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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR022648 | 22,648 | Proliferating cell nuclear antigen, PCNA, N-terminal | Pr_cel_nuc_antig_N | Domain | 7,577 | false | false | Proliferating cell nuclear antigen (PCNA), or cyclin, is a non-histone acidic nuclear protein [ ] that plays a key role in the control of eukaryotic DNA replication [ ]. It acts as a co-factor for DNA polymerase delta, which is responsible for leading strand DNA replication [ ]. The sequence of PCNA is well conserved b... | [
"GO:0003677",
"GO:0006275"
] | [
"DNA binding",
"regulation of DNA replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00705"
] | [
"PCNA_N"
] | [
7577
] | 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-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-174411",
"R-BTA-174414",
"R-BTA-174417",
"R-BTA-174437",
"R-BTA-4615885",
"R-BTA-5358565",
"R-BTA-5651801",
"R-BTA-5655862",
"R-BTA-5656121",
"R-BTA-5656169",
"R-BTA-5685942",
"R-BTA-5696397",
"R-BTA-5696400",
"R-BTA-6782135",
... | [
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-174414",
"REACTOME:R-BTA-174417",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-4615885",
"REACTOME:R-BTA-5358565",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5655862",
"REACTOME:R-BTA... | 208 | [
"1axc",
"1ge8",
"1isq",
"1iz4",
"1iz5",
"1plq",
"1plr",
"1rwz",
"1rxm",
"1rxz",
"1sxj",
"1u76",
"1u7b",
"1ud9",
"1ul1",
"1vyj",
"1vym",
"1w60",
"2hii",
"2hik",
"2ijx",
"2io4",
"2ix2",
"2izo",
"2nti",
"2od8",
"2zvk",
"2zvl",
"2zvm",
"2zvv",
"2zvw",
"3a2f"... | 229 | [
"PUB00001160",
"PUB00001388",
"PUB00001407",
"PUB00002545",
"PUB00015005",
"PUB00059204",
"PUB00059205"
] | [
"2884104",
"1671766",
"1346518",
"2565339",
"8001157",
"10438605",
"10542158"
] | [
"Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin.",
"Highly conserved structure of proliferating cell nuclear antigen (DNA polymerase delta auxiliary protein) gene in plants.",
"Identification of carrot cDNA clones encoding a second putative proliferating cell-nuclear a... | [
1987,
1991,
1992,
1989,
1994,
1999,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria candidate phyla",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1263,
2,
5751,
147,
414
] | 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,
1,
4,
7,
4,
1,
1,
2,
1,
1,
8
] | 12 | true | Domain | Proliferating cell nuclear antigen, PCNA, N-terminal | Proliferating cell nuclear antigen, PCNA, N-terminal | Pr_cel_nuc_antig_N | 8 |
IPR022649 | 22,649 | Proliferating cell nuclear antigen, PCNA, C-terminal | Pr_cel_nuc_antig_C | Domain | 7,033 | false | false | Proliferating cell nuclear antigen (PCNA), or cyclin, is a non-histone acidic nuclear protein [ ] that plays a key role in the control of eukaryotic DNA replication [ ]. It acts as a co-factor for DNA polymerase delta, which is responsible for leading strand DNA replication [ ]. The sequence of PCNA is well conserved b... | [
"GO:0003677",
"GO:0006275"
] | [
"DNA binding",
"regulation of DNA replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02747"
] | [
"PCNA_C"
] | [
7033
] | 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-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-174411",
"R-BTA-174414",
"R-BTA-174417",
"R-BTA-174437",
"R-BTA-4615885",
"R-BTA-5358565",
"R-BTA-5651801",
"R-BTA-5655862",
"R-BTA-5656121",
"R-BTA-5656169",
"R-BTA-5685942",
"R-BTA-5696397",
"R-BTA-5696400",
"R-BTA-6782135",
... | [
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-174414",
"REACTOME:R-BTA-174417",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-4615885",
"REACTOME:R-BTA-5358565",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5655862",
"REACTOME:R-BTA... | 208 | [
"1axc",
"1ge8",
"1isq",
"1iz4",
"1iz5",
"1plq",
"1plr",
"1rwz",
"1rxm",
"1rxz",
"1sxj",
"1u76",
"1u7b",
"1ud9",
"1ul1",
"1vyj",
"1vym",
"1w60",
"2hii",
"2hik",
"2ijx",
"2io4",
"2ix2",
"2izo",
"2nti",
"2od8",
"2zvk",
"2zvl",
"2zvm",
"2zvv",
"2zvw",
"3a2f"... | 228 | [
"PUB00001160",
"PUB00001388",
"PUB00001407",
"PUB00002545",
"PUB00015005",
"PUB00059204",
"PUB00059205"
] | [
"2884104",
"1671766",
"1346518",
"2565339",
"8001157",
"10438605",
"10542158"
] | [
"Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin.",
"Highly conserved structure of proliferating cell nuclear antigen (DNA polymerase delta auxiliary protein) gene in plants.",
"Identification of carrot cDNA clones encoding a second putative proliferating cell-nuclear a... | [
1987,
1991,
1992,
1989,
1994,
1999,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
931,
4,
5596,
114,
388
] | 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,
1,
3,
3,
4,
1,
1,
4,
1,
1,
7
] | 12 | true | Domain | Proliferating cell nuclear antigen, PCNA, C-terminal | Proliferating cell nuclear antigen, PCNA, C-terminal | Pr_cel_nuc_antig_C | 2 |
IPR022650 | 22,650 | S-layer protein, central domain | S_layer_central | Domain | 111 | false | false | This entry represents the central domain of archaeal S-layer proteins. Members of this family are found in (for example) Pyrococcus horikoshii (split into two tandem reading frames), Methanocaldococcus jannaschii (Methanococcus jannaschii), and related species. Some local similarity can be found to other S-layer protei... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05123"
] | [
"S_layer_N"
] | [
111
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Methanobacteriota"
] | [
111
] | 1 | [] | [] | 0 | true | Domain | S-layer protein, central domain | S-layer protein, central domain | S_layer_central | 5 |
IPR022651 | 22,651 | S-layer protein, outer domain | S_layer_C | Domain | 392 | false | false | This entry represents the outer domain of archaeal S-layer proteins. Members of this family are found in (for example) Pyrococcus horikoshii (split into two tandem reading frames), Methanocaldococcus jannaschii (Methanococcus jannaschii), and related species. Some local similarity can be found to other S-layer protein ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05124"
] | [
"S_layer_C"
] | [
392
] | 1 | [] | [] | [] | 0 | [
"9fsa"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Geodia barretti",
"ecological metagenomes"
] | [
375,
8,
1,
8
] | 4 | [] | [] | 0 | true | Domain | S-layer protein, outer domain | S-layer protein, outer domain | S_layer_C | 1 |
IPR022652 | 22,652 | Zinc finger, XPA-type, conserved site | Znf_XPA_CS | Conserved_site | 1,665 | false | false | Xeroderma pigmentosum (XP) [ ] is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. Skin cells of individual's with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genet... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE"
] | [
"PF01286",
"PS00752"
] | [
"XPA_N",
"XPA_1"
] | [
1629,
1080
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5696395",
"R-DME-5696400",
"R-DME-6781823",
"R-DME-6782135",
"R-GGA-353303",
"R-HSA-5696395",
"R-HSA-5696400",
"R-HSA-6781823",
"R-HSA-6782135",
"R-MMU-5696395",
"R-MMU-5696400",
"R-MMU-6781823",
"R-MMU-6782135",
"R-SCE-6781823",
"R-SCE-6782135",
"R-SPO-5696395",
"R-SPO-569640... | [
"REACTOME:R-DME-5696395",
"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6781823",
"REACTOME:R-DME-6782135",
"REACTOME:R-GGA-353303",
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6781823",
"REACTOME:R-HSA-6782135",
"REACTOME:R-MMU-5696395",
"REACTOME:R-MMU-5696400",
"REACTOME... | 19 | [
"1d4u",
"1xpa",
"5a39",
"5a3d",
"5g32",
"5g33",
"5g34",
"5g35",
"5lcl",
"5lcm",
"6j44",
"6lae",
"6ro4",
"7ad8",
"8ebt",
"8ebu",
"8ebx",
"8eby"
] | 18 | [
"PUB00000206",
"PUB00002661",
"PUB00004114",
"PUB00005433"
] | [
"1764072",
"1918083",
"1741034",
"8160271"
] | [
"Molecular cloning of human XPAC gene homologs from chicken, Xenopus laevis and Drosophila melanogaster.",
"Identification and characterization of xpac protein, the gene product of the human XPAC (xeroderma pigmentosum group A complementing) gene.",
"Yeast RAD14 and human xeroderma pigmentosum group A DNA-repai... | [
1991,
1991,
1992,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
1665
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
4,
3,
3,
4,
8,
1,
1
] | 8 | true | Conserved_site | Zinc finger, XPA-type, conserved site | Zinc finger, XPA-type, conserved site | Znf_XPA_CS | 9 |
IPR022653 | 22,653 | Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site | De-COase2_pyr-phos_BS | Binding_site | 36,990 | false | false | These enzymes are collectively known as group IV decarboxylases [ ]. Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [ , ]. Members of this family while most probably evolutionary related,... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00878"
] | [
"ODR_DC_2_1"
] | [
36990
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1",
"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-MMU-350562",
"R-MMU-351202",
"R-RNO-350562",
"R-RNO-351202",
... | [
"EC:4.1.1",
"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:R-DME-350562",
"REACTOME:R-DME-351143",
"REACTOME:R-DME-351202",
"REACTOME:R-HSA-350562",
"REAC... | 23 | [
"1d7k",
"1f3t",
"1hkv",
"1hkw",
"1knw",
"1ko0",
"1njj",
"1qu4",
"1szr",
"1tuf",
"1twi",
"2o0t",
"2on3",
"2oo0",
"2p3e",
"2qgh",
"2yxx",
"3c5q",
"3n2b",
"3nzp",
"3nzq",
"3vab",
"4aib",
"4xg1",
"4zgy",
"5bwa",
"5gjm",
"5gjn",
"5gjo",
"5gjp",
"5x7m",
"5x7n"... | 42 | [
"PUB00001452",
"PUB00002726",
"PUB00003632"
] | [
"8181483",
"1730582",
"3143046"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites.",
"Pseudomonas aeruginosa diami... | [
1994,
1992,
1988
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
648,
27557,
8306,
12,
467
] | 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",... | [
15,
1,
1,
2,
2,
3,
5,
1,
14,
4,
1,
1,
22
] | 13 | true | Binding_site | Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site | Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site | De-COase2_pyr-phos_BS | 5 |
IPR022655 | 22,655 | Domain of unknown function DUF1553 | DUF1553 | Domain | 8,452 | false | false | The function of this domain is not known. It is found associated with . It is also found associated with the Planctomycete cytochrome C domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07587"
] | [
"PSD1"
] | [
8452
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3,
8175,
42,
232
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1553 | Domain of unknown function DUF1553 | DUF1553 | 4 |
IPR022656 | 22,656 | XPA, C-terminal | XPA_C | Domain | 3,638 | false | false | Xeroderma pigmentosum (XP) [ ] is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. Skin cells of individual's with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genet... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05181"
] | [
"XPA_C"
] | [
3638
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5696395",
"R-DME-5696400",
"R-DME-6781823",
"R-DME-6782135",
"R-GGA-353303",
"R-HSA-5696395",
"R-HSA-5696400",
"R-HSA-6781823",
"R-HSA-6782135",
"R-MMU-5696395",
"R-MMU-5696400",
"R-MMU-6781823",
"R-MMU-6782135",
"R-SCE-6781823",
"R-SCE-6782135",
"R-SPO-5696395",
"R-SPO-569640... | [
"REACTOME:R-DME-5696395",
"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6781823",
"REACTOME:R-DME-6782135",
"REACTOME:R-GGA-353303",
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6781823",
"REACTOME:R-HSA-6782135",
"REACTOME:R-MMU-5696395",
"REACTOME:R-MMU-5696400",
"REACTOME... | 19 | [
"1d4u",
"1xpa",
"5a39",
"5a3d",
"5g32",
"5g33",
"5g34",
"5g35",
"5lcl",
"5lcm",
"6j44",
"6lae",
"6ro4",
"7ad8",
"8ebt",
"8ebu",
"8ebx",
"8eby"
] | 18 | [
"PUB00000206",
"PUB00002661",
"PUB00004114",
"PUB00005433"
] | [
"1764072",
"1918083",
"1741034",
"8160271"
] | [
"Molecular cloning of human XPAC gene homologs from chicken, Xenopus laevis and Drosophila melanogaster.",
"Identification and characterization of xpac protein, the gene product of the human XPAC (xeroderma pigmentosum group A complementing) gene.",
"Yeast RAD14 and human xeroderma pigmentosum group A DNA-repai... | [
1991,
1991,
1992,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"seawater metagenome",
"unclassified viruses"
] | [
6,
3628,
1,
3
] | 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... | [
1,
4,
3,
3,
4,
1,
8,
1,
1
] | 9 | true | Domain | XPA, C-terminal | XPA, C-terminal | XPA_C | 5 |
IPR022657 | 22,657 | Orn/DAP/Arg decarboxylase 2, conserved site | De-COase2_CS | Conserved_site | 32,811 | false | false | These enzymes are collectively known as group IV decarboxylases [ ]. Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [ , ]. Members of this family while most probably evolutionary related,... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00879"
] | [
"ODR_DC_2_2"
] | [
32811
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1",
"R-BTA-350562",
"R-BTA-351202",
"R-DME-350562",
"R-DME-351143",
"R-DME-351202",
"R-HSA-350562",
"R-HSA-351143",
"R-HSA-351202",
"R-MMU-350562",
"R-MMU-351143",
"R-MMU-351202",
"R-RNO-350562",
"R-RNO-351143",
"R-RNO-351202",
"R-SCE-351143",
"R-SCE-351202"
] | [
"EC:4.1.1",
"REACTOME:R-BTA-350562",
"REACTOME:R-BTA-351202",
"REACTOME:R-DME-350562",
"REACTOME:R-DME-351143",
"REACTOME:R-DME-351202",
"REACTOME:R-HSA-350562",
"REACTOME:R-HSA-351143",
"REACTOME:R-HSA-351202",
"REACTOME:R-MMU-350562",
"REACTOME:R-MMU-351143",
"REACTOME:R-MMU-351202",
"REAC... | 17 | [
"1d7k",
"1hkv",
"1hkw",
"1knw",
"1ko0",
"1tuf",
"1twi",
"2j66",
"2o0t",
"2on3",
"2oo0",
"2p3e",
"2plj",
"2plk",
"3btn",
"3n2b",
"3nzq",
"3vab",
"4aib",
"4pgg",
"4pgh",
"4xg1",
"4zgy",
"4zgz",
"5bwa",
"5gjm",
"5gjn",
"5gjo",
"5gjp",
"5x7m",
"5x7n",
"6n2a"... | 44 | [
"PUB00001452",
"PUB00002116",
"PUB00003632"
] | [
"8181483",
"2198270",
"3143046"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli.",
"Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino ... | [
1994,
1990,
1988
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
415,
24798,
7224,
8,
366
] | 5 | [
"Arabidopsis thaliana",
"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",
"Saccharomyces cerevisiae... | [
15,
3,
1,
2,
10,
10,
1,
4,
15,
1,
30
] | 11 | true | Conserved_site | Orn/DAP/Arg decarboxylase 2, conserved site | Orn/DAP/Arg decarboxylase 2, conserved site | De-COase2_CS | 1 |
IPR022658 | 22,658 | XPA, conserved site | XPA_CS | Conserved_site | 1,888 | false | false | Xeroderma pigmentosum (XP) [ ] is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. Skin cells of individual's with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genet... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00753"
] | [
"XPA_2"
] | [
1888
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5696395",
"R-DME-5696400",
"R-DME-6781823",
"R-DME-6782135",
"R-GGA-353303",
"R-HSA-5696395",
"R-HSA-5696400",
"R-HSA-6781823",
"R-HSA-6782135",
"R-MMU-5696395",
"R-MMU-5696400",
"R-MMU-6781823",
"R-MMU-6782135",
"R-SCE-6781823",
"R-SCE-6782135"
] | [
"REACTOME:R-DME-5696395",
"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6781823",
"REACTOME:R-DME-6782135",
"REACTOME:R-GGA-353303",
"REACTOME:R-HSA-5696395",
"REACTOME:R-HSA-5696400",
"REACTOME:R-HSA-6781823",
"REACTOME:R-HSA-6782135",
"REACTOME:R-MMU-5696395",
"REACTOME:R-MMU-5696400",
"REACTOME... | 15 | [
"1d4u",
"1xpa",
"5a39",
"5a3d",
"5g32",
"5g33",
"5g34",
"5g35",
"5lcl",
"5lcm",
"6j44",
"6lae",
"6ro4",
"7ad8",
"8ebt",
"8ebu",
"8ebx",
"8eby"
] | 18 | [
"PUB00000206",
"PUB00002661",
"PUB00004114",
"PUB00005433"
] | [
"1764072",
"1918083",
"1741034",
"8160271"
] | [
"Molecular cloning of human XPAC gene homologs from chicken, Xenopus laevis and Drosophila melanogaster.",
"Identification and characterization of xpac protein, the gene product of the human XPAC (xeroderma pigmentosum group A complementing) gene.",
"Yeast RAD14 and human xeroderma pigmentosum group A DNA-repai... | [
1991,
1991,
1992,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
1888
] | 1 | [
"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)"
] | [
3,
3,
4,
1,
8,
1
] | 6 | true | Conserved_site | XPA, conserved site | XPA, conserved site | XPA_CS | 4 |
IPR022659 | 22,659 | Proliferating cell nuclear antigen, PCNA, conserved site | Pr_cel_nuc_antig_CS | Conserved_site | 5,593 | false | false | This entry represents two conserved regions located in the N-terminal section. The second one has been proposed to bind DNA. Proliferating cell nuclear antigen (PCNA), or cyclin, is a non-histone acidic nuclear protein [ ] that plays a key role in the control of eukaryotic DNA replication [ ]. It acts as a co-factor fo... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00293",
"PS01251"
] | [
"PCNA_2",
"PCNA_1"
] | [
4142,
5161
] | 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-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-174411",
"R-BTA-174414",
"R-BTA-174417",
"R-BTA-174437",
"R-BTA-4615885",
"R-BTA-5358565",
"R-BTA-5651801",
"R-BTA-5655862",
"R-BTA-5656121",
"R-BTA-5656169",
"R-BTA-5685942",
"R-BTA-5696397",
"R-BTA-5696400",
"R-BTA-6782135",
... | [
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-174414",
"REACTOME:R-BTA-174417",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-4615885",
"REACTOME:R-BTA-5358565",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5655862",
"REACTOME:R-BTA... | 195 | [
"1axc",
"1ge8",
"1isq",
"1iz4",
"1iz5",
"1plq",
"1plr",
"1rwz",
"1rxm",
"1rxz",
"1sxj",
"1u76",
"1u7b",
"1ud9",
"1ul1",
"1vyj",
"1vym",
"1w60",
"2hii",
"2hik",
"2ijx",
"2io4",
"2ix2",
"2izo",
"2nti",
"2od8",
"2zvk",
"2zvl",
"2zvm",
"2zvv",
"2zvw",
"3a2f"... | 228 | [
"PUB00001160",
"PUB00001388",
"PUB00001407",
"PUB00002545",
"PUB00059204",
"PUB00059205"
] | [
"2884104",
"1671766",
"1346518",
"2565339",
"10438605",
"10542158"
] | [
"Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin.",
"Highly conserved structure of proliferating cell nuclear antigen (DNA polymerase delta auxiliary protein) gene in plants.",
"Identification of carrot cDNA clones encoding a second putative proliferating cell-nuclear a... | [
1987,
1991,
1992,
1989,
1999,
1999
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
646,
4894,
29,
24
] | 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... | [
6,
1,
1,
2,
6,
4,
1,
1,
2,
1,
1,
8
] | 12 | true | Conserved_site | Proliferating cell nuclear antigen, PCNA, conserved site | Proliferating cell nuclear antigen, PCNA, conserved site | Pr_cel_nuc_antig_CS | 7 |
IPR022660 | 22,660 | Domain of unknown function DUF1581 | DUF1581 | Domain | 114 | false | false | Several Rhodopirellula baltica proteins share this domain. They also match ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07619"
] | [
"DUF1581"
] | [
114
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Durusdinium trenchii",
"Planctomycetia"
] | [
1,
113
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1581 | Domain of unknown function DUF1581 | DUF1581 | 7 |
IPR022663 | 22,663 | Dihydrodipicolinate reductase, C-terminal | DapB_C | Domain | 27,862 | false | false | This entry represents the C-terminal region of Dihydrodipicolinate reductase. Dihydrodipicolinate reductase catalyzes the second step in the biosynthesis of diaminopimelic acid and lysine, the NAD or NADP-dependent reduction of 2,3-dihydrodipicolinate into 2,3,4,5-tetrahydrodipicolinate [ , , ]. In Escherichia coli and... | [
"GO:0008839",
"GO:0009089"
] | [
"4-hydroxy-tetrahydrodipicolinate reductase activity",
"L-lysine biosynthetic process via diaminopimelate"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF05173"
] | [
"DapB_C"
] | [
27862
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.17.1.8",
"PWY-2941",
"PWY-2942",
"PWY-5097"
] | [
"EC:1.17.1.8",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097"
] | 4 | [
"1arz",
"1c3v",
"1dih",
"1dru",
"1drv",
"1drw",
"1p9l",
"1vm6",
"1yl5",
"1yl6",
"1yl7",
"3ijp",
"3qy9",
"4f3y",
"4ywj",
"5eer",
"5ees",
"5kt0",
"5tej",
"5tek",
"5tem",
"5ten",
"5tjy",
"5tjz",
"5u5i",
"5u5n",
"5ua0",
"5ugj",
"5ugv",
"5us6",
"5wol",
"5z2d"... | 37 | [
"PUB00000417",
"PUB00019387",
"PUB00019388",
"PUB00043321"
] | [
"7893645",
"8873595",
"9398235",
"18250105"
] | [
"Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase.",
"Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.",
"Three-dimensional structure of Escherichia coli dihydrodipicolinate ... | [
1995,
1996,
1997,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
598,
24992,
1662,
1,
609
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
11,
13
] | 4 | true | Domain | Dihydrodipicolinate reductase, C-terminal | Dihydrodipicolinate reductase, C-terminal | DapB_C | 2 |
IPR022664 | 22,664 | Dihydrodipicolinate reductase, conserved site | DapB_N_CS | Conserved_site | 22,496 | false | false | Dihydrodipicolinate reductase catalyzes the second step in the biosynthesis of diaminopimelic acid and lysine, the NAD or NADP-dependent reduction of 2,3-dihydrodipicolinate into 2,3,4,5-tetrahydrodipicolinate [ , , ]. In Escherichia coli and Mycobacterium tuberculosis, dihydrodipicolinate reductase has equal specifici... | [
"GO:0008839",
"GO:0009089"
] | [
"4-hydroxy-tetrahydrodipicolinate reductase activity",
"L-lysine biosynthetic process via diaminopimelate"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01298"
] | [
"DAPB"
] | [
22496
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.17.1.8",
"PWY-2941",
"PWY-2942",
"PWY-5097"
] | [
"EC:1.17.1.8",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097"
] | 4 | [
"1arz",
"1c3v",
"1dih",
"1dru",
"1drv",
"1drw",
"1p9l",
"1vm6",
"1yl5",
"1yl6",
"1yl7",
"3ijp",
"3qy9",
"4f3y",
"4ywj",
"5eer",
"5ees",
"5kt0",
"5tej",
"5tek",
"5tem",
"5ten",
"5tjy",
"5tjz",
"5ugj",
"5ugv",
"5us6",
"5wol",
"5z2d",
"5z2e",
"5z2f",
"6bdx"... | 33 | [
"PUB00000417",
"PUB00019387",
"PUB00019388",
"PUB00043321"
] | [
"7893645",
"8873595",
"9398235",
"18250105"
] | [
"Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase.",
"Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.",
"Three-dimensional structure of Escherichia coli dihydrodipicolinate ... | [
1995,
1996,
1997,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
581,
21316,
125,
474
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Dihydrodipicolinate reductase, conserved site | Dihydrodipicolinate reductase, conserved site | DapB_N_CS | 4 |
IPR022665 | 22,665 | Methylaspartate ammonia-lyase, N-terminal | MeAsp_NH4-lyase_N | Domain | 915 | false | false | Methylaspartate ammonia-lyase catalyses the second step of fermentation of glutamate. It is a homodimer. This domain represents the N-terminal region of methylaspartate ammonia-lyase. This domain is structurally related to [ ]. This domain is associated with the catalytic domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05034"
] | [
"MAAL_N"
] | [
915
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.3.1.2",
"PWY-5087",
"PWY-6728"
] | [
"EC:4.3.1.2",
"METACYC:PWY-5087",
"METACYC:PWY-6728"
] | 3 | [
"1kcz",
"1kd0",
"1kko",
"1kkr",
"3zvh",
"3zvi"
] | 6 | [
"PUB00019827"
] | [
"11796115"
] | [
"Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Fungi",
"Halobacteriales",
"metagenomes"
] | [
678,
81,
143,
13
] | 4 | [] | [] | 0 | true | Domain | Methylaspartate ammonia-lyase, N-terminal | Methylaspartate ammonia-lyase, N-terminal | MeAsp_NH4-lyase_N | 9 |
IPR022666 | 22,666 | Large ribosomal subunit protein uL2, RNA-binding domain | Ribosomal_uL2_RNA-bd_dom | Domain | 52,443 | false | false | This entry represents the N-terminal RNA-binding domain of the large ribosomal subunit protein uL2. Ribosomal protein uL2 is one of the proteins from the large ribosomal subunit. The best conserved region is located in the C-terminal section of these proteins. In Escherichia coli, uL2 is known to bind to the 23S rRNA a... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF00181",
"SM01383"
] | [
"Ribosomal_L2_N",
"Ribosomal_L2"
] | [
52060,
52140
] | 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-156827",
"R-BTA-1799339",
"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-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-9629569",
"R-CEL-975956",
"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-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-9629569",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL... | 98 | [
"1c04",
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1rl2",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9"... | 1,898 | [
"PUB00004403",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"1579444",
"11297922",
"11290319",
"11114498"
] | [
"cDNA nucleotide sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1992,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
930,
24267,
26828,
418
] | 4 | [
"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,
2,
3,
5,
1,
9,
7,
2,
10,
9,
3,
4,
16
] | 13 | true | Domain | Large ribosomal subunit protein uL2, RNA-binding domain | Large ribosomal subunit protein uL2, RNA-binding domain | Ribosomal_uL2_RNA-bd_dom | 5 |
IPR022667 | 22,667 | Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, N-terminal | ForMFR_H4MPT_ForTrfase_N | Domain | 1,173 | false | false | This entry represents the ferredoxin-like Ftr N-terminal domain. Formylmethanofuran:tetrahyromethanopterin formyltransferase (Ftr) is involved in C1 metabolism in methanogenic archaea, sulphate-reducing archaea and methylotrophic bacteria. It catalyses the following reversible reaction: N-formylmethanofuran + 5,6,7,8-t... | [
"GO:0016740",
"GO:0006730"
] | [
"transferase activity",
"one-carbon metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01913"
] | [
"FTR"
] | [
1173
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.101",
"PWY-5209",
"PWY-7784",
"PWY-8305"
] | [
"EC:2.3.1.101",
"METACYC:PWY-5209",
"METACYC:PWY-7784",
"METACYC:PWY-8305"
] | 4 | [
"1ftr",
"1m5h",
"1m5s",
"2fhj",
"2fhk",
"6s6y"
] | 6 | [
"PUB00005787",
"PUB00016939",
"PUB00016940"
] | [
"9195883",
"12192072",
"12123819"
] | [
"Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.",
"Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.",
"Generation of for... | [
1997,
2002,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cladocopium goreaui",
"unclassified sequences"
] | [
355,
771,
2,
45
] | 4 | [] | [] | 0 | true | Domain | Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, N-terminal | Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, N-terminal | ForMFR_H4MPT_ForTrfase_N | 5 |
IPR022669 | 22,669 | Large ribosomal subunit protein uL2, C-terminal | Ribosomal_uL2_C | Domain | 54,194 | false | false | This entry represents the C-terminal domain of the large ribosomal subunit protein uL2. Ribosomal protein uL2 is one of the proteins from the large ribosomal subunit. The best conserved region is located in the C-terminal section of these proteins. In Escherichia coli, uL2 is known to bind to the 23S rRNA and to have p... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF03947",
"SM01382"
] | [
"Ribosomal_L2_C",
"Ribosomal_L2_C"
] | [
54123,
53960
] | 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-156827",
"R-BTA-1799339",
"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-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-9629569",
"R-CEL-975956",
"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-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-9629569",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL... | 98 | [
"1c04",
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1rl2",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9"... | 1,895 | [
"PUB00004403",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"1579444",
"11297922",
"11290319",
"11114498"
] | [
"cDNA nucleotide sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1992,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
935,
24458,
28361,
440
] | 4 | [
"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,
2,
3,
5,
1,
8,
6,
2,
9,
12,
3,
4,
24
] | 13 | true | Domain | Large ribosomal subunit protein uL2, C-terminal | Large ribosomal subunit protein uL2, C-terminal | Ribosomal_uL2_C | 3 |
IPR022671 | 22,671 | Large ribosomal subunit protein uL2, conserved site | Ribosomal_uL2_CS | Conserved_site | 45,641 | false | false | This entry represents the best conserved region located in the C-terminal section of the large ribosomal subunit protein uL2. Ribosomal protein uL2 is one of the proteins from the large ribosomal subunit. The best conserved region is located in the C-terminal section of these proteins. In Escherichia coli, uL2 is known... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00467"
] | [
"RIBOSOMAL_L2"
] | [
45641
] | 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-72689",
"R-BTA-72706",
"R-BTA-9629569",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-9629569",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-7... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"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-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72... | 85 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql"... | 1,739 | [
"PUB00004403",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"1579444",
"11297922",
"11290319",
"11114498"
] | [
"cDNA nucleotide sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1992,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
417,
21356,
23538,
330
] | 4 | [
"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,
1,
2,
1,
3,
3,
1,
8,
4,
3,
4,
21
] | 13 | true | Conserved_site | Large ribosomal subunit protein uL2, conserved site | Large ribosomal subunit protein uL2, conserved site | Ribosomal_uL2_CS | 6 |
IPR022672 | 22,672 | Hexokinase, N-terminal | Hexokinase_N | Domain | 21,863 | false | false | Hexokinase is an important enzyme that catalyses the ATP-dependent conversion of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). The enzyme can catalyse this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways [ ]. The addition of a phos... | [
"GO:0005524",
"GO:0005975"
] | [
"ATP binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00349"
] | [
"Hexokinase_1"
] | [
21863
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"2.7.1.1",
"GenProp1492",
"GenProp1580",
"GenProp1639",
"R-DME-170822",
"R-DME-446205",
"R-DME-6798695",
"R-DME-70171",
"R-HSA-170822",
"R-HSA-210745",
"R-HSA-446205",
"R-HSA-5619056",
"R-HSA-5619073",
"R-HSA-5619107",
"R-HSA-6798695",
"R-HSA-70171",
"R-HSA-9615017",
"R-MMU-170822"... | [
"EC:2.7.1.1",
"GP:GenProp1492",
"GP:GenProp1580",
"GP:GenProp1639",
"REACTOME:R-DME-170822",
"REACTOME:R-DME-446205",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-70171",
"REACTOME:R-HSA-170822",
"REACTOME:R-HSA-210745",
"REACTOME:R-HSA-446205",
"REACTOME:R-HSA-5619056",
"REACTOME:R-HSA-5619073... | 33 | [
"1bdg",
"1bg3",
"1cza",
"1dgk",
"1hkb",
"1hkc",
"1hkg",
"1ig8",
"1qha",
"1v4s",
"1v4t",
"2nzt",
"2yhx",
"3a0i",
"3b8a",
"3f9m",
"3fgu",
"3fr0",
"3goi",
"3h1v",
"3hm8",
"3id8",
"3idh",
"3imx",
"3o08",
"3o1b",
"3o1w",
"3o4w",
"3o5b",
"3o6w",
"3o80",
"3o8m"... | 89 | [
"PUB00001951",
"PUB00014214",
"PUB00014215",
"PUB00103708"
] | [
"1783373",
"12756287",
"10749890",
"36216916"
] | [
"Mammalian hexokinase 1: evolutionary conservation and structure to function analysis.",
"Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function.",
"The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into it... | [
1991,
2003,
2000,
2022
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
414,
21442,
7
] | 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... | [
29,
4,
8,
12,
42,
27,
5,
25,
38,
5,
2,
44
] | 12 | true | Domain | Hexokinase, N-terminal | Hexokinase, N-terminal | Hexokinase_N | 3 |
IPR022673 | 22,673 | Hexokinase, C-terminal | Hexokinase_C | Domain | 22,202 | false | false | Hexokinase is an important enzyme that catalyses the ATP-dependent conversion of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). The enzyme can catalyse this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways [ ]. The addition of a phos... | [
"GO:0005524",
"GO:0005975"
] | [
"ATP binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF03727"
] | [
"Hexokinase_2"
] | [
22202
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"2.7.1.1",
"GenProp1492",
"GenProp1580",
"GenProp1639",
"R-DME-170822",
"R-DME-446205",
"R-DME-6798695",
"R-DME-70171",
"R-HSA-170822",
"R-HSA-210745",
"R-HSA-446205",
"R-HSA-5619056",
"R-HSA-5619073",
"R-HSA-5619107",
"R-HSA-6798695",
"R-HSA-70171",
"R-HSA-9615017",
"R-MMU-170822"... | [
"EC:2.7.1.1",
"GP:GenProp1492",
"GP:GenProp1580",
"GP:GenProp1639",
"REACTOME:R-DME-170822",
"REACTOME:R-DME-446205",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-70171",
"REACTOME:R-HSA-170822",
"REACTOME:R-HSA-210745",
"REACTOME:R-HSA-446205",
"REACTOME:R-HSA-5619056",
"REACTOME:R-HSA-5619073... | 33 | [
"1bdg",
"1bg3",
"1cza",
"1dgk",
"1hkb",
"1hkc",
"1hkg",
"1ig8",
"1qha",
"1v4s",
"1v4t",
"2nzt",
"2yhx",
"3a0i",
"3b8a",
"3f9m",
"3fgu",
"3fr0",
"3goi",
"3h1v",
"3hm8",
"3id8",
"3idh",
"3imx",
"3o08",
"3o1b",
"3o1w",
"3o4w",
"3o5b",
"3o6w",
"3o80",
"3o8m"... | 89 | [
"PUB00001951",
"PUB00014214",
"PUB00014215",
"PUB00103708"
] | [
"1783373",
"12756287",
"10749890",
"36216916"
] | [
"Mammalian hexokinase 1: evolutionary conservation and structure to function analysis.",
"Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function.",
"The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into it... | [
1991,
2003,
2000,
2022
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
432,
21759,
11
] | 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... | [
33,
6,
7,
16,
51,
23,
5,
29,
36,
5,
2,
49
] | 12 | true | Domain | Hexokinase, C-terminal | Hexokinase, C-terminal | Hexokinase_C | 3 |
IPR022674 | 22,674 | Glucose-6-phosphate dehydrogenase, NAD-binding | G6P_DH_NAD-bd | Domain | 36,542 | false | false | This entry represents the NAD-binding domain of glucose-6-phosphate dehydrogenase. Glucose-6-phosphate dehydrogenase ( ) (G6PDH) is a ubiquitous protein, present in bacteria and all eukaryotic cell types [ ]. The enzyme catalyses the the first step in the pentose pathway, i.e. the conversion of glucose-6-phosphate to g... | [
"GO:0050661",
"GO:0006006"
] | [
"NADP binding",
"glucose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00479"
] | [
"G6PD_N"
] | [
36542
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.49",
"PWY-7268",
"PWY-8004",
"R-CEL-5628897",
"R-CEL-71336",
"R-DDI-5628897",
"R-DDI-71336",
"R-DME-5628897",
"R-DME-71336",
"R-HSA-5628897",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-5628897",
"R-MMU-71336",
"R-PFA-5628897",
"R-PFA-71336",
"R-RNO-5628897",
"R-RNO-71... | [
"EC:1.1.1",
"EC:1.1.1.49",
"METACYC:PWY-7268",
"METACYC:PWY-8004",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-5628897",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-5628897",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",... | 23 | [
"1dpg",
"1e77",
"1e7m",
"1e7y",
"1h93",
"1h94",
"1h9a",
"1h9b",
"1qki",
"2bh9",
"2bhl",
"2dpg",
"4lgv",
"5aq1",
"5ukw",
"6d23",
"6d24",
"6e07",
"6e08",
"6jyu",
"6va0",
"6va7",
"6va8",
"6va9",
"6vaq",
"7e6h",
"7e6i",
"7seh",
"7sei",
"7snf",
"7sng",
"7snh"... | 58 | [
"PUB00001763",
"PUB00097191",
"PUB00097192"
] | [
"2838391",
"26479991",
"24769394"
] | [
"Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene.",
"Severe G6PD Deficiency Due to a New Missense Mutation in an Infant of Northern European Descent.",
"Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cel... | [
1988,
2015,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
5,
25798,
23,
10442,
274
] | 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",... | [
32,
1,
10,
3,
1,
33,
10,
1,
18,
5,
1,
3,
32
] | 13 | true | Domain | Glucose-6-phosphate dehydrogenase, NAD-binding | Glucose-6-phosphate dehydrogenase, NAD-binding | G6P_DH_NAD-bd | 9 |
IPR022675 | 22,675 | Glucose-6-phosphate dehydrogenase, C-terminal | G6P_DH_C | Domain | 37,612 | false | false | Glucose-6-phosphate dehydrogenase ( ) (G6PDH) is a ubiquitous protein, present in bacteria and all eukaryotic cell types [ ]. The enzyme catalyses the the first step in the pentose pathway, i.e. the conversion of glucose-6-phosphate to gluconolactone 6-phosphate in the presence of NADP, producing NADPH. The ubiquitous ... | [
"GO:0004345",
"GO:0050661",
"GO:0006006"
] | [
"glucose-6-phosphate dehydrogenase activity",
"NADP binding",
"glucose metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF02781"
] | [
"G6PD_C"
] | [
37612
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.49",
"PWY-7268",
"PWY-8004",
"R-CEL-5628897",
"R-CEL-71336",
"R-DDI-5628897",
"R-DDI-71336",
"R-DME-5628897",
"R-DME-71336",
"R-HSA-5628897",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-5628897",
"R-MMU-71336",
"R-PFA-5628897",
"R-PFA-71336",
"R-RNO-5628897",
"R-RNO-71... | [
"EC:1.1.1",
"EC:1.1.1.49",
"METACYC:PWY-7268",
"METACYC:PWY-8004",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-71336",
"REACTOME:R-DDI-5628897",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-5628897",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",... | 23 | [
"1dpg",
"1e77",
"1e7m",
"1e7y",
"1h93",
"1h94",
"1h9a",
"1h9b",
"1qki",
"2bh9",
"2bhl",
"2dpg",
"4lgv",
"5aq1",
"5ukw",
"6d23",
"6d24",
"6e07",
"6e08",
"6jyu",
"6va0",
"6va7",
"6va8",
"6va9",
"6vaq",
"7e6h",
"7e6i",
"7seh",
"7sei",
"7snf",
"7sng",
"7snh"... | 58 | [
"PUB00001763",
"PUB00097191",
"PUB00097192"
] | [
"2838391",
"26479991",
"24769394"
] | [
"Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene.",
"Severe G6PD Deficiency Due to a New Missense Mutation in an Infant of Northern European Descent.",
"Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cel... | [
1988,
2015,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4,
26475,
10788,
24,
321
] | 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",... | [
31,
1,
10,
3,
1,
24,
9,
1,
18,
5,
1,
3,
35
] | 13 | true | Domain | Glucose-6-phosphate dehydrogenase, C-terminal | Glucose-6-phosphate dehydrogenase, C-terminal | G6P_DH_C | 1 |
IPR022676 | 22,676 | Glycylpeptide N-tetradecanoyltransferase, N-terminal | NMT_N | Domain | 7,144 | false | false | Glycylpeptide N-tetradecanoyltransferase, also known as Myristoyl-CoA:protein N-myristoyltransferase ( ) (Nmt), is the enzyme responsible for transferring a myristate group on the N-terminal glycine of a number of cellular eukaryotics and viral proteins [ ]. Nmt is a monomeric protein of about 50 to 60kDa whose sequenc... | [
"GO:0004379"
] | [
"glycylpeptide N-tetradecanoyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01233"
] | [
"NMT"
] | [
7144
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.97",
"R-BTA-2514859",
"R-DDI-2514859",
"R-DRE-2514859",
"R-HSA-162599",
"R-HSA-174490",
"R-HSA-203615",
"R-HSA-2514859",
"R-HSA-75108",
"R-MMU-2514859",
"R-MMU-75108",
"R-RNO-2514859",
"R-RNO-75108",
"R-SCE-2514859",
"R-SPO-2514859"
] | [
"EC:2.3.1.97",
"REACTOME:R-BTA-2514859",
"REACTOME:R-DDI-2514859",
"REACTOME:R-DRE-2514859",
"REACTOME:R-HSA-162599",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-203615",
"REACTOME:R-HSA-2514859",
"REACTOME:R-HSA-75108",
"REACTOME:R-MMU-2514859",
"REACTOME:R-MMU-75108",
"REACTOME:R-RNO-2514859",
... | 15 | [
"1iic",
"1iid",
"1iyk",
"1iyl",
"1nmt",
"1rxt",
"2nmt",
"2p6e",
"2p6f",
"2p6g",
"2wsa",
"2wuu",
"2ync",
"2ynd",
"2yne",
"3h5z",
"3iu1",
"3iu2",
"3iwe",
"3jtk",
"4a2z",
"4a30",
"4a31",
"4a32",
"4a33",
"4a95",
"4b10",
"4b11",
"4b12",
"4b13",
"4b14",
"4bbh"... | 157 | [
"PUB00000005",
"PUB00019930",
"PUB00100072"
] | [
"8322618",
"9501915",
"11139338"
] | [
"MyristoylCoA:protein N-myristoyltransferase.",
"Crystal structure of the anti-fungal target N-myristoyl transferase.",
"Drosophila embryos lacking N-myristoyltransferase have multiple developmental defects."
] | [
1993,
1998,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Nucleocytoviricota",
"metagenomes"
] | [
7049,
55,
40
] | 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,
2,
8,
1,
13,
6,
1,
4,
11,
1,
1,
6
] | 12 | true | Domain | Glycylpeptide N-tetradecanoyltransferase, N-terminal | Glycylpeptide N-tetradecanoyltransferase, N-terminal | NMT_N | 1 |
IPR022677 | 22,677 | Glycylpeptide N-tetradecanoyltransferase, C-terminal | NMT_C | Domain | 7,137 | false | false | Glycylpeptide N-tetradecanoyltransferase, also known as Myristoyl-CoA:protein N-myristoyltransferase ( ) (Nmt), is the enzyme responsible for transferring a myristate group on the N-terminal glycine of a number of cellular eukaryotics and viral proteins [ ]. Nmt is a monomeric protein of about 50 to 60kDa whose sequenc... | [
"GO:0004379"
] | [
"glycylpeptide N-tetradecanoyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02799"
] | [
"NMT_C"
] | [
7137
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.97",
"R-BTA-2514859",
"R-DDI-2514859",
"R-DRE-2514859",
"R-HSA-162599",
"R-HSA-174490",
"R-HSA-203615",
"R-HSA-2514859",
"R-HSA-75108",
"R-MMU-2514859",
"R-MMU-75108",
"R-RNO-2514859",
"R-RNO-75108",
"R-SCE-2514859",
"R-SPO-2514859"
] | [
"EC:2.3.1.97",
"REACTOME:R-BTA-2514859",
"REACTOME:R-DDI-2514859",
"REACTOME:R-DRE-2514859",
"REACTOME:R-HSA-162599",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-203615",
"REACTOME:R-HSA-2514859",
"REACTOME:R-HSA-75108",
"REACTOME:R-MMU-2514859",
"REACTOME:R-MMU-75108",
"REACTOME:R-RNO-2514859",
... | 15 | [
"1iic",
"1iid",
"1iyk",
"1iyl",
"1nmt",
"1rxt",
"2nmt",
"2p6e",
"2p6f",
"2p6g",
"2wsa",
"2wuu",
"2ync",
"2ynd",
"2yne",
"3h5z",
"3iu1",
"3iu2",
"3iwe",
"3jtk",
"4a2z",
"4a30",
"4a31",
"4a32",
"4a33",
"4a95",
"4b10",
"4b11",
"4b12",
"4b13",
"4b14",
"4bbh"... | 157 | [
"PUB00000005",
"PUB00019930",
"PUB00100072"
] | [
"8322618",
"9501915",
"11139338"
] | [
"MyristoylCoA:protein N-myristoyltransferase.",
"Crystal structure of the anti-fungal target N-myristoyl transferase.",
"Drosophila embryos lacking N-myristoyltransferase have multiple developmental defects."
] | [
1993,
1998,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Megaviricetes",
"Pseudomyxococcus hansupus",
"metagenomes"
] | [
7087,
41,
1,
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... | [
7,
2,
8,
1,
13,
6,
1,
3,
11,
1,
1,
6
] | 12 | true | Domain | Glycylpeptide N-tetradecanoyltransferase, C-terminal | Glycylpeptide N-tetradecanoyltransferase, C-terminal | NMT_C | 9 |
IPR022678 | 22,678 | Glycylpeptide N-tetradecanoyltransferase, conserved site | NMT_CS | Conserved_site | 6,530 | false | false | Glycylpeptide N-tetradecanoyltransferase, also known as Myristoyl-CoA:protein N-myristoyltransferase ( ) (Nmt), is the enzyme responsible for transferring a myristate group on the N-terminal glycine of a number of cellular eukaryotics and viral proteins [ ]. Nmt is a monomeric protein of about 50 to 60kDa whose sequenc... | [
"GO:0004379"
] | [
"glycylpeptide N-tetradecanoyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00975",
"PS00976"
] | [
"NMT_1",
"NMT_2"
] | [
5744,
5682
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.97",
"R-BTA-2514859",
"R-DDI-2514859",
"R-DRE-2514859",
"R-HSA-162599",
"R-HSA-174490",
"R-HSA-203615",
"R-HSA-2514859",
"R-HSA-75108",
"R-MMU-2514859",
"R-MMU-75108",
"R-RNO-2514859",
"R-RNO-75108",
"R-SCE-2514859",
"R-SPO-2514859"
] | [
"EC:2.3.1.97",
"REACTOME:R-BTA-2514859",
"REACTOME:R-DDI-2514859",
"REACTOME:R-DRE-2514859",
"REACTOME:R-HSA-162599",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-203615",
"REACTOME:R-HSA-2514859",
"REACTOME:R-HSA-75108",
"REACTOME:R-MMU-2514859",
"REACTOME:R-MMU-75108",
"REACTOME:R-RNO-2514859",
... | 15 | [
"1iic",
"1iid",
"1iyk",
"1iyl",
"1nmt",
"1rxt",
"2nmt",
"2p6e",
"2p6f",
"2p6g",
"2wsa",
"2wuu",
"2ync",
"2ynd",
"2yne",
"3h5z",
"3iu1",
"3iu2",
"3iwe",
"3jtk",
"4a2z",
"4a30",
"4a31",
"4a32",
"4a33",
"4a95",
"4b10",
"4b11",
"4b12",
"4b13",
"4b14",
"4bbh"... | 154 | [
"PUB00000005",
"PUB00100072"
] | [
"8322618",
"11139338"
] | [
"MyristoylCoA:protein N-myristoyltransferase.",
"Drosophila embryos lacking N-myristoyltransferase have multiple developmental defects."
] | [
1993,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Orpheovirus IHUMI-LCC2",
"viral metagenome"
] | [
27,
6501,
1,
1
] | 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... | [
7,
2,
4,
1,
13,
6,
1,
3,
11,
1,
1,
6
] | 12 | true | Conserved_site | Glycylpeptide N-tetradecanoyltransferase, conserved site | Glycylpeptide N-tetradecanoyltransferase, conserved site | NMT_CS | 1 |
IPR022679 | 22,679 | Methyl-coenzyme M reductase, beta subunit, C-terminal | Me_CoM_Rdtase_bsu_C | Domain | 335 | 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"
] | [
"coenzyme-B sulfoethylthiotransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02241"
] | [
"MCR_beta"
] | [
335
] | 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",
"metagenomes"
] | [
328,
7
] | 2 | [] | [] | 0 | true | Domain | Methyl-coenzyme M reductase, beta subunit, C-terminal | Methyl-coenzyme M reductase, beta subunit, C-terminal | Me_CoM_Rdtase_bsu_C | 6 |
IPR022680 | 22,680 | Methyl-coenzyme M reductase, beta subunit, N-terminal | Me_CoM_Rdtase_bsu_N | Domain | 332 | false | false | This entry represents the N-terminal domain from the beta subunit of methyl-conenzyme M reductase (MCR). The N-terminal domain has an α/β ferredoxin-like fold. This entry is found in assocation with . Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to me... | [
"GO:0050524"
] | [
"coenzyme-B sulfoethylthiotransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02783"
] | [
"MCR_beta_N"
] | [
332
] | 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",
"ecological metagenomes"
] | [
326,
6
] | 2 | [] | [] | 0 | true | Domain | Methyl-coenzyme M reductase, beta subunit, N-terminal | Methyl-coenzyme M reductase, beta subunit, N-terminal | Me_CoM_Rdtase_bsu_N | 3 |
IPR022682 | 22,682 | Peptidase C2, calpain, large subunit, domain III | Calpain_domain_III | Domain | 24,177 | false | false | This entry represents domain III. The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions. This group of cysteine peptidases belong to the MER... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01067"
] | [
"Calpain_III"
] | [
24177
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.22",
"R-BTA-1474228",
"R-BTA-9856530",
"R-BTA-9860927",
"R-CEL-6798695",
"R-DDI-6798695",
"R-DME-6798695",
"R-HSA-1474228",
"R-HSA-6798695",
"R-HSA-6809371",
"R-HSA-8862803",
"R-HSA-9856530",
"R-HSA-9860927",
"R-MMU-1474228",
"R-MMU-6798695",
"R-MMU-9856530",
"R-MMU-9860927",
... | [
"EC:3.4.22",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-9856530",
"REACTOME:R-BTA-9860927",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-6798695",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-8862803",
"REACTOME:R-HSA-98565... | 23 | [
"1df0",
"1kfu",
"1kfx",
"1qxp",
"1u5i",
"2qfe",
"3bow",
"3df0",
"7x79",
"8gx3"
] | 10 | [
"PUB00000551",
"PUB00002525",
"PUB00002542",
"PUB00003577",
"PUB00007140",
"PUB00014535",
"PUB00018208",
"PUB00018209",
"PUB00081543",
"PUB00081544",
"PUB00081545"
] | [
"9396712",
"2555341",
"2539381",
"7845226",
"11914728",
"12843408",
"11854009",
"11950589",
"11328585",
"11517928",
"21864727"
] | [
"Structure and physiological function of calpains.",
"Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle.",
"Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the la... | [
1997,
1989,
1989,
1994,
2002,
2003,
2002,
2002,
2001,
2001,
2012
] | 11 | [] | [
"IPR022683"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
24177
] | 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",
"Zea mays"
] | [
5,
7,
63,
7,
52,
42,
2,
4,
56,
14
] | 10 | true | Domain | Peptidase C2, calpain, large subunit, domain III | Peptidase C2, calpain, large subunit, domain III | Calpain_domain_III | 6 |
IPR022683 | 22,683 | Peptidase C2, calpain, domain III | Calpain_III | Domain | 24,247 | false | false | A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic ... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00720"
] | [
"calpain_III"
] | [
24247
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.22",
"R-BTA-1474228",
"R-BTA-9856530",
"R-BTA-9860927",
"R-CEL-6798695",
"R-DDI-6798695",
"R-DME-6798695",
"R-HSA-1474228",
"R-HSA-6798695",
"R-HSA-6809371",
"R-HSA-8862803",
"R-HSA-9856530",
"R-HSA-9860927",
"R-MMU-1474228",
"R-MMU-6798695",
"R-MMU-9856530",
"R-MMU-9860927",
... | [
"EC:3.4.22",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-9856530",
"REACTOME:R-BTA-9860927",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-6798695",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-8862803",
"REACTOME:R-HSA-98565... | 23 | [
"1df0",
"1kfu",
"1kfx",
"1qxp",
"1u5i",
"2qfe",
"3bow",
"3df0",
"7x79",
"8gx3"
] | 10 | [
"PUB00000551",
"PUB00002525",
"PUB00002542",
"PUB00003577",
"PUB00007140",
"PUB00011704",
"PUB00014535",
"PUB00020025",
"PUB00030423",
"PUB00076953",
"PUB00081543",
"PUB00081544",
"PUB00081545"
] | [
"9396712",
"2555341",
"2539381",
"7845226",
"11914728",
"11517925",
"12843408",
"9891971",
"14725770",
"7044372",
"11328585",
"11517928",
"21864727"
] | [
"Structure and physiological function of calpains.",
"Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle.",
"Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the la... | [
1997,
1989,
1989,
1994,
2002,
2001,
2003,
1998,
2004,
1982,
2001,
2001,
2012
] | 13 | [
"IPR022682"
] | [
"IPR033883"
] | 1 | 1 | 0 | [
"Eukaryota"
] | [
24247
] | 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",
"Zea mays"
] | [
5,
7,
63,
7,
50,
39,
2,
4,
54,
14
] | 10 | true | Domain | Peptidase C2, calpain, domain III | Peptidase C2, calpain, domain III | Calpain_III | 7 |
IPR022684 | 22,684 | Peptidase C2, calpain family | Calpain_cysteine_protease | Family | 35,899 | false | false | This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family, clan CA). A type example is calpain, which is an intracellular protease involved in many important cellular functions that are regulated by calcium [ , , , ]. The protein is a complex of 2 polypeptide chains (light and heavy), w... | [
"GO:0004198",
"GO:0006508"
] | [
"calcium-dependent cysteine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR00704",
"PTHR10183"
] | [
"CALPAIN",
""
] | [
31807,
33109
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.22",
"R-BTA-1474228",
"R-BTA-9856530",
"R-BTA-9860927",
"R-CEL-6798695",
"R-DDI-6798695",
"R-DME-6798695",
"R-HSA-1474228",
"R-HSA-6798695",
"R-HSA-6809371",
"R-HSA-8862803",
"R-HSA-9856530",
"R-HSA-9860927",
"R-MMU-1474228",
"R-MMU-6798695",
"R-MMU-9856530",
"R-MMU-9860927",
... | [
"EC:3.4.22",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-9856530",
"REACTOME:R-BTA-9860927",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-6798695",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-8862803",
"REACTOME:R-HSA-98565... | 23 | [
"1df0",
"1kfu",
"1kfx",
"1kxr",
"1mdw",
"1qxp",
"1tl9",
"1tlo",
"1u5i",
"1zcm",
"1ziv",
"2ary",
"2g8e",
"2g8j",
"2nqa",
"2nqg",
"2nqi",
"2p0r",
"2qfe",
"2r9c",
"2r9f",
"3bow",
"3df0",
"6bdt",
"6bgp",
"6bjd",
"6bkj",
"6p3q",
"7w7o",
"7x79",
"8gx3"
] | 31 | [
"PUB00000551",
"PUB00002525",
"PUB00002542",
"PUB00003577",
"PUB00007140",
"PUB00014535",
"PUB00018208",
"PUB00018209",
"PUB00081543",
"PUB00081544",
"PUB00081545"
] | [
"9396712",
"2555341",
"2539381",
"7845226",
"11914728",
"12843408",
"11854009",
"11950589",
"11328585",
"11517928",
"21864727"
] | [
"Structure and physiological function of calpains.",
"Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle.",
"Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the la... | [
1997,
1989,
1989,
1994,
2002,
2003,
2002,
2002,
2001,
2001,
2012
] | 11 | [] | [] | 0 | 0 | null | [
"Aureococcus anophagefferens virus",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1,
550,
35337,
11
] | 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",
"Zea mays"
] | [
5,
17,
65,
11,
69,
53,
5,
4,
64,
21
] | 10 | true | Family | Peptidase C2, calpain family | Peptidase C2, calpain family | Calpain_cysteine_protease | 3 |
IPR022686 | 22,686 | Replication-associated protein G2P, N-terminal | G2P_N | Domain | 978 | false | false | The entry represents the N-terminal domain found in gene II protein (G2P) from Enterobacteria phage M13 and similar proteins from bacteriophages and bacterial prophages. A much shorter protein of unknown function, translated from a conserved in-frame alternative initiator, is designated gene X protein (G10P). Proteins ... | [
"GO:0006260"
] | [
"DNA replication"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF05144"
] | [
"Phage_CRI"
] | [
978
] | 1 | [
"EC",
"EC"
] | [
"3.1.21.-",
"6.5.1.1"
] | [
"EC:3.1.21.-",
"EC:6.5.1.1"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
913,
5,
30,
30
] | 4 | [] | [] | 0 | true | Domain | Replication-associated protein G2P, N-terminal | Replication-associated protein G2P, N-terminal | G2P_N | 3 |
IPR022688 | 22,688 | Replication-associated protein G2P, C-terminal | G2P_C | Domain | 661 | false | false | The entry represents the C-terminal domain found in gene II protein (G2P) from bacteriophage. A much shorter protein of unknown function, translated from a conserved in-frame alternative initiator, is designated gene X protein (G10P). Proteins containing this domain are involved in viral DNA replication. This domain ro... | [
"GO:0006260"
] | [
"DNA replication"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF05155"
] | [
"G2P_X_C"
] | [
661
] | 1 | [
"EC",
"EC"
] | [
"3.1.21.-",
"6.5.1.1"
] | [
"EC:3.1.21.-",
"EC:6.5.1.1"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Inoviridae",
"unclassified sequences"
] | [
608,
3,
35,
15
] | 4 | [] | [] | 0 | true | Domain | Replication-associated protein G2P, C-terminal | Replication-associated protein G2P, C-terminal | G2P_C | 5 |
IPR022689 | 22,689 | Iron dependent repressor | Iron_dep_repressor | Family | 21,648 | false | false | This entry represents a group of iron dependent repressors, including MntR, IdeR and diphtheria toxin repressor. The diphtheria toxin repressor protein (DTXR) is a member of this group [ ]. In Corynebacterium diphtheriae where it has been studied in some detail this protein acts as an iron-binding repressor of diphther... | [
"GO:0003700",
"GO:0046914",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"transition metal ion binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"SMART"
] | [
"SM00529"
] | [
"HTH_DTXR"
] | [
21648
] | 1 | [] | [] | [] | 0 | [
"1b1b",
"1bi0",
"1bi1",
"1bi2",
"1bi3",
"1c0w",
"1ddn",
"1dpr",
"1f5t",
"1fwz",
"1fx7",
"1g3s",
"1g3t",
"1g3w",
"1g3y",
"1on1",
"1on2",
"1p92",
"1u8r",
"1xcv",
"2dtr",
"2ev0",
"2ev5",
"2ev6",
"2f5c",
"2f5d",
"2f5e",
"2f5f",
"2h09",
"2hyf",
"2hyg",
"2isy"... | 69 | [
"PUB00004874",
"PUB00005267"
] | [
"7568230",
"7743135"
] | [
"Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.",
"Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors."
] | [
1995,
1995
] | 2 | [] | [
"IPR022897"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctevH2",
"unclassified sequences"
] | [
1986,
19280,
21,
1,
360
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Iron dependent repressor | Iron dependent repressor | Iron_dep_repressor | 3 |
IPR022691 | 22,691 | Transcription elongation factor, GreA/GreB, N-terminal | Tscrpt_elong_fac_GreA/B_N | Domain | 33,112 | false | false | Bacterial proteins GreA and GreB are necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. Arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked DNA/RNA/ polymerase ternary complexes. ... | [
"GO:0003677",
"GO:0032784"
] | [
"DNA binding",
"regulation of DNA-templated transcription elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF03449"
] | [
"GreA_GreB_N"
] | [
33112
] | 1 | [] | [] | [] | 0 | [
"1grj",
"2etn",
"2eul",
"2f23",
"2p4v",
"3aoh",
"3aoi",
"4wqt",
"6ri7",
"6rin"
] | 10 | [
"PUB00000884",
"PUB00004205",
"PUB00011909"
] | [
"8431948",
"7854424",
"12914698"
] | [
"Transcript cleavage factors from E. coli.",
"Crystal structure of the GreA transcript cleavage factor from Escherichia coli.",
"Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase."
] | [
1993,
1995,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
32417,
1,
69,
3,
622
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Transcription elongation factor, GreA/GreB, N-terminal | Transcription elongation factor, GreA/GreB, N-terminal | Tscrpt_elong_fac_GreA/B_N | 5 |
IPR022692 | 22,692 | Geminivirus AL1 replication-associated protein, central domain | Gemini_AL1_REP_central | Domain | 9,483 | false | false | Geminiviruses are characterised by a genome of circular single-stranded DNA encapsidated in twinned (geminate) quasi-isometric particles, from which the group derives its name [ ]. Most geminiviruses can be divided into two subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous... | [
"GO:0016888"
] | [
"DNA endonuclease activity, producing 5'-phosphomonoesters"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08283"
] | [
"Gemini_AL1_M"
] | [
9483
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.-",
"3.1.21.-",
"PWY-6322",
"PWY-6626",
"PWY-6749",
"PWY-6955",
"PWY-6998",
"PWY-7127",
"PWY-7419",
"PWY-7529",
"PWY-7706",
"PWY-7719",
"PWY-7735",
"PWY-7737",
"PWY-7769",
"PWY-7888",
"PWY-7904",
"PWY-8117",
"PWY-8179"
] | [
"EC:2.7.7.-",
"EC:3.1.21.-",
"METACYC:PWY-6322",
"METACYC:PWY-6626",
"METACYC:PWY-6749",
"METACYC:PWY-6955",
"METACYC:PWY-6998",
"METACYC:PWY-7127",
"METACYC:PWY-7419",
"METACYC:PWY-7529",
"METACYC:PWY-7706",
"METACYC:PWY-7719",
"METACYC:PWY-7735",
"METACYC:PWY-7737",
"METACYC:PWY-7769",... | 19 | [] | 0 | [
"PUB00001133",
"PUB00001145",
"PUB00003142",
"PUB00003143",
"PUB00004348",
"PUB00004397",
"PUB00005574",
"PUB00005578",
"PUB00017127"
] | [
"6526009",
"16453696",
"1919519",
"1588314",
"2829117",
"1840676",
"1984668",
"1926771",
"12130667"
] | [
"The nucleotide sequence of maize streak virus DNA.",
"The nucleotide sequence of an infectious clone of the geminivirus beet curly top virus.",
"The nucleotide sequence and genome structure of the geminivirus miscanthus streak virus.",
"The nucleotide sequence of an infectious insect-transmissible clone of t... | [
1984,
1986,
1991,
1992,
1988,
1991,
1991,
1991,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
197,
9285,
1
] | 3 | [] | [] | 0 | true | Domain | Geminivirus AL1 replication-associated protein, central domain | Geminivirus AL1 replication-associated protein, central domain | Gemini_AL1_REP_central | 4 |
IPR022694 | 22,694 | 3-hydroxyacyl-CoA dehydrogenase | 3-OHacyl-CoA_DH | Family | 31,309 | false | false | 3-hydroxyacyl-CoA dehydrogenase ( ) (HCDH) [ ] is an enzyme involved in fatty acid metabolism and catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have two fatty-acid beta-oxidation systems, one located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA de... | [
"GO:0016616",
"GO:0070403",
"GO:0006631"
] | [
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"NAD+ binding",
"fatty acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000105"
] | [
"HCDH"
] | [
31309
] | 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-5661270",
"R-CEL-77310",
"R-CEL-77346",
"R-CEL-77348",
"R-CEL-77350",
"R-CEL-77352",
"R-CEL-9837999",
"R-HSA-5661270",
"R-HSA-77310",
"R-HSA-77346",
"R-HSA-77348",
"R-HSA-77350",
"R-HSA-77352",
"R-HSA-9837999",
"R-MMU-5661270",
"R-MMU-77310",
"R-MMU-77346",
"R-MMU... | [
"EC:1.1.1",
"REACTOME:R-BTA-5661270",
"REACTOME:R-CEL-77310",
"REACTOME:R-CEL-77346",
"REACTOME:R-CEL-77348",
"REACTOME:R-CEL-77350",
"REACTOME:R-CEL-77352",
"REACTOME:R-CEL-9837999",
"REACTOME:R-HSA-5661270",
"REACTOME:R-HSA-77310",
"REACTOME:R-HSA-77346",
"REACTOME:R-HSA-77348",
"REACTOME:... | 35 | [
"1f0y",
"1f12",
"1f14",
"1f17",
"1il0",
"1lsj",
"1lso",
"1m75",
"1m76",
"1zej",
"2hdh",
"3ado",
"3adp",
"3f3s",
"3had",
"3hdh",
"3rqs",
"4dyd",
"4e12",
"4e13",
"4j0e",
"4j0f",
"4kue",
"4kug",
"4kuh",
"4om8",
"4pzc",
"4pzd",
"4pze",
"4r1n",
"6aa8",
"6acq"... | 40 | [
"PUB00004380",
"PUB00004646"
] | [
"2204034",
"3479790"
] | [
"Nucleotide sequence of the fadA and fadB genes from Escherichia coli.",
"Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution."
] | [
1990,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
801,
24015,
6155,
338
] | 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",
"Zea mays"
] | [
5,
3,
2,
1,
13,
3,
2,
2,
7,
3
] | 10 | true | Family | 3-hydroxyacyl-CoA dehydrogenase | 3-hydroxyacyl-CoA dehydrogenase | 3-OHacyl-CoA_DH | 5 |
IPR022695 | 22,695 | Histidinol dehydrogenase, monofunctional | Histidinol_DH_monofunct | Family | 27,435 | false | false | Histidinol dehydrogenase (HDH) catalyses the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine. In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermed... | [
"GO:0004399",
"GO:0046872",
"GO:0051287",
"GO:0000105"
] | [
"histidinol dehydrogenase activity",
"metal ion binding",
"NAD binding",
"L-histidine biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF000099"
] | [
"Histidinol_dh"
] | [
27435
] | 1 | [
"EC"
] | [
"1.1.1.23"
] | [
"EC:1.1.1.23"
] | 1 | [
"1k75",
"1kae",
"1kah",
"1kar",
"4g07",
"4g09",
"4gic",
"5vlb",
"5vlc",
"5vld",
"6an0",
"8v35",
"8v36",
"8v37",
"8wwe",
"8xsq",
"9cp7",
"9cp8",
"9cp9",
"9ivy",
"9lbv"
] | 21 | [
"PUB00000285",
"PUB00004740"
] | [
"3533140",
"2034659"
] | [
"A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase.",
"Structural and functional conservation of histidinol dehydrogenase between plants and microbes."
] | [
1986,
1991
] | 2 | [
"IPR012131"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
770,
25252,
1012,
401
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
1,
1,
1,
4
] | 5 | true | Family | Histidinol dehydrogenase, monofunctional | Histidinol dehydrogenase, monofunctional | Histidinol_DH_monofunct | 6 |
IPR022697 | 22,697 | Homoserine dehydrogenase lacking ACT domain | HDH_short | Family | 5,807 | false | false | This group represents a homoserine dehydrogenase lacking the ACT domain, such as HOM6 from Saccharomyces cerevisiae [ ]. It appears to be a naturally occurring feedback resistant homoserine dehydrogenase. | [
"GO:0004412"
] | [
"homoserine dehydrogenase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF036497"
] | [
"HDH_short"
] | [
5807
] | 1 | [
"EC"
] | [
"1.1.1.3"
] | [
"EC:1.1.1.3"
] | 1 | [
"1ebf",
"1ebu",
"1q7g",
"1tve",
"2ejw",
"3c8m",
"3do5",
"3ing",
"3jsa",
"4xb1",
"4xb2",
"4ydr",
"5avo",
"5x9d",
"5xdf",
"6a0r",
"6a0s",
"6a0t",
"6a0u",
"7f4b",
"7f4c",
"7m92"
] | 22 | [
"PUB00001656"
] | [
"8500624"
] | [
"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
851,
2639,
2258,
59
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
8,
1,
4,
1,
1,
6
] | 6 | true | Family | Homoserine dehydrogenase lacking ACT domain | Homoserine dehydrogenase lacking ACT domain | HDH_short | 4 |
IPR022698 | 22,698 | Orsellinic acid/F9775 biosynthesis cluster protein D | OrsD | Family | 2,815 | false | false | This family of proteins includes orsellinic acid/F9775 biosynthesis cluster protein D (orsD) from Emericella nidulans. The orsD gene is part of the cluster that encodes components for the biosynthesis of orsellinic acid, as well as biosynthesis of the cathepsin K inhibitors F9775 A and F9775 B [ , ], but the function o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12013"
] | [
"OrsD"
] | [
2815
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00083127",
"PUB00083128"
] | [
"19666480",
"20174687"
] | [
"Intimate bacterial-fungal interaction triggers biosynthesis of archetypal polyketides in Aspergillus nidulans.",
"Molecular genetic analysis of the orsellinic acid/F9775 gene cluster of Aspergillus nidulans."
] | [
2009,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Blastochloris viridis",
"Eukaryota"
] | [
1,
2814
] | 2 | [] | [] | 0 | true | Family | Orsellinic acid/F9775 biosynthesis cluster protein D | Orsellinic acid/F9775 biosynthesis cluster protein D | OrsD | 2 |
IPR022699 | 22,699 | Stonin-2, N-terminal | Stonin2_N | Domain | 1,004 | false | false | Stonin 2 is involved in clathrin mediated endocytosis [ ]. It binds to Eps15 by its highly conserved NPF motif. The complex formed has been shown to directly associate with the clathrin adaptor complex AP-2, and to localize to clathrin-coated pits (CCPs) [ ]. In addition, stonin2 was recently identified as a specific s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12016"
] | [
"Stonin2_N"
] | [
1004
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-8856825",
"R-RNO-8856828"
] | [
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-8856825",
"REACTOME:R-MMU-8856828",
"REACTOME:R-RNO-8856825",
"REACTOME:R-RNO-8856828"
] | 6 | [
"2jxc"
] | 1 | [
"PUB00053778"
] | [
"18200045"
] | [
"Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1004
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
7,
5,
2
] | 4 | true | Domain | Stonin-2, N-terminal | Stonin-2, N-terminal | Stonin2_N | 4 |
IPR022700 | 22,700 | Proteinase, regulatory CLIP domain | CLIP | Domain | 5,908 | false | false | The CLIP domain is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The domain is restricted to the arthropoda and found in varying copy numbers (from one to five in Drosophila proteins). It is always found N-terminal to the chymotrypsin serine pr... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF12032",
"PS51888",
"SM00680"
] | [
"CLIP",
"CLIP",
"CLIP"
] | [
3932,
4121,
5002
] | 3 | [
"EC",
"METACYC",
"REACTOME"
] | [
"3.4.21.-",
"PWY-7884",
"R-DME-209442"
] | [
"EC:3.4.21.-",
"METACYC:PWY-7884",
"REACTOME:R-DME-209442"
] | 3 | [
"2b9l",
"2ikd",
"2ike",
"2xxl"
] | 4 | [
"PUB00009689",
"PUB00053800",
"PUB00053801",
"PUB00059870"
] | [
"10066809",
"2107028",
"10696585",
"21310954"
] | [
"Prophenoloxidase-activating enzyme of the silkworm, Bombyx mori. Purification, characterization, and cDNA cloning.",
"Dominant and recessive alleles of the Drosophila easter gene are point mutations at conserved sites in the serine protease catalytic domain.",
"The clip-domain family of serine proteinases in a... | [
1999,
1990,
2000,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Arthropoda",
"Bacteria"
] | [
5904,
4
] | 2 | [
"Drosophila melanogaster"
] | [
40
] | 1 | true | Domain | Proteinase, regulatory CLIP domain | Proteinase, regulatory CLIP domain | CLIP | 2 |
IPR022701 | 22,701 | tRNA-queuosine alpha-mannosyltransferase, N-terminal | QTMAN_N | Domain | 2,604 | false | false | This domain is found in tRNA-queuosine alpha-mannosyltransferase (QTMAN, also known as Glycosyltransferase-like domain-containing protein 1 GTDC1) from animals and in uncharacterised bacterial sequences. QTMAN is a glycosyltransferase that specifically catalyses mannosylation of cytoplasmic tRNA(Asp) modified with queu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12038"
] | [
"QTMAN_N"
] | [
2604
] | 1 | [
"EC"
] | [
"2.4.1.110"
] | [
"EC:2.4.1.110"
] | 1 | [] | 0 | [
"PUB00153407"
] | [
"37992713"
] | [
"Glycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
606,
1949,
49
] | 3 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
2,
5,
6,
13
] | 5 | true | Domain | tRNA-queuosine alpha-mannosyltransferase, N-terminal | tRNA-queuosine alpha-mannosyltransferase, N-terminal | QTMAN_N | 5 |
IPR022703 | 22,703 | Domain of unknown function DUF3533 | DUF3533 | Domain | 4,566 | false | false | This transmembrane domain is functionally uncharacterised. It is found in bacterial and eukaryotic proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12051"
] | [
"DUF3533"
] | [
4566
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
1277,
3289
] | 2 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2
] | 1 | true | Domain | Domain of unknown function DUF3533 | Domain of unknown function DUF3533 | DUF3533 | 3 |
IPR022704 | 22,704 | Protein of unknown function DUF2746 | DUF2746 | Family | 452 | false | false | This entry represents proteins found in tailed bacteriophages and some species of Actinomicetes, including Gene 30 protein from Mycobacterium phage D29. Proteins in this entry are uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF10874"
] | [
"DUF2746"
] | [
452
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
51,
401
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF2746 | Protein of unknown function DUF2746 | DUF2746 | 8 |
IPR022706 | 22,706 | Antifungal protein | Antifungal_prot | Family | 166 | false | false | Antifungal proteinσ consists of five antiparallel β-strands which are highly twisted creating a β-barrel stabilised by four internal disulphide bridges [ ]. A cationic site adjacent to a hydrophobic stretch on the protein surface may constitute a phospholipid binding site [ ]. Members of this entry act as inhibitors of... | [
"GO:0050832"
] | [
"defense response to fungus"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF11402"
] | [
"Antifungal_prot"
] | [
166
] | 1 | [] | [] | [] | 0 | [
"1afp",
"2kcn",
"2mhv",
"2nb0",
"2nbf",
"2nc2",
"5oqs",
"6ha4",
"6hah",
"6haj",
"7bad",
"7bae",
"7baf",
"7nxi",
"7pgd",
"7ztf",
"7ztj",
"7zut",
"7zvh",
"7zw2",
"9fqf",
"9fqg",
"9iid"
] | 23 | [
"PUB00036270",
"PUB00101883",
"PUB00101884",
"PUB00101885"
] | [
"7893713",
"19683356",
"36005526",
"29379111"
] | [
"NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism.",
"Selection of antifungal protein-producing molds from dry-cured meat products.",
"Identification of PKS-NRPS Hybrid Metabolites in Marine-Derived <i>Penicillium oxalicum</i>.",
"New Antimic... | [
1995,
2009,
2022,
2018
] | 4 | [] | [] | 0 | 0 | null | [
"leotiomyceta"
] | [
166
] | 1 | [] | [] | 0 | true | Family | Antifungal protein | Antifungal protein | Antifungal_prot | 3 |
IPR022707 | 22,707 | Mot1, central domain | Mot1_central_dom | Domain | 4,779 | false | false | This domain is found in Mot1 and related proteins. The TATA-binding protein (TBP) is a major target for transcriptional regulation. Mot1, a Swi2/Snf2-related ATPase, dissociates TBP from DNA in an ATP dependent process [ ]. The N-terminal domain of Mot1 has been shown to bind TBP, NC2 and DNA. Its ATPase domain is at t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12054"
] | [
"DUF3535"
] | [
4779
] | 1 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"6g7e",
"7z7n",
"7z8s",
"7zb5",
"7zke"
] | 5 | [
"PUB00097645",
"PUB00097647"
] | [
"21658482",
"30289385"
] | [
"One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?",
"Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state."
] | [
2011,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4779
] | 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... | [
6,
1,
1,
4,
4,
3,
1,
4,
5,
1,
1,
21
] | 12 | true | Domain | Mot1, central domain | Mot1, central domain | Mot1_central_dom | 3 |
IPR022708 | 22,708 | Serine/threonine-protein kinase Atg1-like, tMIT domain | Atg1-like_tMIT | Domain | 4,672 | false | false | This the Atg13-binding region of Atg1 which comprises two tandem MIT (microtubule interacting and transport) domains, named tMIT [ ]. Members of this entry are Serine/threonine-protein kinases, including Atg1 from yeasts, Unc-51 from C. elegans and Ulk1-2 from humans. Atg1 is required for vesicle formation in autophagy... | [
"GO:0004674"
] | [
"protein serine/threonine kinase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12063"
] | [
"ATG1-like_MIT1"
] | [
4672
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.11.1",
"R-CEL-1632852",
"R-CEL-8854214",
"R-CEL-8934903",
"R-HSA-1632852",
"R-HSA-5357905",
"R-HSA-8854214",
"R-HSA-8876198",
"R-HSA-8934903",
"R-MMU-1632852",
"R-MMU-5357905",
"R-MMU-8854214",
"R-MMU-8876198",
"R-MMU-8934903",
"R-SCE-1632852",
"R-SCE-8934903",
"R-SPO-1632852",
... | [
"EC:2.7.11.1",
"REACTOME:R-CEL-1632852",
"REACTOME:R-CEL-8854214",
"REACTOME:R-CEL-8934903",
"REACTOME:R-HSA-1632852",
"REACTOME:R-HSA-5357905",
"REACTOME:R-HSA-8854214",
"REACTOME:R-HSA-8876198",
"REACTOME:R-HSA-8934903",
"REACTOME:R-MMU-1632852",
"REACTOME:R-MMU-5357905",
"REACTOME:R-MMU-885... | 19 | [
"4p1n",
"8soi",
"8sqz",
"8srm"
] | 4 | [
"PUB00034854",
"PUB00042769",
"PUB00042770",
"PUB00042782",
"PUB00066530",
"PUB00098424",
"PUB00098425",
"PUB00098426",
"PUB00101056"
] | [
"15014045",
"16887826",
"17890369",
"7389358",
"17204848",
"18936157",
"21795849",
"19377305",
"24793651"
] | [
"Role of Unc51.1 and its binding partners in CNS axon outgrowth.",
"The autophagy-related kinase UNC-51 and its binding partner UNC-14 regulate the subcellular localization of the Netrin receptor UNC-5 in Caenorhabditis elegans.",
"Autophagy genes unc-51 and bec-1 are required for normal cell size in Caenorhabd... | [
2004,
2006,
2007,
1980,
2007,
2009,
2011,
2009,
2014
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4672
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"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 (strain 972 / ATCC 24843)"
] | [
1,
9,
3,
11,
1,
7,
1,
1
] | 8 | true | Domain | Serine/threonine-protein kinase Atg1-like, tMIT domain | Serine/threonine-protein kinase Atg1-like, tMIT domain | Atg1-like_tMIT | 9 |
IPR022709 | 22,709 | Protein SCAI | SCAI | Family | 3,905 | false | false | SCAI is a transcriptional cofactor and tumour suppressor that suppresses MKL1-induced SRF transcriptional activity. It may function in the RHOA-DIAPH1 signal transduction pathway and regulate cell migration through transcriptional regulation of ITGB1 [ ]. | [
"GO:0003714",
"GO:0006351"
] | [
"transcription corepressor activity",
"DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF12070"
] | [
"SCAI"
] | [
3905
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-5663220",
"R-MMU-5663220"
] | [
"REACTOME:R-HSA-5663220",
"REACTOME:R-MMU-5663220"
] | 2 | [] | 0 | [
"PUB00068364"
] | [
"19350017"
] | [
"SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
] | [
2009
] | 1 | [] | [
"IPR016607"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
3905
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
10,
6,
5,
3,
5,
10,
7,
24
] | 8 | true | Family | Protein SCAI | Protein SCAI | SCAI | 3 |
IPR022710 | 22,710 | Metallothionein domain, yeast | Metalthion_dom_yeast | Domain | 21 | false | false | Metallothioneins are characterised by an abundance of cysteine residues and a lack of generic secondary structure motifs. This protein functions in primary metal storage, transport and detoxification [ ]. For the first 40 residues in the protein the polypeptide wraps around the metal by forming two large parallel loops... | [
"GO:0005507",
"GO:0046870",
"GO:0010273",
"GO:0071585"
] | [
"copper ion binding",
"cadmium ion binding",
"detoxification of copper ion",
"detoxification of cadmium ion"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF11403"
] | [
"Metallothio_yeast"
] | [
21
] | 1 | [] | [] | [] | 0 | [
"1aoo",
"1aqq",
"1aqr",
"1aqs",
"1fmy",
"1rju"
] | 6 | [
"PUB00021153",
"PUB00074930"
] | [
"8566237",
"3902832"
] | [
"3D solution structure of copper and silver-substituted yeast metallothioneins.",
"Yeast metallothionein. Sequence and metal-binding properties."
] | [
1996,
1985
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
21
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2
] | 1 | true | Domain | Metallothionein domain, yeast | Metallothionein domain, yeast | Metalthion_dom_yeast | 7 |
IPR022712 | 22,712 | Beta-Casp domain | Beta_Casp | Domain | 27,472 | false | false | The beta-CASP domain is found C-terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains [ ]. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF10996",
"SM01027"
] | [
"Beta-Casp",
"Beta-Casp"
] | [
26801,
27037
] | 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-159231",
"R-BTA-72187",
"R-BTA-72203",
"R-BTA-73856",
"R-BTA-77595",
"R-CEL-72187",
"R-CEL-72203",
"R-CEL-73856",
"R-CEL-77595",
"R-DDI-6807505",
"R-DDI-77595",
"R-DME-159231",
"R-DME-6807505",
"R-DME-72187",
"R-DME-72203",
"R-DME-73856",
"R-DME-77595",
"R-DRE-6807505",
"R... | [
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-72187",
"REACTOME:R-BTA-72203",
"REACTOME:R-BTA-73856",
"REACTOME:R-BTA-77595",
"REACTOME:R-CEL-72187",
"REACTOME:R-CEL-72203",
"REACTOME:R-CEL-73856",
"REACTOME:R-CEL-77595",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-77595",
"REACTOME:R-DME-159231",
... | 35 | [
"2dkf",
"2i7t",
"2i7v",
"2i7x",
"2xr1",
"2ycb",
"3a4y",
"3af5",
"3af6",
"3idz",
"3ie0",
"3ie1",
"3ie2",
"3iek",
"3iel",
"3iem",
"6i1d",
"6m8q",
"6q55",
"6q5a",
"6urg",
"6v4x",
"7bfp",
"7bfq",
"7cun",
"7pks",
"7sn8",
"7ycx",
"7zgq",
"7zgr",
"8r22",
"8r23"... | 51 | [
"PUB00041631"
] | [
"17128255"
] | [
"Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1846,
9879,
15482,
11,
254
] | 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... | [
22,
4,
6,
4,
18,
15,
2,
8,
21,
2,
2,
32
] | 12 | true | Domain | Beta-Casp domain | Beta-Casp domain | Beta_Casp | 8 |
IPR022713 | 22,713 | Proteinase inhibitor I67, bromein | Prot_inhib_I67_bromein | Domain | 5 | false | false | Bromelain inhibitor VI is a double-chain inhibitor consisting of an 11-residue and a 41-residue chain. This protein is the 41-residue heavy chain which is joined to the 11-residue chain by disulphide bonds [ ]. The inhibitor acts to inhibit the cysteine proteinase bromelain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11405"
] | [
"Inhibitor_I67"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"1bi6",
"2bi6"
] | 2 | [
"PUB00036427"
] | [
"8611527"
] | [
"Solution structure of bromelain inhibitor IV from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybean."
] | [
1996
] | 1 | [
"IPR000877"
] | [] | 1 | 0 | 1 | [
"Ananas comosus"
] | [
5
] | 1 | [] | [] | 0 | true | Domain | Proteinase inhibitor I67, bromein | Proteinase inhibitor I67, bromein | Prot_inhib_I67_bromein | 9 |
IPR022714 | 22,714 | Protein of unknown function DUF2670 | DUF2670 | Family | 59 | false | false | This bacterial family of proteins has no known function and appears to be restricted to Rickettsiaceae. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF10875"
] | [
"DUF2670"
] | [
59
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudolycoriella hygida",
"Rickettsiaceae"
] | [
1,
58
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF2670 | Protein of unknown function DUF2670 | DUF2670 | 9 |
IPR022715 | 22,715 | Protein of unknown function DUF2671 | DUF2671 | Family | 62 | false | false | This group of proteins with unknown function is predominantly found in Rickettsiales. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF10877"
] | [
"DUF2671"
] | [
62
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Rickettsiales"
] | [
5,
57
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF2671 | Protein of unknown function DUF2671 | DUF2671 | 6 |
IPR022716 | 22,716 | Gcn1, N-terminal | Gcn1_N | Domain | 1,733 | false | false | This domain is found in the N-terminal region of Gcn1 protein, which acts as a translation activator that mediates translational control by regulating Gcn2 kinase activity [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12074"
] | [
"Gcn1_N"
] | [
1733
] | 1 | [] | [] | [] | 0 | [
"8i9x",
"8i9y",
"8i9z",
"8ia0",
"8onz",
"8pv1",
"8pv2",
"8pv3",
"8pv4",
"8pv5",
"8pv6",
"8pv7",
"8pv8",
"8pvk",
"8pvl"
] | 15 | [
"PUB00042775"
] | [
"11350982"
] | [
"Budding yeast GCN1 binds the GI domain to activate the eIF2alpha kinase GCN2."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
1733
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Domain | Gcn1, N-terminal | Gcn1, N-terminal | Gcn1_N | 8 |
IPR022717 | 22,717 | Antimicrobial peptide tachystatin A | Antimicrobial_tachystatin_A | Family | 4 | false | false | Tachystatin A contains a cysteine-stabilised triple-stranded β-sheet and shows features common to membrane-interactive peptides. Tachystatin A is thought to have an antimicrobial activity similar to defensins.Tachystatin A is also a chitin-binding peptide [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11406"
] | [
"Tachystatin_A"
] | [
4
] | 1 | [] | [] | [] | 0 | [
"1cix"
] | 1 | [
"PUB00028288"
] | [
"11959852"
] | [
"Structure of the antimicrobial peptide tachystatin A."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Protostomia"
] | [
4
] | 1 | [] | [] | 0 | true | Family | Antimicrobial peptide tachystatin A | Antimicrobial peptide tachystatin A | Antimicrobial_tachystatin_A | 9 |
IPR022718 | 22,718 | Protein of unknown function DUF2672 | DUF2672 | Family | 55 | false | false | This group of proteins with unknown function appears to be restricted to Rickettsiaceae. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF10878"
] | [
"DUF2672"
] | [
55
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Rickettsiaceae"
] | [
55
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF2672 | Protein of unknown function DUF2672 | DUF2672 | 2 |
IPR022719 | 22,719 | Gliding motility-associated protein GldM, C-terminal | Motility-assoc_prot_GldM_C | Domain | 2,368 | false | false | This domain is found in bacteria at the C terminus of the GldM protein. This domain is typically between 169 to 182 amino acids in length and has two completely conserved residues (Y and N) that may be functionally important. GldM, is named for the member from Bacteriodetes Flavobacterium johnsoniae, which is required ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12080"
] | [
"GldM_4th"
] | [
2368
] | 1 | [] | [] | [] | 0 | [
"6ey4",
"6ey5",
"6ey6",
"6ys8",
"7cmg"
] | 5 | [
"PUB00045359"
] | [
"16199564"
] | [
"Flavobacterium johnsoniae gliding motility genes identified by mariner mutagenesis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2334,
4,
30
] | 3 | [] | [] | 0 | true | Domain | Gliding motility-associated protein GldM, C-terminal | Gliding motility-associated protein GldM, C-terminal | Motility-assoc_prot_GldM_C | 2 |
IPR022720 | 22,720 | Gliding motility-associated protein GldM, N-terminal | Motility-assoc_prot_GldM_N | Domain | 2,370 | false | false | This domain is found in bacteria at the N terminus of the gliding motility-associated protein, GldM. This domain is typically between 169 to 182 amino acids in length. This domain has two completely conserved residues (Y and N) that may be functionally important. GldM, is named for the member from Flavobacterium johnso... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12081"
] | [
"GldM_1st"
] | [
2370
] | 1 | [] | [] | [] | 0 | [
"6ey0",
"6ey4",
"6ys8",
"7cmg",
"7sat",
"7sau",
"7sax",
"7saz",
"7sb2"
] | 9 | [
"PUB00045359"
] | [
"16199564"
] | [
"Flavobacterium johnsoniae gliding motility genes identified by mariner mutagenesis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2333,
10,
27
] | 3 | [] | [] | 0 | true | Domain | Gliding motility-associated protein GldM, N-terminal | Gliding motility-associated protein GldM, N-terminal | Motility-assoc_prot_GldM_N | 6 |
IPR022722 | 22,722 | Non-structural protein ORF8, betacoronavirus | ORF8_betacoronavirus | Family | 331 | false | false | This entry includes the ORF8 gene products (also known as NS8, accessory protein 8) from human SARS coronavirus (SARS-CoV), SARS-CoV-2, Bat coronavirus HKU3 and pangolin coronaviruses [ ]. ORF8 is an accessory protein that is not shared by all members of subgenus sarbecovirus. The presence and location of ORF8 in the S... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12093"
] | [
"bCoV_NS8"
] | [
331
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-448424",
"R-HSA-9679504",
"R-HSA-9692916",
"R-HSA-9705671",
"R-HSA-9727281",
"R-HSA-983170"
] | [
"REACTOME:R-HSA-448424",
"REACTOME:R-HSA-9679504",
"REACTOME:R-HSA-9692916",
"REACTOME:R-HSA-9705671",
"REACTOME:R-HSA-9727281",
"REACTOME:R-HSA-983170"
] | 6 | [
"7f5f",
"7f8l",
"7jtl",
"7jx6",
"7mx9",
"7xmn"
] | 6 | [
"PUB00094119",
"PUB00094120",
"PUB00095858",
"PUB00095885",
"PUB00095887",
"PUB00095888",
"PUB00100399",
"PUB00100400",
"PUB00100401",
"PUB00100402"
] | [
"16753150",
"16876844",
"26433221",
"32890763",
"32015508",
"32825438",
"31986261",
"33723527",
"34021074",
"34177923"
] | [
"Expression and functional characterization of the putative protein 8b of the severe acute respiratory syndrome-associated coronavirus.",
"The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the enve... | [
2006,
2006,
2016,
2020,
2020,
2020,
2020,
2021,
2021,
2021
] | 10 | [] | [
"IPR044391",
"IPR044392",
"IPR044393"
] | 0 | 3 | 0 | [
"Orthocoronavirinae"
] | [
331
] | 1 | [] | [] | 0 | true | Family | Non-structural protein ORF8, betacoronavirus | Non-structural protein ORF8, betacoronavirus | ORF8_betacoronavirus | 1 |
IPR022723 | 22,723 | RDM domain, Ret finger protein-like | RDM_domain_RFPL | Domain | 262 | false | false | The RFPL defining motif (RDM) is a domain found on RFPL (Ret finger protein like) proteins. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex [ ]. The RDM domain is thought to have emerged from a neofunctionalisa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11002"
] | [
"RDM"
] | [
262
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053779"
] | [
"18656177"
] | [
"Evolutionary forces shape the human RFPL1,2,3 genes toward a role in neocortex development."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Eutheria"
] | [
262
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
2,
1
] | 3 | true | Domain | RDM domain, Ret finger protein-like | RDM domain, Ret finger protein-like | RDM_domain_RFPL | 7 |
IPR022724 | 22,724 | RNA methyltransferase, SpoU/TrmH type, C-terminal domain | rRNA_MeTrfase_SpoU_C | Domain | 2,372 | false | false | This domain is found in bacteria and is about 60 amino acids in length. It is found in association with . This domain has a conserved LFE sequence motif. Some members of the Pfam family SpoU_methylase, , carry this very distinctive sequence at their extreme C terminus. The exact function of this domain is not known. | [
"GO:0141100"
] | [
"tRNA (guanine(18)-2'-O)-methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12105"
] | [
"SpoU_methylas_C"
] | [
2372
] | 1 | [
"EC"
] | [
"2.1.1.34"
] | [
"EC:2.1.1.34"
] | 1 | [
"1v2x",
"1zjr",
"7edc"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2350,
9,
13
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | RNA methyltransferase, SpoU/TrmH type, C-terminal domain | RNA methyltransferase, SpoU/TrmH type, C-terminal domain | rRNA_MeTrfase_SpoU_C | 8 |
IPR022725 | 22,725 | Type II restriction enzyme MunI | Restrct_endonuc_II_MunI | Family | 26 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11407"
] | [
"RestrictionMunI"
] | [
26
] | 1 | [] | [] | [] | 0 | [
"1d02"
] | 1 | [
"PUB00028317",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"10545092",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 A resolution.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between different subgroups... | [
1999,
2005,
2003,
2002,
2001,
2004,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cenarchaeum symbiosum (strain A)",
"freshwater metagenome"
] | [
23,
1,
2
] | 3 | [] | [] | 0 | true | Family | Type II restriction enzyme MunI | Type II restriction enzyme MunI | Restrct_endonuc_II_MunI | 5 |
IPR022726 | 22,726 | CXC chemokine receptor 4 N-terminal domain | Chemokine_CXCR4_N_dom | Domain | 711 | false | false | This entry represents the N-terminal region of the CXC type 4 chemokine receptor. CXCR4 and its ligand stromal cell-derived factor-1 (also known as CXCL12) are essential for proper fetal development. CXCR4 is also the major coreceptor for T-tropic strains of Human immunodeficiency virus 1, and SDF-1 inhibits HIV-1 infe... | [
"GO:0019955"
] | [
"cytokine binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12109"
] | [
"CXCR4_N"
] | [
711
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-376176",
"R-BTA-380108",
"R-BTA-418594",
"R-HSA-173107",
"R-HSA-376176",
"R-HSA-380108",
"R-HSA-418594",
"R-HSA-9823730",
"R-HSA-9827857",
"R-HSA-9937080",
"R-MMU-376176",
"R-MMU-380108",
"R-MMU-418594",
"R-RNO-380108",
"R-RNO-418594",
"R-SSC-380108",
"R-SSC-418594"
] | [
"REACTOME:R-BTA-376176",
"REACTOME:R-BTA-380108",
"REACTOME:R-BTA-418594",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-376176",
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-9823730",
"REACTOME:R-HSA-9827857",
"REACTOME:R-HSA-9937080",
"REACTOME:R-MMU-376176",
"REACTOME:R-MMU-... | 17 | [
"2k03",
"2k04",
"2k05",
"2n55",
"3odu",
"3oe0",
"3oe6",
"3oe8",
"3oe9",
"4rws",
"8u4n",
"8u4o",
"8u4p",
"8u4q",
"8u4r",
"8u4s",
"8u4t",
"8yu7",
"8zpl",
"8zpm",
"8zpn",
"9mdu",
"9me1",
"9mej",
"9men",
"9met",
"9meu"
] | 27 | [
"PUB00009401",
"PUB00048158",
"PUB00064589",
"PUB00064621",
"PUB00064622",
"PUB00067945",
"PUB00067946"
] | [
"11544102",
"18799424",
"10714678",
"10601351",
"9500790",
"9689100",
"7592998"
] | [
"Chemokine receptors.",
"Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12.",
"Chemokines: a new classification system and their role in immunity.",
"Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.",
"Flexible ... | [
2001,
2008,
2000,
1999,
1998,
1998,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Euteleostomi"
] | [
711
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
3,
5
] | 3 | true | Domain | CXC chemokine receptor 4 N-terminal domain | CXC chemokine receptor 4 N-terminal domain | Chemokine_CXCR4_N_dom | 2 |
IPR022727 | 22,727 | Pupal cuticle protein C1 | Cuticle_C1 | Family | 913 | false | false | Insect cuticles are composite structures whose mechanical properties are optimised for biological function. The major components are the chitin filament system and the cuticular proteins, and the cuticle's properties are determined largely by the interactions between these two sets of molecules. The proteins can be ord... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF11018",
"PTHR39068"
] | [
"Cuticle_3",
""
] | [
786,
788
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Devosia marina",
"Eukaryota"
] | [
1,
912
] | 2 | [
"Drosophila melanogaster"
] | [
7
] | 1 | true | Family | Pupal cuticle protein C1 | Pupal cuticle protein C1 | Cuticle_C1 | 2 |
IPR022728 | 22,728 | Period circadian-like, C-terminal | Period_circadian-like_C | Domain | 4,253 | false | false | This domain is found in the family of Period circadian protein homologues (PER1, PER2, PER3) found in vertebrates. Sequences represented by this entry are found C-terminal to . PER proteins (PER 1-3) are transcriptional repressors which form the core component of the circadian clock. They play a critical role in rhythm... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12114"
] | [
"Period_C"
] | [
4253
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-9931510",
"R-HSA-9931521",
"R-HSA-9931530",
"R-HSA-9932298",
"R-MMU-9932298",
"R-RNO-9932298"
] | [
"REACTOME:R-HSA-9931510",
"REACTOME:R-HSA-9931521",
"REACTOME:R-HSA-9931530",
"REACTOME:R-HSA-9932298",
"REACTOME:R-MMU-9932298",
"REACTOME:R-RNO-9932298"
] | 6 | [
"4ct0",
"4u8h",
"6of7"
] | 3 | [
"PUB00061105",
"PUB00107296"
] | [
"22653727",
"24005054"
] | [
"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex.",
"A meeting of two chronobiological systems: circadian proteins Period1 and BMAL1 modulate the human hair cycle clock."
] | [
2012,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Janthinobacterium lividum"
] | [
4252,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
20,
12,
13,
17
] | 4 | true | Domain | Period circadian-like, C-terminal | Period circadian-like, C-terminal | Period_circadian-like_C | 5 |
IPR022730 | 22,730 | DAZ associated protein 2 | DAZ_assoc-2 | Family | 1,628 | false | false | DAZ associated protein 2 has a highly conserved sequence throughout evolution including a conserved polyproline region and several SH2/SH3 binding sites. It occurs as a single copy gene with a four-exon organisation and is located on chromosome 12. It encodes a ubiquitously expressed protein and binds to DAZ and DAZL1 ... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF11029",
"PTHR31638"
] | [
"DAZAP2",
""
] | [
1562,
1555
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053781",
"PUB00053782"
] | [
"10857750",
"15629043"
] | [
"Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1.",
"The structure, expression and function prediction of DAZAP2, a down-regulated gene in multiple myeloma."
] | [
2000,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1628
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
4,
2,
2
] | 5 | true | Family | DAZ associated protein 2 | DAZ associated protein 2 | DAZ_assoc-2 | 6 |
IPR022731 | 22,731 | Dermaseptin domain | Dermaseptin_dom | Domain | 92 | false | false | This entry represents the dermaseptin domain found in dermaseptin precursor polypeptides and similar proteins from tree frogs. Dermaseptin proteins are used in eukaryotes as an antimicrobial agent. Dermaseptins are typically between 30 to 76 amino acids in length. This domain is found associated with a propeptide ( ). ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12121"
] | [
"DD_K"
] | [
92
] | 1 | [] | [] | [] | 0 | [
"2jx6",
"2k9b",
"6wpo"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Deefgea chitinilytica"
] | [
91,
1
] | 2 | [] | [] | 0 | true | Domain | Dermaseptin domain | Dermaseptin domain | Dermaseptin_dom | 1 |
IPR022733 | 22,733 | DPUP/SUD, C-terminal, betacoronavirus | DPUP_SUD_C_bCoV | Domain | 5,481 | false | false | This domain is found in betacoronavirus non-structural protein NSP3, and is about 65 amino acids in length. It was originally thought to exist only in SARS-coronaviruses, and so was termed the SARS-unique domain (SUD), however this has since been shown to be incorrect. The domain is also known as DPUP (domain preceding... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF12124",
"PS51942",
"cd21525"
] | [
"bCoV_SUD_C",
"BCOV_NSP3C_C",
"SUD_C_SARS-CoV_Nsp3"
] | [
3960,
5247,
3864
] | 3 | [
"EC",
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.50",
"3.4.19.12",
"3.4.22.-",
"PWY-7375",
"R-HSA-191859",
"R-HSA-918233",
"R-HSA-9679504",
"R-HSA-9682706",
"R-HSA-9682708",
"R-HSA-9683439",
"R-HSA-9684325",
"R-HSA-9692916",
"R-HSA-9694271",
"R-HSA-9694301",
"R-HSA-9694676",
"R-HSA-9694686",
"R-HSA-9694786",
"R-HSA-9705671... | [
"EC:2.7.7.50",
"EC:3.4.19.12",
"EC:3.4.22.-",
"METACYC:PWY-7375",
"REACTOME:R-HSA-191859",
"REACTOME:R-HSA-918233",
"REACTOME:R-HSA-9679504",
"REACTOME:R-HSA-9682706",
"REACTOME:R-HSA-9682708",
"REACTOME:R-HSA-9683439",
"REACTOME:R-HSA-9684325",
"REACTOME:R-HSA-9692916",
"REACTOME:R-HSA-9694... | 20 | [
"2kaf",
"2kqv",
"2kqw",
"4ypt",
"5utv",
"6mwm",
"7p2o",
"7thh",
"8yax",
"8yb5",
"8yb7"
] | 11 | [
"PUB00050012",
"PUB00062522",
"PUB00094069"
] | [
"19436709",
"20493876",
"29128390"
] | [
"The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes.",
"SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.",
"Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein."
] | [
2009,
2010,
2018
] | 3 | [] | [
"IPR044352",
"IPR044381",
"IPR044382"
] | 0 | 3 | 0 | [
"Coronaviridae"
] | [
5481
] | 1 | [] | [] | 0 | true | Domain | DPUP/SUD, C-terminal, betacoronavirus | DPUP/SUD, C-terminal, betacoronavirus | DPUP_SUD_C_bCoV | 9 |
IPR022734 | 22,734 | Apolipoprotein M | ApoM | Family | 1,023 | false | false | ApoM is a 25kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells [ ]. Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniqu... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF11032",
"PTHR32028"
] | [
"ApoM",
""
] | [
1021,
480
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-975634",
"R-MMU-975634",
"R-RNO-975634",
"R-SSC-975634"
] | [
"REACTOME:R-HSA-975634",
"REACTOME:R-MMU-975634",
"REACTOME:R-RNO-975634",
"REACTOME:R-SSC-975634"
] | 4 | [
"2wew",
"2wex",
"2xkl",
"2yg2"
] | 4 | [
"PUB00053783",
"PUB00053784"
] | [
"18490703",
"18460466"
] | [
"Levels of apolipoprotein M are not associated with the risk of coronary heart disease in two independent case-control studies.",
"The signal peptide anchors apolipoprotein M in plasma lipoproteins and prevents rapid clearance of apolipoprotein M from plasma."
] | [
2008,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
1023
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
2,
4
] | 4 | true | Family | Apolipoprotein M | Apolipoprotein M | ApoM | 5 |
IPR022736 | 22,736 | Non-structural protein NS6, betacoronavirus | NS6_bCoV | Family | 198 | false | false | This entry represents the non-structural protein NS6 (also known as ORF6, accessory protein 6, or X3 protein), which is highly conserved among SARS-related coronaviruses [ ] (this is distinct from NSP6 which is encoded on the replicase polyprotein). NS6 is located in the endoplasmic reticulum [ ]. It has been reported ... | [
"GO:0044165"
] | [
"host cell endoplasmic reticulum"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF12133"
] | [
"bCoV_NS6"
] | [
198
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-9692916",
"R-HSA-9705671",
"R-HSA-9727281"
] | [
"REACTOME:R-HSA-9692916",
"REACTOME:R-HSA-9705671",
"REACTOME:R-HSA-9727281"
] | 3 | [
"7f60",
"7f90",
"7vpg"
] | 3 | [
"PUB00094122",
"PUB00094123",
"PUB00100229"
] | [
"16310783",
"25907116",
"33849972"
] | [
"The putative protein 6 of the severe acute respiratory syndrome-associated coronavirus: expression and functional characterization.",
"Severe acute respiratory syndrome coronavirus protein 6 mediates ubiquitin-dependent proteosomal degradation of N-Myc (and STAT) interactor.",
"SARS-CoV-2 ORF6 Disrupts Bidirec... | [
2005,
2015,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Orthocoronavirinae"
] | [
198
] | 1 | [] | [] | 0 | true | Family | Non-structural protein NS6, betacoronavirus | Non-structural protein NS6, betacoronavirus | NS6_bCoV | 8 |
IPR022737 | 22,737 | RNA polymerase recycling, bacterial, C-terminal | RapA_C | Domain | 4,933 | false | false | This domain is found in bacteria. This domain is about 360 amino acids in length. This domain is found associated with , . The function of this domain is not known, but structurally it forms an α-β fold in nature with a central β-sheet flanked by helices and loops, the β-sheet being mainly antiparallel and flanked by f... | [
"GO:0016817"
] | [
"hydrolase activity, acting on acid anhydrides"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12137"
] | [
"RapA_C"
] | [
4933
] | 1 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"4s20",
"6bog",
"7m8e",
"7mkn",
"7mkq",
"8so8",
"8sp4",
"8spg",
"8t0l"
] | 9 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
4860,
6,
22,
45
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | RNA polymerase recycling, bacterial, C-terminal | RNA polymerase recycling, bacterial, C-terminal | RapA_C | 4 |
IPR022738 | 22,738 | Adenylylsulphate reductase, beta subunit, C-terminal | AprB_C | Domain | 715 | false | false | During dissimilatory sulphate reduction and sulphur oxidation, adenylylsulphate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulphite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently b... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12139"
] | [
"APS-reductase_C"
] | [
715
] | 1 | [] | [] | [] | 0 | [
"1jnr",
"1jnz",
"2fja",
"2fjb",
"2fjd",
"2fje",
"3gyx"
] | 7 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Metazoa",
"unclassified sequences"
] | [
43,
594,
10,
68
] | 4 | [] | [] | 0 | true | Domain | Adenylylsulphate reductase, beta subunit, C-terminal | Adenylylsulphate reductase, beta subunit, C-terminal | AprB_C | 7 |
IPR022739 | 22,739 | Polyphenol oxidase, central domain | Polyphenol_oxidase_cen | Domain | 3,549 | false | false | This domain is found in bacteria and eukaryotes and is approximately 50 amino acids in length. It is found in association with and . Most members are annotated as being polyphenol oxidases, and many are from plants or plastids. There is a conserved DWL sequence motif. | [
"GO:0004097"
] | [
"catechol oxidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12142"
] | [
"PPO1_DWL"
] | [
3549
] | 1 | [
"EC",
"METACYC"
] | [
"1.10.3.1",
"PWY-6752"
] | [
"EC:1.10.3.1",
"METACYC:PWY-6752"
] | 2 | [
"1bt1",
"1bt2",
"1bt3",
"1bug",
"2p3x",
"4z0y",
"4z0z",
"4z10",
"4z11",
"4z12",
"4z13",
"4z14",
"5ce9",
"6els",
"6hqi",
"6hqj",
"8b74"
] | 17 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
118,
3429,
2
] | 3 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
18
] | 2 | true | Domain | Polyphenol oxidase, central domain | Polyphenol oxidase, central domain | Polyphenol_oxidase_cen | 3 |
IPR022740 | 22,740 | Polyphenol oxidase, C-terminal | Polyphenol_oxidase_C | Domain | 3,594 | false | false | This domain represents the C terminus of polyphenol oxidases. This region is primarily found in eukaryotes, although a few bacterial members also exist. It is typically between 138 and 152 amino acids in length and the family is found in association with and . Many members are plant or plastid polyphenol oxidases, and ... | [
"GO:0004097"
] | [
"catechol oxidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12143"
] | [
"PPO1_KFDV"
] | [
3594
] | 1 | [
"EC",
"METACYC"
] | [
"1.10.3.1",
"PWY-6752"
] | [
"EC:1.10.3.1",
"METACYC:PWY-6752"
] | 2 | [
"4z11",
"4z12",
"4z13",
"4z14",
"6els",
"6elt",
"6elv",
"6hqi",
"6hqj",
"7xio"
] | 10 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"Streptophyta"
] | [
26,
3568
] | 2 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
12,
18
] | 2 | true | Domain | Polyphenol oxidase, C-terminal | Polyphenol oxidase, C-terminal | Polyphenol_oxidase_C | 5 |
IPR022741 | 22,741 | Bacteriophage B103, Gp8, head fibre | Phage_B103_Gp8 | Family | 446 | false | false | This entry is represented by Bacteriophage B103, Gp8. The characteristics of the protein distribution suggest prophage matches in addition to the phage matches. Gp8 (Gene locus 8.5 in contig X99260_GR) is a structural head protein in phage and is dispensable. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11133"
] | [
"Phage_head_fibr"
] | [
446
] | 1 | [] | [] | [] | 0 | [
"3qc7",
"6qvk",
"6qyd",
"6qyy",
"6qz0",
"7qof",
"7qoh",
"7qoi",
"8ckb",
"9d82"
] | 10 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses",
"metagenomes"
] | [
338,
99,
9
] | 3 | [] | [] | 0 | true | Family | Bacteriophage B103, Gp8, head fibre | Bacteriophage B103, Gp8, head fibre | Phage_B103_Gp8 | 1 |
IPR022742 | 22,742 | Alpha/beta hydrolase domain-containing protein 17C-like | ABHD17C-like | Domain | 115,980 | false | false | This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. The majority of the members in this entry carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in . α/β hydrolase domain-containing protein 17C (ABHD17C) belongs to the AB hydrolase superfamily and ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12146"
] | [
"Hydrolase_4"
] | [
115980
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9648002",
"R-CEL-9648002",
"R-DDI-1482883",
"R-DDI-426048",
"R-DRE-9648002",
"R-GGA-9648002",
"R-HSA-1482883",
"R-HSA-163560",
"R-HSA-426048",
"R-HSA-9648002",
"R-HSA-9841922",
"R-MMU-1482883",
"R-MMU-426048",
"R-MMU-9648002",
"R-RNO-1482883",
"R-RNO-426048",
"R-RNO-9648002",
... | [
"REACTOME:R-BTA-9648002",
"REACTOME:R-CEL-9648002",
"REACTOME:R-DDI-1482883",
"REACTOME:R-DDI-426048",
"REACTOME:R-DRE-9648002",
"REACTOME:R-GGA-9648002",
"REACTOME:R-HSA-1482883",
"REACTOME:R-HSA-163560",
"REACTOME:R-HSA-426048",
"REACTOME:R-HSA-9648002",
"REACTOME:R-HSA-9841922",
"REACTOME:R... | 22 | [
"1r1d",
"1tqh",
"2rau",
"2wtm",
"2wtn",
"3dkr",
"3dlt",
"3dyi",
"3dyv",
"3e1g",
"3fnb",
"3hju",
"3jw8",
"3jwe",
"3pe6",
"3pf8",
"3pf9",
"3pfb",
"3pfc",
"3qm1",
"3rli",
"3rm3",
"3s2z",
"4ao6",
"4ao7",
"4ao8",
"4diu",
"4ke6",
"4ke7",
"4ke8",
"4ke9",
"4kea"... | 95 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
509,
78168,
36157,
154,
992
] | 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",... | [
186,
6,
7,
22,
3,
27,
11,
3,
86,
13,
3,
1,
170
] | 13 | true | Domain | Alpha/beta hydrolase domain-containing protein 17C-like | Alpha/beta hydrolase domain-containing protein 17C-like | ABHD17C-like | 3 |
IPR022744 | 22,744 | Methyltransferase domain, putative | MeTrfase_dom_put | Domain | 2,171 | false | false | This domain is predominantly found in bacterial proteins and is approximately 110 amino acids in length. It shows some similarity to methyltransferase domains. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12147"
] | [
"Methyltransf_20"
] | [
2171
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2154,
8,
9
] | 3 | [
"Escherichia coli (strain K12)",
"Mus musculus"
] | [
1,
1
] | 2 | true | Domain | Methyltransferase domain, putative | Methyltransferase domain, putative | MeTrfase_dom_put | 6 |
IPR022745 | 22,745 | Eukaryotic translation initiation factor 4G1, eIF4E-binding domain | eIF4G1_eIF4E-bd | Domain | 1,939 | false | false | The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent tran... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12152"
] | [
"eIF_4G1"
] | [
1939
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-SCE-156827",
"R-SCE-166208",
"R-SCE-429947",
"R-SCE-72649",
"R-SCE-72662",
"R-SCE-72702",
"R-SCE-975956",
"R-SCE-975957",
"R-SPO-156827",
"R-SPO-166208",
"R-SPO-72649",
"R-SPO-72662",
"R-SPO-72702",
"R-SPO-72706",
"R-SPO-975956",
"R-SPO-975957"
] | [
"REACTOME:R-SCE-156827",
"REACTOME:R-SCE-166208",
"REACTOME:R-SCE-429947",
"REACTOME:R-SCE-72649",
"REACTOME:R-SCE-72662",
"REACTOME:R-SCE-72702",
"REACTOME:R-SCE-975956",
"REACTOME:R-SCE-975957",
"REACTOME:R-SPO-156827",
"REACTOME:R-SPO-166208",
"REACTOME:R-SPO-72649",
"REACTOME:R-SPO-72662",... | 16 | [
"1rf8",
"6fbz",
"6fc0"
] | 3 | [
"PUB00030644"
] | [
"14675538"
] | [
"Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Candidatus Berkiella aquae",
"Eukaryota"
] | [
1,
1938
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
2,
1
] | 3 | true | Domain | Eukaryotic translation initiation factor 4G1, eIF4E-binding domain | Eukaryotic translation initiation factor 4G1, eIF4E-binding domain | eIF4G1_eIF4E-bd | 5 |
IPR022746 | 22,746 | Cathelicidin, antimicrobial peptide, C-terminal | Cathlecidin_C | Domain | 159 | false | false | This entry represents the cathlecidin antimicrobial C-terminal peptides. The C terminus is cleaved from the cathlecidin precursor, and is approximately 30 amino acids in length with a helical structure. This entry is found in association with . The C terminus peptides possess antimicrobial activity by virtue of their b... | [
"GO:0042742"
] | [
"defense response to bacterium"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF12153"
] | [
"CAP18_C"
] | [
159
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6798695",
"R-HSA-6803157",
"R-MMU-6798695",
"R-MMU-6803157"
] | [
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6803157",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-6803157"
] | 4 | [
"1lyp",
"2fbs",
"2fcg",
"2k6o",
"2l5m",
"2lmf",
"2na3",
"5nmn",
"5nnk",
"5nnm",
"5nnt",
"5xng",
"5xrx",
"6s6m",
"6s6n",
"7pdc",
"7say",
"8dew"
] | 18 | [
"PUB00040613",
"PUB00048248"
] | [
"16637646",
"18818205"
] | [
"Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region.",
"Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles."
] | [
2006,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
4,
155
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
3
] | 3 | true | Domain | Cathelicidin, antimicrobial peptide, C-terminal | Cathelicidin, antimicrobial peptide, C-terminal | Cathlecidin_C | 4 |
IPR022748 | 22,748 | NADH dehydrogenase subunit 2, N-terminal | NADH_DH_su2_N | Domain | 686 | false | false | This domain is found in eukaryotes, and is approximately 90 amino acids in length. It is found N-terminal to . All members are annotated as being NADH dehydrogenase subunit 2. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12155"
] | [
"NADHdh-2_N"
] | [
686
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Anthozoa"
] | [
686
] | 1 | [] | [] | 0 | true | Domain | NADH dehydrogenase subunit 2, N-terminal | NADH dehydrogenase subunit 2, N-terminal | NADH_DH_su2_N | 2 |
IPR022749 | 22,749 | N6 adenine-specific DNA methyltransferase, N-terminal domain | D12N6_MeTrfase_N | Domain | 26,094 | false | false | This domain is found at the N-terminal of the methylase subunit of Type I DNA methyltransferases. This domain is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. It is found in association with . Mutations in this region of EcoKI methyltransferase abolish the normally strong pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12161"
] | [
"HsdM_N"
] | [
26094
] | 1 | [
"EC"
] | [
"2.1.1.72"
] | [
"EC:2.1.1.72"
] | 1 | [
"2ar0",
"2okc",
"2y7c",
"2y7h",
"3khk",
"3lkd",
"5ybb",
"7bst",
"7bto",
"7btp",
"7btq",
"7btr",
"7vru",
"7vs4"
] | 14 | [
"PUB00053802"
] | [
"1833555"
] | [
"Mutations that confer de novo activity upon a maintenance methyltransferase."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
737,
25006,
7,
25,
319
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | N6 adenine-specific DNA methyltransferase, N-terminal domain | N6 adenine-specific DNA methyltransferase, N-terminal domain | D12N6_MeTrfase_N | 4 |
IPR022750 | 22,750 | Interferon regulatory factor 2-binding protein 1/2-like, zinc finger | IRF-2BP1_2-like_Znf | Domain | 2,435 | false | false | Interferon regulatory factor 2-binding protein 1 and 2 (IRF-2BP1/2) and their homologue IRF-2BP-like (also known as IRF-2BPL or C14orf4) ( ) are nuclear transcriptional repressor proteins that bind to the C-terminal repression domain of IRF-2 and can inhibit both enhancer-activated and basal transcription. They contain... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11261"
] | [
"IRF-2BP1_2"
] | [
2435
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053789",
"PUB00097578",
"PUB00097579"
] | [
"12799427",
"30057031",
"27016798"
] | [
"Identification of novel co-repressor molecules for Interferon Regulatory Factor-2.",
"IRF2BPL Is Associated with Neurological Phenotypes.",
"Mutation in IRF2BP2 is responsible for a familial form of common variable immunodeficiency disorder."
] | [
2003,
2018,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2435
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
4,
5,
4,
3,
6
] | 6 | true | Domain | Interferon regulatory factor 2-binding protein 1/2-like, zinc finger | Interferon regulatory factor 2-binding protein 1/2-like, zinc finger | IRF-2BP1_2-like_Znf | 5 |
IPR022751 | 22,751 | Alpha-mannosyltransferase | Alpha_mannosyltransferase | Family | 7,416 | false | false | Alpha-mannosyltransferase is responsible for the addition of residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. It is implicated in late Golgi modifications [ , , ]. The proteins matching this entry are conserved in fungi and also found in some phototrophic organisms. | [
"GO:0016757",
"GO:0009101"
] | [
"glycosyltransferase activity",
"glycoprotein biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF11051"
] | [
"Mannosyl_trans3"
] | [
7416
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.4.1.-",
"PWY-1901",
"PWY-1961",
"PWY-1981",
"PWY-2021",
"PWY-2881",
"PWY-2901",
"PWY-2902",
"PWY-4421",
"PWY-4801",
"PWY-5094",
"PWY-5105",
"PWY-5129",
"PWY-5139",
"PWY-5160",
"PWY-5161",
"PWY-5268",
"PWY-5284",
"PWY-5286",
"PWY-5310",
"PWY-5312",
"PWY-5313",
"PWY-5317... | [
"EC:2.4.1.-",
"METACYC:PWY-1901",
"METACYC:PWY-1961",
"METACYC:PWY-1981",
"METACYC:PWY-2021",
"METACYC:PWY-2881",
"METACYC:PWY-2901",
"METACYC:PWY-2902",
"METACYC:PWY-4421",
"METACYC:PWY-4801",
"METACYC:PWY-5094",
"METACYC:PWY-5105",
"METACYC:PWY-5129",
"METACYC:PWY-5139",
"METACYC:PWY-5... | 200 | [
"7xjv"
] | 1 | [
"PUB00053790",
"PUB00053791",
"PUB00053792"
] | [
"6995454",
"6802821",
"9756928"
] | [
"Saccharomyces cerevisiae mannoprotein mutants. Isolation of the mnn5 mutant and comparison with the mnn3 strain.",
"Effects of mannoprotein mutations on Saccharomyces cerevisiae core oligosaccharide structure.",
"Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the ma... | [
1980,
1982,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
141,
7262,
4,
9
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
1,
4,
6,
6
] | 4 | true | Family | Alpha-mannosyltransferase | Alpha-mannosyltransferase | Alpha_mannosyltransferase | 6 |
IPR022752 | 22,752 | Signal transducer and activation of transcription 1, TAZ2 binding domain, C-terminal | STAT1_TAZ2-bd_C | Domain | 1,181 | false | false | This entry represents the C-terminal domain of STAT1, which selectively binds the TAZ2 domain of CRB (CREB-binding protein) [ ]. This group of eukaryotic proteins is approximately 20 amino acids in length, and is found in association with , , , . By binding to CRB, it becomes a transcriptional activator and can initiat... | [
"GO:0003700"
] | [
"DNA-binding transcription factor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12162"
] | [
"STAT1_TAZ2bind"
] | [
1181
] | 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-HSA-1059683",
"R-HSA-1169408",
"R-HSA-1433557",
"R-HSA-1839117",
"R-HSA-186763",
"R-HSA-2173795",
"R-HSA-6785807",
"R-HSA-877300",
"R-HSA-877312",
"R-HSA-8854691",
"R-HSA-8939902",
"R-HSA-8984722",
"R-HSA-8985947",
"R-HSA-9013508",
"R-HSA-9020956",
"R-HSA-9020958",
"R-HSA-909733",... | [
"REACTOME:R-HSA-1059683",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-1433557",
"REACTOME:R-HSA-1839117",
"REACTOME:R-HSA-186763",
"REACTOME:R-HSA-2173795",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-877300",
"REACTOME:R-HSA-877312",
"REACTOME:R-HSA-8854691",
"REACTOME:R-HSA-8939902",
"REACTOME:R... | 45 | [
"2ka6",
"8yyu",
"8yyv"
] | 3 | [
"PUB00048291"
] | [
"19214187"
] | [
"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1181
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
6,
9,
5
] | 4 | true | Domain | Signal transducer and activation of transcription 1, TAZ2 binding domain, C-terminal | Signal transducer and activation of transcription 1, TAZ2 binding domain, C-terminal | STAT1_TAZ2-bd_C | 3 |
IPR022753 | 22,753 | Type IV pilus biogenesis PilP | T4SS_pilus_biogen_PilP | Family | 1,262 | false | false | Type IV pili are required for auto-agglutination, twitching motility, biofilm formation, adherence and DNA uptake during transformation [ ]. PilP is an inner membrane protein, required for pilus expression and transformation [ ]. PilP interacts with PilQ which suggests that the two proteins may have coordinated activit... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03021"
] | [
"pilP_fam"
] | [
1262
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053793"
] | [
"17526700"
] | [
"Interactions between the lipoprotein PilP and the secretin PilQ in Neisseria meningitidis."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Plasmid R64",
"Pseudomonadati",
"Trichuris trichiura",
"ecological metagenomes"
] | [
1,
1254,
1,
6
] | 4 | [] | [] | 0 | true | Family | Type IV pilus biogenesis PilP | Type IV pilus biogenesis PilP | T4SS_pilus_biogen_PilP | 7 |
IPR022754 | 22,754 | DNA polymerase III, gamma subunit, domain III | DNA_pol_III_gamma-3 | Domain | 25,906 | false | false | This domain is found in bacteria and eukaryotes, and is approximately 110 amino acids in length. It is found in association with . This domain is also present in the tau subunit before it undergoes cleavage. Domains I-III are shared between the tau and the gamma subunits, while most of the DnaB-binding Domain IV and al... | [
"GO:0003887"
] | [
"DNA-directed DNA polymerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF12169"
] | [
"DNA_pol3_gamma3"
] | [
25906
] | 1 | [
"EC"
] | [
"2.7.7.7"
] | [
"EC:2.7.7.7"
] | 1 | [
"1jr3",
"1xxh",
"1xxi",
"3glf",
"3glg",
"3glh",
"3gli",
"8giy",
"8giz",
"8gj0",
"8gj1",
"8gj2",
"8gj3",
"8val",
"8vam",
"8van",
"8vap",
"8vaq",
"8var",
"8vas",
"8vat"
] | 21 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_70_D04"
] | [
23795,
11,
1665,
434,
1
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
1,
1,
8,
30
] | 5 | true | Domain | DNA polymerase III, gamma subunit, domain III | DNA polymerase III, gamma subunit, domain III | DNA_pol_III_gamma-3 | 9 |
IPR022755 | 22,755 | Zinc finger, double-stranded RNA binding | Znf_C2H2_jaz | Domain | 26,784 | false | false | This zinc finger is mainly found in eukaryotic sequences, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tis... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12171"
] | [
"zf-C2H2_jaz"
] | [
26784
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-212436",
"R-HSA-381340",
"R-HSA-72163",
"R-MMU-72163",
"R-XTR-6781823",
"R-XTR-6782135",
"R-XTR-6782210",
"R-XTR-72163"
] | [
"REACTOME:R-DME-212436",
"REACTOME:R-HSA-381340",
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-XTR-6781823",
"REACTOME:R-XTR-6782135",
"REACTOME:R-XTR-6782210",
"REACTOME:R-XTR-72163"
] | 8 | [
"1zr9",
"3jct",
"4dgw",
"5nrl",
"5o9z",
"5zwm",
"5zwo",
"6ahd",
"6e93",
"6e94",
"6ft6",
"6g90",
"6lqm",
"6lsr",
"6lss",
"6lu8",
"6m62",
"6n8j",
"6n8k",
"6n8l",
"6ylg",
"6ylh",
"6yly",
"7aav",
"7abf",
"7abg",
"7abi",
"7dco",
"7oqb",
"7oqe",
"7ug6",
"7uoo"... | 76 | [
"PUB00053807"
] | [
"10488071"
] | [
"JAZ requires the double-stranded RNA-binding zinc finger motifs for nuclear localization."
] | [
1999
] | 1 | [
"IPR013087"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
14,
7,
26741,
16,
6
] | 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... | [
16,
4,
35,
18,
36,
25,
9,
11,
44,
3,
4,
15
] | 12 | true | Domain | Zinc finger, double-stranded RNA binding | Zinc finger, double-stranded RNA binding | Znf_C2H2_jaz | 1 |
IPR022756 | 22,756 | Signal transducer and activation of transcription 2, C-terminal | STAT2_C | Domain | 305 | false | false | This region is found in the mammalian signal transducer and activation of transcription (STAT) 2 protein, and is approximately 60 amino acids in length. The family is found in association with , , , . There is a conserved DLP sequence motif. STATs are involved in transcriptional regulation and are the only regulators k... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12188"
] | [
"STAT2_C"
] | [
305
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-8854691",
"R-HSA-909733",
"R-HSA-912694",
"R-HSA-9679191",
"R-HSA-9705671",
"R-HSA-9833109",
"R-MMU-8854691",
"R-MMU-909733",
"R-MMU-912694",
"R-SSC-8854691",
"R-SSC-909733",
"R-SSC-912694"
] | [
"REACTOME:R-HSA-8854691",
"REACTOME:R-HSA-909733",
"REACTOME:R-HSA-912694",
"REACTOME:R-HSA-9679191",
"REACTOME:R-HSA-9705671",
"REACTOME:R-HSA-9833109",
"REACTOME:R-MMU-8854691",
"REACTOME:R-MMU-909733",
"REACTOME:R-MMU-912694",
"REACTOME:R-SSC-8854691",
"REACTOME:R-SSC-909733",
"REACTOME:R-S... | 12 | [
"2ka4",
"6wcz",
"7zn7",
"7znn",
"8t12",
"8t13"
] | 6 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eutheria"
] | [
305
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
8,
1
] | 3 | true | Domain | Signal transducer and activation of transcription 2, C-terminal | Signal transducer and activation of transcription 2, C-terminal | STAT2_C | 4 |
IPR022757 | 22,757 | Glucose signalling factor 2 | Gsf2 | Family | 179 | false | false | This entry represents fungal Glucose singalling factor 2. Gsf2 is localised to the ER and functions to promote the secretion of certain hexose transporters [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11055"
] | [
"Gsf2"
] | [
179
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053794"
] | [
"10377429"
] | [
"Efficient export of the glucose transporter Hxt1p from the endoplasmic reticulum requires Gsf2p."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Dikarya"
] | [
179
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Glucose signalling factor 2 | Glucose signalling factor 2 | Gsf2 | 8 |
IPR022758 | 22,758 | ATP-dependent helicase Sgs1 | Helicase_Sgs1 | Domain | 91 | false | false | This entry represents a domain found in the fungal Sgs1 protein. | [
"GO:0003676",
"GO:0043138"
] | [
"nucleic acid binding",
"3'-5' DNA helicase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF11408"
] | [
"Helicase_Sgs1"
] | [
91
] | 1 | [] | [] | [] | 0 | [
"1d8b"
] | 1 | [
"PUB00014060",
"PUB00074991"
] | [
"10647186",
"18691965"
] | [
"The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins.",
"RecQ helicase, Sgs1, and XPF family endonuclease, Mus81-Mms4, resolve aberrant joint molecules during meiotic recombination."
] | [
1999,
2008
] | 2 | [
"IPR002121"
] | [] | 1 | 0 | 1 | [
"Fungi"
] | [
91
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | ATP-dependent helicase Sgs1 | ATP-dependent helicase Sgs1 | Helicase_Sgs1 | 6 |
IPR022759 | 22,759 | Antirestriction protein Ral | Antirestriction_protein_Ral | Family | 248 | false | false | Ral alleviates restriction and enhances modification by the E.coli restriction and modification system [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11058"
] | [
"Ral"
] | [
248
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053795"
] | [
"3023633"
] | [
"Modification enhancement by the restriction alleviation protein (Ral) of bacteriophage lambda."
] | [
1986
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
219,
29
] | 2 | [] | [] | 0 | true | Family | Antirestriction protein Ral | Antirestriction protein Ral | Antirestriction_protein_Ral | 4 |
IPR022764 | 22,764 | Peptidase S54, rhomboid domain | Peptidase_S54_rhomboid_dom | Domain | 77,492 | false | false | This entry represents a six transmembrane helix rhomboid domain. This domain is found in serine peptidases belonging to the MEROPS peptidase family S54 (Rhomboid, clan ST). They are integral membrane proteins related to the Drosophila melanogaster (Fruit fly) rhomboid protein . Members of this family are found in archa... | [
"GO:0004252",
"GO:0016020"
] | [
"serine-type endopeptidase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF01694"
] | [
"Rhomboid"
] | [
77492
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.105",
"R-HSA-8949664",
"R-HSA-9662834",
"R-MMU-8949664",
"R-RNO-8949664"
] | [
"EC:3.4.21.105",
"REACTOME:R-HSA-8949664",
"REACTOME:R-HSA-9662834",
"REACTOME:R-MMU-8949664",
"REACTOME:R-RNO-8949664"
] | 5 | [
"2ic8",
"2irv",
"2nr9",
"2nrf",
"2o7l",
"2xov",
"2xow",
"2xtu",
"2xtv",
"3b44",
"3b45",
"3odj",
"3txt",
"3ubb",
"3zeb",
"3zmh",
"3zmi",
"3zmj",
"3zot",
"4h1d",
"4njn",
"4njp",
"4qnz",
"4qo0",
"4qo2",
"5f5b",
"5f5d",
"5f5g",
"5f5j",
"5f5k",
"5mt6",
"5mt7"... | 54 | [
"PUB00001897",
"PUB00011885",
"PUB00033263",
"PUB00041666",
"PUB00079038",
"PUB00079039",
"PUB00101383",
"PUB00101384",
"PUB00101385"
] | [
"2110920",
"11672525",
"15047175",
"17051161",
"15616571",
"17040128",
"31369701",
"27378062",
"34477920"
] | [
"rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster.",
"Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases.",
"Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2.",
"Cry... | [
1990,
2001,
2004,
2006,
2005,
2006,
2019,
2016,
2021
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1479,
42719,
32526,
37,
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",... | [
78,
10,
53,
14,
1,
28,
17,
4,
48,
32,
2,
4,
99
] | 13 | true | Domain | Peptidase S54, rhomboid domain | Peptidase S54, rhomboid domain | Peptidase_S54_rhomboid_dom | 3 |
IPR022765 | 22,765 | Dna2/Cas4, domain of unknown function DUF83 | Dna2/Cas4_DUF83 | Domain | 6,606 | false | false | This entry represents an uncharacterised domain found in several proteins, including DNA replication helicase Dna2, clustered regularly interspaced short palindromic repeats (CRISPR)-associated exonuclease Cas4 and putative RecB family exonuclease proteins. Dna2 is a DNA replication factor with single-stranded DNA-depe... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01930"
] | [
"Cas_Cas4"
] | [
6606
] | 1 | [
"EC"
] | [
"3.1.12.1"
] | [
"EC:3.1.12.1"
] | 1 | [
"4r5q",
"7mi4",
"7mi5",
"7mi9",
"7mib",
"7mid",
"8d3l",
"8d3m",
"8d3p",
"8d3q"
] | 10 | [
"PUB00063905"
] | [
"23056615"
] | [
"The CRISPR associated protein Cas4 Is a 5' to 3' DNA exonuclease with an iron-sulfur cluster."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
789,
4776,
889,
36,
116
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Domain | Dna2/Cas4, domain of unknown function DUF83 | Dna2/Cas4, domain of unknown function DUF83 | Dna2/Cas4_DUF83 | 3 |
IPR022768 | 22,768 | Fascin-like domain | Fascin-like_dom | Domain | 3,450 | false | false | This entry represents the fascin-like domain, which is found repeated four times in members of the fascin family. This domain adopts a β-trefoil fold [ ]. The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of ... | [
"GO:0030674",
"GO:0051015"
] | [
"protein-macromolecule adaptor activity",
"actin filament binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF06268"
] | [
"Fascin"
] | [
3450
] | 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",
"3llp",
"3p53",
"4gov",
"4goy",
"4gp0",
"4gp3",
"6b0t",
"6i0z",
"6i10",
"6i11",
"6i12",
"6i13",
"6i14",
"6i15",
"6i16",
"6i17",
"6i18",
"7zau",
"8vo5",
"8vo6",
"8vo7",
"8vo8",
"8vo9",
"8voa",
"9fn6",
"9gs6",
"9gxi"
] | 30 | [
"PUB00012306",
"PUB00012367",
"PUB00065219"
] | [
"11948621",
"1436061",
"23184945"
] | [
"Fascins, and their roles in cell structure and function.",
"Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.",
"Molecular mechanism of fascin function in filopodial formation."
] | [
2002,
1992,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bioreactor metagenome",
"unclassified dsDNA viruses"
] | [
151,
3294,
1,
4
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
3,
10,
5,
11
] | 5 | true | Domain | Fascin-like domain | Fascin-like domain | Fascin-like_dom | 9 |
IPR022770 | 22,770 | Aerobactin siderophore biosynthesis IucA/IucC-like, C-terminal | IucA/IucC-like_C | Domain | 17,787 | false | false | This entry represents the C-terminal domain of this group of proteins which is related to the FhuF iron transporter proteins. FhuF is involved in the reduction of ferric iron in cytoplasmic ferrioxamine B [ ]. Bacteria solve the iron supply problem caused by the insolubility of Fe(3) by synthesizing iron-complexing com... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06276"
] | [
"FhuF"
] | [
17787
] | 1 | [
"GP"
] | [
"GenProp1593"
] | [
"GP:GenProp1593"
] | 1 | [
"2w02",
"2w03",
"2w04",
"2x0o",
"2x0p",
"2x0q",
"2x3j",
"2x3k",
"3ffe",
"3to3",
"5jm7",
"5jm8",
"5o7o",
"6cn7",
"6nl2",
"6p63",
"6xrc",
"7cbb",
"7qp5",
"7tgj",
"7tgk",
"7tgl",
"7tgm",
"7tgn",
"9nom"
] | 25 | [
"PUB00009894",
"PUB00010339",
"PUB00092857",
"PUB00154502",
"PUB00154503"
] | [
"3087960",
"9990318",
"19775248",
"18956041",
"36702957"
] | [
"Characterization of iucA and iucC genes of the aerobactin system of plasmid ColV-K30 in Escherichia coli.",
"FhuF, an iron-regulated protein of Escherichia coli with a new type of [2Fe-2S] center.",
"Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus.",
"Bisucaberin biosynth... | [
1986,
1998,
2009,
2008,
2023
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
16837,
657,
253,
40
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Aerobactin siderophore biosynthesis IucA/IucC-like, C-terminal | Aerobactin siderophore biosynthesis IucA/IucC-like, C-terminal | IucA/IucC-like_C | 8 |
IPR022771 | 22,771 | Wings apart-like protein, C-terminal | WAPL_C | Domain | 5,174 | false | false | This entry represents the conserved region of D. melanogaster wings apart-like protein, WAPL. It is involved in the regulation of heterochromatin structure [ ]. hWAPL ( ), the human homologue, is found to play a role in the development of cervical carcinogenesis, and is thought to have similar functions to Drosophila w... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07814"
] | [
"WAPL"
] | [
5174
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-2468052",
"R-CEL-2470946",
"R-CEL-2500257",
"R-DME-2468052",
"R-DME-2470946",
"R-DME-2500257",
"R-HSA-2467813",
"R-HSA-2468052",
"R-HSA-2470946",
"R-HSA-2500257",
"R-MMU-2467813",
"R-MMU-2468052",
"R-MMU-2470946",
"R-MMU-2500257",
"R-SPO-2470946",
"R-SPO-2500257"
] | [
"REACTOME:R-CEL-2468052",
"REACTOME:R-CEL-2470946",
"REACTOME:R-CEL-2500257",
"REACTOME:R-DME-2468052",
"REACTOME:R-DME-2470946",
"REACTOME:R-DME-2500257",
"REACTOME:R-HSA-2467813",
"REACTOME:R-HSA-2468052",
"REACTOME:R-HSA-2470946",
"REACTOME:R-HSA-2500257",
"REACTOME:R-MMU-2467813",
"REACTOM... | 16 | [
"4k6j"
] | 1 | [
"PUB00016495",
"PUB00016544"
] | [
"10747063",
"15150110"
] | [
"Genetic and molecular analysis of wings apart-like (wapl), a gene controlling heterochromatin organization in Drosophila melanogaster.",
"Expression of a novel human gene, human wings apart-like (hWAPL), is associated with cervical carcinogenesis and tumor progression."
] | [
2000,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5174
] | 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",
"Schizosaccharomyces pombe (stra... | [
10,
4,
3,
23,
5,
4,
1,
6,
3,
1,
29
] | 11 | true | Domain | Wings apart-like protein, C-terminal | Wings apart-like protein, C-terminal | WAPL_C | 5 |
IPR022772 | 22,772 | von Hippel-Lindau disease tumour suppressor, beta/alpha domain | VHL_tumour_suppress_b/a_dom | Domain | 1,634 | false | false | This entry represents both beta and alpha domains of VHL. von Hippel-Landau (pVHL) protein, the gene product of VHL, is a critical regulator of the ubiquitous oxygen-sensing pathway. It is conserved throughout evolution, as its homologues are found in organisms ranging from mammals to Drosophila and Caenorhabditis. pVH... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd05468"
] | [
"pVHL"
] | [
1634
] | 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-1234176",
"R-CEL-3232142",
"R-CEL-8951664",
"R-CEL-9706019",
"R-CEL-983168",
"R-DME-1234176",
"R-DME-8951664",
"R-DME-9706019",
"R-DME-983168",
"R-HSA-1234176",
"R-HSA-3232142",
"R-HSA-8951664",
"R-HSA-9682706",
"R-HSA-9694686",
"R-HSA-9706019",
"R-HSA-983168",
"R-MMU-1234176"... | [
"REACTOME:R-CEL-1234176",
"REACTOME:R-CEL-3232142",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-9706019",
"REACTOME:R-CEL-983168",
"REACTOME:R-DME-1234176",
"REACTOME:R-DME-8951664",
"REACTOME:R-DME-9706019",
"REACTOME:R-DME-983168",
"REACTOME:R-HSA-1234176",
"REACTOME:R-HSA-3232142",
"REACTOME:... | 26 | [
"1lm8",
"1lqb",
"1vcb",
"3zrc",
"3zrf",
"3ztc",
"3ztd",
"3zun",
"4ajy",
"4awj",
"4b95",
"4b9k",
"4bks",
"4bkt",
"4w9c",
"4w9d",
"4w9e",
"4w9f",
"4w9g",
"4w9h",
"4w9i",
"4w9j",
"4w9k",
"4w9l",
"4wqo",
"5lli",
"5n4w",
"5nvv",
"5nvw",
"5nvx",
"5nvy",
"5nvz"... | 138 | [
"PUB00005233",
"PUB00022097",
"PUB00027102",
"PUB00079586",
"PUB00079587",
"PUB00079588",
"PUB00079589",
"PUB00079591",
"PUB00079592",
"PUB00079593",
"PUB00079594",
"PUB00079595",
"PUB00079596",
"PUB00079597",
"PUB00079598",
"PUB00079599",
"PUB00079600",
"PUB00079601",
"PUB000796... | [
"10205047",
"12004076",
"12050673",
"17998064",
"19671042",
"19657325",
"19414081",
"19402056",
"19261475",
"19243301",
"19216840",
"15611513",
"18095884",
"17932373",
"17255293",
"17245122",
"18323857",
"16728571",
"16531988",
"16869749"
] | [
"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.",
"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling.",
"Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.",
"The von hippel-lindau tumor suppressor pro... | [
1999,
2002,
2002,
2007,
2009,
2009,
2009,
2009,
2009,
2009,
2009,
2004,
2008,
2008,
2007,
2007,
2008,
2006,
2006,
2005
] | 20 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
76,
1557,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
3,
8,
2,
4
] | 6 | true | Domain | von Hippel-Lindau disease tumour suppressor, beta/alpha domain | von Hippel-Lindau disease tumour suppressor, beta/alpha domain | VHL_tumour_suppress_b/a_dom | 9 |
IPR022773 | 22,773 | Siva | Siva | Family | 1,345 | false | false | Siva binds to the CD27 cytoplasmic tail. It has a DD homology region, a box-B-like ring finger, and a zinc finger-like domain. Overexpression of Siva in various cell lines induces apoptosis, suggesting an important role for Siva in the CD27-transduced apoptotic pathway [ ]. Siva-1 binds to and inhibits BCL-X(L)-mediate... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF05458",
"PIRSF038096",
"PTHR14365"
] | [
"Siva",
"Siva_cd27_bd",
""
] | [
1279,
236,
1264
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00011475",
"PUB00011476"
] | [
"9177220",
"12011449"
] | [
"CD27, a member of the tumor necrosis factor receptor family, induces apoptosis and binds to Siva, a proapoptotic protein.",
"Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis."
] | [
1997,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1345
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
6,
7,
2,
5,
1
] | 6 | true | Family | Siva | Siva | Siva | 4 |
IPR022775 | 22,775 | AP complex, mu/sigma subunit | AP_mu_sigma_su | Domain | 44,897 | 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... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01217"
] | [
"Clat_adaptor_s"
] | [
44897
] | 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-177504",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-416993",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-437239",
"R-BTA-5099900",
"R-BTA-5140745",
"R-BTA-6798695",
"R-BTA-6807878",
"R-BTA-6811434",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8866427",
"R-BTA-8964038",
... | [
"REACTOME:R-BTA-177504",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-416993",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-5099900",
"REACTOME:R-BTA-5140745",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA... | 139 | [
"1w63",
"2bp5",
"2hf6",
"2jkr",
"2jkt",
"2vgl",
"2xa7",
"3tjz",
"4hmy",
"4nee",
"4p6z",
"4uqi",
"5a1u",
"5a1v",
"5a1w",
"5a1x",
"5a1y",
"5fpi",
"5mc7",
"5mu7",
"5nzr",
"5nzs",
"5nzt",
"5nzu",
"5nzv",
"6cm9",
"6cri",
"6d83",
"6d84",
"6dff",
"6owo",
"6owt"... | 72 | [
"PUB00000652",
"PUB00001249",
"PUB00003074",
"PUB00029720",
"PUB00030524",
"PUB00035753",
"PUB00035768",
"PUB00035769",
"PUB00035771",
"PUB00035772"
] | [
"8373805",
"8157009",
"8276893",
"12858162",
"14690497",
"17449236",
"17041781",
"15261670",
"9002613",
"14729954"
] | [
"Cloning of the YAP19 gene encoding a putative yeast homolog of AP19, the mammalian small chain of the clathrin-assembly proteins.",
"The Saccharomyces cerevisiae APS1 gene encodes a homolog of the small subunit of the mammalian clathrin AP-1 complex: evidence for functional interaction with clathrin at the Golgi... | [
1993,
1994,
1993,
2003,
2004,
2007,
2006,
2004,
1996,
2004
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3,
44890,
4
] | 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... | [
43,
9,
48,
17,
118,
55,
7,
40,
73,
6,
7,
100
] | 12 | true | Domain | AP complex, mu/sigma subunit | AP complex, mu/sigma subunit | AP_mu_sigma_su | 3 |
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