRERVSNMLTMLGGQEVGDVLLEQGSVEIVCDYCNQRYVFDEEDANQLFDYDVVAAAREARH
33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)
243,365
294
32,615
Chaperone;Cytoplasm;Disulfide bond;Redox-active center;Reference proteome;Zinc
GO:0005737; GO:0042026; GO:0044183; GO:0051082
Inferred from homology
2
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}.
null
null
PF01430;
IPR000397;IPR016154;IPR016153;IPR023212;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Neisseriales (order), Chromobacteriaceae (family), Chromobacterium (genus), Chromobacterium violaceum (species)
hslO CV_2000
false
Chromobacterium violaceum
241
row_478179
false
null
529,018
A3RGB0
MKYSLIFILTLACLIASSLARPEGEEKPADDAAGDKKEEGAEGDKTAAGGDEGFTGGDGKNAGGAGNPMKVVQDIIKKITDAVNPLRMTEGFLGGGGSGGSGALFG
Glycine/glutamate-rich protein sgp1
Glossina morsitans morsitans (Savannah tsetse fly)
37,546
106
10,547
Secreted;Signal
GO:0005576
Inferred from homology
1
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
null
null
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)
sgp1
false
Glossina morsitans
15
row_509354
false
null
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