interpro_id string | interpro_numeric_id int64 | name string | short_name string | entry_type string | protein_count int64 | is_llm bool | is_llm_reviewed bool | abstract string | go_ids list | go_terms list | go_categories list | go_count int64 | member_databases list | member_accessions list | member_names list | member_protein_counts list | member_count int64 | external_databases list | external_accessions list | external_xrefs list | external_xref_count int64 | pdb_ids list | structure_count int64 | publication_ids list | pubmed_ids list | publication_titles list | publication_years list | publication_count int64 | parent_ids list | child_ids list | parent_count int64 | child_count int64 | tree_depth float64 | taxonomy_names list | taxonomy_protein_counts list | taxonomy_count int64 | key_species_names list | key_species_protein_counts list | key_species_count int64 | in_entry_list bool | entry_list_type string | entry_list_name string | names_dat_name string | short_names_dat_name string | split_bucket int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR008916 | 8,916 | Retrovirus capsid, C-terminal | Retrov_capsid_C | Homologous_superfamily | 75,177 | false | false | The Gag polyprotein from retroviruses is processed by viral protease to produce the major structural proteins, including the capsid protein. The newly formed capsid protein rearranges to form the capsid core particle that surrounds the viral genome of the mature virus. The capsid is composed of two domains, the N-termi... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.1200.30"
] | [
""
] | [
75177
] | 1 | [
"REACTOME",
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] | [
"R-HSA-1169408",
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"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-174490",
"R-HSA-174495",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910"
] | [
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-174495",
"REACTOME:R-HSA-17... | 16 | [
"1a43",
"1a8o",
"1aum",
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"2l6e",
"2lf4",
"2lmc",
"2m8l",
"2m8n",
"2m8p",
"2ont",
"2p0c"... | 500 | [
"PUB00011708",
"PUB00011709",
"PUB00011710"
] | [
"9346481",
"9931251",
"10669613"
] | [
"Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.",
"Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26.",
"Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses."
] | [
1997,
1999,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Retroviridae",
"Thalassovita mangrovi",
"marine sediment metagenome"
] | [
2516,
72659,
1,
1
] | 4 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
15,
9,
6
] | 3 | true | Homologous_superfamily | Retrovirus capsid, C-terminal | Retrovirus capsid, C-terminal | Retrov_capsid_C | 2 |
IPR008917 | 8,917 | Transcription factor, Skn-1-like, DNA-binding domain superfamily | TF_DNA-bd_sf | Homologous_superfamily | 17,671 | false | false | The DNA-binding domain of certain eukaryotic transcription factors displays a distinctive helix-turn-helix (HTH) motif. The MafG basic region-leucine zipper (bZIP) protein and the Caenorhabditis elegans Skn-1 transcription factor share this HTH motif. MafG is a member of the Maf family of proteins, which are a subgroup... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF47454"
] | [
""
] | [
17671
] | 1 | [
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-983231",
"R-CEL-8951664",
"R-CEL-9755511",
"R-CEL-9759194",
"R-CEL-9762114",
"R-DME-209394",
"R-DME-209409",
"R-DME-209425",
"R-DME-2559580",
"R-DME-2871796",
"R-DME-450341",
"R-DME-8951664",
"R-DME-9018519",
"R-DME-9755511",
"R-DME-9759194",
"R-DME-9762114",
"R-DME-983231",
... | [
"REACTOME:R-BTA-983231",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-9755511",
"REACTOME:R-CEL-9759194",
"REACTOME:R-CEL-9762114",
"REACTOME:R-DME-209394",
"REACTOME:R-DME-209409",
"REACTOME:R-DME-209425",
"REACTOME:R-DME-2559580",
"REACTOME:R-DME-2871796",
"REACTOME:R-DME-450341",
"REACTOME:R-D... | 76 | [
"1k1v",
"1s9k",
"1skn",
"2kz5",
"2lz1",
"2wt7",
"2wty",
"3a5t",
"4auw",
"4eot",
"5vpa",
"5vpb",
"5vpc",
"5vpd",
"5vpe",
"5vpf",
"7o7b",
"7ucc",
"7ucd",
"7x5e",
"7x5f",
"7x5g"
] | 22 | [
"PUB00007700",
"PUB00011711"
] | [
"11875518",
"9628487"
] | [
"Solution structure of the DNA-binding domain of MafG.",
"A new DNA-binding motif in the Skn-1 binding domain-DNA complex."
] | [
2002,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
950,
16714,
5,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
62,
14,
1,
55,
53,
54
] | 7 | true | Homologous_superfamily | Transcription factor, Skn-1-like, DNA-binding domain superfamily | Transcription factor, Skn-1-like, DNA-binding domain superfamily | TF_DNA-bd_sf | 2 |
IPR008918 | 8,918 | Helix-hairpin-helix motif, class 2 | HhH2 | Conserved_site | 55,912 | false | false | The helix-hairpin-helix (HhH) motif is an around 20 amino acids domain present in prokaryotic and eukaryotic non-sequence-specific DNA binding proteins. The HhH motif is similar to, but distinct from, the helix-turn-helix (HtH) and the helix-loop-helix (HLH) motifs. All three motifs have two helices (H1 and H2) connect... | [
"GO:0003677",
"GO:0003824"
] | [
"DNA binding",
"catalytic activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SMART"
] | [
"SM00279"
] | [
"HhH2"
] | [
55912
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-110362",
"R-BTA-174437",
"R-BTA-5651801",
"R-BTA-5685939",
"R-BTA-69166",
"R-CEL-5651801",
"R-CEL-5685939",
"R-CEL-69166",
"R-DDI-110362",
"R-DDI-5358565",
"R-DDI-5651801",
"R-DDI-69166",
"R-DME-5358565",
"R-DME-5651801",
"R-DME-5685939",
"R-DME-5693607",
"R-DME-6804756",
"R... | [
"REACTOME:R-BTA-110362",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5685939",
"REACTOME:R-BTA-69166",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5685939",
"REACTOME:R-CEL-69166",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-5358565",
"REACTOME:R-DDI-5651801",
"REACTOME:R-DDI... | 81 | [
"1a76",
"1a77",
"1b43",
"1bgx",
"1exn",
"1mc8",
"1rxv",
"1rxw",
"1taq",
"1tau",
"1tfr",
"1ul1",
"1ut5",
"1ut8",
"1xo1",
"2ihn",
"2izo",
"3h7i",
"3h8j",
"3h8s",
"3h8w",
"3ory",
"3q8k",
"3q8l",
"3q8m",
"3qe9",
"3qea",
"3qeb",
"3zd8",
"3zd9",
"3zda",
"3zdb"... | 98 | [
"PUB00011712",
"PUB00011713",
"PUB00011714",
"PUB00015243"
] | [
"9699635",
"8674116",
"9874768",
"15356290"
] | [
"The crystal structure of flap endonuclease-1 from Methanococcus jannaschii.",
"Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins.",
"Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease ... | [
1998,
1996,
1999,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
961,
36023,
17498,
606,
824
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
47,
4,
12,
8,
2,
14,
18,
3,
14,
8,
4,
4,
48
] | 13 | true | Conserved_site | Helix-hairpin-helix motif, class 2 | Helix-hairpin-helix motif, class 2 | HhH2 | 3 |
IPR008919 | 8,919 | Retrovirus capsid, N-terminal | Retrov_capsid_N | Homologous_superfamily | 88,534 | false | false | The Gag polyprotein from retroviruses is processed by viral protease to produce the major structural proteins, including the capsid protein. The newly formed capsid protein rearranges to form the capsid core particle that surrounds the viral genome of the mature virus. The capsid is composed of two domains, the N-termi... | [
"GO:0016032"
] | [
"viral process"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.375.10",
"SSF47943"
] | [
"",
""
] | [
87022,
87869
] | 2 | [
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1169408",
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-174490",
"R-HSA-174495",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910"
] | [
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"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-174495",
"REACTOME:R-HSA-17... | 16 | [
"1afv",
"1ak4",
"1d1d",
"1e6j",
"1eia",
"1em9",
"1fgl",
"1g03",
"1gwp",
"1l6n",
"1m9c",
"1m9d",
"1m9e",
"1m9f",
"1m9x",
"1m9y",
"1p7n",
"1qrj",
"1u7k",
"2eia",
"2gol",
"2gon",
"2jpr",
"2kgf",
"2lf4",
"2m8l",
"2m8n",
"2m8p",
"2pwm",
"2pwo",
"2pxr",
"2v4x"... | 328 | [
"PUB00011709",
"PUB00011710"
] | [
"9931251",
"10669613"
] | [
"Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26.",
"Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses."
] | [
1999,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota",
"Viruses",
"marine sediment metagenome"
] | [
5457,
7,
83069,
1
] | 4 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
19,
38,
8
] | 3 | true | Homologous_superfamily | Retrovirus capsid, N-terminal | Retrovirus capsid, N-terminal | Retrov_capsid_N | 4 |
IPR008920 | 8,920 | Transcription regulator FadR/GntR, C-terminal | TF_FadR/GntR_C | Homologous_superfamily | 190,885 | false | false | This superfamily represents the C-terminal ligand binding domain of many members of the Gluconate operon transcriptional repressor (GntR) family. This domain probably binds to a range of effector molecules that regulate the transcription of genes through the action of the N-terminal DNA-binding domain. It is a α helica... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.20.120.530",
"SSF48008"
] | [
"",
""
] | [
190263,
190326
] | 2 | [] | [] | [] | 0 | [
"1e2x",
"1h9g",
"1h9t",
"1hw1",
"1hw2",
"2di3",
"2hs5",
"3c7j",
"3fms",
"3ihu",
"3sxk",
"3sxm",
"3sxy",
"3sxz",
"4p96",
"4p9f",
"4p9u",
"4pdk",
"5dv5",
"5tpm",
"5xgf",
"6az6",
"6ep3",
"6on4",
"6wfq",
"6wg7",
"6z74",
"6za0",
"6za3",
"6za7",
"6zab",
"7c7e"... | 43 | [
"PUB00015228"
] | [
"11013219"
] | [
"Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
48,
189393,
127,
1,
1316
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
13
] | 2 | true | Homologous_superfamily | Transcription regulator FadR/GntR, C-terminal | Transcription regulator FadR/GntR, C-terminal | TF_FadR/GntR_C | 4 |
IPR008921 | 8,921 | DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal | DNA_pol3_clamp-load_cplx_C | Homologous_superfamily | 112,678 | false | false | The Escherichia coli DNA polymerase III gamma complex clamp loader assembles the ring-shaped beta sliding clamp onto DNA. The core polymerase is tethered to the template by beta, enabling progressive replication of the genome. The E. coli complex clamp loader contains five different subunits, clamp loading only require... | [
"GO:0003677",
"GO:0006260"
] | [
"DNA binding",
"DNA replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF48019"
] | [
""
] | [
112678
] | 1 | [
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-174411",
"R-BTA-176187",
"R-BTA-5651801",
"R-BTA-5655862",
"R-BTA-5656121",
"R-BTA-5656169",
"R-BTA-5685938",
"R-BTA-5685942",
"R-BTA-5693607",
"R-BTA-5696397",
"R-BTA-5696400",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6804756",
... | [
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-176187",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5655862",
"REACTOME:R-BTA-5656121",
"REACTOME:R-BTA-5656169",
"REACTOME:R-BTA-5685938",
"REACTOME:R-BTA-5685942",
"REACTOME:R-B... | 161 | [
"1a5t",
"1iqp",
"1jqj",
"1jr3",
"1sxj",
"1xxh",
"1xxi",
"2chq",
"2chv",
"2gno",
"2qw6",
"2r9g",
"3bge",
"3ctd",
"3glf",
"3glg",
"3glh",
"3gli",
"3pvs",
"3zh9",
"6vvo",
"7sgz",
"7sh2",
"7st9",
"7stb",
"7ste",
"7tfh",
"7tfi",
"7tfj",
"7tfk",
"7tfl",
"7thj"... | 99 | [
"PUB00010612"
] | [
"11719243"
] | [
"Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1529,
78913,
30177,
296,
1763
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
52,
4,
11,
6,
4,
21,
22,
6,
29,
22,
6,
6,
92
] | 13 | true | Homologous_superfamily | DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal | DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal | DNA_pol3_clamp-load_cplx_C | 1 |
IPR008922 | 8,922 | Di-copper centre-containing domain superfamily | Di-copper_centre_dom_sf | Homologous_superfamily | 39,178 | false | false | Copper active sites play a major role in biological dioxygen activation. Oxygen intermediates have been studied in detail for the proteins and enzymes involved in reversible O2 binding (hemocyanin), activation (tyrosinase), and four-electron reduction to water (multicopper oxidases). Tyrosinase binds two copper ions (C... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.1280.10",
"SSF48056"
] | [
"",
""
] | [
38229,
38952
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-5662702",
"R-HSA-5662702",
"R-HSA-9824585",
"R-MMU-5662702",
"R-SSC-5662702"
] | [
"REACTOME:R-CEL-5662702",
"REACTOME:R-HSA-5662702",
"REACTOME:R-HSA-9824585",
"REACTOME:R-MMU-5662702",
"REACTOME:R-SSC-5662702"
] | 5 | [
"1bt1",
"1bt2",
"1bt3",
"1bug",
"1hc1",
"1hcy",
"1js8",
"1ll1",
"1lla",
"1lnl",
"1nol",
"1oxy",
"1wx2",
"1wx4",
"1wx5",
"1wxc",
"2ahk",
"2ahl",
"2p3x",
"2y9w",
"2y9x",
"2zmx",
"2zmy",
"2zmz",
"2zwd",
"2zwe",
"2zwf",
"2zwg",
"3aws",
"3awt",
"3awu",
"3awv"... | 159 | [
"PUB00010613"
] | [
"12404359"
] | [
"Oxygen Binding, Activation, and Reduction to Water by Copper Proteins."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
9,
3429,
35713,
27
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
9,
15,
20,
16,
8,
24,
8,
18
] | 9 | true | Homologous_superfamily | Di-copper centre-containing domain superfamily | Di-copper centre-containing domain superfamily | Di-copper_centre_dom_sf | 9 |
IPR008924 | 8,924 | Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal | Me_CoM_Rdtase_asu/bsu_C | Homologous_superfamily | 9,760 | false | false | Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-... | [
"GO:0050524",
"GO:0015948"
] | [
"coenzyme-B sulfoethylthiotransferase activity",
"methanogenesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.20.840.10",
"SSF48081"
] | [
"",
""
] | [
9755,
9759
] | 2 | [
"EC"
] | [
"2.8.4.1"
] | [
"EC:2.8.4.1"
] | 1 | [
"1e6v",
"1e6y",
"1hbm",
"1hbn",
"1hbo",
"1hbu",
"1mro",
"3m1v",
"3m2r",
"3m2u",
"3m2v",
"3m30",
"3m32",
"3pot",
"3sqg",
"5a0y",
"5a8k",
"5a8r",
"5a8w",
"5g0r",
"5n1q",
"5n28",
"5n2a",
"7b1s",
"7b2c",
"7b2h",
"7nkg",
"7suc",
"7sxm",
"8gf5",
"8gf6",
"8s7v"... | 39 | [
"PUB00006391",
"PUB00010614",
"PUB00035993",
"PUB00035994"
] | [
"9367957",
"11491299",
"16260307",
"16234924"
] | [
"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.",
"On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.",
"Methyl-coenzyme M reductase genes: unique functional ma... | [
1997,
2001,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cylicocyclus nassatus",
"unclassified sequences"
] | [
9441,
20,
1,
298
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal | Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal | Me_CoM_Rdtase_asu/bsu_C | 6 |
IPR008925 | 8,925 | Aminoacyl-tRNA synthetase, class I, anticodon-binding superfamily | aa_tRNA-synth_I_cd-bd_sf | Homologous_superfamily | 40,509 | false | false | Structurally, an α-helix-bundle anticodon-binding domain characterises the class Ia synthetases, whereas the class Ib synthetases, GlnRS and GluRS have distinct anticodon-binding domains. The anticodon-binding domain has a multi-helical structure, consisting of two all-alpha subdomains. The Rossmann-fold, made up of al... | [
"GO:0000049"
] | [
"tRNA binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF48163"
] | [
""
] | [
40509
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME"
] | [
"6.1.1",
"6.1.1.17",
"PWY-5188",
"R-HSA-379726"
] | [
"EC:6.1.1",
"EC:6.1.1.17",
"METACYC:PWY-5188",
"REACTOME:R-HSA-379726"
] | 4 | [
"1g59",
"1gln",
"1irx",
"1j09",
"1n75",
"1n77",
"1n78",
"2cfo",
"2cuz",
"2cv0",
"2cv1",
"2cv2",
"2dxi",
"2ja2",
"2o5r",
"3afh",
"3akz",
"3al0",
"3pnv",
"3pny",
"4g6z",
"4gri",
"5h4v",
"5tgt",
"6b1p",
"6b1z",
"6brl",
"7k86",
"8i9i",
"8jpv",
"8vc5",
"9y81"... | 33 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873",
"PUB00098804"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790",
"29305884"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002,
2018
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
816,
34820,
4096,
2,
775
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
4,
1,
8,
3,
1,
3,
1,
1,
2,
3,
1,
1,
15
] | 13 | true | Homologous_superfamily | Aminoacyl-tRNA synthetase, class I, anticodon-binding superfamily | Aminoacyl-tRNA synthetase, class I, anticodon-binding superfamily | aa_tRNA-synth_I_cd-bd_sf | 7 |
IPR008927 | 8,927 | 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily | 6-PGluconate_DH-like_C_sf | Homologous_superfamily | 457,351 | false | false | 6-phosphogluconate dehydrogenase ( ) catalyses the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate with the concomitant reduction of NADP to NADPH. The metazoan 6PGDHs have a well-conserved glycine-serine rich sequence at the C terminus, which is lacking from bacterial enzymes and from those of ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF48179"
] | [
""
] | [
457351
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.1.1",
"R-BTA-173599",
"R-BTA-5661270",
"R-BTA-70895",
"R-BTA-8964539",
"R-CEL-1483166",
"R-CEL-173599",
"R-CEL-70895",
"R-CEL-71336",
"R-CEL-77310",
"R-CEL-77346",
"R-CEL-77348",
"R-CEL-77350",
"R-CEL-77352",
"R-CEL-8964539",
"R-CEL-9837999",
"R-DDI-70895",
"R-DDI-71336",
"R-D... | [
"EC:1.1.1",
"REACTOME:R-BTA-173599",
"REACTOME:R-BTA-5661270",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-8964539",
"REACTOME:R-CEL-1483166",
"REACTOME:R-CEL-173599",
"REACTOME:R-CEL-70895",
"REACTOME:R-CEL-71336",
"REACTOME:R-CEL-77310",
"REACTOME:R-CEL-77346",
"REACTOME:R-CEL-77348",
"REACTOM... | 96 | [
"1bg6",
"1dli",
"1dlj",
"1evy",
"1evz",
"1f0y",
"1f12",
"1f14",
"1f17",
"1i36",
"1il0",
"1jdj",
"1ks9",
"1lj8",
"1lsj",
"1lso",
"1m2w",
"1m66",
"1m67",
"1m75",
"1m76",
"1mfz",
"1muu",
"1mv8",
"1n1e",
"1n1g",
"1np3",
"1pgj",
"1pgn",
"1pgo",
"1pgp",
"1pgq"... | 491 | [
"PUB00010616"
] | [
"9737929"
] | [
"A 2.8 A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7392,
356464,
87155,
146,
6194
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
107,
21,
37,
36,
20,
71,
33,
25,
75,
55,
13,
9,
184
] | 13 | true | Homologous_superfamily | 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily | 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily | 6-PGluconate_DH-like_C_sf | 2 |
IPR008928 | 8,928 | Six-hairpin glycosidase superfamily | 6-hairpin_glycosidase_sf | Homologous_superfamily | 322,932 | false | false | The six-hairpin glycoside transferase domain, with an α/α toroid fold, contains six α-hairpins arranged in closed circular array. The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieti... | [
"GO:0005975"
] | [
"carbohydrate metabolic process"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF48208"
] | [
""
] | [
322932
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.2.1",
"R-BTA-446210",
"R-CEL-70221",
"R-DME-70221",
"R-DME-9840310",
"R-HSA-189085",
"R-HSA-446210",
"R-HSA-4793954",
"R-HSA-532668",
"R-HSA-6798695",
"R-HSA-70221",
"R-HSA-9683686",
"R-HSA-9694548",
"R-HSA-9768727",
"R-HSA-9840310",
"R-MMU-446210",
"R-MMU-70221",
"R-MMU-9768727... | [
"EC:3.2.1",
"REACTOME:R-BTA-446210",
"REACTOME:R-CEL-70221",
"REACTOME:R-DME-70221",
"REACTOME:R-DME-9840310",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-446210",
"REACTOME:R-HSA-4793954",
"REACTOME:R-HSA-532668",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70221",
"REACTOME:R-HSA-9683686",
"REA... | 26 | [
"1agm",
"1ayx",
"1cem",
"1clc",
"1dog",
"1f9d",
"1f9o",
"1fae",
"1fbo",
"1fbw",
"1fce",
"1fp3",
"1g87",
"1g9g",
"1g9j",
"1ga2",
"1gah",
"1gai",
"1glm",
"1h12",
"1h13",
"1h14",
"1h54",
"1ia6",
"1ia7",
"1is9",
"1js4",
"1k72",
"1kfg",
"1ks8",
"1ksc",
"1ksd"... | 557 | [
"PUB00009409"
] | [
"9334165"
] | [
"A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3668,
206023,
110139,
112,
2990
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
241,
23,
50,
41,
7,
54,
40,
30,
124,
49,
9,
9,
287
] | 13 | true | Homologous_superfamily | Six-hairpin glycosidase superfamily | Six-hairpin glycosidase superfamily | 6-hairpin_glycosidase_sf | 9 |
IPR008929 | 8,929 | Chondroitin AC/alginate lyase | Chondroitin_lyas | Homologous_superfamily | 35,308 | false | false | Glycosaminoglycans (GAGs) are highly negatively charged polysaccharides, formed from disaccharide repeating units. For a number of bacterial species, including Flavobacterium heparinum synthesize GAG lyases, these enzymes are used to degrade and utilise glycosaminoglycans as a source of carbon in the bacterium's natura... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.50.10.100",
"SSF48230"
] | [
"",
""
] | [
34884,
30162
] | 2 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"4.2.2",
"R-HSA-2022923",
"R-MMU-2022923"
] | [
"EC:4.2.2",
"REACTOME:R-HSA-2022923",
"REACTOME:R-MMU-2022923"
] | 3 | [
"1c82",
"1cb8",
"1egu",
"1f1s",
"1f9g",
"1hm2",
"1hm3",
"1hmu",
"1hmw",
"1hn0",
"1hv6",
"1i8q",
"1j0m",
"1j0n",
"1loh",
"1lxk",
"1lxm",
"1n7n",
"1n7o",
"1n7p",
"1n7q",
"1n7r",
"1ojm",
"1ojn",
"1ojo",
"1ojp",
"1qaz",
"1rw9",
"1rwa",
"1rwc",
"1rwf",
"1rwg"... | 134 | [
"PUB00010617"
] | [
"11327856"
] | [
"Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
129,
28054,
6618,
218,
289
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
10,
5,
5
] | 4 | true | Homologous_superfamily | Chondroitin AC/alginate lyase | Chondroitin AC/alginate lyase | Chondroitin_lyas | 1 |
IPR008930 | 8,930 | Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid | Terpenoid_cyclase/PrenylTrfase | Homologous_superfamily | 104,931 | false | false | Protein prenyltransferases catalyse the transfer of the carbon moiety of C15 farnesyl pyrophosphate or geranylgeranyl pyrophosphate synthase to a conserved cysteine residue in a CaaX motif of protein and peptide substrates. The addition of a farnesyl group is required to anchor proteins to the cell membrane. In the 3D ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF48239"
] | [
""
] | [
104931
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"4.2.3",
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-198933",
"R-BTA-2514859",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-6798695",
"R-BTA-6803205",
"R-BTA-8873719",
"R-BTA-8957275",
"R-BTA-9648002",
"R-BTA-977606",
"R-CEL-6803205",
"R-CEL-8873719",
"R-DDI-191273",
"R-DDI-68... | [
"EC:4.2.3",
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803205",
"REACTOME:R-BTA-8873719",
"REACTOME:R-BTA-8957275",
... | 99 | [
"1c3d",
"1d8d",
"1d8e",
"1dce",
"1fpp",
"1ft1",
"1ft2",
"1ghq",
"1gsz",
"1h35",
"1h36",
"1h37",
"1h39",
"1h3a",
"1h3b",
"1h3c",
"1hx9",
"1hxa",
"1hxc",
"1hxg",
"1hzf",
"1jcq",
"1jcr",
"1jcs",
"1kzo",
"1kzp",
"1ld7",
"1ld8",
"1ltx",
"1mzc",
"1n1b",
"1n1z"... | 391 | [
"PUB00010618",
"PUB00100414",
"PUB00100415",
"PUB00100416",
"PUB00100417",
"PUB00100418"
] | [
"12135472",
"34942166",
"34970276",
"8494894",
"20565889",
"9545274"
] | [
"Structure, mechanism and function of prenyltransferases.",
"Structural Mechanics of the Alpha-2-Macroglobulin Transformation.",
"Alpha-2-Macroglobulin in Inflammation, Immunity and Infections.",
"Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate bin... | [
2002,
2021,
2021,
1993,
2010,
1998
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
678,
30043,
73476,
3,
731
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
260,
7,
117,
89,
2,
69,
45,
5,
213,
77,
4,
4,
319
] | 13 | true | Homologous_superfamily | Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid | Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid | Terpenoid_cyclase/PrenylTrfase | 5 |
IPR008932 | 8,932 | Large ribosomal subunit protein bL12, oligomerization | Ribosomal_bL12_oligo | Domain | 29,448 | false | false | Large ribosomal subunit protein bL12 consists of two domains that are connected by a flexible region. The N-terminal domain is required for dimer formation and for anchoring the protein to the ribosome by binding to ribosomal protein L10, while the C-terminal domain is required for translation factors binding [ ]. Ribo... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF16320"
] | [
"Ribosomal_L12_N"
] | [
29448
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9837999",
"R-BTA-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9837999",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9837999",
"R-MMU-9937383",
"R-SCE-9837999",
"R-SPO-9837999"
] | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOM... | 15 | [
"1dd3",
"1dd4",
"1rqt",
"1rqu",
"1rqv",
"1zav",
"1zaw",
"1zax",
"2ftc",
"2zjq",
"3j7z",
"4uy8",
"4v42",
"4v4p",
"4v4v",
"4v4w",
"4v5m",
"4v5n",
"4v6f",
"4v7b",
"4v7d",
"4v85",
"4v89",
"4v9o",
"5kcs",
"6gaw",
"6gb2",
"6gsl",
"6i0y",
"6lkq",
"6vlz",
"6vmi"... | 106 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00010619"
] | [
"11297922",
"11290319",
"11114498",
"11231892"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A common structural motif in elongation factor Ts and ribosomal protein L7/12 may be involved in the interaction with elongation factor Tu."
] | [
2001,
2001,
2000,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
23611,
5399,
2,
435,
1
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
16,
1,
2,
2,
1,
3,
1,
1,
7,
2,
1,
1,
10
] | 13 | true | Domain | Large ribosomal subunit protein bL12, oligomerization | Large ribosomal subunit protein bL12, oligomerization | Ribosomal_bL12_oligo | 5 |
IPR008936 | 8,936 | Rho GTPase activation protein | Rho_GTPase_activation_prot | Homologous_superfamily | 203,998 | false | false | Proteins containing a RhoGAP (Rho GTPase Activating Protein) domain usually function to catalyse the hydrolysis of GTP that is bound to Rho, Rac and/or Cdc42, inactivating these regulators of the actin cytoskeleton. The 53 known human RhoGAP domain-containing proteins are the largest known group of Rho GTPase regulator... | [] | [] | [] | 0 | [
"CATHGENE3D",
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.506.10",
"G3DSA:1.10.555.10",
"SSF48350"
] | [
"",
"",
""
] | [
51667,
151178,
202187
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-109704",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1250342",
"R-BTA-1257604",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-1660499",
"R-BTA-180292",
"R-BTA-186763",
"R-BTA-193648",
"R-BTA-1963642",
"R-BTA-198203",
"R-BTA-201556",
"R-BTA-202424",
"R-BTA-2029485",
"R-BTA-210993",
"R-... | [
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-180292",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-193648",
"REACTOME:R-BT... | 471 | [
"1am4",
"1f7c",
"1grn",
"1nf1",
"1ow3",
"1pbw",
"1rgp",
"1tx4",
"1wer",
"1wq1",
"1xa6",
"2ee4",
"2ee5",
"2mbg",
"2ngr",
"2osa",
"2ovj",
"2qv2",
"2xs6",
"3bxj",
"3byi",
"3cxl",
"3eap",
"3fay",
"3fk2",
"3hm6",
"3ig3",
"3iug",
"3kuq",
"3msx",
"3qis",
"3ryt"... | 105 | [
"PUB00010623"
] | [
"12297274"
] | [
"Human RhoGAP domain-containing proteins: structure, function and evolutionary relationships."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Marseillevirus LCMAC101",
"metagenomes"
] | [
122,
203870,
1,
5
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
45,
74,
838,
115,
504,
315,
19,
43,
474,
15,
12,
180
] | 12 | true | Homologous_superfamily | Rho GTPase activation protein | Rho GTPase activation protein | Rho_GTPase_activation_prot | 7 |
IPR008937 | 8,937 | Ras-like guanine nucleotide exchange factor | Ras-like_GEF | Family | 50,926 | false | false | This family also includes S. cerevisiae LTE1, a guanine nucleotide exchange factor for TEM1, a Ras-like protein that is a component of the mitotic exit network [ ]. Small GTPases of the Ras family alternate between 2 conformations induced by the binding of either GTP or GDP. Guanine nucleotide exchange factors (GEFs) i... | [
"GO:0005085",
"GO:0007264"
] | [
"guanyl-nucleotide exchange factor activity",
"small GTPase-mediated signal transduction"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER"
] | [
"PTHR23113"
] | [
""
] | [
50926
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-354192",
"R-BTA-392517",
"R-CEL-1433557",
"R-CEL-1433559",
"R-CEL-179812",
"R-CEL-180336",
"R-CEL-186763",
"R-CEL-193648",
"R-CEL-1963640",
"R-CEL-2179392",
"R-CEL-354192",
"R-CEL-354194",
"R-CEL-375165",
"R-CEL-381676",
"R-CEL-392517",
"R-CEL-416482",
"R-CEL-5654688",
"R-CE... | [
"REACTOME:R-BTA-354192",
"REACTOME:R-BTA-392517",
"REACTOME:R-CEL-1433557",
"REACTOME:R-CEL-1433559",
"REACTOME:R-CEL-179812",
"REACTOME:R-CEL-180336",
"REACTOME:R-CEL-186763",
"REACTOME:R-CEL-193648",
"REACTOME:R-CEL-1963640",
"REACTOME:R-CEL-2179392",
"REACTOME:R-CEL-354192",
"REACTOME:R-CEL... | 221 | [
"1bkd",
"1nvu",
"1nvv",
"1nvw",
"1nvx",
"1xd2",
"1xd4",
"1xdv",
"2byv",
"2ii0",
"2ije",
"3cf6",
"3ksy",
"3qxl",
"4f7z",
"4jgw",
"4l9m",
"4mgi",
"4mgk",
"4mgy",
"4mgz",
"4mh0",
"4nyi",
"4nyj",
"4nym",
"4uru",
"4urv",
"4urw",
"4urx",
"4ury",
"4urz",
"4us0"... | 114 | [
"PUB00010624",
"PUB00073816"
] | [
"10579920",
"7935462"
] | [
"Ras and Rap1: two highly related small GTPases with distinct function.",
"The yeast TEM1 gene, which encodes a GTP-binding protein, is involved in termination of M phase."
] | [
1999,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadati",
"Viruses",
"organismal metagenomes"
] | [
50841,
61,
22,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
18,
179,
35,
144,
90,
4,
123,
4,
2
] | 9 | true | Family | Ras-like guanine nucleotide exchange factor | Ras-like guanine nucleotide exchange factor | Ras-like_GEF | 6 |
IPR008939 | 8,939 | Lytic transglycosylase, superhelical U-shaped | Lytic_TGlycosylase_superhlx_U | Homologous_superfamily | 12,286 | false | false | Bacterial lytic transglycosylases degrade murein via cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine, with the concomitant formation of a 1,6-anhydrobond in the muramic acid residue. There are both soluble (Slt enzymes) and membrane-bound (Mlt enzymes) lytic transglycosylas... | [
"GO:0004553",
"GO:0042597"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"periplasmic space"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"SSF"
] | [
"SSF48435"
] | [
""
] | [
12286
] | 1 | [] | [] | [] | 0 | [
"1qsa",
"1qte",
"1sly",
"2mhk",
"5mpq",
"5o1j",
"5o24",
"5o29",
"5o2n",
"5o2o",
"5ohu",
"6dr3",
"6fbt",
"6fc4",
"6fcq",
"6fcr",
"6fcs",
"6fcu",
"6fpn",
"6h5f",
"7t8n"
] | 21 | [
"PUB00011783"
] | [
"10452894"
] | [
"High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
12133,
35,
118
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Homologous_superfamily | Lytic transglycosylase, superhelical U-shaped | Lytic transglycosylase, superhelical U-shaped | Lytic_TGlycosylase_superhlx_U | 6 |
IPR008942 | 8,942 | ENTH/VHS | ENTH_VHS | Homologous_superfamily | 110,203 | false | false | This superfamily represents domains with a multi-helical, α-α 2-layered structural fold as found in: the ENTH domain of Epsin; the VHS domain of Hrs, Tom1, and ADP-ribosylation factors; the RPR domain of PCF11 protein; and the N-terminal domain of phosphoinositide-binding clathrin adaptor. The epsin NH2-terminal homolo... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.25.40.90",
"SSF48464"
] | [
"",
""
] | [
109169,
100562
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-182971",
"R-BTA-432720",
"R-BTA-5689880",
"R-BTA-6807004",
"R-BTA-6807505",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-9013420",
"R-BTA-917729",
"R-BTA-9706019",
"R-CEL-182971",
"R-CEL-432722",
"R-CEL-6807004",
"R-CEL-6807505",
"R-CEL-72187",
"R-CEL-72203",
"R-CEL-73856",
"R-C... | [
"REACTOME:R-BTA-182971",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-6807004",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-9013420",
"REACTOME:R-BTA-917729",
"REACTOME:R-BTA-9706019",
"REACTOME:R-CEL-182971",
"REACTOME:R-... | 113 | [
"1dvp",
"1edu",
"1elk",
"1eyh",
"1h0a",
"1hf8",
"1hfa",
"1hg2",
"1hg5",
"1hx8",
"1inz",
"1jpl",
"1juq",
"1jwf",
"1jwg",
"1lf8",
"1mhq",
"1py1",
"1sz9",
"1sza",
"1ujj",
"1ujk",
"1vdy",
"1x5b",
"1xgw",
"2bf0",
"2dcp",
"2diw",
"2km4",
"2l0i",
"2l0t",
"2lo6"... | 107 | [
"PUB00007107",
"PUB00008037"
] | [
"11911874",
"10985773"
] | [
"The ENTH domain.",
"Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes."
] | [
2002,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Satyrvirus sp."
] | [
4,
110198,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
214,
22,
272,
56,
179,
104,
18,
124,
143,
16,
14,
384
] | 12 | true | Homologous_superfamily | ENTH/VHS | ENTH/VHS | ENTH_VHS | 8 |
IPR008944 | 8,944 | Bacteriophage T4, Gp59, helicase assembly protein | Phage_T4_Gp59 | Family | 513 | false | false | The Bacteriophage T4 gene 59 helicase assembly protein (Gp59) is required for recombination-dependent DNA replication and repair, which is the predominant mode of DNA replication in the late stage of T4 infection. Gp59 accelerates the loading of the T4 gene 41 helicase during DNA synthesis by the T4 replication system ... | [] | [] | [] | 0 | [
"HAMAP",
"PIRSF"
] | [
"MF_04156",
"PIRSF004374"
] | [
"HELIC_LOADER_T4",
"Phage-associated_Gp59"
] | [
513,
293
] | 2 | [] | [] | [] | 0 | [
"1c1k"
] | 1 | [
"PUB00010626",
"PUB00097909"
] | [
"10669611",
"22427673"
] | [
"Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical two-domain fold.",
"Mutational analysis of the T4 gp59 helicase loader reveals its sites for interaction with helicase, single-stranded binding protein, and DNA."
] | [
2000,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Flagellimonas marina",
"Viruses",
"metagenomes"
] | [
1,
496,
16
] | 3 | [] | [] | 0 | true | Family | Bacteriophage T4, Gp59, helicase assembly protein | Bacteriophage T4, Gp59, helicase assembly protein | Phage_T4_Gp59 | 2 |
IPR008947 | 8,947 | Phospholipase C/P1 nuclease domain superfamily | PLipase_C/P1_nuclease_dom_sf | Homologous_superfamily | 14,242 | false | false | The enzymes belonging to this superfamily are involved in phosphate ester hydrolysis and contain a triad of closely spaced zinc ions at their active centres. Both families of enzymes hydrolyse phosphodiesters. Substrates for phospholipase C are phosphatidylinositol and phosphatidylcholine, while P1 nuclease is an endon... | [
"GO:0016788"
] | [
"hydrolase activity, acting on ester bonds"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.575.10",
"SSF48537"
] | [
"",
""
] | [
13779,
14049
] | 2 | [] | [] | [] | 0 | [
"1ah7",
"1ak0",
"1ca1",
"1gyg",
"1kho",
"1olp",
"1p5x",
"1p6d",
"1p6e",
"1qm6",
"1qmd",
"2ffz",
"2fgn",
"2huc",
"2wxt",
"2wxu",
"2wy6",
"3sng",
"3w52",
"4cwm",
"4cxo",
"4cxp",
"4cxv",
"4dj4",
"4jdg",
"5fb9",
"5fba",
"5fbb",
"5fbc",
"5fbd",
"5fbf",
"5fbg"... | 42 | [
"PUB00010629"
] | [
"1525473"
] | [
"Structure and mechanism of alkaline phosphatase."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Ascovirus",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
191,
8,
7671,
6247,
125
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
28,
2,
14,
25
] | 4 | true | Homologous_superfamily | Phospholipase C/P1 nuclease domain superfamily | Phospholipase C/P1 nuclease domain superfamily | PLipase_C/P1_nuclease_dom_sf | 5 |
IPR008948 | 8,948 | L-Aspartase-like | L-Aspartase-like | Homologous_superfamily | 148,741 | false | false | The enzyme L-aspartate ammonia-lyase (aspartase) catalyses the reversible deamination of the amino acid L-aspartic acid, using a carbanion mechanism to produce fumaric acid and ammonium ion. Aspartases from different organisms show high sequence homology, and this homology extends to functionally related enzymes such a... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF48557"
] | [
""
] | [
148741
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"4.3.2",
"R-BTA-70635",
"R-BTA-70921",
"R-CEL-70921",
"R-CEL-71403",
"R-CEL-73817",
"R-CEL-9837999",
"R-DDI-70921",
"R-DDI-71403",
"R-DDI-9837999",
"R-DRE-71403",
"R-GGA-187630",
"R-GGA-419140",
"R-GGA-421203",
"R-GGA-70635",
"R-HSA-70635",
"R-HSA-70921",
"R-HSA-71403",
"R-HSA-73... | [
"EC:4.3.2",
"REACTOME:R-BTA-70635",
"REACTOME:R-BTA-70921",
"REACTOME:R-CEL-70921",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-73817",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-70921",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DRE-71403",
"REACTOME:R-GGA-187630",
"REACTOME:R... | 39 | [
"1aos",
"1auw",
"1b8f",
"1c3c",
"1c3u",
"1dcn",
"1dof",
"1eb4",
"1f1o",
"1fuo",
"1fup",
"1fuq",
"1fur",
"1gk2",
"1gk3",
"1gkj",
"1gkm",
"1hy0",
"1hy1",
"1i0a",
"1j3u",
"1jsw",
"1k62",
"1k7w",
"1kq7",
"1q5n",
"1re5",
"1t6j",
"1t6p",
"1tj7",
"1tju",
"1tjv"... | 186 | [
"PUB00011785"
] | [
"9230045"
] | [
"The structure of L-aspartate ammonia-lyase from Escherichia coli."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2535,
115002,
28824,
16,
2364
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
46,
3,
13,
17,
4,
59,
18,
4,
53,
18,
3,
5,
139
] | 13 | true | Homologous_superfamily | L-Aspartase-like | L-Aspartase-like | L-Aspartase-like | 6 |
IPR008949 | 8,949 | Isoprenoid synthase domain superfamily | Isoprenoid_synthase_dom_sf | Homologous_superfamily | 169,773 | false | false | This superfamily represents a domain found in the isoprenoid synthase family [ ], which is mostly all α-helical with a core bundle of anti-parallel α-helices [ ]. | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.600.10",
"SSF48576"
] | [
"",
""
] | [
168851,
167939
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.2.3",
"R-BTA-191273",
"R-BTA-6799198",
"R-DDI-191273",
"R-DDI-2142789",
"R-DME-6799198",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2142789",
"R-HSA-2426168",
"R-HSA-6799198",
"R-MMU-191273",
"R-MMU-2142789",
"R-MMU-6799198",
"R-RNO-191273",
"R-RNO-2142789",
"R-RNO-6799198",
"R-SCE... | [
"EC:4.2.3",
"REACTOME:R-BTA-191273",
"REACTOME:R-BTA-6799198",
"REACTOME:R-DDI-191273",
"REACTOME:R-DDI-2142789",
"REACTOME:R-DME-6799198",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2142789",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-6799198",
"REACTOME:R-MMU-191273",
... | 21 | [
"1dgp",
"1di1",
"1ezf",
"1fps",
"1hm4",
"1hm7",
"1hx9",
"1hxa",
"1hxc",
"1hxg",
"1jfa",
"1jfg",
"1kiy",
"1kiz",
"1n1b",
"1n1z",
"1n20",
"1n21",
"1n22",
"1n23",
"1n24",
"1ps1",
"1rqi",
"1rqj",
"1rtr",
"1ubv",
"1ubw",
"1ubx",
"1uby",
"1v4e",
"1v4h",
"1v4i"... | 794 | [
"PUB00065025",
"PUB00072944"
] | [
"23493556",
"23438177"
] | [
"Prediction of function for the polyprenyl transferase subgroup in the isoprenoid synthase superfamily.",
"Rational engineering of plasticity residues of sesquiterpene synthases from Artemisia annua: product specificity and catalytic efficiency."
] | [
2013,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2811,
87705,
77316,
37,
1904
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
262,
3,
15,
11,
2,
45,
28,
8,
200,
27,
4,
5,
349
] | 13 | true | Homologous_superfamily | Isoprenoid synthase domain superfamily | Isoprenoid synthase domain superfamily | Isoprenoid_synthase_dom_sf | 2 |
IPR008952 | 8,952 | Tetraspanin, EC2 domain superfamily | Tetraspanin_EC2_sf | Homologous_superfamily | 51,448 | false | false | This superfamily represents the EC2 domain from tetraspanins, consisting of 5 helices in an irregular disulphide-linked array which plays a role in form homodimerization. Tetraspanins are a distinct family of cell surface proteins, containing four conserved transmembrane domains: a small outer loop (EC1), a larger oute... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.1450.10",
"SSF48652"
] | [
"",
""
] | [
49324,
50897
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-1300645",
"R-BTA-198933",
"R-BTA-6798695",
"R-BTA-977606",
"R-CEL-6798695",
"R-DME-6798695",
"R-DRE-6798695",
"R-HSA-114608",
"R-HSA-1300645",
"R-HSA-198933",
"R-HSA-2022090",
"R-HSA-202733",
"R-HSA-416993",
"R-HSA-446107",
"R-HSA-5336415",
"R-HSA-6798695",
"... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1300645",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-977606",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DME-6798695",
"REACTOME:R-DRE-6798695",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-1300645",
"REACTOME:R-HSA-198933",
"REACTOME:R-H... | 33 | [
"1g8q",
"1iv5",
"2m7z",
"3x0e",
"3x0f",
"3x0g",
"5dfv",
"5dfw",
"5m2c",
"5m33",
"5m3d",
"5m3t",
"5m4r",
"5tcx",
"6ejg",
"6ejm",
"6ek2",
"6k4j",
"6rlo",
"6rlr",
"6u9s",
"6wvg",
"6z1v",
"6z20",
"7jic",
"7mws",
"7mwx",
"7rd5",
"7rdb",
"7zw1",
"8esv",
"8jj5"... | 32 | [
"PUB00010633"
] | [
"12575999"
] | [
"Functional domains in tetraspanin proteins."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Actinoallomurus acaciae",
"Eukaryota",
"bird metagenome"
] | [
1,
51444,
3
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
22,
139,
61,
125,
95,
125
] | 6 | true | Homologous_superfamily | Tetraspanin, EC2 domain superfamily | Tetraspanin, EC2 domain superfamily | Tetraspanin_EC2_sf | 1 |
IPR008954 | 8,954 | Moesin tail domain superfamily | Moesin_tail_sf | Homologous_superfamily | 10,510 | false | false | The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module [ ]. ERM proteins are highly related members of the larger protein 4.1 superfamily. The sole Dr... | [
"GO:0003779"
] | [
"actin binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:6.10.360.10",
"SSF48678"
] | [
"",
""
] | [
9916,
10399
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-373752",
"R-DME-2029482",
"R-DME-373752",
"R-DME-5627123",
"R-HSA-2029482",
"R-HSA-373752",
"R-HSA-437239",
"R-HSA-5627123",
"R-HSA-8950505",
"R-HSA-9662360",
"R-HSA-9662361",
"R-HSA-9725370",
"R-MMU-2029482",
"R-MMU-373752",
"R-MMU-437239",
"R-MMU-5627123",
"R-RNO-2029482",
... | [
"REACTOME:R-BTA-373752",
"REACTOME:R-DME-2029482",
"REACTOME:R-DME-373752",
"REACTOME:R-DME-5627123",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-373752",
"REACTOME:R-HSA-437239",
"REACTOME:R-HSA-5627123",
"REACTOME:R-HSA-8950505",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361",
"REACTOME:R-... | 20 | [
"1ef1",
"2i1j",
"2i1k",
"4rm8",
"4rm9",
"4zrj",
"7edr"
] | 7 | [
"PUB00010635",
"PUB00013213"
] | [
"12511959",
"10847681"
] | [
"Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity.",
"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain."
] | [
2003,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Diatraea saccharalis granulovirus",
"Eukaryota"
] | [
12,
1,
10497
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
20,
8,
25,
20,
25
] | 6 | true | Homologous_superfamily | Moesin tail domain superfamily | Moesin tail domain superfamily | Moesin_tail_sf | 6 |
IPR008956 | 8,956 | Protease A inhibitor IA3 domain superfamily | IA3_dom_sf | Homologous_superfamily | 16 | false | false | This superfamily represents a domain found in N-terminal of IA3 protein (also known as Pai3). The IA3 polypeptide of Saccharomyces cerevisiae (also known as Pai3) is an 8kDa inhibitor of the vacuolar aspartic proteinase (proteinase A or saccharopepsin, MEROPS peptidase family A1). It belongs to MEROPS inhibitor family ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF48686"
] | [
""
] | [
16
] | 1 | [] | [] | [] | 0 | [
"1dp5",
"1dpj",
"1g0v"
] | 3 | [
"PUB00010637"
] | [
"11042188"
] | [
"The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomyces"
] | [
16
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Homologous_superfamily | Protease A inhibitor IA3 domain superfamily | Protease A inhibitor IA3 domain superfamily | IA3_dom_sf | 7 |
IPR008958 | 8,958 | Transglutaminase, C-terminal | Transglutaminase_C | Domain | 10,931 | false | false | Transglutaminases catalyse the post-translational modification of proteins at glutamine residues, with formation of isopeptide bonds. Members of the transglutaminase family usually have three domains: N-terminal ( ), middle ( ) and C-terminal. The middle domain is usually well conserved, but family members can display ... | [
"GO:0003810",
"GO:0018149"
] | [
"protein-glutamine gamma-glutamyltransferase activity",
"peptide cross-linking"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00927"
] | [
"Transglut_C"
] | [
10931
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.13",
"R-HSA-114608",
"R-HSA-140875",
"R-HSA-6785807",
"R-HSA-6809371",
"R-MMU-114608",
"R-MMU-140875",
"R-MMU-6809371",
"R-RNO-114608",
"R-RNO-140875",
"R-RNO-6809371"
] | [
"EC:2.3.2.13",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140875",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6809371",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-140875",
"REACTOME:R-MMU-6809371",
"REACTOME:R-RNO-114608",
"REACTOME:R-RNO-140875",
"REACTOME:R-RNO-6809371"
] | 11 | [
"1evu",
"1ex0",
"1f13",
"1fie",
"1g0d",
"1ggt",
"1ggu",
"1ggy",
"1kv3",
"1l9m",
"1l9n",
"1nud",
"1nuf",
"1nug",
"1qrk",
"2q3z",
"2xzz",
"3ly6",
"3s3j",
"3s3p",
"3s3s",
"4kty",
"4pyg",
"5mhl",
"5mhm",
"5mhn",
"5mho",
"6a8p",
"6kzb",
"7tvz",
"7tw0",
"7tw1"... | 51 | [
"PUB00001513",
"PUB00002570",
"PUB00010639",
"PUB00095164",
"PUB00095165"
] | [
"1683845",
"1974250",
"10411627",
"15692067",
"19269200"
] | [
"Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues.",
"Structure of transglutaminases.",
"The structural basis for the regulation of tissue transglutaminase by calcium ions.",
"Protein-4.2 association with band 3 (AE1, SLCA4) in Xenopus oocytes: effects of three natural protein-4... | [
1991,
1990,
1999,
2005,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Ciceribacter ferrooxidans",
"Eukaryota"
] | [
1,
10930
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
52,
3,
35,
24,
27
] | 5 | true | Domain | Transglutaminase, C-terminal | Transglutaminase, C-terminal | Transglutaminase_C | 9 |
IPR008963 | 8,963 | Purple acid phosphatase-like, N-terminal | Purple_acid_Pase-like_N | Homologous_superfamily | 25,640 | false | false | Purple acid phosphatases (PAPs) are ubiquitous binuclear metal-containing acid hydrolases characterised by their acidic pH optima and their intense purple colour due to a TyrO-to-FeIII charge-transfer transition. The amino acid residues coordinating the metal ions are conserved in all PAPs. Active PAPs contain an FeIII... | [
"GO:0003993",
"GO:0046872"
] | [
"acid phosphatase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SSF"
] | [
"SSF49363"
] | [
""
] | [
25640
] | 1 | [
"EC",
"METACYC"
] | [
"3.1.3.2",
"PWY-6348"
] | [
"EC:3.1.3.2",
"METACYC:PWY-6348"
] | 2 | [
"1kbp",
"1xzw",
"2qfp",
"2qfr",
"3kbp",
"3zk4",
"4dhl",
"4dsy",
"4dt2",
"4kbp",
"6g46",
"6git",
"6giz",
"6gj2",
"6gj9",
"6gja",
"6hwr",
"6of5",
"6ofd",
"6py9",
"6vj7",
"8brn"
] | 22 | [
"PUB00010641",
"PUB00010642",
"PUB00088140"
] | [
"12440878",
"10510276",
"25217636"
] | [
"New insights into the mechanism of purple acid phosphatase through (1)H NMR spectroscopy of the recombinant human enzyme.",
"Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean.",
"Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iro... | [
2002,
1999,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
115,
8800,
16567,
2,
156
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
82,
8,
1,
4,
3,
3,
2,
74,
3,
95
] | 10 | true | Homologous_superfamily | Purple acid phosphatase-like, N-terminal | Purple acid phosphatase-like, N-terminal | Purple_acid_Pase-like_N | 2 |
IPR008964 | 8,964 | Invasin/intimin cell-adhesion fragments | Invasin/intimin_cell_adhesion | Homologous_superfamily | 40,507 | false | false | Two types of pathogenic Escherichia coli, enteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC), cause diarrhoeal disease by disrupting the intestinal environment through the intimate attachment of the bacteria to the intestinal epithelium. This process is mediated by intimin, an outer membrane protein t... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF49373"
] | [
""
] | [
40507
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-DME-170822",
"R-DME-3108214",
"R-DME-3301854",
"R-DME-4085377",
"R-DME-4551638",
"R-DME-4615885",
"R-DME-5578749",
"R-HSA-1169408",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"R-HSA-165054",
"R-... | [
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-DME-170822",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3301854",
"REACTOME:R-DME-4085377",
"REACTOME:R-DME-4551638",
"REACTOME:R-DME-4615885",
"REACTOME:R-DME-5578749",
"REACTOME:R-H... | 69 | [
"1cwv",
"1e5u",
"1f00",
"1f02",
"2l04",
"2lv4",
"2mh4",
"2mog",
"2mqg",
"2n7s",
"2zqk",
"2zwk",
"3ncw",
"3ncx",
"4e9l",
"4hu8",
"4uid",
"4uj6",
"4ypj",
"5dmy",
"5ftx",
"5ldy",
"5n40",
"5ngj",
"5t98",
"5t99",
"6hhu",
"6n1a",
"6n1b",
"6qub",
"6quc",
"6qud"... | 85 | [
"PUB00010643"
] | [
"12615225"
] | [
"Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1516,
33891,
3466,
1069,
565
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
2,
1,
1,
3,
4,
1,
7,
7
] | 10 | true | Homologous_superfamily | Invasin/intimin cell-adhesion fragments | Invasin/intimin cell-adhesion fragments | Invasin/intimin_cell_adhesion | 5 |
IPR008965 | 8,965 | CBM2/CBM3, carbohydrate-binding domain superfamily | CBM2/CBM3_carb-bd_dom_sf | Homologous_superfamily | 41,570 | false | false | This carbohydrate-binding domain superfamily is found in a number of proteins, such as the chitobiase/beta-hexosaminidase family of glycoside hydrolases, bacterial cellulases and xylanases, and the bacterial scafoldin, cellobiose and cohesin proteins. The carbohydrate-binding domain consists of a β-sandwich formed of 9... | [
"GO:0030246"
] | [
"carbohydrate binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF49384"
] | [
""
] | [
41570
] | 1 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1anu",
"1aoh",
"1c7s",
"1c7t",
"1e5b",
"1e5c",
"1exg",
"1exh",
"1g1k",
"1g43",
"1g87",
"1ga2",
"1heh",
"1hej",
"1js4",
"1k72",
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"1nbc",
"1ohz",
"1qba",
"1qbb",
"1qzn",
"1tf4",
"1tyj",
"1xbd",
"1zv9",
"2b59",
"2bm3",
"2ccl",
"2cwr",
"2czn",
"2jh2"... | 123 | [
"PUB00001296"
] | [
"8918451"
] | [
"Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
755,
39026,
1492,
24,
273
] | 5 | [
"Arabidopsis thaliana"
] | [
7
] | 1 | true | Homologous_superfamily | CBM2/CBM3, carbohydrate-binding domain superfamily | CBM2/CBM3, carbohydrate-binding domain superfamily | CBM2/CBM3_carb-bd_dom_sf | 3 |
IPR008967 | 8,967 | p53-like transcription factor, DNA-binding domain superfamily | p53-like_TF_DNA-bd_sf | Homologous_superfamily | 75,324 | false | false | This domain superfamily is found in a number of transcription factors, including p53, NFATC, TonEBP, STAT-1, and NFkappaB, where it is responsible for DNA-binding. These transcription factors play diverse roles in the regulation of cellular functions: the p53 tumour suppressor upregulates the expression of genes involv... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF49417"
] | [
""
] | [
75324
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"REACTOME:R-BTA-5689896",
"REACTOME:R-... | 623 | [
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"1nfa"... | 420 | [
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"Structure of a TonEBP-DNA complex reveals DNA encircled by a transcription factor.",
"STAT1 mediates differentiation of chronic lymphocytic leukemia cells in response to B... | [
2003,
1997,
2002,
2003,
2003,
2002,
1998
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota",
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"bird metagenome"
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75319,
2,
3
] | 3 | [
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"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
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28,
328,
66,
492,
218,
7,
200,
1,
2
] | 9 | true | Homologous_superfamily | p53-like transcription factor, DNA-binding domain superfamily | p53-like transcription factor, DNA-binding domain superfamily | p53-like_TF_DNA-bd_sf | 7 |
IPR008969 | 8,969 | Carboxypeptidase-like, regulatory domain superfamily | CarboxyPept-like_regulatory | Homologous_superfamily | 226,422 | false | false | This domain superfamily identifies a number of eukaryotic carboxypeptidases, these include carboxypeptidase D, E (H), N, X, X2 and Z. These are metallopeptidases belong to MEROPS peptidase family M14 (clan MC), subfamily M14B. Carboxypeptidase D (CPD) is a new B-type metallocarboxypeptidase that is membrane bound and h... | [] | [] | [] | 0 | [
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"6z9a",
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"6zm1"... | 52 | [
"PUB00010644"
] | [
"11080148"
] | [
"Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1949,
199272,
22501,
143,
2557
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
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] | [
14,
3,
168,
14,
2,
49,
20,
2,
69,
20
] | 10 | true | Homologous_superfamily | Carboxypeptidase-like, regulatory domain superfamily | Carboxypeptidase-like, regulatory domain superfamily | CarboxyPept-like_regulatory | 7 |
IPR008971 | 8,971 | HSP40/DnaJ peptide-binding | HSP40/DnaJ_pept-bd | Homologous_superfamily | 88,902 | false | false | The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at intermediate stages of folding, assembly, and translocation across membranes [ ]. Binding of protein substrates to the DnaK C-terminal domain is controlled by ATP binding and hydrolysis in the N-terminal ATPase domain. The interactio... | [
"GO:0051082",
"GO:0006457"
] | [
"unfolded protein binding",
"protein folding"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF49493"
] | [
""
] | [
88902
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"REACTOME:R-HSA-3371497",
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"REACTOME:R-HSA-3371571",
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"8x2u",
"9dvi",
"9e5c",
"9fqr"... | 32 | [
"PUB00010645"
] | [
"9600925"
] | [
"Role of the J-domain in the cooperation of Hsp40 with Hsp70."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
724,
43804,
43009,
98,
1267
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
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92,
5,
24,
27,
2,
37,
27,
5,
60,
36,
6,
5,
201
] | 13 | true | Homologous_superfamily | HSP40/DnaJ peptide-binding | HSP40/DnaJ peptide-binding | HSP40/DnaJ_pept-bd | 2 |
IPR008972 | 8,972 | Cupredoxin | Cupredoxin | Homologous_superfamily | 302,484 | false | false | Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Since free copper is toxic, even at very low concentrations, its homeostasis in living organisms is tightly controlled by subtle molecular mechanisms. In eukaryotes, befor... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.60.40.420",
"SSF49503"
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] | [
297980,
298722
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"REACTOME:R-CEL-2682334",
"REACTOME:R-CEL-3928662",
"REACTOME:R-CEL-3928663",
"REACTOME... | 106 | [
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"PUB00011817"
] | [
"11867755"
] | [
"Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7806,
104091,
186784,
213,
3590
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
375,
9,
38,
29,
4,
630,
58,
17,
294,
85,
4,
2,
394
] | 13 | true | Homologous_superfamily | Cupredoxin | Cupredoxin | Cupredoxin | 6 |
IPR008974 | 8,974 | TRAF-like | TRAF-like | Homologous_superfamily | 70,269 | false | false | The tumour necrosis factor receptor (TNFR) associated factors (TRAFs) act as signal transducers for both TNFRs and interleukin-1/Toll-like receptors. TRAFs function in immunity, embryonic development, stress response and bone metabolism through their induction of cell proliferation, differentiation, and apoptosis [ ]. ... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.210.10"
] | [
""
] | [
70269
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"2f1z",
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"2fop"... | 114 | [
"PUB00011815",
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] | [
"10518213",
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"All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction.",
"Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling."
] | [
1999,
2002,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Endozoicomonadaceae",
"Eukaryota",
"Megaviricetes",
"organismal metagenomes"
] | [
9,
70232,
24,
4
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
459,
104,
53,
19,
57,
54,
1,
338,
74,
1,
2,
304
] | 12 | true | Homologous_superfamily | TRAF-like | TRAF-like | TRAF-like | 7 |
IPR008977 | 8,977 | PHM/PNGase F domain superfamily | PHM/PNGase_F_dom_sf | Homologous_superfamily | 13,300 | false | false | Peptidyl-glycine alpha-amidating monooxygenase (PAM) is involved in the amidation of of bioactive peptides. It has two enzymatically active domains with catalytic activities -peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), each of which binds one co... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF49742"
] | [
""
] | [
13300
] | 1 | [
"EC",
"REACTOME",
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"R-DME-209905",
"R-HSA-209905",
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"R-RNO-209905"
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"REACTOME:R-DME-209905",
"REACTOME:R-HSA-209905",
"REACTOME:R-MMU-209905",
"REACTOME:R-RNO-209905"
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"4r4x",
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"4zel",
"5wja",
"5wkw",
"5wm0",
"6ala"... | 42 | [
"PUB00011821"
] | [
"10504734"
] | [
"Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"metagenomes"
] | [
2760,
10347,
7,
186
] | 4 | [
"Caenorhabditis elegans",
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"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
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4,
19,
8,
12,
9,
19
] | 6 | true | Homologous_superfamily | PHM/PNGase F domain superfamily | PHM/PNGase F domain superfamily | PHM/PNGase_F_dom_sf | 5 |
IPR008978 | 8,978 | HSP20-like chaperone | HSP20-like_chaperone | Homologous_superfamily | 152,337 | false | false | This homologous superfamily represents HSP20-like chaperones and related proteins. Hsp20 is a mammalian small heat-shock protein family that occurs most abundantly in skeletal muscle and heart. It has a tendency to form dimers, via a disulphide linkage formed by an N-terminal cysteine, low heat stability and a poor cha... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.60.40.790",
"SSF49764"
] | [
"",
""
] | [
149667,
145462
] | 2 | [
"REACTOME",
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"R-BTA-9009391",
"R-BTA-9648025",
"R-BTA-9696270",
"R-CEL-171319",
"R... | [
"REACTOME:R-BTA-1237044",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-171319",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-450408",
"REACTOME:R-BTA-5663220",
"REACTOME:R-BTA-5687128",
"REACTOME:R-BTA-68877",
"REACTOME:R-B... | 123 | [
"1ejf",
"1gme",
"1rl1",
"1shs",
"1wfi",
"1wgv",
"1wh0",
"1x5m",
"2bol",
"2byu",
"2cg9",
"2cr0",
"2h50",
"2h53",
"2jki",
"2k8q",
"2klr",
"2kmw",
"2mnw",
"2n0k",
"2n3j",
"2o30",
"2rh0",
"2wj5",
"2wj7",
"2xcm",
"2y1y",
"2y1z",
"2y22",
"2ygd",
"3aab",
"3aac"... | 113 | [
"PUB00011822"
] | [
"11702068"
] | [
"Crystal structure and assembly of a eukaryotic small heat shock protein."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3599,
45612,
102199,
167,
760
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
226,
32,
64,
42,
2,
115,
64,
9,
121,
102,
5,
6,
273
] | 13 | true | Homologous_superfamily | HSP20-like chaperone | HSP20-like chaperone | HSP20-like_chaperone | 9 |
IPR008979 | 8,979 | Galactose-binding-like domain superfamily | Galactose-bd-like_sf | Homologous_superfamily | 446,877 | false | false | Proteins containing a galactose-binding-like domain fold can be found in several different protein families, in both eukaryotes and prokaryotes. The common function of these domains is to bind to specific ligands, such as cell-surface-attached carbohydrate substrates for galactose oxidase and sialidase [ ], phospholipi... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF49785"
] | [
""
] | [
446877
] | 1 | [
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"REACTOME",
"REACTOM... | [
"R-BTA-8951664",
"R-BTA-983168",
"R-CEL-1257604",
"R-CEL-1433557",
"R-CEL-1433559",
"R-CEL-1592389",
"R-CEL-186763",
"R-CEL-186797",
"R-CEL-216083",
"R-CEL-2173789",
"R-CEL-2173796",
"R-CEL-2682334",
"R-CEL-3928662",
"R-CEL-3928663",
"R-CEL-3928664",
"R-CEL-3928665",
"R-CEL-4420097",... | [
"REACTOME:R-BTA-8951664",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-1257604",
"REACTOME:R-CEL-1433557",
"REACTOME:R-CEL-1433559",
"REACTOME:R-CEL-1592389",
"REACTOME:R-CEL-186763",
"REACTOME:R-CEL-186797",
"REACTOME:R-CEL-216083",
"REACTOME:R-CEL-2173789",
"REACTOME:R-CEL-2173796",
"REACTOME:R-... | 367 | [
"1bhg",
"1cfg",
"1ciy",
"1cx1",
"1czs",
"1czt",
"1czv",
"1d7p",
"1dlc",
"1dp0",
"1dyo",
"1eut",
"1euu",
"1f4a",
"1f4h",
"1fac",
"1gmm",
"1gny",
"1gof",
"1gog",
"1goh",
"1gqp",
"1gu3",
"1gui",
"1gwk",
"1gwl",
"1gwm",
"1h6x",
"1h6y",
"1hn0",
"1hn1",
"1i5p"... | 1,031 | [
"PUB00004093",
"PUB00005865",
"PUB00010664",
"PUB00010665"
] | [
"2002850",
"10467102",
"10586886",
"11780069"
] | [
"Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.",
"Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.",
"Crystal structures of the membrane-binding C2 domain of human coagulation factor V.",
"Crystal structure of an Eph receptor-ephrin compl... | [
1991,
1999,
1999,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1300,
223238,
219204,
622,
2513
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
321,
55,
431,
94,
4,
403,
254,
19,
173,
338,
4,
7,
438
] | 13 | true | Homologous_superfamily | Galactose-binding-like domain superfamily | Galactose-binding-like domain superfamily | Galactose-bd-like_sf | 6 |
IPR008980 | 8,980 | Viral capsid/haemagglutinin protein | Capsid_hemagglutn | Homologous_superfamily | 160,611 | false | false | Representatives of this viral protein domain are found in the vp7 capsid protein of Bluetongue virus [ ], and African horsesickness virus [ ], the vp6 capsid protein of Bovine rotavirus [ ], and in the haemagglutinin protein of various influenza viruses [ , ]. The vp7 and vp6 capsid proteins each consist of two domains... | [
"GO:0046789",
"GO:0019064",
"GO:0019031"
] | [
"host cell surface receptor binding",
"fusion of virus membrane with host plasma membrane",
"viral envelope"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"SSF"
] | [
"SSF49818"
] | [
""
] | [
160611
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] | [
"R-HSA-168255",
"R-HSA-168275",
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"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168316",
"R-HSA-168336",
"R-HSA-168874",
"R-HSA-192823",
"R-HSA-198933"
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"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-168336",
"REACTOME:R-HSA-168874",
"REACTOME:R-HSA-192823",
"REACTOME:R-HSA-198933"
] | 11 | [
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"1qhd",
"1rd8",
"1ru7",
"1ruy",
"1ruz",
"1rv0",
"1rvt",
"1rvx",
"1rvz"... | 840 | [
"PUB00003521",
"PUB00004198",
"PUB00010622",
"PUB00010666",
"PUB00010667"
] | [
"8648715",
"7816101",
"11285213",
"11867515",
"9817207"
] | [
"Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7.",
"The crystal structure of bluetongue virus VP7.",
"Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion.",
"H5 avian and H9 swine influenza v... | [
1996,
1995,
2001,
2002,
1998
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
24,
10,
160577
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Viral capsid/haemagglutinin protein | Viral capsid/haemagglutinin protein | Capsid_hemagglutn | 3 |
IPR008981 | 8,981 | F-MuLV receptor-binding | FMuLV_rcpt-bd | Homologous_superfamily | 2,652 | false | false | The F-MuLV receptor-binding domain forms part of the retroviral envelope glycoprotein in the murine leukaemia virus. Envelope glycoproteins are synthesized as single chain precursors, which are subsequently cleaved into the surface subunit (SU) and the transmembrane subunit TM. The N-terminal half of SU forms the recep... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.90.310.10",
"SSF49830"
] | [
"",
""
] | [
2611,
2643
] | 2 | [] | [] | [] | 0 | [
"1aol",
"1lcs",
"6w5y",
"9fqt",
"9fqu",
"9fqv",
"9fqw"
] | 7 | [
"PUB00010668",
"PUB00010669"
] | [
"9287219",
"12634359"
] | [
"Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.",
"Distinct mechanisms of neutralization by monoclonal antibodies specific for sites in the N-terminal or C-terminal domain of murine leukemia virus SU."
] | [
1997,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota",
"Retroviridae"
] | [
959,
2,
1691
] | 3 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
61,
10
] | 3 | true | Homologous_superfamily | F-MuLV receptor-binding | F-MuLV receptor-binding | FMuLV_rcpt-bd | 7 |
IPR008982 | 8,982 | Adenovirus pIV-like, attachment domain | Adenovirus_pIV-like_att | Homologous_superfamily | 1,572 | false | false | The viral attachment protein domain forms part of the fibre proteins in adenoviruses [ ], and the sigma 1 protein in reoviruses [ ]. Both proteins are trimers that contain fibrous tails and globular heads (reovirus), or knobs (adenovirus), which are structurally very similar. Both domain cores consist of eight anti-par... | [
"GO:0007155",
"GO:0019058",
"GO:0019062"
] | [
"cell adhesion",
"viral life cycle",
"virion attachment to host cell"
] | [
"biological_process",
"biological_process",
"biological_process"
] | 3 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.60.90.10",
"SSF49835"
] | [
"",
""
] | [
1239,
1572
] | 2 | [] | [] | [] | 0 | [
"1h7z",
"1kac",
"1kke",
"1knb",
"1nob",
"1p69",
"1p6a",
"1qhv",
"1qiu",
"1uxa",
"1uxb",
"1uxe",
"1zru",
"2bsd",
"2bse",
"2bzu",
"2bzv",
"2f0c",
"2j12",
"2j1k",
"2j2j",
"2o39",
"2oj5",
"2oj6",
"2qlk",
"2w9l",
"2wbv",
"2wbw",
"2wgt",
"2wgu",
"2wst",
"2wzp"... | 115 | [
"PUB00010670",
"PUB00010671",
"PUB00010720"
] | [
"11782420",
"11437664",
"10567268"
] | [
"Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber.",
"Structure of the fiber head of Ad3, a non-CAR-binding serotype of adenovirus.",
"Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR."
] | [
2002,
2001,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
39,
3,
1530
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Adenovirus pIV-like, attachment domain | Adenovirus pIV-like, attachment domain | Adenovirus_pIV-like_att | 4 |
IPR008983 | 8,983 | Tumour necrosis factor-like domain superfamily | Tumour_necrosis_fac-like_dom | Homologous_superfamily | 63,521 | false | false | The tumour necrosis factor (TNF)-like domains are found in both TNF and C1q protein families. Structurally these domains self-associate to make a compact bell-shaped homotrimer, each monomer being composed of an anti-parallel β-sheet sandwich with a jellyroll topology. Both TNF and C1q family members can be expressed a... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.60.120.40",
"SSF49842"
] | [
"",
""
] | [
62171,
59856
] | 2 | [
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-166663",
"R-BTA-173623",
"R-BTA-5668541",
"R-BTA-5669034",
"R-BTA-5676594",
"R-BTA-977606",
"R-CFA-198933",
"R-CFA-5357786",
"R-CFA-5357905",
"R-CFA-5357956",
"R-CFA-5626978",
"R-CFA-5668541",
"R-CFA-5669034",
"R-CFA-5676594",
"R-CFA-75893",
"R-DDI-114608",
"R-DDI-434313",
"... | [
"REACTOME:R-BTA-166663",
"REACTOME:R-BTA-173623",
"REACTOME:R-BTA-5668541",
"REACTOME:R-BTA-5669034",
"REACTOME:R-BTA-5676594",
"REACTOME:R-BTA-977606",
"REACTOME:R-CFA-198933",
"REACTOME:R-CFA-5357786",
"REACTOME:R-CFA-5357905",
"REACTOME:R-CFA-5357956",
"REACTOME:R-CFA-5626978",
"REACTOME:R-... | 115 | [
"1a8m",
"1aly",
"1c28",
"1c3h",
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"1o91",
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"1s55",
"1tnf",
"1tnr",
"1u5x",
"1u5y",
"1u5z",
"1wck",
"1xu1",
"1xu2"... | 199 | [
"PUB00010301",
"PUB00010672",
"PUB00010673",
"PUB00010674",
"PUB00010675",
"PUB00010676",
"PUB00088215"
] | [
"8589998",
"9442056",
"10651627",
"11733492",
"11862220",
"11839302",
"22449980"
] | [
"2 A crystal structure of an extracellular fragment of human CD40 ligand.",
"High resolution crystal structure of a human tumor necrosis factor-alpha mutant with low systemic toxicity.",
"A unique zinc-binding site revealed by a high-resolution X-ray structure of homotrimeric Apo2L/TRAIL.",
"Crystal structure... | [
1995,
1998,
2000,
2002,
2002,
2002,
2012
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
17,
5800,
57034,
477,
193
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
177,
1,
183,
152,
164
] | 6 | true | Homologous_superfamily | Tumour necrosis factor-like domain superfamily | Tumour necrosis factor-like domain superfamily | Tumour_necrosis_fac-like_dom | 6 |
IPR008984 | 8,984 | SMAD/FHA domain superfamily | SMAD_FHA_dom_sf | Homologous_superfamily | 189,024 | false | false | FHA and SMAD (MH2) domains share a common structure consisting of a sandwich of eleven β-strands in two sheets with Greek key topology. Forkhead-associated (FHA) domains were originally identified as a sequence profile of about 75 amino acids, whereas the full-length domain is closer to about 150 amino acids. FHA domai... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF49879"
] | [
""
] | [
189024
] | 1 | [
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1169408",
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"R-BTA-3270619",
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"R-BTA-918233",
"R-BTA-933541",
"R-BTA-936440",
"R-BTA-936964",
"... | [
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"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-5693571",
"REACTOME:R-BTA-5693607",
"REACTOME:R-BTA-69473",
"REACTOME:R-... | 285 | [
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"1k3n",
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"1khu",
"1khx",
"1lgp",
"1lgq",
"1mjs",
"1mk2",
"1mr1",
"1mzk",
"1qu5",
"1qwt",
"1r21",
"1u7f"... | 177 | [
"PUB00010677",
"PUB00010678",
"PUB00010679",
"PUB00010680",
"PUB00010681",
"PUB00010682",
"PUB00030421"
] | [
"11106755",
"12121644",
"12049740",
"11779503",
"9214508",
"11483516",
"14555996"
] | [
"The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.",
"Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.",
"Structural and functional versatility of the FHA domain in DNA-damag... | [
2000,
2002,
2002,
2001,
1997,
2001,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
328,
59998,
127726,
95,
877
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
116,
44,
439,
77,
314,
174,
12,
58,
228,
15,
8,
220
] | 12 | true | Homologous_superfamily | SMAD/FHA domain superfamily | SMAD/FHA domain superfamily | SMAD_FHA_dom_sf | 9 |
IPR008987 | 8,987 | Baseplate structural protein Gp9/Gp10, N-terminal domain | Baseplate_struct_prot_Gp9/10_N | Domain | 745 | false | false | This entry represents the N-terminal domain of Gp10 and Gp9 which includes an N-terminal helix and a seven-stranded β-sandwich with unique topology. The members of this family are similar to gene products 9 (gp9) and 10 (gp10) of bacteriophage T4. Both proteins are components of the viral baseplate [ ]. Gp9 connects th... | [
"GO:0019076"
] | [
"viral release from host cell"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF07880"
] | [
"T4_gp9_10_N"
] | [
745
] | 1 | [] | [] | [] | 0 | [
"1pdp",
"1qex",
"1s2e",
"1tja",
"1zku",
"2fl8",
"2fl9",
"5hx2",
"5iv5",
"5iv7",
"9f4a",
"9f4b"
] | 12 | [
"PUB00010705",
"PUB00016498"
] | [
"10545330",
"12626685"
] | [
"The structure of bacteriophage T4 gene product 9: the trigger for tail contraction.",
"Bacteriophage T4 genome."
] | [
1999,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"Viruses",
"metagenomes"
] | [
13,
720,
12
] | 3 | [] | [] | 0 | true | Domain | Baseplate structural protein Gp9/Gp10, N-terminal domain | Baseplate structural protein Gp9/Gp10, N-terminal domain | Baseplate_struct_prot_Gp9/10_N | 8 |
IPR008990 | 8,990 | Electron transport accessory-like domain superfamily | Elect_transpt_acc-like_dom_sf | Homologous_superfamily | 8,686 | false | false | The electron transport accessory proteins adopt the β topology of an SH3 domain, with a partly opened β barrel and a 3-10 helical turn interrupting the last strand. Other proteins displaying this topology include R67 dihydrofolate reductase, which catalyses the hydration of nitriles to amides [ ], photosystem I accesso... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50090"
] | [
""
] | [
8686
] | 1 | [] | [] | [] | 0 | [
"1ahj",
"1dj7",
"1gxi",
"1ire",
"1jb0",
"1pse",
"1psf",
"1qp2",
"1qp3",
"1ugp",
"1ugq",
"1ugr",
"1ugs",
"1v29",
"1vie",
"1vif",
"2ahj",
"2cyz",
"2cz0",
"2cz1",
"2cz6",
"2cz7",
"2d0q",
"2dd4",
"2dd5",
"2dpp",
"2dxb",
"2dxc",
"2gqv",
"2o01",
"2p4t",
"2pu9"... | 240 | [
"PUB00006378",
"PUB00010711",
"PUB00010712",
"PUB00010713"
] | [
"9195885",
"10521281",
"10649999",
"12501195"
] | [
"Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold.",
"The solution structure of photosystem I accessory protein E from the cyanobacterium Nostoc sp. strain PCC 8009.",
"Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.",
"Breaking symmetry: mu... | [
1997,
1999,
2000,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Viruses",
"unclassified sequences"
] | [
6185,
2352,
38,
12,
99
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
17,
9,
19
] | 3 | true | Homologous_superfamily | Electron transport accessory-like domain superfamily | Electron transport accessory-like domain superfamily | Elect_transpt_acc-like_dom_sf | 1 |
IPR008991 | 8,991 | Translation protein SH3-like domain superfamily | Translation_prot_SH3-like_sf | Homologous_superfamily | 224,248 | false | false | This entry represents domains with SH3-like topology that are found in various proteins associated with translation machinery. The fundamental activity of the ribosome is two-fold: to decode the message of the mRNA in the small subunit, and to form a peptide bond between peptidyl-tRNA and aminoacyl-tRNA by a peptidyl t... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50104"
] | [
""
] | [
224248
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-204626",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-9629569",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-204626",
"R-CE... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-204626",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-9629569",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-BTA-... | 185 | [
"1bkb",
"1c04",
"1eif",
"1ffk",
"1iz6",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1khi",
"1kqs",
"1m1g",
"1m1h",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1npp",
"1npr",
"1nwx",
"1nwy",
"1nz9",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg"... | 2,191 | [
"PUB00010714",
"PUB00010715",
"PUB00010716",
"PUB00046010"
] | [
"10075918",
"9724718",
"9753699",
"19424157"
] | [
"The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome.",
"Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution.",
"Structure of translation initiation factor ... | [
1999,
1998,
1998,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4889,
128089,
88409,
59,
2802
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
123,
14,
24,
18,
6,
67,
37,
12,
82,
93,
18,
16,
194
] | 13 | true | Homologous_superfamily | Translation protein SH3-like domain superfamily | Translation protein SH3-like domain superfamily | Translation_prot_SH3-like_sf | 7 |
IPR008992 | 8,992 | Enterotoxin | Enterotoxin | Homologous_superfamily | 2,053 | false | false | Cholera toxin produced by Vibrio cholerae and heat-labile enterotoxin, produced by enterotoxigenic Escherichia coli, are AB5 heterohexamers, consisting of one A polypeptide and five identical B polypeptides, with an ADP-ribosylating A subunit and a GM1 receptor binding B pentamer. These toxins are among the most potent... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50203"
] | [
""
] | [
2053
] | 1 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"1an8",
"1aw7",
"1b1z",
"1b44",
"1bcp",
"1bos",
"1bxt",
"1c48",
"1c4q",
"1chp",
"1chq",
"1ck1",
"1cqf",
"1cqv",
"1ct1",
"1czg",
"1czw",
"1d1i",
"1d1k",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1djr",
"1dm0",
"1dyq",
"1eef",
"1eei",
"1efi",
"1enf",
"1esf",
"1et6"... | 296 | [
"PUB00011767"
] | [
"11395467"
] | [
"Biological and biochemical characterization of variant A subunits of cholera toxin constructed by site-directed mutagenesis."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Plasmid pIB485",
"Viruses"
] | [
1932,
4,
1,
116
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Enterotoxin | Enterotoxin | Enterotoxin | 3 |
IPR008993 | 8,993 | Tissue inhibitor of metalloproteinases-like, OB-fold | TIMP-like_OB-fold | Homologous_superfamily | 30,768 | false | false | Tissue inhibitors of metalloproteinases (TIMP) are a family of proteins that can form complexes with extracellular matrix metalloproteinases (such as collagenases) and irreversibly inactivate them [ ]. TIMP and related proteins contains a five-stranded antiparallel β-sheet that is rolled over on itself to form a closed... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.40.50.120",
"SSF50242"
] | [
"",
""
] | [
29814,
29287
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-198933",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-6798695",
"R-BTA-8957275",
"R-BTA-977606",
"R-CEL-114608",
"R-CEL-1592389",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-8957275",
"R-CFA-1592389",
"R-CFA-6798695",
"R-CFA-9839383",
"R... | [
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-977606",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-1592389",
"REACTOME:R-CEL-... | 103 | [
"1bqq",
"1br9",
"1buv",
"1d2b",
"1gxd",
"1jb3",
"1jc7",
"1oo9",
"1pxu",
"1uap",
"1uea",
"1xwe",
"2a73",
"2a74",
"2e2d",
"2i07",
"2ice",
"2icf",
"2j0t",
"2qki",
"2tmp",
"2wii",
"2win",
"2xwb",
"2xwj",
"3cki",
"3cu7",
"3frp",
"3g6j",
"3hrz",
"3hs0",
"3i70"... | 108 | [
"PUB00000392",
"PUB00002515"
] | [
"7918391",
"2793861"
] | [
"Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family.",
"Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family."
] | [
1994,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
17,
1786,
28954,
11
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
96,
7,
77,
69,
79
] | 6 | true | Homologous_superfamily | Tissue inhibitor of metalloproteinases-like, OB-fold | Tissue inhibitor of metalloproteinases-like, OB-fold | TIMP-like_OB-fold | 2 |
IPR008996 | 8,996 | Cytokine IL1/FGF | IL1/FGF | Homologous_superfamily | 31,112 | false | false | This entry includes IL-1 and FGF. The interleukin-1 (IL-1) and fibroblast growth factor (FGF, also known as heparin-binding growth factor) families share low sequence similarity (about 25% [ ]) but have very similar structures. They belong to a superfamily that also contains the Kunitz-type soybean trypsin inhibitors (... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50353"
] | [
""
] | [
31112
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-109704",
"R-BTA-1257604",
"R-BTA-190322",
"R-BTA-190370",
"R-BTA-190371",
"R-BTA-190372",
"R-BTA-190373",
"R-BTA-190375",
"R-BTA-190377",
"R-BTA-3000170",
"R-BTA-448706",
"R-BTA-5620971",
"R-BTA-5654219",
"R-BTA-5654221",
"R-BTA-5654227",
"R-BTA-5654228",
"R-BTA-5654687",
"R... | [
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-190322",
"REACTOME:R-BTA-190370",
"REACTOME:R-BTA-190371",
"REACTOME:R-BTA-190372",
"REACTOME:R-BTA-190373",
"REACTOME:R-BTA-190375",
"REACTOME:R-BTA-190377",
"REACTOME:R-BTA-3000170",
"REACTOME:R-BTA-448706",
"REACTOME:R-BTA-5... | 336 | [
"1afc",
"1axm",
"1bar",
"1bas",
"1bfb",
"1bfc",
"1bff",
"1bfg",
"1bla",
"1bld",
"1cvs",
"1djs",
"1dzc",
"1dzd",
"1e0o",
"1ev2",
"1evt",
"1fga",
"1fmm",
"1fq9",
"1g82",
"1hib",
"1hkn",
"1i1b",
"1ihk",
"1ii4",
"1iil",
"1ijt",
"1ilr",
"1ilt",
"1iob",
"1ira"... | 296 | [
"PUB00003281",
"PUB00004736",
"PUB00004737",
"PUB00005097"
] | [
"1738162",
"1707542",
"1849658",
"4071057"
] | [
"beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.",
"Three-dimensional structure of human basic fibroblast growth factor.",
"Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of i... | [
1992,
1991,
1991,
1985
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
11,
30841,
260
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
2,
108,
8,
108,
119,
125
] | 7 | true | Homologous_superfamily | Cytokine IL1/FGF | Cytokine IL1/FGF | IL1/FGF | 8 |
IPR008999 | 8,999 | Actin-crosslinking | Actin-crosslinking | Homologous_superfamily | 17,795 | false | false | This superfamily represents an actin-crosslinking domain with a β-trefoil structure, consisting of a triplet of β-hairpins packed against a six-stranded antiparallel β-barrel. Proteins containing this domain include fascin, which carries a tandem repeat of four copies of this domain, and the histidine-rich actin-bindin... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50405"
] | [
""
] | [
17795
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6785807",
"R-HSA-9662360",
"R-HSA-9662361"
] | [
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361"
] | 3 | [
"1dfc",
"1hcd",
"1hce",
"2yug",
"3llp",
"3o4a",
"3p53",
"3p6i",
"3q7w",
"3q7x",
"3q7y",
"4f34",
"4gov",
"4goy",
"4gp0",
"4gp3",
"4qkr",
"4qks",
"6b0t",
"6i0z",
"6i10",
"6i11",
"6i12",
"6i13",
"6i14",
"6i15",
"6i16",
"6i17",
"6i18",
"6zym",
"7a5p",
"7zau"... | 47 | [
"PUB00011774",
"PUB00035979",
"PUB00035980",
"PUB00035981"
] | [
"11847289",
"15992772",
"12507891",
"11996675"
] | [
"Conserved and nonconserved features of the folding pathway of hisactophilin, a beta-trefoil protein.",
"How actin crosslinking and bundling proteins cooperate to generate an enhanced cell mechanical response.",
"Fascin, an actin-bundling protein, modulates colonic epithelial cell invasiveness and differentiati... | [
2002,
2005,
2003,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"metagenomes"
] | [
3678,
13954,
13,
136,
14
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (stra... | [
34,
4,
6,
4,
18,
8,
1,
52,
17,
1,
66
] | 11 | true | Homologous_superfamily | Actin-crosslinking | Actin-crosslinking | Actin-crosslinking | 7 |
IPR009000 | 9,000 | Translation protein, beta-barrel domain superfamily | Transl_B-barrel_sf | Homologous_superfamily | 464,794 | false | false | A β-barrel of circularly permuted topology is found in many transcription proteins, including initiation and elongation factors, and also some ribosomal proteins, although in these cases the fold is elaborated with additional structures. The β-barrel domain is represented by domain 2 of the elongation factors EF-Tu [ ]... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50447"
] | [
""
] | [
464794
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-156842",
"R-BTA-156902",
"R-BTA-1799339",
"R-BTA-3371511",
"R-BTA-381042",
"R-BTA-382556",
"R-BTA-5358493",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-6798695",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-7... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-156842",
"REACTOME:R-BTA-156902",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-3371511",
"REACTOME:R-BTA-381042",
"REACTOME:R-BTA-382556",
"REACTOME:R-BTA-5358493",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-B... | 237 | [
"1aip",
"1b23",
"1d1n",
"1d2e",
"1d8t",
"1dar",
"1dg1",
"1efc",
"1efg",
"1efm",
"1eft",
"1efu",
"1elo",
"1etu",
"1exm",
"1f60",
"1ffk",
"1fnm",
"1g7c",
"1g7r",
"1g7s",
"1g7t",
"1ha3",
"1ije",
"1ijf",
"1jj2",
"1jny",
"1jqm",
"1k73",
"1k8a",
"1k9m",
"1kc8"... | 2,480 | [
"PUB00011746",
"PUB00011832",
"PUB00011834",
"PUB00011835",
"PUB00011836"
] | [
"11054294",
"11106763",
"10715211",
"11927566",
"11114334"
] | [
"Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.",
"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.",
"High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP.",
"T... | [
2000,
2000,
2000,
2002,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
8978,
264776,
185242,
102,
5696
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
216,
32,
88,
59,
11,
163,
118,
22,
126,
133,
20,
23,
326
] | 13 | true | Homologous_superfamily | Translation protein, beta-barrel domain superfamily | Translation protein, beta-barrel domain superfamily | Transl_B-barrel_sf | 2 |
IPR009001 | 9,001 | Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal | Transl_elong_EF1A/Init_IF2_C | Homologous_superfamily | 124,305 | false | false | A β barrel of circularly permuted topology is found in the C terminus of many translation elongation and initiation factors. This domain is found in the elongation factors EF1A (or EF-Tu) of both eukaryotes and prokaryotes, which functions to recognise and transport aminoacyl-tRNA to the acceptor (A) site of the riboso... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50465"
] | [
""
] | [
124305
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.5.3",
"R-BTA-156827",
"R-BTA-156842",
"R-BTA-3371511",
"R-BTA-381042",
"R-BTA-382556",
"R-BTA-6798695",
"R-BTA-72649",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72731",
"R-BTA-8876725",
"R-BTA-9840373",
"R-CEL-3371511",
"R-CEL-6798695",
"R-CEL-8876725",
"R-DDI-156827",
"R-DDI-15684... | [
"EC:3.6.5.3",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-156842",
"REACTOME:R-BTA-3371511",
"REACTOME:R-BTA-381042",
"REACTOME:R-BTA-382556",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72731",
"REACTOME:R-BTA-8876725",
"REA... | 139 | [
"1aip",
"1b23",
"1d2e",
"1d8t",
"1dg1",
"1efc",
"1efm",
"1eft",
"1efu",
"1etu",
"1exm",
"1f60",
"1g7c",
"1ha3",
"1ije",
"1ijf",
"1jny",
"1kjz",
"1kk0",
"1kk1",
"1kk2",
"1kk3",
"1ls2",
"1mj1",
"1ob2",
"1ob5",
"1qzd",
"1r5b",
"1r5n",
"1r5o",
"1s0u",
"1skq"... | 296 | [
"PUB00011832",
"PUB00011834",
"PUB00011835"
] | [
"11106763",
"10715211",
"11927566"
] | [
"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.",
"High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP.",
"The large subunit of initiation factor aIF2 is a close structural homologue of elongation factor... | [
2000,
2000,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2520,
55348,
65298,
79,
1060
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
62,
13,
43,
21,
4,
81,
33,
8,
40,
48,
5,
7,
149
] | 13 | true | Homologous_superfamily | Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal | Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal | Transl_elong_EF1A/Init_IF2_C | 9 |
IPR009003 | 9,003 | Peptidase S1, PA clan | Peptidase_S1_PA | Homologous_superfamily | 462,028 | false | false | This superfamily represents a domain found in proteases belonging to the MEROPS peptidase family S1 (clan PA). This domain has a two β-barrel structure with the active site located at the interface between the barrels. The PA clan contains both cysteine and serine proteases that can be found in plants, animals, fungi, ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50494"
] | [
""
] | [
462028
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"R-BTA-114608",
"R-BTA-140834",
"R-BTA-140837",
"R-BTA-1592389",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-166663",
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-189451",
"R-BTA-381426",
"R-BTA-6798695",
"R-BTA-75205",
"R-BTA-8957275",
"R-BTA-977606",
"R-BTA-9837999... | [
"EC:3.4.21",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-166663",
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-189451",
"RE... | 282 | [
"1a0h",
"1a0j",
"1a0l",
"1a1q",
"1a1r",
"1a2c",
"1a3b",
"1a3e",
"1a46",
"1a4w",
"1a5g",
"1a5h",
"1a5i",
"1a61",
"1a7s",
"1ab9",
"1abi",
"1abj",
"1acb",
"1ad8",
"1ae5",
"1ae8",
"1afe",
"1afq",
"1agj",
"1aht",
"1ai8",
"1aix",
"1aks",
"1amh",
"1an1",
"1anb"... | 6,295 | [
"PUB00004667",
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00076953"
] | [
"3186696",
"11517925",
"9891971",
"14725770",
"7044372"
] | [
"Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.",
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidase... | [
1988,
2001,
1998,
2004,
1982
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1223,
144076,
228199,
86252,
2278
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
82,
22,
375,
609,
4,
642,
448,
3,
197,
615,
2,
2,
149
] | 13 | true | Homologous_superfamily | Peptidase S1, PA clan | Peptidase S1, PA clan | Peptidase_S1_PA | 9 |
IPR009004 | 9,004 | Transposase, Mu, C-terminal | Transposase_Mu_C | Homologous_superfamily | 3,023 | false | false | Transposons are abundant in nature and they play critical roles in pathogenesis, the spread of antibiotic resistance, and genome evolution. Transposition involves cleavage at the 3' ends of the transposon followed by the rejoining of the 3' OH termini to a target DNA. These steps are catalyzed by transposon-encoded tra... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.30.30.130",
"SSF50610"
] | [
"",
""
] | [
2160,
2984
] | 2 | [] | [] | [] | 0 | [
"1bcm",
"1bco",
"4fcy",
"7svw",
"8aa5",
"8ea3",
"8ea4",
"8rdu",
"8rkv"
] | 9 | [
"PUB00011775"
] | [
"12535534"
] | [
"Progressive structural transitions within Mu transpositional complexes."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
2944,
9,
52,
18
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Transposase, Mu, C-terminal | Transposase, Mu, C-terminal | Transposase_Mu_C | 9 |
IPR009006 | 9,006 | Alanine racemase/group IV decarboxylase, C-terminal | Ala_racemase/Decarboxylase_C | Homologous_superfamily | 101,695 | false | false | This superfamily represents a β-barrel domain found at the C-terminal of alanine racemase ( ) and in group IV pyridoxal-5'-phosphate (PLP)-dependent decarboxylases, such as eukaryotic ornithine decarboxylase ( ), arginine decarboxylase ( ) and diaminopimelate decarboxylase ( ). These enzymes belong to the same structur... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.40.37.10",
"SSF50621"
] | [
"",
""
] | [
101648,
98743
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"5.1.1",
"5.1.1.1",
"PWY-7383",
"PWY-8040",
"PWY-8072",
"PWY-8443",
"R-BTA-350562",
"R-BTA-351202",
"R-CEL-350562",
"R-CEL-351143",
"R-CEL-351202",
"R-DDI-351143",
"R-DDI-351202",
"R-DME-350562",
"R-DME-351143",
"R-DME-351202",
"R-HSA-350562",
"R-HSA-351143",
"R-HSA-351202",
"R... | [
"EC:5.1.1",
"EC:5.1.1.1",
"METACYC:PWY-7383",
"METACYC:PWY-8040",
"METACYC:PWY-8072",
"METACYC:PWY-8443",
"REACTOME:R-BTA-350562",
"REACTOME:R-BTA-351202",
"REACTOME:R-CEL-350562",
"REACTOME:R-CEL-351143",
"REACTOME:R-CEL-351202",
"REACTOME:R-DDI-351143",
"REACTOME:R-DDI-351202",
"REACTOME... | 30 | [
"1bd0",
"1d7k",
"1epv",
"1f3t",
"1ftx",
"1hkv",
"1hkw",
"1knw",
"1ko0",
"1l6f",
"1l6g",
"1niu",
"1njj",
"1qu4",
"1rcq",
"1sft",
"1szr",
"1tuf",
"1twi",
"1vfh",
"1vfs",
"1vft",
"1xfc",
"1xqk",
"1xql",
"2dy3",
"2j66",
"2nv9",
"2nva",
"2o0t",
"2odo",
"2on3"... | 143 | [
"PUB00000440",
"PUB00006264",
"PUB00006317",
"PUB00011776",
"PUB00036036"
] | [
"9063881",
"1676385",
"7871888",
"10378276",
"16997906"
] | [
"Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.",
"Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria.",
"The sequence of a 22.4 kb DNA fragment from the left... | [
1997,
1991,
1994,
1999,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
823,
86847,
12236,
29,
1760
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
16,
2,
8,
2,
4,
12,
11,
1,
18,
15,
1,
3,
24
] | 13 | true | Homologous_superfamily | Alanine racemase/group IV decarboxylase, C-terminal | Alanine racemase/group IV decarboxylase, C-terminal | Ala_racemase/Decarboxylase_C | 3 |
IPR009009 | 9,009 | RlpA-like protein, double-psi beta-barrel domain | RlpA-like_DPBB | Domain | 46,343 | false | false | Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi β-barrel (DPBB) fold [ , ]. RlpA is a bacterial septal ring protein and a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa [ ]. It has been shown to act as a prc mutant suppressor in ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03330"
] | [
"DPBB_1"
] | [
46343
] | 1 | [] | [] | [] | 0 | [
"1n10",
"2bh0",
"2hcz",
"3d30",
"4avr",
"4fer",
"4fft",
"4fg2",
"4fg4",
"4jcw",
"4jjo",
"4js7",
"4l48",
"5ntb",
"7wvr",
"7xc8",
"8kea",
"9ms5"
] | 18 | [
"PUB00007745",
"PUB00011777",
"PUB00019439",
"PUB00041365",
"PUB00074369"
] | [
"8576052",
"10368289",
"10610264",
"16984999",
"24806796"
] | [
"Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA.",
"A six-stranded double-psi beta barrel is shared by several protein superfamilies.",
"N-ethylmaleimide-sensitive fusion protein (NSF) and CDC48 confirmed as members of the doubl... | [
1996,
1999,
1999,
2006,
2014
] | 5 | [] | [
"IPR007112",
"IPR012997"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
18997,
27100,
27,
219
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
163,
1,
1,
118,
266
] | 5 | true | Domain | RlpA-like protein, double-psi beta-barrel domain | RlpA-like protein, double-psi beta-barrel domain | RlpA-like_DPBB | 5 |
IPR009010 | 9,010 | Aspartate decarboxylase-like domain superfamily | Asp_de-COase-like_dom_sf | Homologous_superfamily | 142,501 | false | false | β-barrels are commonly observed in protein structures. They are classified in terms of two integral parameters: the number of strands in the sheet, n, and the shear number, S, a measure of the stagger of the strands in the β-sheet. These two parameters have been shown to determine the major geometrical features of β-ba... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50692"
] | [
""
] | [
142501
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-110320",
"R-CEL-204005",
"R-CEL-3371511",
"R-CEL-382556",
"R-CEL-532668",
"R-CEL-5358346",
"R-CEL-5689877",
"R-CEL-6798695",
"R-CEL-6807878",
"R-CEL-6811434",
"R-CEL-6811438",
"R-CEL-6811440",
"R-CEL-8876725",
"R-CEL-8951664",
"R-CEL-9013407",
"R-CEL-9755511",
"R-DDI-204005",
... | [
"REACTOME:R-CEL-110320",
"REACTOME:R-CEL-204005",
"REACTOME:R-CEL-3371511",
"REACTOME:R-CEL-382556",
"REACTOME:R-CEL-532668",
"REACTOME:R-CEL-5358346",
"REACTOME:R-CEL-5689877",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811434",
"REACTOME:R-CEL-6811438",
"REACTOME:R-... | 141 | [
"1aa6",
"1aw8",
"1cr5",
"1cz4",
"1cz5",
"1dmr",
"1dms",
"1e18",
"1e32",
"1e5v",
"1e60",
"1e61",
"1eu1",
"1fdi",
"1fdo",
"1g8j",
"1g8k",
"1h0h",
"1h5n",
"1kqf",
"1kqg",
"1ogy",
"1ppy",
"1pqe",
"1pqf",
"1pqh",
"1pt0",
"1pt1",
"1pyq",
"1pyu",
"1q16",
"1qcs"... | 447 | [
"PUB00011777"
] | [
"10368289"
] | [
"A six-stranded double-psi beta barrel is shared by several protein superfamilies."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5047,
116638,
18447,
17,
2352
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
23,
6,
11,
9,
15,
39,
10,
3,
8,
17,
2,
3,
45
] | 13 | true | Homologous_superfamily | Aspartate decarboxylase-like domain superfamily | Aspartate decarboxylase-like domain superfamily | Asp_de-COase-like_dom_sf | 4 |
IPR009011 | 9,011 | Mannose-6-phosphate receptor binding domain superfamily | Man6P_isomerase_rcpt-bd_dom_sf | Homologous_superfamily | 25,113 | false | false | Mannose-6-phosphate receptors (MPRs) are transmembrane proteins involved in the transport of lysosomal enzymes from the Golgi complex and the cell surface to lysosomes [ ]. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to MPRs in the Golgi apparatus and the resulting receptor-ligand complex is tr... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.70.130.10",
"SSF50911"
] | [
"",
""
] | [
23951,
23423
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-381426",
"R-BTA-432720",
"R-BTA-6811440",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8957275",
"R-BTA-9768727",
"R-BTA-9840310",
"R-HSA-381426",
"R-HSA-382556",
"R-HSA-432720",
"R-HSA-432722",
"R-HSA-532668",
"R-HSA-5358346",
"R-HSA-5362768",
"R-HSA-5678895",
"R-HSA-6798695",
... | [
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-6811440",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-9768727",
"REACTOME:R-BTA-9840310",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-382556",
"REACTOME:R-HSA-432720",
"REACTOME:R-H... | 52 | [
"1c39",
"1e6f",
"1gp0",
"1gp3",
"1gqb",
"1keo",
"1m6p",
"1q25",
"1syo",
"1sz0",
"2cnj",
"2kva",
"2kvb",
"2l21",
"2l29",
"2l2a",
"2l2g",
"2lla",
"2lvx",
"2m68",
"2m6t",
"2n1h",
"2rl7",
"2rl8",
"2rl9",
"2rlb",
"2v5n",
"2v5o",
"2v5p",
"3aih",
"3cy4",
"3k41"... | 66 | [
"PUB00002714",
"PUB00011730",
"PUB00011760",
"PUB00097535",
"PUB00097536"
] | [
"1376319",
"11867533",
"11786557",
"26062005",
"23609449"
] | [
"Gene and pseudogene of the mouse cation-dependent mannose 6-phosphate receptor. Genomic organization, expression, and chromosomal localization.",
"Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur.",
"Twists and turns of the cation-dependent mannose 6-phosphate recepto... | [
1992,
2002,
2002,
2015,
2013
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Vibrio spartinae",
"bird metagenome"
] | [
25109,
2,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
10,
3,
33,
8,
79,
30,
4,
5,
37,
4,
4,
26
] | 12 | true | Homologous_superfamily | Mannose-6-phosphate receptor binding domain superfamily | Mannose-6-phosphate receptor binding domain superfamily | Man6P_isomerase_rcpt-bd_dom_sf | 6 |
IPR009012 | 9,012 | GrpE nucleotide exchange factor, head | GrpE_head | Homologous_superfamily | 36,232 | false | false | In prokaryotes, the nucleotide exchange factor GrpE and the chaperone DnaJ are required for nucleotide binding of the molecular chaperone DnaK [ ]. The DnaK reaction cycle involves rapid peptide binding and release, which is dependent upon nucleotide binding. DnaJ accelerates the hydrolysis of ATP by DnaK, which enable... | [
"GO:0006457"
] | [
"protein folding"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.30.22.10",
"SSF51064"
] | [
"",
""
] | [
36091,
35915
] | 2 | [
"REACTOME"
] | [
"R-HSA-1268020"
] | [
"REACTOME:R-HSA-1268020"
] | 1 | [
"1dkg",
"3a6m",
"4ani",
"8gb3",
"9bls",
"9blt",
"9blu"
] | 7 | [
"PUB00005226"
] | [
"9103205"
] | [
"Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
711,
27785,
7132,
7,
597
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
17,
1,
2,
3,
1,
4,
5,
1,
11,
10,
1,
1,
20
] | 13 | true | Homologous_superfamily | GrpE nucleotide exchange factor, head | GrpE nucleotide exchange factor, head | GrpE_head | 4 |
IPR009013 | 9,013 | Attachment protein shaft domain superfamily | Attachment_protein_shaft_sf | Homologous_superfamily | 1,852 | false | false | The attachment proteins in adenoviruses and reoviruses display structural similarity, indicating similar cell-surface receptor binding strategies, even though these viruses differ from one another in design, capsid composition and genome composition [ , ]. The dsDNA adenoviruses are responsible for diseases such as pne... | [
"GO:0019062"
] | [
"virion attachment to host cell"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF51225"
] | [
""
] | [
1852
] | 1 | [] | [] | [] | 0 | [
"1kke",
"1qiu",
"1v1h",
"1v1i",
"2oj5",
"2oj6",
"3eoy",
"3izo",
"3s6x",
"3s6y",
"3s6z",
"5mhr",
"7tau",
"8on5",
"8qjx",
"8qjy",
"8qk3",
"8uut",
"9fae",
"9faf",
"9fag",
"9fah",
"9qgo"
] | 23 | [
"PUB00005680",
"PUB00010670"
] | [
"10553913",
"11782420"
] | [
"A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein.",
"Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber."
] | [
1999,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Haloarcula pellucida",
"Viruses"
] | [
127,
31,
1,
1693
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Attachment protein shaft domain superfamily | Attachment protein shaft domain superfamily | Attachment_protein_shaft_sf | 9 |
IPR009014 | 9,014 | Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II | Transketo_C/PFOR_II | Homologous_superfamily | 194,981 | false | false | Transketolase C-terminal-like domains [ ] can be found in a number of different enzymes, including the C-terminal domain of the pyruvate dehydrogenase E1 component [ ], the C-terminal domain of branched-chain alpha-keto acid dehydrogenases [ ], and domain II of pyruvate-ferredoxin oxidoreductase (PFOR) [ ]. Structural ... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.40.50.920",
"SSF52922"
] | [
"",
""
] | [
189133,
186202
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"2.2.1.7",
"PWY-6891",
"PWY-6892",
"PWY-7560",
"R-BTA-204174",
"R-BTA-5362517",
"R-BTA-70895",
"R-BTA-9837999",
"R-BTA-9859138",
"R-BTA-9861559",
"R-CEL-204174",
"R-CEL-5362517",
"R-CEL-9837999",
"R-CEL-9861559",
"R-DDI-9837999",
"R-DDI-9859138",
"R-DDI-9861559",
"R-DME-204174",
... | [
"EC:2.2.1.7",
"METACYC:PWY-6891",
"METACYC:PWY-6892",
"METACYC:PWY-7560",
"REACTOME:R-BTA-204174",
"REACTOME:R-BTA-5362517",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9859138",
"REACTOME:R-BTA-9861559",
"REACTOME:R-CEL-204174",
"REACTOME:R-CEL-5362517",
"REACTOME:R-CE... | 57 | [
"1ay0",
"1b0p",
"1dtw",
"1gpu",
"1ik6",
"1itz",
"1kek",
"1l8a",
"1ngs",
"1ni4",
"1ols",
"1olu",
"1olx",
"1qgd",
"1qs0",
"1r9j",
"1rp7",
"1tka",
"1tkb",
"1tkc",
"1trk",
"1u5b",
"1um9",
"1umb",
"1umc",
"1umd",
"1v11",
"1v16",
"1v1m",
"1v1r",
"1w85",
"1w88"... | 211 | [
"PUB00001222",
"PUB00003323",
"PUB00011731",
"PUB00011732",
"PUB00011733"
] | [
"1628611",
"8176731",
"11955070",
"10426958",
"11752578"
] | [
"Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.",
"Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution.",
"Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolu... | [
1992,
1994,
2002,
1999,
2001
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
4101,
157674,
29476,
3729,
1
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
50,
3,
5,
10,
5,
28,
8,
7,
28,
21,
5,
5,
64
] | 13 | true | Homologous_superfamily | Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II | Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II | Transketo_C/PFOR_II | 8 |
IPR009015 | 9,015 | L-fucose isomerase, N-terminal/central domain superfamily | Fucose_isomerase_N/cen_sf | Homologous_superfamily | 15,241 | false | false | L-fucose isomerase ( ) converts the aldose L-fucose into the corresponding ketose L-fuculose during the first step in fucose metabolism using Mn2+ as a cofactor. The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. L-f... | [
"GO:0016861",
"GO:0005996",
"GO:0005737"
] | [
"intramolecular oxidoreductase activity, interconverting aldoses and ketoses",
"monosaccharide metabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"SSF"
] | [
"SSF53743"
] | [
""
] | [
15241
] | 1 | [
"EC",
"EC"
] | [
"5.3.1",
"5.3.1.4"
] | [
"EC:5.3.1",
"EC:5.3.1.4"
] | 2 | [
"1fui",
"2ajt",
"2hxg",
"3a9r",
"3a9s",
"3a9t",
"4c20",
"4c21",
"4c22",
"4f2d",
"4lql",
"4r1o",
"4r1p",
"4r1q",
"6k1f",
"6k1g",
"7ch3",
"7chl",
"7cwv",
"7cx7",
"7cxo",
"7cyy"
] | 22 | [
"PUB00007428"
] | [
"9367760"
] | [
"Structure and mechanism of L-fucose isomerase from Escherichia coli."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
241,
14499,
97,
404
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Homologous_superfamily | L-fucose isomerase, N-terminal/central domain superfamily | L-fucose isomerase, N-terminal/central domain superfamily | Fucose_isomerase_N/cen_sf | 4 |
IPR009016 | 9,016 | Iron hydrogenase | Fe_hydrogenase | Homologous_superfamily | 15,802 | false | false | The iron-only hydrogenases ( ) catalyse the two-electron reduction of two protons to yield dihydrogen, as part of an energy cycle. Fe-only hydrogenases are restricted to strictly anaerobic microbes, and are often very sensitive to molecular oxygen. The cytoplasmic monomeric Fe hydrogenases are involved in hydrogen prod... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF53920"
] | [
""
] | [
15802
] | 1 | [
"REACTOME"
] | [
"R-HSA-2564830"
] | [
"REACTOME:R-HSA-2564830"
] | 1 | [
"1c4a",
"1c4c",
"1e08",
"1feh",
"1gx7",
"1hfe",
"2n0s",
"3c8y",
"3lx4",
"4r0v",
"4xdc",
"4xdd",
"5byq",
"5byr",
"5bys",
"5la3",
"5oef",
"6gl6",
"6gly",
"6glz",
"6gm0",
"6gm1",
"6gm2",
"6gm3",
"6gm4",
"6gm5",
"6gm6",
"6gm7",
"6gm8",
"6h63",
"6n59",
"6n6p"... | 70 | [
"PUB00006430",
"PUB00011734"
] | [
"10368269",
"9836629"
] | [
"Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center.",
"X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution."
] | [
1999,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
11,
8409,
6821,
2,
559
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
3,
3,
20,
3,
1,
4,
9,
1,
1,
10
] | 12 | true | Homologous_superfamily | Iron hydrogenase | Iron hydrogenase | Fe_hydrogenase | 9 |
IPR009017 | 9,017 | Green fluorescent protein | GFP | Homologous_superfamily | 7,349 | false | false | The green fluorescent-like protein family consists of fluorescent proteins and non-fluorescent chromoproteins, derived from several species of Cnidarians, as well as certain diazotrophic bacteria [ , ]. These proteins range in their absorption wavelength maximum, and are often classified by their colour: green, yellow,... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.40.155.10",
"SSF54511"
] | [
"",
""
] | [
7208,
6671
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1474228",
"R-HSA-3000157",
"R-MMU-1474228",
"R-MMU-3000157",
"R-RNO-3000157"
] | [
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-3000157",
"REACTOME:R-MMU-1474228",
"REACTOME:R-MMU-3000157",
"REACTOME:R-RNO-3000157"
] | 5 | [
"1b9c",
"1bfp",
"1c4f",
"1cv7",
"1ema",
"1emb",
"1emc",
"1eme",
"1emf",
"1emg",
"1emk",
"1eml",
"1emm",
"1f09",
"1f0b",
"1g7k",
"1gfl",
"1ggx",
"1gl4",
"1h4u",
"1h6r",
"1hcj",
"1huy",
"1jby",
"1jbz",
"1jc0",
"1jc1",
"1kp5",
"1kyp",
"1kyr",
"1kys",
"1mou"... | 1,362 | [
"PUB00007972",
"PUB00011761",
"PUB00011762"
] | [
"11427896",
"11929996",
"12502888"
] | [
"Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.",
"Diversity and evolution of the green fluorescent protein family.",
"Green fluorescent protein-like proteins in reef Anthozoa animals."
] | [
2001,
2002,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
146,
7178,
23,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
16,
1,
13,
10,
11
] | 6 | true | Homologous_superfamily | Green fluorescent protein | Green fluorescent protein | GFP | 3 |
IPR009018 | 9,018 | Signal recognition particle, SRP9/SRP14 subunit | Signal_recog_particle_SRP9/14 | Homologous_superfamily | 7,223 | false | false | The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [ , , ]. SRP recognises the signal sequence of the nascent po... | [
"GO:0008312",
"GO:0006614",
"GO:0048500"
] | [
"7S RNA binding",
"SRP-dependent cotranslational protein targeting to membrane",
"signal recognition particle"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.720.10",
"SSF54762"
] | [
"",
""
] | [
7209,
7074
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1799339",
"R-BTA-6798695",
"R-CEL-1799339",
"R-CEL-6798695",
"R-DDI-1799339",
"R-DDI-6798695",
"R-DME-1799339",
"R-HSA-1799339",
"R-HSA-6798695",
"R-MMU-1799339",
"R-MMU-6798695",
"R-SCE-1799339",
"R-SCE-6798695",
"R-SPO-1799339",
"R-SPO-6798695"
] | [
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-1799339",
"REACTOME:R-HSA-1799339",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-1799339",
"REACTOME:R-MMU-6798695",
"REACTOM... | 15 | [
"1914",
"1e8o",
"1e8s",
"1ry1",
"2w9j",
"3jaj",
"3jan",
"4ue5",
"4uyj",
"4uyk",
"5aox",
"6frk",
"6r6g",
"7nfx",
"7obr"
] | 15 | [
"PUB00011467",
"PUB00028143",
"PUB00035998",
"PUB00035999",
"PUB00053948",
"PUB00063486",
"PUB00100261"
] | [
"7730321",
"16469117",
"17622352",
"17507650",
"12364595",
"12605305",
"34020957"
] | [
"Human signal recognition particle (SRP) Alu-associated protein also binds Alu interspersed repeat sequence RNAs. Characterization of human SRP9.",
"Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.",
"X-ray structures of the signal recognition... | [
1995,
2006,
2007,
2007,
2002,
2003,
2021
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
7223
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
2,
2,
4,
8,
6,
1,
3,
7,
1,
2,
17
] | 12 | true | Homologous_superfamily | Signal recognition particle, SRP9/SRP14 subunit | Signal recognition particle, SRP9/SRP14 subunit | Signal_recog_particle_SRP9/14 | 9 |
IPR009019 | 9,019 | K homology domain superfamily, prokaryotic type | KH_sf_prok-type | Homologous_superfamily | 114,079 | false | false | The K homology domain is a common RNA-binding motif present in one or multiple copies in both prokaryotic and eukaryotic regulatory proteins. The KH motifs may act cooperatively to bind RNA in the case of multiple motifs, or independently in the case of single KH motif proteins. Prokaryotic (pKH) and eukaryotic (eKH) K... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF54814"
] | [
""
] | [
114079
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-9759... | 128 | [
"1ega",
"1fjg",
"1hh2",
"1hnw",
"1hnx",
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"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
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"1j5e",
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"1n34",
"1n36",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1wf3",
"1wh9"... | 1,778 | [
"PUB00011737",
"PUB00011738",
"PUB00011739"
] | [
"11014182",
"10411886",
"11430821"
] | [
"Structure of the 30S ribosomal subunit.",
"Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif.",
"An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA."
] | [
2000,
1999,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
3202,
82760,
25959,
3,
2155
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
23,
2,
2,
3,
3,
18,
13,
1,
14,
25,
1,
1,
41
] | 13 | true | Homologous_superfamily | K homology domain superfamily, prokaryotic type | K homology domain superfamily, prokaryotic type | KH_sf_prok-type | 2 |
IPR009022 | 9,022 | Elongation factor G, domain III | EFG_III | Domain | 44,131 | false | false | EF2 (or EFG) participates in the elongation phase of protein synthesis by promoting the GTP-dependent translocation of the peptidyl tRNA of the nascent protein chain from the A-site (acceptor site) to the P-site (peptidyl tRNA site) of the ribosome. EF2 also has a role after the termination phase of translation, where,... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd16262"
] | [
"EFG_III"
] | [
44131
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5419276",
"R-CEL-5389840",
"R-DME-5389840",
"R-DME-5419276",
"R-DRE-5389840",
"R-HSA-5389840",
"R-HSA-5419276",
"R-MMU-5389840",
"R-MMU-5419276",
"R-RNO-5389840",
"R-RNO-5419276"
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"REACTOME:R-CEL-5389840",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DRE-5389840",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOME:R-RNO-5389840",
"REACTOME:R-RNO-5419276"
] | 11 | [
"1dar",
"1efg",
"1elo",
"1fnm",
"1jqm",
"1ktv",
"1pn6",
"1wdt",
"1zn0",
"2bm0",
"2bm1",
"2bv3",
"2dy1",
"2efg",
"2j7k",
"2mzw",
"2om7",
"2rdo",
"2xex",
"3izp",
"3j0e",
"3j9z",
"3ja1",
"3zz0",
"3zzt",
"3zzu",
"4fn5",
"4m1k",
"4myt",
"4myu",
"4v5f",
"4v5m"... | 110 | [
"PUB00011746",
"PUB00014828"
] | [
"11054294",
"12471894"
] | [
"Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.",
"Translational elongation factor G: a GTP-driven motor of the ribosome."
] | [
2000,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
9,
34668,
8898,
2,
554
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
12,
2,
3,
4,
1,
6,
5,
2,
6,
9,
2,
2,
14
] | 13 | true | Domain | Elongation factor G, domain III | Elongation factor G, domain III | EFG_III | 8 |
IPR009023 | 9,023 | Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain superfamily | HMG_CoA_Rdtase_NAD(P)-bd_sf | Homologous_superfamily | 15,087 | false | false | There are two distinct classes of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase enzymes: class I consists of eukaryotic and most archaeal enzymes ( ), while class II consists of prokaryotic enzymes ( ) [ , ]. Class I HMG-CoA reductases catalyse the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-methylgl... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.70.420",
"SSF55035"
] | [
"",
""
] | [
10462,
14836
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME"
] | [
"1.1.1.34",
"PWY-6174",
"PWY-7391",
"PWY-7524",
"PWY-8125",
"PWY-922",
"R-BTA-191273",
"R-DDI-191273",
"R-DME-191273",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-HSA-9619665",
"R-MMU-191273",
"R-RNO-191273",
"R-SCE-191273",
"R-SPO-191273"
] | [
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"METACYC:PWY-6174",
"METACYC:PWY-7391",
"METACYC:PWY-7524",
"METACYC:PWY-8125",
"METACYC:PWY-922",
"REACTOME:R-BTA-191273",
"REACTOME:R-DDI-191273",
"REACTOME:R-DME-191273",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-9619665",
... | 17 | [
"1dq8",
"1dq9",
"1dqa",
"1hw8",
"1hw9",
"1hwi",
"1hwj",
"1hwk",
"1hwl",
"1qax",
"1qay",
"1r31",
"1r7i",
"1t02",
"2q1l",
"2q6b",
"2q6c",
"2r4f",
"3bgl",
"3cct",
"3ccw",
"3ccz",
"3cd0",
"3cd5",
"3cd7",
"3cda",
"3cdb",
"3qae",
"3qau",
"4i4b",
"4i56",
"4i64"... | 53 | [
"PUB00011747",
"PUB00019711",
"PUB00036052",
"PUB00036053",
"PUB00036054"
] | [
"10698924",
"15535874",
"10068515",
"10600463",
"15028676"
] | [
"Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.",
"The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.",
"Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase.",
"Expression and charac... | [
2000,
2004,
1999,
1999,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Marseilleviridae",
"unclassified sequences"
] | [
945,
5993,
8034,
2,
113
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
1,
7,
3,
7,
6,
1,
10,
7,
2,
1,
31
] | 12 | true | Homologous_superfamily | Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain superfamily | Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain superfamily | HMG_CoA_Rdtase_NAD(P)-bd_sf | 5 |
IPR009024 | 9,024 | Methyl-coenzyme M reductase, ferredoxin-like fold | Me_CoM_Rdtase_Fd-like_fold | Homologous_superfamily | 2,558 | false | false | Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-... | [
"GO:0050524",
"GO:0015948"
] | [
"coenzyme-B sulfoethylthiotransferase activity",
"methanogenesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF55088"
] | [
""
] | [
2558
] | 1 | [
"EC"
] | [
"2.8.4.1"
] | [
"EC:2.8.4.1"
] | 1 | [
"1e6v",
"1e6y",
"1hbm",
"1hbn",
"1hbo",
"1hbu",
"1mro",
"3m1v",
"3m2r",
"3m2u",
"3m2v",
"3m30",
"3m32",
"3pot",
"3sqg",
"5a0y",
"5a8k",
"5a8r",
"5a8w",
"5g0r",
"5n1q",
"5n28",
"5n2a",
"7b1s",
"7b2c",
"7b2h",
"7nkg",
"7suc",
"7sxm",
"8gf5",
"8gf6",
"8s7v"... | 39 | [
"PUB00006391",
"PUB00010614",
"PUB00035993",
"PUB00035994"
] | [
"9367957",
"11491299",
"16260307",
"16234924"
] | [
"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.",
"On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.",
"Methyl-coenzyme M reductase genes: unique functional ma... | [
1997,
2001,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Nicrophorus vespilloides",
"unclassified sequences"
] | [
2392,
18,
1,
147
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Methyl-coenzyme M reductase, ferredoxin-like fold | Methyl-coenzyme M reductase, ferredoxin-like fold | Me_CoM_Rdtase_Fd-like_fold | 1 |
IPR009025 | 9,025 | DNA-directed RNA polymerase, RBP11-like dimerisation domain | RBP11-like_dimer | Domain | 9,852 | false | false | RNA polymerase (RNAP) II, which is responsible for all mRNA synthesis in eukaryotes, consists of 12 subunits. Subunits Rpb3 and Rpb11 form a heterodimer that is functionally analogous to the archaeal RNAP D/L heterodimer, and the prokaryotic RNAP alpha subunit homodimer. In each case, they play a key role in RNAP assem... | [
"GO:0046983",
"GO:0006351"
] | [
"protein dimerization activity",
"DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF13656"
] | [
"RNA_pol_L_2"
] | [
9852
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-112382",
"R-BTA-113418",
"R-BTA-5578749",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",
"R-BTA-759... | [
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-72086",
"REACTOME:R-B... | 182 | [
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1xpp",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 548 | [
"PUB00005231",
"PUB00008731",
"PUB00011749",
"PUB00013986",
"PUB00013987",
"PUB00097382"
] | [
"9657722",
"11313498",
"12000971",
"12191485",
"11453250",
"16537912"
] | [
"Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain.",
"Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.",
"Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution.",
"Structure of the yeast RNA polymerase II holoenzyme: ... | [
1998,
2001,
2002,
2002,
2001,
2006
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Candidatus Buchananbacteria bacterium RIFCSPHIGHO2_01_FULL_39_14",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
895,
1,
8748,
65,
143
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
2,
2,
9,
12,
7,
3,
8,
5,
2,
2,
26
] | 12 | true | Domain | DNA-directed RNA polymerase, RBP11-like dimerisation domain | DNA-directed RNA polymerase, RBP11-like dimerisation domain | RBP11-like_dimer | 8 |
IPR009027 | 9,027 | Large ribosomal subunit protein bL9/RNase H1, N-terminal | Ribosomal_bL9/RNase_H1_N | Homologous_superfamily | 40,583 | false | false | The N-terminal domain of the large ribosomal subunit protein bL9 (previously known as ribosomal protein L9) is a regulatory RNA-binding module that binds to 23rRNA. bL9 is composed of two domains and functions as a structural protein in the large subunit of the ribosome. The N-terminal domain of eukaryotic RNase HI, wh... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF55658"
] | [
""
] | [
40583
] | 1 | [
"REACTOME",
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
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"R-BTA-5419276",
"R-BTA-9937383",
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"R-DME-5419276",
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"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383",
"R-RNO-5389840",
"R-RNO-5419276",
"R-RNO-99373... | [
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"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9913635",
"REACTOME:R-HSA-9937383",
"REACTOM... | 17 | [
"1cqu",
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"3j8g",
"3j9m",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd"... | 1,056 | [
"PUB00001252",
"PUB00011751"
] | [
"8306963",
"10448044"
] | [
"Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.",
"NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9."
] | [
1994,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"unclassified sequences"
] | [
26965,
12804,
21,
209,
584
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
13,
4,
3,
4,
1,
9,
7,
2,
7,
12,
1,
2,
28
] | 13 | true | Homologous_superfamily | Large ribosomal subunit protein bL9/RNase H1, N-terminal | Large ribosomal subunit protein bL9/RNase H1, N-terminal | Ribosomal_bL9/RNase_H1_N | 9 |
IPR009028 | 9,028 | Coatomer/calthrin adaptor appendage, C-terminal subdomain | Coatomer/calthrin_app_sub_C | Homologous_superfamily | 18,199 | false | false | Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. This traffic is bidirectional, to ensure that proteins required to form vesicles ar... | [
"GO:0006886",
"GO:0016192",
"GO:0030117"
] | [
"intracellular protein transport",
"vesicle-mediated transport",
"membrane coat"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"SSF"
] | [
"SSF55711"
] | [
""
] | [
18199
] | 1 | [
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"REACTOM... | [
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"R-BTA-8964038",
"R-CEL-6807878",
"R-CEL-6811434",
"R-DDI-432720",
"R-DDI-437239",
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"REACTOME:R-BTA-6811434",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R... | 107 | [
"1b9k",
"1e42",
"1ky6",
"1ky7",
"1kyd",
"1kyf",
"1kyu",
"1pzd",
"1qtp",
"1qts",
"1r4x",
"1w80",
"2g30",
"2iv8",
"2iv9",
"2mj7",
"2vj0",
"3h1z",
"3hs8",
"3hs9",
"5a1u",
"5a1v",
"5a1w",
"5a1x",
"5a1y",
"5nzr",
"5nzs",
"5nzt",
"5nzu",
"5nzv",
"6owt",
"6yaf"... | 49 | [
"PUB00011753",
"PUB00011791",
"PUB00029720",
"PUB00030524",
"PUB00035753",
"PUB00035768",
"PUB00035769"
] | [
"10944104",
"10430869",
"12858162",
"14690497",
"17449236",
"17041781",
"15261670"
] | [
"The structure and function of the beta 2-adaptin appendage domain.",
"Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.",
"Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3.",
"Gamma-COP appendage domain - structure and f... | [
2000,
1999,
2003,
2004,
2007,
2006,
2004
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
18199
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
23,
6,
25,
7,
31,
20,
2,
16,
36,
2,
2,
95
] | 12 | true | Homologous_superfamily | Coatomer/calthrin adaptor appendage, C-terminal subdomain | Coatomer/calthrin adaptor appendage, C-terminal subdomain | Coatomer/calthrin_app_sub_C | 8 |
IPR009029 | 9,029 | Hydroxymethylglutaryl-CoA reductase, class I/II, substrate-binding domain superfamily | HMG_CoA_Rdtase_sub-bd_dom_sf | Homologous_superfamily | 15,412 | false | false | There are two distinct classes of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase enzymes: class I consists of eukaryotic and most archaeal enzymes ( ), while class II consists of prokaryotic enzymes ( ) [ , ]. Class I HMG-CoA reductases catalyse the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-methylgl... | [
"GO:0016616",
"GO:0015936"
] | [
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"coenzyme A metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF56542"
] | [
""
] | [
15412
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.34",
"PWY-6174",
"PWY-7391",
"PWY-7524",
"PWY-8125",
"PWY-922",
"R-BTA-191273",
"R-DDI-191273",
"R-DME-191273",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-HSA-9619665",
"R-MMU-191273",
"R-RNO-191273",
"R-SCE-191273",
"R-SPO-191273"
] | [
"EC:1.1.1.34",
"METACYC:PWY-6174",
"METACYC:PWY-7391",
"METACYC:PWY-7524",
"METACYC:PWY-8125",
"METACYC:PWY-922",
"REACTOME:R-BTA-191273",
"REACTOME:R-DDI-191273",
"REACTOME:R-DME-191273",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-9619665",
... | 17 | [
"1dq8",
"1dq9",
"1dqa",
"1hw8",
"1hw9",
"1hwi",
"1hwj",
"1hwk",
"1hwl",
"1qax",
"1qay",
"1r31",
"1r7i",
"1t02",
"2q1l",
"2q6b",
"2q6c",
"2r4f",
"3bgl",
"3cct",
"3ccw",
"3ccz",
"3cd0",
"3cd5",
"3cd7",
"3cda",
"3cdb",
"3qae",
"3qau",
"4i4b",
"4i56",
"4i64"... | 53 | [
"PUB00011747",
"PUB00011748",
"PUB00019711",
"PUB00036052",
"PUB00036053",
"PUB00036054"
] | [
"10698924",
"10377386",
"15535874",
"10068515",
"10600463",
"15028676"
] | [
"Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.",
"Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.",
"The 3-hy... | [
2000,
1999,
2004,
1999,
1999,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
975,
5957,
8330,
3,
147
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
7,
3,
7,
6,
1,
12,
7,
2,
1,
33
] | 12 | true | Homologous_superfamily | Hydroxymethylglutaryl-CoA reductase, class I/II, substrate-binding domain superfamily | Hydroxymethylglutaryl-CoA reductase, class I/II, substrate-binding domain superfamily | HMG_CoA_Rdtase_sub-bd_dom_sf | 3 |
IPR009030 | 9,030 | Growth factor receptor cysteine-rich domain superfamily | Growth_fac_rcpt_cys_sf | Homologous_superfamily | 213,620 | false | false | This growth factor receptor domain is a cysteine-rich region that is found in a variety of eukaryotic proteins that are involved in the mechanism of signal transduction by receptor tyrosine kinases. Proteins containing the growth factor receptor domain include the insulin-like growth factor-binding proteins (IGFBP) [ ]... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF57184"
] | [
""
] | [
213620
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-140837",
"R-BTA-140875",
"R-BTA-1474228",
"R-BTA-1566948",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-166665",
"R-BTA-202733",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA-2173789",
"R-BTA-381426",
"R-BTA-4641263",
"R-BTA-6803211",
"R-BTA-8856825",
"R-... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-140875",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-... | 527 | [
"1boe",
"1emn",
"1emo",
"1h59",
"1hj7",
"1hz8",
"1i0u",
"1igr",
"1ivo",
"1m6b",
"1mox",
"1n7d",
"1n8y",
"1n8z",
"1nql",
"1s78",
"1toz",
"1wqj",
"1yy9",
"2a91",
"2ahx",
"2bo2",
"2bou",
"2box",
"2dsp",
"2dsq",
"2dsr",
"2hr7",
"2vj3",
"2w2m",
"2w2n",
"2w2o"... | 341 | [
"PUB00004283",
"PUB00011763",
"PUB00011765",
"PUB00076912"
] | [
"9690478",
"11447105",
"12154198",
"7567962"
] | [
"Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor.",
"The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5.",
"Structure of the extracellular region of HER3 reveals an interdomain tether.",
"Insulin and epidermal growth factor rece... | [
1998,
2001,
2002,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
33,
680,
212809,
41,
57
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
70,
603,
365,
556,
346,
68,
546,
62
] | 8 | true | Homologous_superfamily | Growth factor receptor cysteine-rich domain superfamily | Growth factor receptor cysteine-rich domain superfamily | Growth_fac_rcpt_cys_sf | 8 |
IPR009031 | 9,031 | Carbohydrate binding module family 10 | CBM10 | Domain | 311 | false | false | Plant cell wall hydrolases from aerobic microorganisms generally have a modular structure consisting of a catalytic domain linked to one or more carbohydrate-binding modules (CBMs). CBMs function to attach the enzyme to the polymeric substrate, thereby increasing the catalytic activity. Most CBMs bind cellulose and are... | [
"GO:0030248",
"GO:0005975"
] | [
"cellulose binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SMART"
] | [
"SM01064"
] | [
"CBM_10"
] | [
311
] | 1 | [] | [] | [] | 0 | [
"1e8r",
"1qld"
] | 2 | [
"PUB00011754"
] | [
"10653641"
] | [
"Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A."
] | [
2000
] | 1 | [
"IPR002883"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
272,
39
] | 2 | [] | [] | 0 | true | Domain | Carbohydrate binding module family 10 | Carbohydrate binding module family 10 | CBM10 | 5 |
IPR009033 | 9,033 | Calreticulin/calnexin, P domain superfamily | Calreticulin/calnexin_P_dom_sf | Homologous_superfamily | 12,872 | false | false | The type-I integral membrane protein calnexin (CNX) and its soluble paralog calreticulin (CRT) are members of a family of molecular chaperones that function in the endoplasmic reticulum (ER) of eukaryotic cells. These calcium-binding proteins are lectins that bind newly synthesised N-linked glycoproteins to help promot... | [
"GO:0005509",
"GO:0005515"
] | [
"calcium ion binding",
"protein binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.10.250.10",
"SSF63887"
] | [
"",
""
] | [
12592,
12819
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-901042",
"R-DDI-901042",
"R-DME-901042",
"R-HSA-1236974",
"R-HSA-168316",
"R-HSA-2132295",
"R-HSA-3000480",
"R-HSA-3000484",
"R-HSA-381183",
"R-HSA-8984722",
"R-HSA-901042",
"R-HSA-9020956",
"R-HSA-9683686",
"R-HSA-9694548",
"R-HSA-9768727",
"R-HSA-983170",
"R-MMU-1236974",
... | [
"REACTOME:R-CEL-901042",
"REACTOME:R-DDI-901042",
"REACTOME:R-DME-901042",
"REACTOME:R-HSA-1236974",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-3000480",
"REACTOME:R-HSA-3000484",
"REACTOME:R-HSA-381183",
"REACTOME:R-HSA-8984722",
"REACTOME:R-HSA-901042",
"REACTOME:R-HS... | 38 | [
"1hhn",
"1jhn",
"1k91",
"1k9c",
"3ici",
"3rg0",
"5v8z",
"5v90",
"6eny",
"7qpd",
"8rjc",
"8rjd",
"8tzo",
"8tzr"
] | 14 | [
"PUB00010698",
"PUB00011766"
] | [
"11583625",
"11248044"
] | [
"The Structure of calnexin, an ER chaperone involved in quality control of protein folding.",
"NMR structure of the calreticulin P-domain."
] | [
2001,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrosotalea"
] | [
6,
12864,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
32,
3,
9,
12,
27,
13,
1,
18,
21,
1,
1,
50
] | 12 | true | Homologous_superfamily | Calreticulin/calnexin, P domain superfamily | Calreticulin/calnexin, P domain superfamily | Calreticulin/calnexin_P_dom_sf | 1 |
IPR009034 | 9,034 | Fungal dockerin domain superfamily | Dockerin_dom_fun_sf | Homologous_superfamily | 1,022 | false | false | In anaerobic microorganisms, the degradation of plant cell walls in order to recycle the photosynthetically fixed carbon is carried out by a multifunctional complex termed the cellulosome. This consists of a number of independent enzyme components, each of which contains a conserved dockerin domain, which functions to ... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.90.1220.10",
"SSF64571"
] | [
"",
""
] | [
1020,
1012
] | 2 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1e8p",
"1e8q",
"2j4m",
"2j4n"
] | 4 | [
"PUB00010608"
] | [
"11524680"
] | [
"Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Fungi"
] | [
1022
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Fungal dockerin domain superfamily | Fungal dockerin domain superfamily | Dockerin_dom_fun_sf | 4 |
IPR009038 | 9,038 | GOLD domain | GOLD_dom | Domain | 45,208 | false | false | The GOLD (for Golgi dynamics) domain is a protein module found in several eukaryotic Golgi and lipid-traffic proteins. It is typically between 90 and 150 amino acids long. Most of the size difference observed in the GOLD-domain superfamily is traceable to a single large low-complexity insert that is seen in some versio... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01105",
"PF13897",
"PS50866",
"SM01190"
] | [
"EMP24_GP25L",
"GOLD_2",
"GOLD",
"EMP24_GP25L"
] | [
29766,
3396,
41987,
28124
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50866",
"R-BTA-204005",
"R-BTA-3238698",
"R-BTA-5694530",
"R-BTA-6807878",
"R-BTA-6811434",
"R-CEL-1912420",
"R-CEL-6807878",
"R-CEL-6811434",
"R-DDI-6807878",
"R-DDI-6811434",
"R-DME-6807878",
"R-DME-6811434",
"R-HSA-1912420",
"R-HSA-204005",
"R-HSA-3238698",
"R-HSA-432722",
... | [
"PROSITEDOC:PDOC50866",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-3238698",
"REACTOME:R-BTA-5694530",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811434",
"REACTOME:R-CEL-1912420",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811434",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-6811434",
"REACTOME:R... | 39 | [
"1o6u",
"1olm",
"4tlg",
"4uyb",
"5azw",
"5azx",
"5azy",
"5gu5",
"5lz1",
"5lz3",
"5lz6",
"5tdq",
"6hln",
"6hlt",
"6hlv",
"6hlw",
"6hm8",
"6hmv",
"6q67",
"6q68",
"6q69",
"7rrm",
"9cjk",
"9cjl"
] | 24 | [
"PUB00011844",
"PUB00160400"
] | [
"12049664",
"36493393"
] | [
"The GOLD domain, a novel protein module involved in Golgi function and secretion.",
"SEC14-GOLD protein PATELLIN2 binds IRON-REGULATED TRANSPORTER1 linking root iron uptake to vitamin E."
] | [
2002,
2023
] | 2 | [] | [
"IPR056794"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
23,
204,
44973,
8
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
82,
20,
40,
17,
69,
55,
4,
43,
70,
9,
5,
76
] | 12 | true | Domain | GOLD domain | GOLD domain | GOLD_dom | 2 |
IPR009039 | 9,039 | EAR | EAR | Repeat | 6,626 | false | false | Most of the hereditary idiopathic epilepsies are due to mutation in ion channels expressed in brain. Recently two non-ion channel genes LGI1 and VGLR1 have emerged as important causes of specific epilepsy syndromes. The product of these two genes share a conserved repeated region of about 44 amino acid residues, the EA... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50912"
] | [
"EAR"
] | [
6626
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50912",
"R-BTA-5682910",
"R-HSA-5682910",
"R-HSA-9619665",
"R-MMU-5682910",
"R-RNO-5682910"
] | [
"PROSITEDOC:PDOC50912",
"REACTOME:R-BTA-5682910",
"REACTOME:R-HSA-5682910",
"REACTOME:R-HSA-9619665",
"REACTOME:R-MMU-5682910",
"REACTOME:R-RNO-5682910"
] | 6 | [
"5y2z",
"5y31",
"8hpy",
"8hq1",
"8hq2",
"8y6b",
"9kzc",
"9kzt"
] | 8 | [
"PUB00011794",
"PUB00011796"
] | [
"12095917",
"11545713"
] | [
"A common protein interaction domain links two recently identified epilepsy genes.",
"A novel gene causing a mendelian audiogenic mouse epilepsy."
] | [
2002,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
123,
6503
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
26,
1,
19,
16,
19
] | 5 | true | Repeat | EAR | EAR | EAR | 9 |
IPR009040 | 9,040 | Ferritin-like diiron domain | Ferritin-like_diiron | Domain | 48,625 | false | false | This entry represents a group of proteins, containing ferritin-like domain, which is an about 145-residue domain made of a four-helix bundle surrounding a non-heme, non-sulphur, oxo-bridged diiron site. The diiron site is contained within a twisted, left-handed four-helix-bundle constituted of two anti-parallel helix p... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50905"
] | [
"FERRITIN_LIKE"
] | [
48625
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.16.3",
"PDOC50905",
"R-BTA-6798695",
"R-BTA-917937",
"R-CFA-432722",
"R-CFA-6798695",
"R-CFA-917937",
"R-GGA-432722",
"R-GGA-6798695",
"R-GGA-917937",
"R-HSA-1222449",
"R-HSA-3000480",
"R-HSA-432722",
"R-HSA-6798695",
"R-HSA-917937",
"R-MMU-432722",
"R-MMU-6798695",
"R-MMU-91793... | [
"EC:1.16.3",
"PROSITEDOC:PDOC50905",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-917937",
"REACTOME:R-CFA-432722",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-917937",
"REACTOME:R-GGA-432722",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-917937",
"REACTOME:R-HSA-1222449",
"REACTOME:R-HSA-3000480",
... | 21 | [
"1aew",
"1b71",
"1bcf",
"1bfr",
"1bg7",
"1dat",
"1dvb",
"1eum",
"1fha",
"1gwg",
"1h96",
"1hrs",
"1ier",
"1ies",
"1j30",
"1jgc",
"1jyb",
"1krq",
"1lb3",
"1lkm",
"1lko",
"1lkp",
"1mfr",
"1nf4",
"1nf6",
"1nfv",
"1nnq",
"1nwm",
"1o3x",
"1qyb",
"1r03",
"1rcc"... | 726 | [
"PUB00008767"
] | [
"8646540"
] | [
"The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1373,
34824,
11776,
22,
630
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
22,
2,
14,
7,
3,
26,
24,
10,
43,
16
] | 10 | true | Domain | Ferritin-like diiron domain | Ferritin-like diiron domain | Ferritin-like_diiron | 8 |
IPR009042 | 9,042 | RNA polymerase sigma-70 region 1.2 | RNA_pol_sigma70_r1_2 | Domain | 51,473 | false | false | The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with th... | [
"GO:0003677",
"GO:0003700",
"GO:0016987",
"GO:0006352",
"GO:0006355"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"sigma factor activity",
"DNA-templated transcription initiation",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"PFAM"
] | [
"PF00140"
] | [
"Sigma70_r1_2"
] | [
51473
] | 1 | [] | [] | [] | 0 | [
"1iw7",
"1ku2",
"1l9u",
"1l9z",
"1smy",
"1zyr",
"2a68",
"2a69",
"2a6e",
"2a6h",
"2be5",
"2cw0",
"3dxj",
"3eql",
"3iyd",
"3ugo",
"3ugp",
"3wod",
"4g7h",
"4g7o",
"4g7z",
"4jk1",
"4jk2",
"4jkr",
"4ki2",
"4kmu",
"4kn4",
"4kn7",
"4ljz",
"4lk0",
"4lk1",
"4llg"... | 329 | [
"PUB00000061",
"PUB00002181",
"PUB00004340",
"PUB00088319"
] | [
"3052291",
"1597408",
"3092189",
"25596450"
] | [
"Structure and function of bacterial sigma factors.",
"The sigma 70 family: sequence conservation and evolutionary relationships.",
"Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.",
"Plastid sigma factors: Their individual functions and regulation in transcription."... | [
1988,
1992,
1986,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Methanolobus chelungpuianus",
"unclassified sequences"
] | [
50281,
13,
300,
1,
878
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | RNA polymerase sigma-70 region 1.2 | RNA polymerase sigma-70 region 1.2 | RNA_pol_sigma70_r1_2 | 7 |
IPR009044 | 9,044 | ssDNA-binding transcriptional regulator | ssDNA-bd_transcriptional_reg | Homologous_superfamily | 9,738 | false | false | This superfamily represents a ssDNA-binding transcriptional regulator domain consisting of a helix-swapped dimer of β(4)-α motifs. This domain is found as a C-terminal domain in the transcriptional co-activator PC4 (also known as P15; where it is a dimer of two separate motifs), and in the plant transcriptional regulat... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.30.31.10",
"SSF54447"
] | [
"",
""
] | [
9622,
9445
] | 2 | [] | [] | [] | 0 | [
"1l3a",
"1pcf",
"2c62",
"2gia",
"2gid",
"2gje",
"2it9",
"2nvn",
"2phe",
"3n1h",
"3n1i",
"3n1j",
"3n1k",
"3n1l",
"3r9y",
"3r9z",
"3ra0",
"4agh",
"4bg7",
"4bhm",
"4koo",
"4kop",
"4koq",
"4usg",
"5a4n",
"5a4o",
"5zg9",
"6ycs",
"7e4w"
] | 29 | [
"PUB00011849",
"PUB00011850",
"PUB00011851",
"PUB00011852"
] | [
"12080340",
"10432316",
"9360603",
"12590132"
] | [
"A new family of plant transcription factors displays a novel ssDNA-binding surface.",
"Expression, DNA-binding specificity and transcriptional regulation of nuclear factor 1 family proteins from rat.",
"C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site.",
"Alleviation of PC4-... | [
2002,
1999,
1997,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"ecological metagenomes"
] | [
834,
8568,
11,
251,
74
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
32,
1,
3,
2,
5,
1,
1,
11,
3,
1,
1,
26
] | 12 | true | Homologous_superfamily | ssDNA-binding transcriptional regulator | ssDNA-binding transcriptional regulator | ssDNA-bd_transcriptional_reg | 8 |
IPR009045 | 9,045 | Peptidase M74/Hedgehog-like, zinc-binding domain superfamily | Zn_M74/Hedgehog-like | Homologous_superfamily | 58,472 | false | false | This entry represents the zinc-binding domain superfamily in peptidases belonging to MEROPS peptidase family M74 (murein endopeptidase MepA), Protein hedgehog, D-D dipeptidase and related proteins. The structure of the N-terminal signalling domain of hedgehog proteins has been solved and reveals a tetrahedrally coordin... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.1380.10",
"SSF55166"
] | [
"",
""
] | [
56235,
57750
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-DME-209338",
"R-DME-209471",
"R-DME-5358346",
"R-DME-5362798",
"R-DME-5632681",
"R-DRE-5358346",
"R-DRE-5362798",
"R-DRE-5632681",
"R-GGA-5358346",
"R-GGA-5362798",
"R-GGA-5632681",
"R-HSA-373080",
"R-HSA-5358346",
"R-HSA-5362768",
"R-HSA-5362798",
"R-HSA-5632681",
"R-HSA-5632684"... | [
"REACTOME:R-DME-209338",
"REACTOME:R-DME-209471",
"REACTOME:R-DME-5358346",
"REACTOME:R-DME-5362798",
"REACTOME:R-DME-5632681",
"REACTOME:R-DRE-5358346",
"REACTOME:R-DRE-5362798",
"REACTOME:R-DRE-5632681",
"REACTOME:R-GGA-5358346",
"REACTOME:R-GGA-5362798",
"REACTOME:R-GGA-5632681",
"REACTOME:... | 31 | [
"1lbu",
"1r44",
"1tzp",
"1u10",
"1vhh",
"2ibg",
"2mxz",
"2vo9",
"2wfq",
"2wfr",
"2wfx",
"2wg3",
"2wg4",
"3d1m",
"3ho5",
"3k7g",
"3k7h",
"3k7i",
"3k7j",
"3m1n",
"3mxw",
"3n1f",
"3n1g",
"3n1m",
"3n1o",
"3n1p",
"3n1q",
"3n1r",
"4c4m",
"4c4n",
"4d0y",
"4f78"... | 70 | [
"PUB00004222"
] | [
"7477329"
] | [
"A potential catalytic site revealed by the 1.7-A crystal structure of the amino-terminal signalling domain of Sonic hedgehog."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
14,
51022,
4914,
1669,
853
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
22,
1,
3,
10,
8,
10
] | 7 | true | Homologous_superfamily | Peptidase M74/Hedgehog-like, zinc-binding domain superfamily | Peptidase M74/Hedgehog-like, zinc-binding domain superfamily | Zn_M74/Hedgehog-like | 6 |
IPR009047 | 9,047 | Methyl-coenzyme M reductase, alpha subunit, C-terminal | Me_CoM_Rdtase_asu_C | Domain | 9,492 | false | false | This entry represents the C-terminal domain of the alpha subunit, which is comprised of an all-α multi-helical bundle. Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in meth... | [
"GO:0050524",
"GO:0015948"
] | [
"coenzyme-B sulfoethylthiotransferase activity",
"methanogenesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02249"
] | [
"MCR_alpha"
] | [
9492
] | 1 | [
"EC"
] | [
"2.8.4.1"
] | [
"EC:2.8.4.1"
] | 1 | [
"1e6v",
"1e6y",
"1hbm",
"1hbn",
"1hbo",
"1hbu",
"1mro",
"3m1v",
"3m2r",
"3m2u",
"3m2v",
"3m30",
"3m32",
"3pot",
"3sqg",
"5a0y",
"5a8k",
"5a8r",
"5a8w",
"5g0r",
"5n1q",
"5n28",
"5n2a",
"7b1s",
"7b2c",
"7b2h",
"7nkg",
"7suc",
"7sxm",
"8gf5",
"8gf6",
"8s7v"... | 39 | [
"PUB00006391",
"PUB00010614",
"PUB00035993",
"PUB00035994"
] | [
"9367957",
"11491299",
"16260307",
"16234924"
] | [
"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.",
"On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.",
"Methyl-coenzyme M reductase genes: unique functional ma... | [
1997,
2001,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Cylicocyclus nassatus",
"unclassified sequences",
"uncultured rumen bacterium"
] | [
9183,
1,
291,
17
] | 4 | [] | [] | 0 | true | Domain | Methyl-coenzyme M reductase, alpha subunit, C-terminal | Methyl-coenzyme M reductase, alpha subunit, C-terminal | Me_CoM_Rdtase_asu_C | 2 |
IPR009048 | 9,048 | Alpha-macroglobulin, receptor-binding | A-macroglobulin_rcpt-bd | Domain | 18,301 | false | false | This entry represents the receptor-binding domain (RBD) of alpha-2-macroglobulin and related proteins. The RBD is located at the C terminus, its structure having an immunoglobulin-like fold consists of a sandwich of nine strands in two sheets with a Greek-key topology [ , ]. The alpha-macroglobulin (aM) family of prote... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF07677",
"SM01361"
] | [
"A2M_recep",
"A2M_recep"
] | [
18236,
17644
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-198933",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-6798695",
"R-BTA-8957275",
"R-BTA-977606",
"R-HSA-114608",
"R-HSA-140837",
"R-HSA-1474228",
"R-HSA-163125",
"R-HSA-166663",
"R-HSA-166665",
"R-HSA-173736",
"R-HSA-174577",
"R-HSA-... | [
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-977606",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA-1... | 57 | [
"1ayo",
"1bv8",
"1edy",
"2a73",
"2a74",
"2i07",
"2ice",
"2icf",
"2pn5",
"2qki",
"2wii",
"2win",
"2xwb",
"2xwj",
"3cu7",
"3frp",
"3g6j",
"3hrz",
"3hs0",
"3kls",
"3km9",
"3l3o",
"3l5n",
"3nms",
"3ohx",
"3prx",
"3pvm",
"3t4a",
"4a5w",
"4d94",
"4e0s",
"4lnv"... | 102 | [
"PUB00002498",
"PUB00011876",
"PUB00011877",
"PUB00015030",
"PUB00015031",
"PUB00015032",
"PUB00015033",
"PUB00015034",
"PUB00100415"
] | [
"2473064",
"11106161",
"9634697",
"2472396",
"2469470",
"2430968",
"9914899",
"10426429",
"34970276"
] | [
"Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation.",
"Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer.",
"Crystal structure of the receptor-binding domain of alpha 2-macroglobulin.",
"Proteinase binding and inhibition by the monomeric alpha-macroglob... | [
1989,
2000,
1998,
1989,
1989,
1986,
1998,
1999,
2021
] | 9 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcinales",
"marine sediment metagenome"
] | [
111,
18170,
19,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
112,
82,
34,
25,
53
] | 6 | true | Domain | Alpha-macroglobulin, receptor-binding | Alpha-macroglobulin, receptor-binding | A-macroglobulin_rcpt-bd | 5 |
IPR009051 | 9,051 | Alpha-helical ferredoxin | Helical_ferredxn | Homologous_superfamily | 133,656 | false | false | The α-helical ferredoxin domain contains two Fe4-S4 clusters, typical of bacterial ferredoxin. Iron-sulphur proteins play an important role in electron transfer processes and in various enzymatic reactions. In eukaryotes, the mitochondria are the major site of Fe-S cluster biosynthesis in the cell, used for the assembl... | [
"GO:0051536"
] | [
"iron-sulfur cluster binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.1060.10"
] | [
""
] | [
133656
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-71403",
"R-CEL-73621",
"R-DDI-71403",
"R-DDI-73621",
"R-DME-71403",
"R-DRE-71403",
"R-DRE-73621",
"R-GGA-372987",
"R-HSA-611105",
"R-HSA-71403",
"R-HSA-73621",
"R-HSA-9854311",
"R-MMU-71403",
"R-MMU-73621",
"R-MMU-9854311",
"R-RNO-71403",
"R-RNO-73621",
"R-SCE-71403",
"R-S... | [
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-73621",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-73621",
"REACTOME:R-DME-71403",
"REACTOME:R-DRE-71403",
"REACTOME:R-DRE-73621",
"REACTOME:R-GGA-372987",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-71403",
"REACTOME:R-HSA-73621",
"REACTOME:R-HSA-9854311",
... | 21 | [
"1e7p",
"1gt8",
"1gte",
"1gth",
"1h7w",
"1h7x",
"1kf6",
"1kfy",
"1l0v",
"1nek",
"1nen",
"1qlb",
"1yq3",
"1yq4",
"1zoy",
"1zp0",
"2acz",
"2b76",
"2bs2",
"2bs3",
"2bs4",
"2fbw",
"2h88",
"2h89",
"2vdc",
"2wdq",
"2wdr",
"2wdv",
"2wp9",
"2wqy",
"2ws3",
"2wu2"... | 142 | [
"PUB00013184",
"PUB00013185"
] | [
"11850430",
"11796730"
] | [
"Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.",
"Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer."
] | [
2002,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"CRESS virus sp. ctBnw2",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
4214,
114266,
1,
12333,
1,
2841
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
17,
5,
6,
9,
10,
10,
7,
2,
12,
11,
2,
2,
105
] | 13 | true | Homologous_superfamily | Alpha-helical ferredoxin | Alpha-helical ferredoxin | Helical_ferredxn | 3 |
IPR009052 | 9,052 | DNA polymerase III-theta, bacterial | DNA_pol_III_theta_bac | Family | 1,815 | false | false | This entry represents the theta subunit of DNA polymerase III from bacteria, whose core structure consists of an irregular array of three helices [ ]. DNA polymerase III (Pol III) is the primary enzyme responsible for replication of Escherichia coli chromosomal DNA. The holoenzyme consists of 17 proteins and contains t... | [
"GO:0003677",
"GO:0003887",
"GO:0006260"
] | [
"DNA binding",
"DNA-directed DNA polymerase activity",
"DNA replication"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF06440"
] | [
"DNA_pol3_theta"
] | [
1815
] | 1 | [
"EC",
"GP",
"GP"
] | [
"2.7.7.7",
"GenProp0263",
"GenProp1155"
] | [
"EC:2.7.7.7",
"GP:GenProp0263",
"GP:GenProp1155"
] | 3 | [
"1du2",
"1se7",
"2ae9",
"2axd",
"2ido",
"2xy8",
"5m1s"
] | 7 | [
"PUB00013186",
"PUB00035668",
"PUB00035670"
] | [
"10794414",
"16753031",
"15576035"
] | [
"NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.",
"DnaA: controlling the initiation of bacterial DNA replication and more.",
"Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III.... | [
2000,
2006,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"Viruses",
"human gut metagenome"
] | [
1800,
5,
9,
1
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | DNA polymerase III-theta, bacterial | DNA polymerase III-theta, bacterial | DNA_pol_III_theta_bac | 9 |
IPR009053 | 9,053 | Prefoldin | Prefoldin | Homologous_superfamily | 32,526 | false | false | The Prefoldin/GimC family of proteins are found in eukaryotes and archaea [ ]. Prefoldin is part of a molecular chaperone system that promotes the correct folding of nascent polypeptide chains. Prefoldin/GimC interacts with the nascent chain to stabilise it prior to its folding within the central cavity of a chaperonin... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.287.370"
] | [
""
] | [
32526
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-389957",
"R-HSA-8953750"
] | [
"REACTOME:R-HSA-389957",
"REACTOME:R-HSA-8953750"
] | 2 | [
"1fxk",
"2zdi",
"2zqm",
"3aei",
"6nr8",
"6nr9",
"6nrb",
"6nrc",
"6nrd",
"6vy1",
"7wu7"
] | 11 | [
"PUB00013187",
"PUB00013306",
"PUB00015158",
"PUB00080715"
] | [
"12456645",
"11106732",
"9463374",
"18412953"
] | [
"Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.",
"Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins.",
"A novel protein complex promoting formation of functional alpha- and ga... | [
2002,
2000,
1998,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1877,
36,
30527,
86
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
29,
7,
12,
15,
24,
29,
6,
30,
33,
7,
5,
77
] | 12 | true | Homologous_superfamily | Prefoldin | Prefoldin | Prefoldin | 9 |
IPR009056 | 9,056 | Cytochrome c-like domain | Cyt_c-like_dom | Domain | 217,990 | false | false | After cytochrome c is synthesized in the cytoplasm as apocytochrome c, it is transported through the outer mitochondrial membrane to the intermembrane space, where haem is covalently attached by thioester bonds to two cysteine residues located in the cytochrome c centre. Cytochrome c is required during oxidative phosph... | [
"GO:0009055",
"GO:0020037"
] | [
"electron transfer activity",
"heme binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00034",
"PF13442",
"PF21342",
"PS51007"
] | [
"Cytochrom_C",
"Cytochrome_CBB3",
"SoxA-TsdA_cyt-c",
"CYTC"
] | [
94075,
65604,
5192,
213670
] | 4 | [
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
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"GenProp1254",
"GenProp1729",
"PDOC00169",
"R-BTA-111457",
"R-BTA-111458",
"R-BTA-111459",
"R-BTA-2151201",
"R-BTA-3299685",
"R-BTA-5620971",
"R-BTA-5628897",
"R-BTA-611105",
"R-BTA-9627069",
"R-BTA-9707564",
"R-BTA-9865881",
"R-CEL-111457",
"R-CEL-3299685",
"R-CEL-5... | [
"GP:GenProp0613",
"GP:GenProp1254",
"GP:GenProp1729",
"PROSITEDOC:PDOC00169",
"REACTOME:R-BTA-111457",
"REACTOME:R-BTA-111458",
"REACTOME:R-BTA-111459",
"REACTOME:R-BTA-2151201",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-611105",
"REACTOME:... | 124 | [
"155c",
"1a2s",
"1a56",
"1a8c",
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"1aof",
"1aom",
"1aoq",
"1ayg",
"1b7v",
"1bcc",
"1be3",
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"1bl9",
"1c2n",
"1c2r",
"1c52",
"1c53",
"1c6o",
"1c6r",
"1c6s",
"1c75",
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"1cc5",
"1cch",
"1ccr",
"1ced",
"1chh",
"1chi",
"1chj",
"1cie",
"1cif"... | 854 | [
"PUB00013190",
"PUB00013191",
"PUB00013307",
"PUB00016256",
"PUB00016257",
"PUB00016258"
] | [
"12729583",
"2166169",
"11315568",
"10707095",
"12594933",
"10647174"
] | [
"Mitochondrial intermembrane proteins in cell death.",
"High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c.",
"Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution.",
"Cytochrome c release from mitochond... | [
2003,
1990,
2001,
2000,
2003,
1999
] | 6 | [] | [
"IPR004852",
"IPR013427",
"IPR029490"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
192,
199881,
14052,
11,
3854
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
18,
3,
2,
5,
1,
3,
6,
2,
18,
8,
3,
2,
35
] | 13 | true | Domain | Cytochrome c-like domain | Cytochrome c-like domain | Cyt_c-like_dom | 3 |
IPR009057 | 9,057 | Homedomain-like superfamily | Homeodomain-like_sf | Homologous_superfamily | 2,236,308 | false | false | Homeodomain (HD)-containing proteins are transcription factors that share a related DNA binding domain [ ]. HD was first identified in a number of Drosophila homeotic and segmentation proteins, but is now known to be well conserved in organisms from all domains in life. The domain binds DNA through a helix-turn-helix (... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF46689"
] | [
""
] | [
2236308
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-110330",
"R-BTA-110331",
"R-BTA-1660661",
"R-BTA-171306",
"R-BTA-171319",
"R-BTA-174411",
"R-BTA-174414",
"R-BTA-174417",
"R-BTA-174430",
"R-BTA-174437",
"R-BTA-2559586",
"R-BTA-3371453",
"R-BTA-72163",
"R-BTA-9670095",
"R-BTA-9772755",
"R-CEL-2173795",
"R-CEL-3214842",
"R-C... | [
"REACTOME:R-BTA-110330",
"REACTOME:R-BTA-110331",
"REACTOME:R-BTA-1660661",
"REACTOME:R-BTA-171306",
"REACTOME:R-BTA-171319",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-174414",
"REACTOME:R-BTA-174417",
"REACTOME:R-BTA-174430",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-3... | 308 | [
"1a5j",
"1a6i",
"1ahd",
"1akh",
"1apl",
"1au7",
"1b72",
"1b8i",
"1ba5",
"1bjz",
"1bl0",
"1bw5",
"1bw6",
"1cqt",
"1d5y",
"1du0",
"1du6",
"1e3o",
"1enh",
"1etk",
"1eto",
"1etq",
"1etv",
"1etw",
"1etx",
"1ety",
"1f36",
"1f43",
"1fex",
"1fia",
"1fip",
"1fjl"... | 1,425 | [
"PUB00003347",
"PUB00013192",
"PUB00013193",
"PUB00013194"
] | [
"7707374",
"10377888",
"12215502",
"9739097"
] | [
"The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance.",
"Target genes of homeodomain proteins.",
"Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators.",
"Solution structure of the DNA-bindin... | [
1995,
1999,
2002,
1998
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
4400,
1477438,
743274,
1048,
22,
10126
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
1987,
204,
1367,
473,
94,
1086,
854,
36,
1101,
942,
31,
24,
2514
] | 13 | true | Homologous_superfamily | Homedomain-like superfamily | Homedomain-like superfamily | Homeodomain-like_sf | 7 |
IPR009060 | 9,060 | UBA-like superfamily | UBA-like_sf | Homologous_superfamily | 171,074 | false | false | UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signalling via protein kinases [ ]. HHR23A, the human homologue of yeast Rad23A is a nucleotide excision-repair prote... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF46934"
] | [
""
] | [
171074
] | 1 | [
"REACTOME",
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"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-159227",
"R-BTA-159230",
"R-BTA-159231",
"R-BTA-159236",
"R-BTA-532668",
"R-BTA-5689877",
"R-BTA-5689880",
"R-BTA-5693565",
"R-BTA-5693571",
"R-BTA-5696394",
"R-BTA-5696395",
"R-BTA-6798695",
"R-BTA-8866652",
"R-BTA-8948751",
"R-BTA-8980692",
"R-BTA-9013407",
"R-BTA-9020702",
... | [
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"REACTOME:R-BTA-159230",
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-532668",
"REACTOME:R-BTA-5689877",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-5693571",
"REACTOME:R-BTA-5696394",
"REACTOME:R-BTA-5696395",
"REACTOME:R-B... | 229 | [
"1aip",
"1dv0",
"1efu",
"1f4i",
"1go5",
"1ify",
"1jkg",
"1jn5",
"1mn3",
"1oai",
"1oqy",
"1otr",
"1p3q",
"1pgy",
"1q02",
"1qze",
"1tr8",
"1tte",
"1v92",
"1vdl",
"1veg",
"1vej",
"1vek",
"1vg5",
"1wgl",
"1wgn",
"1whc",
"1wiv",
"1wj7",
"1wji",
"1wr1",
"1xb2"... | 173 | [
"PUB00007089",
"PUB00013202",
"PUB00013203"
] | [
"12079361",
"11744709",
"12581645"
] | [
"Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions.",
"Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base.",
"Structural basis for the interaction between the Tap/NXF1 UBA domain and... | [
2002,
2002,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
764,
25899,
143806,
21,
584
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
255,
46,
274,
95,
2,
211,
196,
21,
115,
244,
18,
13,
381
] | 13 | true | Homologous_superfamily | UBA-like superfamily | UBA-like superfamily | UBA-like_sf | 7 |
IPR009061 | 9,061 | Putative DNA-binding domain superfamily | DNA-bd_dom_put_sf | Homologous_superfamily | 305,111 | false | false | A putative DNA-binding domain with a conserved structure is found in several different protein families. The core structure of the domain consists of a three-helical fold that is architecturally similar to that of the "winged-helix" fold, but is topologically distinct. Representatives of this domain can be found in dom... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF46955"
] | [
""
] | [
305111
] | 1 | [
"REACTOME",
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"REACTOME",
"REACTOM... | [
"R-DME-5696395",
"R-DME-5696400",
"R-DME-6781823",
"R-DME-6782135",
"R-GGA-353303",
"R-HSA-201451",
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"R-MMU-201451",
"R-MMU-2173795",
"R-MMU-5696395",
"R-MMU-5696400",
"R-MMU-6781823",... | [
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"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6781823",
"REACTOME:R-DME-6782135",
"REACTOME:R-GGA-353303",
"REACTOME:R-HSA-201451",
"REACTOME:R-HSA-2173795",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6781823",
"REACTOME:R... | 24 | [
"1b70",
"1b7y",
"1d4u",
"1eiy",
"1exi",
"1exj",
"1g4d",
"1j9i",
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"1jjc",
"1l8r",
"1lx8",
"1nd9",
"1pm6",
"1pys",
"1q05",
"1q06",
"1q07",
"1q08",
"1q09",
"1q0a",
"1qpm",
"1r8d",
"1r8e",
"1rh6",
"1sbx",
"1tns",
"1tnt",
"1xpa",
"2akw",
"2aly",
"2amc"... | 178 | [
"PUB00013204",
"PUB00013205",
"PUB00013206",
"PUB00013207",
"PUB00013208"
] | [
"11679717",
"10563794",
"11201751",
"12057194",
"12049735"
] | [
"Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese.",
"Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.",
"Crystal structure of the tra... | [
2001,
1999,
2001,
2002,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
1497,
278021,
20562,
1151,
4,
3876
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
4,
82,
28,
13,
26,
38,
2,
3,
40,
2,
2,
9
] | 13 | true | Homologous_superfamily | Putative DNA-binding domain superfamily | Putative DNA-binding domain superfamily | DNA-bd_dom_put_sf | 3 |
IPR009062 | 9,062 | Smac/DIABLO-like superfamily | Smac/DIABLO-like_sf | Homologous_superfamily | 1,585 | false | false | Smac (Second Mitochondria-derived Activator of Caspase) and DIABLO (Direct IAP-Binding protein with Low PI) are 29kDa mitochondrial precursor proteins. Apoptosis, or programmed cell death, is an essential process in metazoan development and homeostasis. Apoptosis is carried out by caspases, which are under tight regula... | [
"GO:0006915",
"GO:0005739"
] | [
"apoptotic process",
"mitochondrion"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"SSF"
] | [
"SSF46984"
] | [
""
] | [
1585
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
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"R-HSA-111463",
"R-HSA-111464",
"R-HSA-111469",
"R-HSA-9627069",
"R-MMU-111457",
"R-MMU-111463",
"R-MMU-111464",
"R-MMU-111469",
"R-MMU-9627069",
"R-XTR-111457",
"R-XTR-111463",
"R-XTR-111464",
"R-XTR-111469",
"R-XTR-9627069"
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"REACTOME:R-HSA-111463",
"REACTOME:R-HSA-111464",
"REACTOME:R-HSA-111469",
"REACTOME:R-HSA-9627069",
"REACTOME:R-MMU-111457",
"REACTOME:R-MMU-111463",
"REACTOME:R-MMU-111464",
"REACTOME:R-MMU-111469",
"REACTOME:R-MMU-9627069",
"REACTOME:R-XTR-111457",
"REACTOME:R-XTR-1... | 15 | [
"1few",
"1g73",
"4tx5",
"6jx6",
"8ato",
"8auw",
"8e2i",
"8e2j"
] | 8 | [
"PUB00013209",
"PUB00013210"
] | [
"11140638",
"10972280"
] | [
"Structural basis of IAP recognition by Smac/DIABLO.",
"Structural and biochemical basis of apoptotic activation by Smac/DIABLO."
] | [
2000,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
26,
1559
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
9,
7,
6
] | 4 | true | Homologous_superfamily | Smac/DIABLO-like superfamily | Smac/DIABLO-like superfamily | Smac/DIABLO-like_sf | 7 |
IPR009063 | 9,063 | Immunoglobulin/albumin-binding domain superfamily | Ig/albumin-bd_sf | Homologous_superfamily | 2,055 | false | false | This superfamily represents immunoglobulin and albumin-binding (GA module) domains from various bacterial proteins, which share a common fold consisting of a left-handed three-helical bundle (mirror topology to spectrin-like fold). The Staphylococcus aureus virulence factor protein A (SpA) contains five highly homologo... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF46997"
] | [
""
] | [
2055
] | 1 | [] | [] | [] | 0 | [
"1bdc",
"1bdd",
"1dee",
"1edi",
"1edj",
"1edk",
"1edl",
"1fc2",
"1gab",
"1gjs",
"1gjt",
"1h0t",
"1l6x",
"1lp1",
"1oqo",
"1oqx",
"1prb",
"1q2n",
"1ss1",
"1tf0",
"1zda",
"1zdb",
"1zdc",
"1zdd",
"1zxg",
"2b87",
"2b88",
"2b89",
"2dgj",
"2fs1",
"2j5y",
"2jwd"... | 199 | [
"PUB00003376",
"PUB00013211",
"PUB00031434",
"PUB00035975",
"PUB00035976"
] | [
"9086265",
"10805799",
"15269208",
"16906768",
"7589548"
] | [
"Solution structure of the albumin-binding GA module: a versatile bacterial protein domain.",
"Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity.",
"Crystal structu... | [
1997,
2000,
2004,
2006,
1995
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
2052,
3
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Immunoglobulin/albumin-binding domain superfamily | Immunoglobulin/albumin-binding domain superfamily | Ig/albumin-bd_sf | 2 |
IPR009064 | 9,064 | Pheromone, protozoan | Pheromone_protoz | Family | 15 | false | false | Protozoan pheromones are cell-type specific protein signals. This entry represents a family of mating ciliate pheromones (or gamones) from the protozoan Euplotes raikovi, including Er-1, Er-2, Er-10, Er11 and Er22. These pheromones are diffusible extracellular communication signals that distinguish different intra-spec... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06360"
] | [
"E_raikovi_mat"
] | [
15
] | 1 | [] | [] | [] | 0 | [
"1erc",
"1erd",
"1erp",
"1ery",
"1hd6",
"2erl",
"6e6n",
"6e6o"
] | 8 | [
"PUB00013212",
"PUB00013310",
"PUB00024644",
"PUB00024650",
"PUB00025620",
"PUB00036664"
] | [
"12681291",
"7833812",
"7833811",
"8515452",
"11246857",
"8844842"
] | [
"Cross-talk between the autocrine (mitogenic) pheromone loop of the ciliate Euplotes raikovi and the intracellular cyclic AMP concentration.",
"The NMR solution structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi.",
"The NMR solution structure of the pheromone Er-2 from the ciliated pro... | [
2003,
1994,
1994,
1993,
2001,
1996
] | 6 | [] | [] | 0 | 0 | null | [
"Euplotes raikovi"
] | [
15
] | 1 | [] | [] | 0 | true | Family | Pheromone, protozoan | Pheromone, protozoan | Pheromone_protoz | 4 |
IPR009067 | 9,067 | TAFII-230 TBP-binding | TAF_II_230-bd | Domain | 3,025 | false | false | In eukaryotes, the general transcription factor TFIID helps to regulate transcription by RNA polymerase II from class II promoters. TFIID consists of TATA-box-binding proteins (TBP) and TBP-associated factors (TAFIIs), which together mediate both activation and inhibition of transcription. In Drosophila, the N-terminal... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09247"
] | [
"TBP-binding"
] | [
3025
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-674695",
"R-DME-6804756",
"R-DME-73776",
"R-DME-73779",
"R-DME-75953",
"R-DME-76042",
"R-HSA-167161",
"R-HSA-167162",
"R-HSA-167172",
"R-HSA-674695",
"R-HSA-6804756",
"R-HSA-73776",
"R-HSA-73779",
"R-HSA-75953",
"R-HSA-76042",
"R-MMU-674695",
"R-MMU-6804756",
"R-MMU-73776",
... | [
"REACTOME:R-DME-674695",
"REACTOME:R-DME-6804756",
"REACTOME:R-DME-73776",
"REACTOME:R-DME-73779",
"REACTOME:R-DME-75953",
"REACTOME:R-DME-76042",
"REACTOME:R-HSA-167161",
"REACTOME:R-HSA-167162",
"REACTOME:R-HSA-167172",
"REACTOME:R-HSA-674695",
"REACTOME:R-HSA-6804756",
"REACTOME:R-HSA-73776... | 21 | [
"1tba",
"5fur",
"6mzd",
"6mzl",
"7edx",
"7eg7",
"7eg8",
"7eg9",
"7ega",
"7egb",
"7egc",
"7egd",
"7ege",
"7egh",
"7egi",
"7egj",
"7ena",
"7enc",
"8gxq",
"8gxs",
"8wak",
"8wal",
"8wan",
"8wao",
"8wap",
"8waq",
"8war",
"8was"
] | 28 | [
"PUB00013214"
] | [
"9741622"
] | [
"Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3025
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
6,
5,
4,
4,
2,
3,
9
] | 8 | true | Domain | TAFII-230 TBP-binding | TAFII-230 TBP-binding | TAF_II_230-bd | 1 |
IPR009068 | 9,068 | uS15/NS1, RNA-binding domain superfamily | uS15_NS1_RNA-bd_sf | Homologous_superfamily | 124,931 | false | false | The RNA-binding domains of the small ribosomal subunit protein uS15, also known as ribosomal protein S15, and the influenza virus non-structural protein NS1 share the same structural fold, consisting of three helices in an irregular array. uS15 is one of 21 proteins in the small, bacterial 30S ribosomal subunit, and is... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF47060"
] | [
""
] | [
124931
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702"... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-179933... | 133 | [
"1a32",
"1ab3",
"1ail",
"1d2d",
"1dk1",
"1eg0",
"1f7y",
"1fjg",
"1fka",
"1fyj",
"1g1x",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1kuq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36"... | 1,999 | [
"PUB00013215",
"PUB00013311"
] | [
"11123902",
"10742169"
] | [
"Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.",
"Crystal structure of the S15-rRNA complex."
] | [
2000,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Orthomyxoviridae",
"unclassified sequences"
] | [
933,
23184,
33590,
66705,
519
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
20,
7,
11,
9,
1,
63,
23,
2,
26,
34,
2,
3,
24
] | 13 | true | Homologous_superfamily | uS15/NS1, RNA-binding domain superfamily | uS15/NS1, RNA-binding domain superfamily | uS15_NS1_RNA-bd_sf | 4 |
IPR009069 | 9,069 | Cysteine alpha-hairpin motif superfamily | Cys_alpha_HP_mot_SF | Homologous_superfamily | 15,483 | false | false | This entry represents the cysteine α-hairpin motif. Proteins with this structure include mature T-cell proliferation 1 neighbour protein and cytochrome c oxidase-assembly factors COX23 and COX19. | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF47072"
] | [
""
] | [
15483
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9864848",
"R-CFA-9864848",
"R-HSA-1268020",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9864848",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9864848",
"R-MMU-9937383"
] | [
"REACTOME:R-BTA-9864848",
"REACTOME:R-CFA-9864848",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9864848",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOME:R-MMU-9864848",
"REACTOM... | 12 | [
"1ei0",
"1hp8",
"1u96",
"1u97",
"1z2g",
"2hp8",
"2l0y",
"2lgq",
"2lqt",
"2rn9",
"2rnb",
"3j9m",
"3jd5",
"5aj3",
"5aj4",
"6gaw",
"6gaz",
"6neq",
"6nf8",
"6nu2",
"6nu3",
"6rw4",
"6rw5",
"6vlz",
"6vmi",
"6xyw",
"6ydp",
"6ydw",
"6zm5",
"6zm6",
"6zs9",
"6zsa"... | 77 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadati",
"viral metagenome"
] | [
15477,
3,
3
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
30,
1,
6,
7,
14,
16,
3,
31,
13,
3,
3,
41
] | 12 | true | Homologous_superfamily | Cysteine alpha-hairpin motif superfamily | Cysteine alpha-hairpin motif superfamily | Cys_alpha_HP_mot_SF | 1 |
IPR009071 | 9,071 | High mobility group box domain | HMG_box_dom | Domain | 119,395 | false | false | High mobility group (HMG) box domains are involved in binding DNA, and may be involved in protein-protein interactions as well. The structure of the HMG-box domain consists of three helices in an irregular array. HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family inv... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00505",
"PF09011",
"PS50118",
"SM00398"
] | [
"HMG_box",
"HMG_box_2",
"HMG_BOX_2",
"HMG"
] | [
107071,
12654,
114506,
108919
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-140342",
"R-BTA-3214815",
"R-BTA-445989",
"R-BTA-5620971",
"R-BTA-5686938",
"R-BTA-6798695",
"R-BTA-879415",
"R-BTA-933542",
"R-BTA-983231",
"R-CEL-112382",
"R-CEL-140342",
"R-CEL-201722",
"R-CEL-3769402",
"R-CEL-4086398",
"R-CEL-4641265",
"R-CEL-5620971",
"R-CEL-5686938",
"... | [
"REACTOME:R-BTA-140342",
"REACTOME:R-BTA-3214815",
"REACTOME:R-BTA-445989",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-5686938",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-879415",
"REACTOME:R-BTA-933542",
"REACTOME:R-BTA-983231",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-140342",
"REACTOME:R-CEL... | 260 | [
"1aab",
"1cg7",
"1ckt",
"1gt0",
"1hma",
"1hme",
"1hmf",
"1hry",
"1hrz",
"1hsm",
"1hsn",
"1i11",
"1j3c",
"1j3d",
"1j3x",
"1j46",
"1j47",
"1j5n",
"1k99",
"1l8y",
"1l8z",
"1lwm",
"1nhm",
"1nhn",
"1o4x",
"1qrv",
"1v63",
"1v64",
"1wgf",
"1wxl",
"1wz6",
"2co9"... | 134 | [
"PUB00015128",
"PUB00015129",
"PUB00015130",
"PUB00015131"
] | [
"12920151",
"10890911",
"11779632",
"12781674"
] | [
"The molecular action and regulation of the testis-determining factors, SRY (sex-determining region on the Y chromosome) and SOX9 [SRY-related high-mobility group (HMG) box 9].",
"Association of Smads with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming... | [
2003,
2000,
2001,
2003
] | 4 | [] | [
"IPR029215",
"IPR047443",
"IPR048016",
"IPR049523",
"IPR055339",
"IPR058607"
] | 0 | 6 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
31,
119153,
56,
155
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
71,
22,
383,
62,
320,
237,
12,
28,
250,
8,
10,
88
] | 12 | true | Domain | High mobility group box domain | High mobility group box domain | HMG_box_dom | 8 |
IPR009072 | 9,072 | Histone-fold | Histone-fold | Homologous_superfamily | 235,249 | false | false | Histones mediate DNA organisation and play a dominant role in regulating eukaryotic transcription. The histone-fold consists of a core of three helices, where the long middle helix is flanked at each end by shorter ones. The histone fold is a structural element that facilitates heterodimerisation [ , , ]. Proteins disp... | [
"GO:0046982"
] | [
"protein heterodimerization activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.20.10",
"SSF47113"
] | [
"",
""
] | [
233776,
218237
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-110314",
"R-BTA-110330",
"R-BTA-110331",
"R-BTA-1266695",
"R-BTA-141444",
"R-BTA-171306",
"R-BTA-201722",
"R-BTA-212300",
"R-BTA-2299718",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-2559580",
"R-BTA-2559582",
"R-BTA-2559586",
"R-BTA-3214815",
"R-BTA-3214841",
"R-BTA-3214842",
... | [
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110330",
"REACTOME:R-BTA-110331",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-171306",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-212300",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA... | 708 | [
"1a7w",
"1aoi",
"1b67",
"1b6w",
"1bfm",
"1bh8",
"1bh9",
"1eqz",
"1f1e",
"1f66",
"1h3o",
"1hio",
"1hq3",
"1hta",
"1id3",
"1jfi",
"1ku5",
"1kx3",
"1kx4",
"1kx5",
"1m18",
"1m19",
"1m1a",
"1n1j",
"1p34",
"1p3a",
"1p3b",
"1p3f",
"1p3g",
"1p3i",
"1p3k",
"1p3l"... | 1,171 | [
"PUB00039806",
"PUB00060941",
"PUB00060942"
] | [
"16260604",
"8670811",
"8754798"
] | [
"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions.",
"A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains.",
"Determination of functional domains in ... | [
2005,
1996,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1769,
598,
232564,
190,
128
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
312,
47,
154,
55,
249,
190,
29,
209,
234,
25,
29,
491
] | 12 | true | Homologous_superfamily | Histone-fold | Histone-fold | Histone-fold | 8 |
IPR009073 | 9,073 | Co-chaperone HscB, C-terminal oligomerisation domain | HscB_oligo_C | Domain | 9,886 | false | false | This entry represents the C-terminal oligomerisation domain found in HscB (heat shock cognate protein B), which is also known as HSC20 (20K heat shock cognate protein) and J-protein Jac1 in yeast mitochondria [ ]. HscB acts as a co-chaperone to regulate the ATPase activity and peptide-binding specificity of the molecul... | [
"GO:0051259"
] | [
"protein complex oligomerization"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF07743"
] | [
"HSCB_C"
] | [
9886
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1268020",
"R-HSA-1362409",
"R-HSA-6799198",
"R-HSA-9865881",
"R-MMU-1268020",
"R-MMU-1362409",
"R-MMU-6799198",
"R-MMU-9865881",
"R-SCE-1268020",
"R-SCE-1362409",
"R-SCE-9865881",
"R-SPO-1268020",
"R-SPO-1362409",
"R-SPO-9865881"
] | [
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-1362409",
"REACTOME:R-HSA-6799198",
"REACTOME:R-HSA-9865881",
"REACTOME:R-MMU-1268020",
"REACTOME:R-MMU-1362409",
"REACTOME:R-MMU-6799198",
"REACTOME:R-MMU-9865881",
"REACTOME:R-SCE-1268020",
"REACTOME:R-SCE-1362409",
"REACTOME:R-SCE-9865881",
"REACTOM... | 14 | [
"1fpo",
"3bvo",
"3uo2",
"3uo3",
"4it5"
] | 5 | [
"PUB00013224",
"PUB00083482"
] | [
"11124030",
"22306468"
] | [
"Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.",
"Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution."
] | [
2000,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5538,
4282,
66
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
3,
2,
1,
1,
1,
2,
2,
1,
2,
7,
1,
1,
2
] | 13 | true | Domain | Co-chaperone HscB, C-terminal oligomerisation domain | Co-chaperone HscB, C-terminal oligomerisation domain | HscB_oligo_C | 9 |
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