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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR018113 | 18,113 | Phosphotransferase system EIIB, cysteine phosphorylation site | PTrfase_EIIB_Cys | Conserved_site | 43,952 | false | false | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosp... | [
"GO:0008982"
] | [
"protein-N(PI)-phosphohistidine-sugar phosphotransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROSITE",
"CDD"
] | [
"PF00367",
"PS01035",
"cd00212"
] | [
"PTS_EIIB",
"PTS_EIIB_TYPE_1_CYS",
"PTS_IIB_glc"
] | [
43878,
38391,
41985
] | 3 | [
"EC",
"GP"
] | [
"2.7.1",
"GenProp0119"
] | [
"EC:2.7.1",
"GP:GenProp0119"
] | 2 | [
"1iba",
"1o2f",
"3bp3",
"3bp8",
"3ipj",
"8qsr",
"8qst",
"9hnp"
] | 8 | [
"PUB00000073",
"PUB00002162",
"PUB00003612"
] | [
"2197982",
"1537788",
"8246840"
] | [
"The bacterial phosphoenolpyruvate: glycose phosphotransferase system.",
"Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.",
"Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria."
] | [
1990,
1992,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
43841,
40,
71
] | 3 | [
"Escherichia coli (strain K12)"
] | [
8
] | 1 | true | Conserved_site | Phosphotransferase system EIIB, cysteine phosphorylation site | Phosphotransferase system EIIB, cysteine phosphorylation site | PTrfase_EIIB_Cys | 7 |
IPR018114 | 18,114 | Serine proteases, trypsin family, histidine active site | TRYPSIN_HIS | Active_site | 153,072 | false | false | This entry represents the histidine active site of serine proteases belonging to the MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)). The catalytic activity of the serine proteases from the chymotrypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a hist... | [
"GO:0004252",
"GO:0006508"
] | [
"serine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00134"
] | [
"TRYPSIN_HIS"
] | [
153072
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"R-BTA-114608",
"R-BTA-140834",
"R-BTA-140837",
"R-BTA-1592389",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-166663",
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-381426",
"R-BTA-6798695",
"R-BTA-75205",
"R-BTA-8957275",
"R-BTA-977606",
"R-CFA-140875",
"R-CFA-1433557... | [
"EC:3.4.21",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-166663",
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-381426",
"RE... | 181 | [
"1a0h",
"1a0j",
"1a0l",
"1a2c",
"1a3b",
"1a3e",
"1a46",
"1a4w",
"1a5g",
"1a5h",
"1a5i",
"1a61",
"1ab9",
"1abi",
"1abj",
"1acb",
"1ad8",
"1ae8",
"1afe",
"1afq",
"1aht",
"1ai8",
"1aix",
"1aks",
"1amh",
"1an1",
"1anb",
"1anc",
"1and",
"1ane",
"1ao5",
"1aq7"... | 2,547 | [
"PUB00003576",
"PUB00004028"
] | [
"7845208",
"3136396"
] | [
"Families of serine peptidases.",
"The molecular evolution of genes and proteins: a tale of two serines."
] | [
1994,
1988
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
17,
20305,
132610,
21,
119
] | 5 | [
"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)",
"Rattus norvegicus"
] | [
6,
213,
402,
1,
418,
318,
1,
431
] | 8 | true | Active_site | Serine proteases, trypsin family, histidine active site | Serine proteases, trypsin family, histidine active site | TRYPSIN_HIS | 3 |
IPR018116 | 18,116 | Somatotropin hormone, conserved site | Somatotropin_CS | Conserved_site | 5,600 | false | false | Somatotropin is a hormone that plays an important role in growth control. It belongs to a family that includes choriomammotropin (lactogen), its placental analogue; prolactin, which promotes lactation in the mammary gland, and placental prolactin-related proteins; proliferin and proliferin related protein; and somatola... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00266",
"PS00338"
] | [
"SOMATOTROPIN_1",
"SOMATOTROPIN_2"
] | [
4514,
4696
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-1170546",
"R-CFA-422085",
"R-CFA-982772",
"R-GGA-1170546",
"R-GGA-422085",
"R-GGA-982772",
"R-HSA-1170546",
"R-HSA-422085",
"R-HSA-977225",
"R-HSA-982772",
"R-MMU-1170546",
"R-MMU-422085",
"R-MMU-982772",
"R-RNO-1170546",
"R-RNO-422085",
"R-RNO-982772",
"R-SSC-1170546",
"R-S... | [
"REACTOME:R-CFA-1170546",
"REACTOME:R-CFA-422085",
"REACTOME:R-CFA-982772",
"REACTOME:R-GGA-1170546",
"REACTOME:R-GGA-422085",
"REACTOME:R-GGA-982772",
"REACTOME:R-HSA-1170546",
"REACTOME:R-HSA-422085",
"REACTOME:R-HSA-977225",
"REACTOME:R-HSA-982772",
"REACTOME:R-MMU-1170546",
"REACTOME:R-MMU... | 19 | [
"1a22",
"1axi",
"1bp3",
"1f6f",
"1hgu",
"1huw",
"1hwg",
"1hwh",
"1kf9",
"1rw5",
"1z7c",
"2q98",
"3d48",
"3ew3",
"3hhr",
"3mzg",
"3n06",
"3n0p",
"3ncb",
"3ncc",
"3nce",
"3ncf",
"3npz"
] | 23 | [
"PUB00000308",
"PUB00000338",
"PUB00000346",
"PUB00000588"
] | [
"2765528",
"1993170",
"2021631",
"2790033"
] | [
"A subfamily of bovine prolactin-related transcripts distinct from placental lactogen in the fetal placenta.",
"Isolation and characterization of somatolactin, a new protein related to growth hormone and prolactin from Atlantic cod (Gadus morhua) pituitary glands.",
"A heuristic approach to predicting the terti... | [
1989,
1991,
1991,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Heunggongvirae",
"organismal metagenomes"
] | [
7,
5589,
2,
2
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
1,
13,
36,
50,
71,
1
] | 6 | true | Conserved_site | Somatotropin hormone, conserved site | Somatotropin hormone, conserved site | Somatotropin_CS | 6 |
IPR018117 | 18,117 | DNA methylase, C-5 cytosine-specific, active site | C5_DNA_meth_AS | Active_site | 32,102 | false | false | C-5 cytosine-specific DNA methylases (C5 Mtase) are enzymes that specifically methylate the C-5 carbon of cytosines in DNA [ , , ]. Such enzymes are found in the proteins described below. As a component of type II restriction-modification systems in prokaryotes and some bacteriophages. Such enzymes recognise a specific... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00094"
] | [
"C5_MTASE_1"
] | [
32102
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1.37",
"R-HSA-212300",
"R-HSA-3214858",
"R-HSA-427413",
"R-HSA-4655427",
"R-HSA-5334118",
"R-HSA-9701898",
"R-HSA-9710421",
"R-HSA-9725371",
"R-HSA-9845323",
"R-MMU-212300",
"R-MMU-3214858",
"R-MMU-4655427",
"R-RNO-212300",
"R-RNO-3214858",
"R-RNO-4655427"
] | [
"EC:2.1.1.37",
"REACTOME:R-HSA-212300",
"REACTOME:R-HSA-3214858",
"REACTOME:R-HSA-427413",
"REACTOME:R-HSA-4655427",
"REACTOME:R-HSA-5334118",
"REACTOME:R-HSA-9701898",
"REACTOME:R-HSA-9710421",
"REACTOME:R-HSA-9725371",
"REACTOME:R-HSA-9845323",
"REACTOME:R-MMU-212300",
"REACTOME:R-MMU-321485... | 16 | [
"10mh",
"1dct",
"1fjx",
"1hmy",
"1m0e",
"1mht",
"1skm",
"1svu",
"2c7o",
"2c7p",
"2c7q",
"2c7r",
"2hmy",
"2hr1",
"2i9k",
"2qrv",
"2uyc",
"2uyh",
"2uz4",
"2z6q",
"2z6u",
"2zcj",
"3av4",
"3av5",
"3av6",
"3eeo",
"3g7u",
"3lx6",
"3me5",
"3mht",
"3pt6",
"3pt9"... | 120 | [
"PUB00000336",
"PUB00001771",
"PUB00003244",
"PUB00004446"
] | [
"1932026",
"3248729",
"2716049",
"8127644"
] | [
"Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase.",
"Sequence motifs specific for cytosine methyltransferases.",
"Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains.",
"The DNA (cytosine-5) methyltrans... | [
1991,
1988,
1989,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
317,
19752,
10941,
602,
490
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"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",
"Zea mays"
] | [
28,
52,
1,
22,
13,
1,
9,
14,
49
] | 9 | true | Active_site | DNA methylase, C-5 cytosine-specific, active site | DNA methylase, C-5 cytosine-specific, active site | C5_DNA_meth_AS | 2 |
IPR018120 | 18,120 | Glycoside hydrolase family 1, active site | Glyco_hydro_1_AS | Active_site | 31,377 | false | false | Glycoside hydrolase family 1 comprises enzymes with a number of known activities; beta-glucosidase ( ); beta-galactosidase ( ); 6-phospho-beta-galactosidase ( ); 6-phospho-beta-glucosidase ( ); lactase-phlorizin hydrolase ( )/( ); beta-mannosidase ( ); myrosinase ( ). This entry represents a conserved region found in t... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00572"
] | [
"GLYCOSYL_HYDROL_F1_1"
] | [
31377
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.1",
"R-HSA-189085",
"R-HSA-5659898",
"R-RNO-189085"
] | [
"EC:3.2.1",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-5659898",
"REACTOME:R-RNO-189085"
] | 4 | [
"1bga",
"1bgg",
"1cbg",
"1dwa",
"1dwf",
"1dwg",
"1dwh",
"1dwi",
"1dwj",
"1e1e",
"1e1f",
"1e4i",
"1e4l",
"1e4m",
"1e4n",
"1e55",
"1e56",
"1e6q",
"1e6s",
"1e6x",
"1e70",
"1e71",
"1e72",
"1e73",
"1gnx",
"1gon",
"1gow",
"1h49",
"1hxj",
"1myr",
"1np2",
"1od0"... | 213 | [
"PUB00002205"
] | [
"1732212"
] | [
"Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
158,
23136,
6,
7962,
115
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
50,
12,
1,
3,
5,
3,
2,
4,
44
] | 9 | true | Active_site | Glycoside hydrolase family 1, active site | Glycoside hydrolase family 1, active site | Glyco_hydro_1_AS | 8 |
IPR018122 | 18,122 | Fork head domain conserved site1 | TF_fork_head_CS_1 | Conserved_site | 33,258 | false | false | The fork head domain is a conserved domain of about 100 amino-acid residues found in some eukaryotic transcription factors. It is involved in DNA-binding [ ]. This entry represents a conserved site found in the N-terminal section of the fork head domain. | [
"GO:0003700",
"GO:0043565",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"sequence-specific DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00657"
] | [
"FORK_HEAD_1"
] | [
33258
] | 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-3232118",
"R-CEL-3232118",
"R-DME-9018519",
"R-DME-9617828",
"R-GGA-9617828",
"R-HSA-156711",
"R-HSA-210745",
"R-HSA-2892247",
"R-HSA-3232118",
"R-HSA-5689603",
"R-HSA-69273",
"R-HSA-9018519",
"R-HSA-9022692",
"R-HSA-9617828",
"R-HSA-9725371",
"R-HSA-9758920",
"R-HSA-9761174",... | [
"REACTOME:R-BTA-3232118",
"REACTOME:R-CEL-3232118",
"REACTOME:R-DME-9018519",
"REACTOME:R-DME-9617828",
"REACTOME:R-GGA-9617828",
"REACTOME:R-HSA-156711",
"REACTOME:R-HSA-210745",
"REACTOME:R-HSA-2892247",
"REACTOME:R-HSA-3232118",
"REACTOME:R-HSA-5689603",
"REACTOME:R-HSA-69273",
"REACTOME:R-... | 40 | [
"1d5v",
"1jxs",
"1kq8",
"1vtn",
"2a3s",
"2c6y",
"2d2w",
"2hdc",
"2hfh",
"3g73",
"5a5u",
"5x07",
"6ako",
"6akp",
"6fec",
"6lbm",
"6nce",
"6ncm",
"6o3t",
"7cby",
"7fj2",
"7vou",
"7vov",
"7vox",
"7yze",
"7yzf",
"8bzm",
"8vfy",
"8vfz",
"8vg1",
"8vg2",
"9efw"... | 32 | [
"PUB00004151"
] | [
"8332212"
] | [
"Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Avian sarcoma virus (strain 31)",
"Eukaryota",
"Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a)"
] | [
2,
33255,
1
] | 3 | [
"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... | [
8,
83,
30,
88,
60,
1,
87,
4,
1
] | 9 | true | Conserved_site | Fork head domain conserved site1 | Fork head domain conserved site1 | TF_fork_head_CS_1 | 7 |
IPR018123 | 18,123 | WWE domain, subgroup | WWE-dom_subgr | Domain | 11,434 | false | false | The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein-protein interactions in ubiquitin and ADP ribose conjugation systems. This domain is found as a tandem repeat at the N-terminal of Deltex, a cytosolic effector of Notch signalling thought to bind the N-terminal of... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"SMART"
] | [
"SM00678"
] | [
"WWE"
] | [
11434
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"2.3.2.27",
"PWY-7511",
"R-BTA-201681",
"R-BTA-4641257",
"R-BTA-5689880",
"R-BTA-8948751",
"R-DME-2122948",
"R-DRE-8948751",
"R-HSA-1606341",
"R-HSA-201681",
"R-HSA-2122948",
"R-HSA-3134975",
"R-HSA-3270619",
"R-HSA-4641257",
"R-HSA-5689880",
"R-HSA-8948751",
"R-HSA-983168",
"R-MMU... | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-BTA-201681",
"REACTOME:R-BTA-4641257",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8948751",
"REACTOME:R-DME-2122948",
"REACTOME:R-DRE-8948751",
"REACTOME:R-HSA-1606341",
"REACTOME:R-HSA-201681",
"REACTOME:R-HSA-2122948",
"REACTOME:R-HSA-3134975",
... | 31 | [
"1ujr",
"2a90",
"2rsf",
"3v3l",
"4qpl",
"8r5n",
"8r6a",
"8r6b",
"9bkr",
"9bks"
] | 10 | [
"PUB00018391",
"PUB00039194"
] | [
"11343911",
"16271883"
] | [
"The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation.",
"Structure and Notch receptor binding of the tandem WWE domain of Deltex."
] | [
2001,
2005
] | 2 | [
"IPR004170"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Viruses",
"organismal metagenomes"
] | [
11428,
4,
2
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
74,
17,
15,
11,
22
] | 6 | true | Domain | WWE domain, subgroup | WWE domain, subgroup | WWE-dom_subgr | 4 |
IPR018124 | 18,124 | Calreticulin/calnexin, conserved site | Calret/calnex_CS | Conserved_site | 13,831 | false | false | null | [
"GO:0005509"
] | [
"calcium ion binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS00803",
"PS00804",
"PS00805"
] | [
"CALRETICULIN_1",
"CALRETICULIN_2",
"CALRETICULIN_REPEAT"
] | [
10868,
12271,
9204
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-901042",
"R-DDI-901042",
"R-DME-901042",
"R-HSA-1236974",
"R-HSA-168316",
"R-HSA-2132295",
"R-HSA-3000480",
"R-HSA-3000484",
"R-HSA-381183",
"R-HSA-8984722",
"R-HSA-901042",
"R-HSA-9020956",
"R-HSA-9683686",
"R-HSA-9694548",
"R-HSA-9768727",
"R-HSA-983170",
"R-MMU-1236974",
... | [
"REACTOME:R-CEL-901042",
"REACTOME:R-DDI-901042",
"REACTOME:R-DME-901042",
"REACTOME:R-HSA-1236974",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-3000480",
"REACTOME:R-HSA-3000484",
"REACTOME:R-HSA-381183",
"REACTOME:R-HSA-8984722",
"REACTOME:R-HSA-901042",
"REACTOME:R-HS... | 38 | [
"1hhn",
"1jhn",
"1k91",
"1k9c",
"3ici",
"3o0v",
"3o0w",
"3o0x",
"3pos",
"3pow",
"3rg0",
"5hca",
"5hcb",
"5hcf",
"5lk5",
"5v8z",
"5v90",
"6eny",
"7qpd",
"8rjc",
"8rjd",
"8tzo",
"8tzr",
"8xvf"
] | 24 | [
"PUB00000513",
"PUB00002891",
"PUB00005415"
] | [
"1497605",
"8126001",
"8203019"
] | [
"Calreticulin.",
"Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development.",
"Calnexin: a membrane-bound chaperone of the endoplasmic reticulum."
] | [
1992,
1994,
1994
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
8,
13823
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
32,
2,
8,
12,
35,
12,
1,
21,
21,
1,
1,
43
] | 12 | true | Conserved_site | Calreticulin/calnexin, conserved site | Calreticulin/calnexin, conserved site | Calret/calnex_CS | 8 |
IPR018129 | 18,129 | Phosphoenolpyruvate carboxylase, Lys active site | PEP_COase_Lys_AS | Active_site | 15,880 | false | false | Phosphoenolpyruvate carboxylase (PEPcase) catalyzes the irreversible β-carboxylation of phosphoenolpyruvate by bicarbonate to yield oxaloacetate and phosphate. The enzyme is found in all plants and in a variety of microorganisms. A histidine [ ] and a lysine [ ] have been implicated in the catalytic mechanism of this e... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00781"
] | [
"PEPCASE_1"
] | [
15880
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.31",
"PWY-1622",
"PWY-241",
"PWY-5913",
"PWY-6142",
"PWY-6146",
"PWY-6549",
"PWY-7115",
"PWY-7117",
"PWY-7124"
] | [
"EC:4.1.1.31",
"METACYC:PWY-1622",
"METACYC:PWY-241",
"METACYC:PWY-5913",
"METACYC:PWY-6142",
"METACYC:PWY-6146",
"METACYC:PWY-6549",
"METACYC:PWY-7115",
"METACYC:PWY-7117",
"METACYC:PWY-7124"
] | 10 | [
"1fiy",
"1jqn",
"1jqo",
"1qb4",
"3zgb",
"3zge",
"4bxc",
"4bxh",
"5fdn",
"5vyj",
"6mgi",
"6u2t",
"6v3o",
"8cj5",
"8cj8",
"8oj9",
"8oje",
"8ojf",
"8ojq",
"8ojy",
"8ojz",
"8qtm",
"8qx1",
"8qx3"
] | 24 | [
"PUB00000601",
"PUB00001406"
] | [
"2268676",
"1765093"
] | [
"Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate.",
"Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction."
] | [
1990,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
12268,
3160,
280,
172
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
19,
38
] | 4 | true | Active_site | Phosphoenolpyruvate carboxylase, Lys active site | Phosphoenolpyruvate carboxylase, Lys active site | PEP_COase_Lys_AS | 2 |
IPR018130 | 18,130 | Small ribosomal subunit protein uS2, conserved site | Ribosomal_uS2_CS | Conserved_site | 48,980 | false | false | Ribosomal protein uS2 is is a protein of 235 to 394 amino-acid residues and is one of the proteins from the small ribosomal subunit. uS2 belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ , ], groups: Eubacterial uS2. Algal and plant chloroplast uS2. Cyanelle uS2. Archaebacterial u... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00962",
"PS00963"
] | [
"RIBOSOMAL_S2_1",
"RIBOSOMAL_S2_2"
] | [
42255,
36027
] | 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-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9837999",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-9759... | 148 | [
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1vi5",
"1vi6",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1x18",
"1xmo",
"1xmq",
"1xnq"... | 1,780 | [
"PUB00001672",
"PUB00044781"
] | [
"8119397",
"531984"
] | [
"Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit.",
"Butvar B-98 as a thin support film."
] | [
1994,
1979
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
820,
23482,
24150,
8,
520
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
17,
1,
4,
2,
1,
11,
6,
2,
12,
11,
3,
3,
33
] | 13 | true | Conserved_site | Small ribosomal subunit protein uS2, conserved site | Small ribosomal subunit protein uS2, conserved site | Ribosomal_uS2_CS | 9 |
IPR018131 | 18,131 | Restriction endonuclease, type II, EcoRI, Proteobacteria | Restrct_endonuc_II_EcoRI_Pbac | Family | 3 | false | false | This entry represents restriction endonucleases EcoRI in Proteobacteria, which requires magnesium as a cofactor. EcoRI recognises the DNA sequence GAATTC and cleaves after G-1 [ ]. | [
"GO:0000287",
"GO:0003677",
"GO:0009036",
"GO:0009307"
] | [
"magnesium ion binding",
"DNA binding",
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF001002"
] | [
"Restrict_endonuc_II_EcoRI"
] | [
3
] | 1 | [] | [] | [] | 0 | [
"1ckq",
"1cl8",
"1eri",
"1qc9",
"2oxv"
] | 5 | [
"PUB00035695"
] | [
"11170385"
] | [
"Solution conformation of EcoRI restriction endonuclease changes upon binding of cognate DNA and Mg2+ cofactor."
] | [
2001
] | 1 | [
"IPR004221"
] | [] | 1 | 0 | 1 | [
"Plasmid P6",
"Pseudomonadota"
] | [
1,
2
] | 2 | [] | [] | 0 | true | Family | Restriction endonuclease, type II, EcoRI, Proteobacteria | Restriction endonuclease, type II, EcoRI, Proteobacteria | Restrct_endonuc_II_EcoRI_Pbac | 3 |
IPR018136 | 18,136 | Aconitase family, 4Fe-4S cluster binding site | Aconitase_4Fe-4S_BS | Binding_site | 72,051 | false | false | Aconitase (aconitate hydratase) [ ] is the enzyme from the tricarboxylic acid cycle that catalyzes the reversible isomerization of citrate and isocitrate. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mi... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00450",
"PS01244"
] | [
"ACONITASE_1",
"ACONITASE_2"
] | [
65853,
64472
] | 2 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"4.2.1",
"4.2.1.33",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-389542",
"R-CEL-71403",
"R-CEL-917937",
"R-CEL-9837999",
"R-CEL-9854311",
"R-DDI-389542",
"R-DDI-71403",
"R-DDI-917937",
"R-DDI-9837999",
"R-DDI-9854311",
"R-HSA-1268020",
"R-HSA-389542",
"R-HSA-71403",
... | [
"EC:4.2.1",
"EC:4.2.1.33",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-389542",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-917937",
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-389542",
"REACTOME:R-DDI-71403",
"REACTOME:R-DD... | 39 | [
"1aco",
"1ami",
"1amj",
"1b0j",
"1b0k",
"1b0m",
"1c96",
"1c97",
"1fgh",
"1l5j",
"1nis",
"1nit",
"2b3x",
"2b3y",
"4kp1",
"4kp2",
"4nqy",
"5acn",
"6acn",
"6vcd",
"7acn",
"8acn"
] | 22 | [
"PUB00005471"
] | [
"9020582"
] | [
"The aconitase family: three structural variations on a common theme."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1941,
52890,
16084,
1136
] | 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",... | [
11,
2,
5,
9,
3,
24,
5,
4,
10,
15,
4,
5,
76
] | 13 | true | Binding_site | Aconitase family, 4Fe-4S cluster binding site | Aconitase family, 4Fe-4S cluster binding site | Aconitase_4Fe-4S_BS | 4 |
IPR018141 | 18,141 | Nitrile hydratase, alpha subunit | Nitrile_hydratase_asu | Family | 2,178 | false | false | Nitrile hydratases ( ) are bacterial enzymes that catalyse the hydration of nitrile compounds to the corresponding amides. They are used as biocatalysts in acrylamide production, one of the few commercial scale bioprocesses, as well as in environmental remediation for the removal of nitriles from waste streams. Nitrile... | [
"GO:0018822",
"GO:0046914"
] | [
"nitrile hydratase activity",
"transition metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01323"
] | [
"nitrile_alph"
] | [
2178
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.84",
"GenProp0899",
"PWY-5025",
"PWY-581",
"PWY-7308"
] | [
"EC:4.2.1.84",
"GP:GenProp0899",
"METACYC:PWY-5025",
"METACYC:PWY-581",
"METACYC:PWY-7308"
] | 5 | [
"1ahj",
"1ire",
"1ugp",
"1ugq",
"1ugr",
"1ugs",
"1v29",
"2ahj",
"2cyz",
"2cz0",
"2cz1",
"2cz6",
"2cz7",
"2d0q",
"2dpp",
"2qdy",
"2zcf",
"2zpb",
"2zpe",
"2zpf",
"2zpg",
"2zph",
"2zpi",
"3a8g",
"3a8h",
"3a8l",
"3a8m",
"3a8o",
"3hht",
"3qxe",
"3qyg",
"3qyh"... | 63 | [
"PUB00006378",
"PUB00019922",
"PUB00031767",
"PUB00035663",
"PUB00044782",
"PUB00044783"
] | [
"9195885",
"9586994",
"14717710",
"17267045",
"16417356",
"9573140"
] | [
"Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold.",
"Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms.",
"Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding.",
"Influence of cobalt subst... | [
1997,
1998,
2004,
2007,
2006,
1998
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"ecological metagenomes"
] | [
2121,
11,
19,
27
] | 4 | [] | [] | 0 | true | Family | Nitrile hydratase, alpha subunit | Nitrile hydratase, alpha subunit | Nitrile_hydratase_asu | 5 |
IPR018142 | 18,142 | Somatostatin/Cortistatin, C-terminal | Somatostatin/Cortistatin_C | Domain | 1,998 | false | false | This entry represents the C-terminal region of somatostatin and cortistatin. | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF03002"
] | [
"Somatostatin"
] | [
1998
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-375276",
"R-CFA-418594",
"R-GGA-375276",
"R-GGA-418594",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-9022702",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594",
"R-SSC-375276",
"R-SSC-418594"
] | [
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-418594",
"REACTOME:R-GGA-375276",
"REACTOME:R-GGA-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-9022702",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594",
"REACTOME:R-SSC-37... | 13 | [
"2mi1",
"6y1q",
"7s8l",
"7s8m",
"7t10",
"7vdl",
"7vv4",
"7wic",
"7wj5",
"7xat",
"7xmr",
"7xms",
"7y27",
"8x8l",
"8zbi",
"8zbj"
] | 16 | [
"PUB00007453"
] | [
"8622767"
] | [
"A cortical neuropeptide with neuronal depressant and sleep-modulating properties."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
1998
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
4,
3,
4
] | 4 | true | Domain | Somatostatin/Cortistatin, C-terminal | Somatostatin/Cortistatin, C-terminal | Somatostatin/Cortistatin_C | 5 |
IPR018143 | 18,143 | Folate receptor-like | Folate_rcpt-like | Domain | 6,599 | false | false | This entry represents a domain found in folate receptors and at the N terminus of hedgehog-interacting proteins. Folate receptors bind to folate and reduced folic acid derivatives and mediate delivery of 5-methyltetrahydrofolate to the interior of cells. These proteins are attached to the membrane by a GPI-anchor. A ri... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03024"
] | [
"Folate_rec"
] | [
6599
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-163125",
"R-HSA-196757",
"R-HSA-204005",
"R-HSA-5632681",
"R-HSA-5694530",
"R-HSA-6798695",
"R-HSA-6807878",
"R-MMU-163125",
"R-MMU-196757",
"R-MMU-204005",
"R-MMU-5632681",
"R-MMU-5694530",
"R-MMU-6798695",
"R-MMU-6807878",
"R-RNO-163125"
] | [
"REACTOME:R-HSA-163125",
"REACTOME:R-HSA-196757",
"REACTOME:R-HSA-204005",
"REACTOME:R-HSA-5632681",
"REACTOME:R-HSA-5694530",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6807878",
"REACTOME:R-MMU-163125",
"REACTOME:R-MMU-196757",
"REACTOME:R-MMU-204005",
"REACTOME:R-MMU-5632681",
"REACTOME:R-MM... | 15 | [
"4km6",
"4km7",
"4kmx",
"4kmy",
"4kmz",
"4kn0",
"4kn1",
"4kn2",
"4lrh",
"5ejn",
"5f4e",
"5f4q",
"5izq",
"5jka",
"5jkb",
"5jkc",
"5jkd",
"5jke",
"5jyj",
"6hce",
"7pgk",
"7pgl"
] | 22 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
6598,
1
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
9,
13,
34,
23,
3,
18,
6
] | 7 | true | Domain | Folate receptor-like | Folate receptor-like | Folate_rcpt-like | 4 |
IPR018145 | 18,145 | Type IV secretion system ATPase VirB4/TrbE, middle domain | VirB4_CagE_M | Domain | 8,609 | false | false | This domain is found in the Helicobacter pylori protein CagE, Protein virB4 and related proteins. VirB4 is one of three conserved ATPases (along with VirB11 and VirD4) that power type IV secretion systems (T4SSs) [ ]. It provides energy, via hydrolysis of ATP, for the translocation of virulence proteins or the transfer... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF03135"
] | [
"CagE_TrbE_VirB"
] | [
8609
] | 1 | [
"GP"
] | [
"GenProp0485"
] | [
"GP:GenProp0485"
] | 1 | [
"7o41",
"7o42",
"7o43",
"7oiu",
"8rtb",
"8rtd"
] | 6 | [
"PUB00007538",
"PUB00007539",
"PUB00076811",
"PUB00097878",
"PUB00097879",
"PUB00163229",
"PUB00163230"
] | [
"11104802",
"11447179",
"22745169",
"31088930",
"26565397",
"34424036",
"21118511"
] | [
"Virulence factors of Helicobacter pylori responsible for gastric diseases in Mongolian gerbil.",
"Epithelial intestinal cell apoptosis induced by Helicobacter pylori depends on expression of the cag pathogenicity island phenotype.",
"Structure of the VirB4 ATPase, alone and bound to the core complex of a type ... | [
2000,
2001,
2012,
2019,
2015,
2021,
2010
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes",
"plasmids",
"uncultured Caudovirales phage"
] | [
55,
8459,
40,
44,
10,
1
] | 6 | [] | [] | 0 | true | Domain | Type IV secretion system ATPase VirB4/TrbE, middle domain | Type IV secretion system ATPase VirB4/TrbE, middle domain | VirB4_CagE_M | 2 |
IPR018146 | 18,146 | Glyoxalase I, conserved site | Glyoxalase_1_CS | Conserved_site | 27,462 | false | false | Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction: glutathione + methylglyoxal = (R)-S-lactoylglutathione S-lactoylglutathione is then converted by glyoxalase II to lactic acid [ ]. Glyoxalase I is a ubiquitous enzyme which binds one mole of zinc per subun... | [
"GO:0004462",
"GO:0046872"
] | [
"lactoylglutathione lyase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00934",
"PS00935"
] | [
"GLYOXALASE_I_1",
"GLYOXALASE_I_2"
] | [
25988,
9826
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.4.1.5",
"PWY-5386",
"R-HSA-70268",
"R-MMU-70268",
"R-RNO-70268",
"R-SCE-70268",
"R-SPO-70268"
] | [
"EC:4.4.1.5",
"METACYC:PWY-5386",
"REACTOME:R-HSA-70268",
"REACTOME:R-MMU-70268",
"REACTOME:R-RNO-70268",
"REACTOME:R-SCE-70268",
"REACTOME:R-SPO-70268"
] | 7 | [
"1bh5",
"1f9z",
"1fa5",
"1fa6",
"1fa7",
"1fa8",
"1fro",
"1qin",
"1qip",
"2c21",
"2za0",
"3kol",
"3l7t",
"3vw9",
"3w0t",
"3w0u",
"4kyh",
"4kyk",
"4opn",
"4pv5",
"4x2a",
"5d7z",
"5umw",
"6a4z",
"6bnn",
"6bnx",
"6bnz",
"6cky",
"6l0u",
"6l3w",
"7vq6",
"7w5e"... | 43 | [
"PUB00002779"
] | [
"7684374"
] | [
"Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
436,
19453,
7258,
2,
313
] | 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,
5,
2,
1,
3,
5,
1,
14,
2,
1,
1,
27
] | 12 | true | Conserved_site | Glyoxalase I, conserved site | Glyoxalase I, conserved site | Glyoxalase_1_CS | 6 |
IPR018148 | 18,148 | Methylglyoxal synthase, active site | Methylglyoxal_synth_AS | Active_site | 8,258 | false | false | Methylglyoxal synthase (MGS) catalyses the conversion of dihydroxyacetone phosphate (DHAP) to methylglyoxal and phosphate: Glycerone phosphate = methylglyoxal + phosphate The first part of the catalytic mechanism is believed to be similar to TIM (triosephosphate isomerase) in that both enzymes utilise DHAP to form an e... | [
"GO:0008929",
"GO:0019242"
] | [
"methylglyoxal synthase activity",
"methylglyoxal biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01335"
] | [
"METHYLGLYOXAL_SYNTH"
] | [
8258
] | 1 | [
"EC"
] | [
"4.2.3.3"
] | [
"EC:4.2.3.3"
] | 1 | [
"1b93",
"1egh",
"1ik4",
"1s89",
"1s8a",
"1vmd",
"1wo8",
"2x8w",
"2xw6",
"5h3l",
"6f2c",
"6phe",
"8u2v"
] | 13 | [
"PUB00006181",
"PUB00028433"
] | [
"10368300",
"10715115"
] | [
"The crystal structure of methylglyoxal synthase from Escherichia coli.",
"Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate."
] | [
1999,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes",
"uncultured Caudovirales phage"
] | [
7904,
132,
150,
71,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Active_site | Methylglyoxal synthase, active site | Methylglyoxal synthase, active site | Methylglyoxal_synth_AS | 6 |
IPR018149 | 18,149 | Lysyl-tRNA synthetase, class II, C-terminal | Lys-tRNA-synth_II_C | Domain | 37,629 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000166",
"GO:0004824",
"GO:0005524",
"GO:0006430",
"GO:0005737"
] | [
"nucleotide binding",
"lysine-tRNA ligase activity",
"ATP binding",
"lysyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS",
"CDD"
] | [
"PR00982",
"cd00775"
] | [
"TRNASYNTHLYS",
"LysRS_core"
] | [
37477,
24126
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1.6",
"R-CEL-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-9856649",
"R-MMU-9856649",
"R-RNO-9856649",
"R-SCE-9856649",
"R-SPO-9856649"
] | [
"EC:6.1.1.6",
"REACTOME:R-CEL-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649",
"REACTOME:R-RNO-9856649",
"REACTOME:R-SCE-9856649",
"REACTOME:R-SPO-9856649"
] | 10 | [
"1bbu",
"1bbw",
"1e1o",
"1e1t",
"1e22",
"1e24",
"1lyl",
"3a5y",
"3a5z",
"3a74",
"3bju",
"3e9h",
"3e9i",
"3g1z",
"4dpg",
"4ex5",
"4h02",
"4pg3",
"4up7",
"4up8",
"4up9",
"4upa",
"4ycu",
"4ycv",
"4ycw",
"5eln",
"5elo",
"5hgq",
"5vl1",
"5yzx",
"5zh2",
"5zh3"... | 87 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00005800",
"PUB00006477",
"PUB00006540",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"9353192",
"10673435",
"10913247",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
1997,
2000,
2000,
1990,
1999,
2000,
2002
] | 11 | [
"IPR004364"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
177,
28430,
8427,
13,
582
] | 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",... | [
10,
2,
3,
3,
3,
2,
7,
3,
8,
3,
2,
2,
28
] | 13 | true | Domain | Lysyl-tRNA synthetase, class II, C-terminal | Lysyl-tRNA synthetase, class II, C-terminal | Lys-tRNA-synth_II_C | 1 |
IPR018151 | 18,151 | Transcription elongation factor, GreA/GreB, conserved site | TF_GreA/GreB_CS | Conserved_site | 30,524 | false | false | Bacterial proteins GreA and GreB [ , ], are related proteins of about 160 amino-acid residues, and 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 th... | [
"GO:0003677",
"GO:0032784"
] | [
"DNA binding",
"regulation of DNA-templated transcription elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00829",
"PS00830"
] | [
"GREAB_1",
"GREAB_2"
] | [
26094,
21016
] | 2 | [] | [] | [] | 0 | [
"1grj",
"2etn",
"2eul",
"2f23",
"2p4v",
"3aoh",
"3aoi",
"4wqt",
"6ri7",
"6rin"
] | 10 | [
"PUB00000884",
"PUB00004205"
] | [
"8431948",
"7854424"
] | [
"Transcript cleavage factors from E. coli.",
"Crystal structure of the GreA transcript cleavage factor from Escherichia coli."
] | [
1993,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctHip2",
"unclassified sequences"
] | [
29916,
60,
1,
547
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Conserved_site | Transcription elongation factor, GreA/GreB, conserved site | Transcription elongation factor, GreA/GreB, conserved site | TF_GreA/GreB_CS | 8 |
IPR018152 | 18,152 | Superoxide dismutase, copper/zinc, binding site | SOD_Cu/Zn_BS | Binding_site | 18,138 | false | false | Copper/Zinc superoxide dismutase (SODC) [ , , ] is one of the three forms of an enzyme that catalyzes the dismutation of superoxide radicals. SODC binds one atom each of zinc and copper. Various forms of SODC are known: a cytoplasmic form in eukaryotes, an additional chloroplast form in plants, an extracellular form in... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00087",
"PS00332"
] | [
"SOD_CU_ZN_1",
"SOD_CU_ZN_2"
] | [
11502,
15883
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"1.15.1.1",
"PWY-6854",
"R-BTA-114608",
"R-BTA-3299685",
"R-CEL-114608",
"R-CEL-3299685",
"R-DDI-114608",
"R-DDI-3299685",
"R-DME-114608",
"R-DME-3299685",
"R-DRE-114608",
"R-DRE-3299685",
"R-HSA-114608",
"R-HSA-1222387",
"R-HSA-3299685",
"R-HSA-8950505",
"R-HSA-9818027",
"R-MMU-11... | [
"EC:1.15.1.1",
"METACYC:PWY-6854",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-3299685",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-3299685",
"REACTOME:R-DDI-114608",
"REACTOME:R-DDI-3299685",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-3299685",
"REACTOME:R-DRE-114608",
"REACTOME:R-DRE-3299685",
"R... | 29 | [
"1azv",
"1b4l",
"1b4t",
"1ba9",
"1bzo",
"1cb4",
"1cbj",
"1cob",
"1do5",
"1dsw",
"1e9o",
"1e9p",
"1e9q",
"1eqw",
"1eso",
"1f18",
"1f1a",
"1f1d",
"1f1g",
"1fun",
"1hl4",
"1hl5",
"1ib5",
"1ibb",
"1ibd",
"1ibf",
"1ibh",
"1jcv",
"1jk9",
"1kmg",
"1l3n",
"1mfm"... | 250 | [
"PUB00001002",
"PUB00004789",
"PUB00026910",
"PUB00044787"
] | [
"3315461",
"1463506",
"11952792",
"556751"
] | [
"Aspects of the structure, function, and applications of superoxide dismutase.",
"Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.",
"The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization.",
"The i... | [
1987,
1992,
2002,
1977
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"Viruses",
"metagenomes"
] | [
7619,
10210,
20,
185,
104
] | 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",... | [
11,
4,
11,
8,
1,
13,
11,
1,
14,
14,
1,
1,
58
] | 13 | true | Binding_site | Superoxide dismutase, copper/zinc, binding site | Superoxide dismutase, copper/zinc, binding site | SOD_Cu/Zn_BS | 6 |
IPR018154 | 18,154 | TLV/ENV coat polyprotein | TLV/ENV_coat_polyprotein | Family | 13,180 | false | false | Enveloped viruses such as Human immunodeficiency virus 1, influenza virus, and Ebola virus sp. express a surface glycoprotein that mediates both cell attachment and fusion of viral and cellular membranes. The ENV polyprotein (coat polyprotein) usually contains two coat proteins which differ depending on the source. The... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF00429",
"PTHR10424"
] | [
"TLV_coat",
""
] | [
11848,
9320
] | 2 | [] | [] | [] | 0 | [
"1aol",
"1lcs",
"1mg1",
"1mof",
"1y4m",
"2xz3",
"4jf3",
"4jgs",
"5ha6",
"6rx1",
"6rx3",
"7oix",
"7s94",
"8ouh",
"8ouj",
"9fqt",
"9fqu",
"9fqv",
"9fqw"
] | 19 | [
"PUB00010668",
"PUB00027393"
] | [
"9287219",
"8612078"
] | [
"Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.",
"Retrovirus envelope domain at 1.7 angstrom resolution."
] | [
1997,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota",
"Viruses"
] | [
7103,
2,
6075
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
33,
74,
18
] | 4 | true | Family | TLV/ENV coat polyprotein | TLV/ENV coat polyprotein | TLV/ENV_coat_polyprotein | 8 |
IPR018155 | 18,155 | Hyaluronidase | Hyaluronidase | Family | 7,634 | false | false | Glycoside hydrolase family 56 comprises enzymes with only one known activity; hyaluronidase . The venom of Apis mellifera (Honeybee) contains several biologically-active peptides and two enzymes, one of which is a hyaluronidase [ ]. The amino acid sequence of bee venom hyaluronidase contains 349 amino acids, and includ... | [
"GO:0004415",
"GO:0005975"
] | [
"hyalurononglucosaminidase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER"
] | [
"PF01630",
"PIRSF038193",
"PR00846",
"PTHR11769"
] | [
"Glyco_hydro_56",
"Hyaluronidase",
"GLHYDRLASE56",
""
] | [
7628,
5702,
6979,
7557
] | 4 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.1.35",
"PWY-6573",
"R-BTA-2142845",
"R-BTA-2160916",
"R-CEL-2024101",
"R-CEL-2160916",
"R-CEL-2534343",
"R-HSA-2024101",
"R-HSA-2142845",
"R-HSA-2160916",
"R-HSA-2206280",
"R-HSA-2534343",
"R-HSA-9953097",
"R-MMU-2024101",
"R-MMU-2142845",
"R-MMU-2160916",
"R-MMU-2534343",
"R-... | [
"EC:3.2.1.35",
"METACYC:PWY-6573",
"REACTOME:R-BTA-2142845",
"REACTOME:R-BTA-2160916",
"REACTOME:R-CEL-2024101",
"REACTOME:R-CEL-2160916",
"REACTOME:R-CEL-2534343",
"REACTOME:R-HSA-2024101",
"REACTOME:R-HSA-2142845",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2206280",
"REACTOME:R-HSA-2534343",... | 20 | [
"1fcq",
"1fcu",
"1fcv",
"2atm",
"2j88",
"2pe4",
"9jub"
] | 7 | [
"PUB00003064",
"PUB00004814",
"PUB00004870",
"PUB00005266"
] | [
"2269661",
"7682712",
"7624375",
"8535779"
] | [
"cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals.",
"Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm.",
"Conserved catalytic machinery and the prediction of a common ... | [
1990,
1993,
1995,
1995
] | 4 | [] | [
"IPR001329",
"IPR001439",
"IPR027260"
] | 0 | 3 | 0 | [
"Eukaryota",
"Pseudomonadati",
"bird metagenome"
] | [
7615,
18,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
17,
25,
22,
23
] | 5 | true | Family | Hyaluronidase | Hyaluronidase | Hyaluronidase | 3 |
IPR018159 | 18,159 | Spectrin/alpha-actinin | Spectrin/alpha-actinin | Repeat | 73,896 | false | false | Spectrin repeats are found in several proteins involved in cytoskeletal structure and in proteins with a more regulatory role mostly in animals [ , ]. This entry includes spectrin alpha and beta subunits, alpha-actinin and dystrophin [ , , ]. | [] | [] | [] | 0 | [
"SMART",
"CDD"
] | [
"SM00150",
"cd00176"
] | [
"SPEC",
"SPEC"
] | [
70467,
67514
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-390522",
"R-BTA-438066",
"R-BTA-446388",
"R-BTA-5673001",
"R-BTA-9013405",
"R-BTA-9013418",
"R-BTA-9035034",
"R-CEL-375165",
"R-CEL-5673001",
"R-CEL-6807878",
"R-CEL-9913351",
"R-DDI-114608",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9013418",
"R-DDI-9013420",
... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-390522",
"REACTOME:R-BTA-438066",
"REACTOME:R-BTA-446388",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-9013405",
"REACTOME:R-BTA-9013418",
"REACTOME:R-BTA-9035034",
"REACTOME:R-CEL-375165",
"REACTOME:R-CEL-5673001",
"REACTOME:R-CEL-6807878",
"REACTOME:R-C... | 186 | [
"1aj3",
"1cun",
"1g8x",
"1hci",
"1owa",
"1quu",
"1s35",
"1sjj",
"1u4q",
"1u5p",
"1wlx",
"2iak",
"2spc",
"3edu",
"3edv",
"3f31",
"3f57",
"3fb2",
"3kbt",
"3kbu",
"3lbx",
"3pdy",
"3pe0",
"3r6n",
"3uul",
"3uum",
"3uun",
"4d1e",
"4pd3",
"5i4e",
"5j1i",
"5j4o"... | 44 | [
"PUB00005178",
"PUB00029619",
"PUB00030394",
"PUB00030886",
"PUB00099886"
] | [
"8266097",
"12672815",
"10481917",
"15062087",
"11911890"
] | [
"Crystal structure of the repetitive segments of spectrin.",
"Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.",
"Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments.",
"Structural insights into the stability and flexibility of unusual ... | [
1993,
2003,
1999,
2004,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
10,
28,
73856,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
43,
501,
82,
251,
187,
209
] | 6 | true | Repeat | Spectrin/alpha-actinin | Spectrin/alpha-actinin | Spectrin/alpha-actinin | 3 |
IPR018161 | 18,161 | Wnt protein, conserved site | Wnt_CS | Conserved_site | 25,004 | false | false | Wnt-1 (previously known as int-1) [ ] is a proto-oncogene induced by the integration of the mouse mammary tumor virus. It is thought to play a role in intercellular communication and seems to be a signalling molecule important in the development of the central nervous system (CNS). The sequence of wnt-1 is highly conse... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00246"
] | [
"WNT1"
] | [
25004
] | 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-3238698",
"R-CEL-3238698",
"R-CEL-4086398",
"R-CEL-4086400",
"R-CEL-4608870",
"R-CEL-5099900",
"R-CEL-5140745",
"R-CEL-8856825",
"R-CEL-8856828",
"R-DME-201681",
"R-DME-209387",
"R-DME-209440",
"R-DME-209472",
"R-DME-3238698",
"R-DME-4086398",
"R-DME-4086400",
"R-DME-4608870",... | [
"REACTOME:R-BTA-3238698",
"REACTOME:R-CEL-3238698",
"REACTOME:R-CEL-4086398",
"REACTOME:R-CEL-4086400",
"REACTOME:R-CEL-4608870",
"REACTOME:R-CEL-5099900",
"REACTOME:R-CEL-5140745",
"REACTOME:R-CEL-8856825",
"REACTOME:R-CEL-8856828",
"REACTOME:R-DME-201681",
"REACTOME:R-DME-209387",
"REACTOME:... | 75 | [
"4f0a",
"6ahy",
"7drt",
"7kc4",
"7urd",
"8ctg",
"8tzo",
"8tzp",
"8tzr"
] | 9 | [
"PUB00000724",
"PUB00000872",
"PUB00005515",
"PUB00017903",
"PUB00017904"
] | [
"8471061",
"1617723",
"3076290",
"9425102",
"10656974"
] | [
"In pursuit of the functions of the Wnt family of developmental regulators: insights from Xenopus laevis.",
"Wnt genes.",
"The int genes in mammary tumorigenesis and in normal development.",
"Signal transduction by the Wnt family of ligands.",
"Biochemical interactions in the wnt pathway."
] | [
1993,
1992,
1988,
1998,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Lymphocystis disease virus 4"
] | [
25003,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
47,
13,
48,
44,
61
] | 6 | true | Conserved_site | Wnt protein, conserved site | Wnt protein, conserved site | Wnt_CS | 6 |
IPR018162 | 18,162 | Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily | Ala-tRNA-ligase_IIc_anticod-bd | Homologous_superfamily | 39,138 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000166",
"GO:0004813",
"GO:0005524",
"GO:0006419",
"GO:0005737"
] | [
"nucleotide binding",
"alanine-tRNA ligase activity",
"ATP binding",
"alanyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"SSF"
] | [
"SSF101353"
] | [
""
] | [
39138
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"6.1.1.7",
"R-HSA-379716",
"R-HSA-379726"
] | [
"EC:6.1.1.7",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726"
] | 3 | [
"1riq",
"1yfr",
"1yfs",
"1yft",
"1ygb",
"2ztg",
"2zze",
"2zzf",
"2zzg",
"3htz",
"3hxu",
"3hxv",
"3hxw",
"3hxx",
"3hxy",
"3hxz",
"3hy0",
"3hy1",
"3wqy",
"3wqz",
"4xem",
"4xeo",
"5knn",
"5v59",
"9jc7",
"9jdn"
] | 26 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
950,
27747,
9773,
15,
653
] | 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",... | [
11,
2,
14,
6,
1,
16,
5,
1,
7,
7,
1,
1,
28
] | 13 | true | Homologous_superfamily | Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily | Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily | Ala-tRNA-ligase_IIc_anticod-bd | 5 |
IPR018163 | 18,163 | Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily | Thr/Ala-tRNA-synth_IIc_edit | Homologous_superfamily | 92,217 | false | false | This superfamily represents a structural domain containing a two-layer core α/β structure: α-β(2)-α-β(2). This domain is thought to be a putative editing domain found in the N-terminal part of threonyl-tRNA synthetase (ThrRS), the C-terminal of alanyl-tRNA synthetase (AlaRS), and as the stand-alone hypothetical protein... | [
"GO:0000166"
] | [
"nucleotide binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF55186"
] | [
""
] | [
92217
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383"
] | [
"EC:6.1.1",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276"... | 13 | [
"1nyq",
"1nyr",
"1qf6",
"1tje",
"1tke",
"1tkg",
"1tky",
"1v4p",
"1v7o",
"1wnu",
"1wxo",
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"2zze",
"2zzf",
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"4ce4",
"4v1a",
"5aj4",
"5ool",
"5oom",
"6gaw",
"6gb2",
"6i9r",
"6nu2"... | 114 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
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"PUB00007363",
"PUB00031476",
"PUB00037917",
"PUB00044788",
"PUB00044789",
"PUB00079872",
"PUB00079873"
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"2203971",
"10447505",
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"16374837",
"15079065",
"12554667",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2004,
2006,
2004,
2003,
2000,
2002
] | 13 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2344,
64808,
23537,
10,
1518
] | 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,
5,
13,
13,
2,
32,
25,
3,
13,
31,
3,
2,
47
] | 13 | true | Homologous_superfamily | Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily | Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily | Thr/Ala-tRNA-synth_IIc_edit | 7 |
IPR018164 | 18,164 | Alanyl-tRNA synthetase, class IIc, N-terminal | Ala-tRNA-synth_IIc_N | Domain | 47,769 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000166",
"GO:0004813",
"GO:0005524",
"GO:0006419"
] | [
"nucleotide binding",
"alanine-tRNA ligase activity",
"ATP binding",
"alanyl-tRNA aminoacylation"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF01411"
] | [
"tRNA-synt_2c"
] | [
47769
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"6.1.1.7",
"R-HSA-379716",
"R-HSA-379726"
] | [
"EC:6.1.1.7",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726"
] | 3 | [
"1riq",
"1yfr",
"1yfs",
"1yft",
"1ygb",
"2e1b",
"2ztg",
"2zze",
"2zzf",
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"3wqz",
"4xem",
"4xeo",
"5knn",
"5v59",
"9iuw",
"9jc7",
"9jdn"
] | 28 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
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"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1715,
32021,
13077,
14,
942
] | 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",... | [
19,
2,
13,
7,
1,
19,
7,
2,
11,
7,
1,
1,
50
] | 13 | true | Domain | Alanyl-tRNA synthetase, class IIc, N-terminal | Alanyl-tRNA synthetase, class IIc, N-terminal | Ala-tRNA-synth_IIc_N | 3 |
IPR018165 | 18,165 | Alanyl-tRNA synthetase, class IIc, core domain | Ala-tRNA-synth_IIc_core | Domain | 50,152 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0003676",
"GO:0004813",
"GO:0005524",
"GO:0006419"
] | [
"nucleic acid binding",
"alanine-tRNA ligase activity",
"ATP binding",
"alanyl-tRNA aminoacylation"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PROFILE"
] | [
"PS50860"
] | [
"AA_TRNA_LIGASE_II_ALA"
] | [
50152
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"6.1.1.7",
"R-HSA-379716",
"R-HSA-379726"
] | [
"EC:6.1.1.7",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726"
] | 3 | [
"1riq",
"1yfr",
"1yfs",
"1yft",
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"2e1b",
"2ztg",
"2zze",
"2zzf",
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"3wqz",
"4xem",
"4xeo",
"5knn",
"5v59",
"9iuw",
"9jc7",
"9jdn"
] | 28 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
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"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
1803,
33471,
13889,
12,
977
] | 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",... | [
14,
2,
13,
8,
1,
21,
10,
2,
11,
9,
1,
1,
47
] | 13 | true | Domain | Alanyl-tRNA synthetase, class IIc, core domain | Alanyl-tRNA synthetase, class IIc, core domain | Ala-tRNA-synth_IIc_core | 7 |
IPR018166 | 18,166 | S-adenosylmethionine decarboxylase, conserved site | S-AdoMet_deCO2ase_CS | Conserved_site | 5,898 | false | false | S-adenosylmethionine decarboxylase (AdoMetDC) [ ] catalyses the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines spermidine and spermine from putrescine. The catalytic mechanism of AdoMe... | [
"GO:0004014"
] | [
"adenosylmethionine decarboxylase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01336"
] | [
"ADOMETDC"
] | [
5898
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.50",
"PWY-6834",
"R-BTA-351202",
"R-CEL-351202",
"R-DDI-351202",
"R-DME-351202",
"R-HSA-351202",
"R-MMU-351202",
"R-RNO-351202",
"R-SCE-351202",
"R-SPO-351202"
] | [
"EC:4.1.1.50",
"METACYC:PWY-6834",
"REACTOME:R-BTA-351202",
"REACTOME:R-CEL-351202",
"REACTOME:R-DDI-351202",
"REACTOME:R-DME-351202",
"REACTOME:R-HSA-351202",
"REACTOME:R-MMU-351202",
"REACTOME:R-RNO-351202",
"REACTOME:R-SCE-351202",
"REACTOME:R-SPO-351202"
] | 11 | [
"1jl0"
] | 1 | [
"PUB00006224"
] | [
"10378277"
] | [
"The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
156,
5742
] | 2 | [
"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... | [
13,
1,
1,
2,
3,
3,
1,
10,
4,
1,
1,
14
] | 12 | true | Conserved_site | S-adenosylmethionine decarboxylase, conserved site | S-adenosylmethionine decarboxylase, conserved site | S-AdoMet_deCO2ase_CS | 5 |
IPR018168 | 18,168 | Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site | Ubi_Hdrlase_CS | Conserved_site | 18,468 | false | false | This entry represents FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway [ ]. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions [ ]. In Escherichia coli, three enzyme activities have been descri... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01304"
] | [
"UBIH"
] | [
18468
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.15.45",
"1.14.15.46",
"R-BTA-2142789",
"R-CEL-2142789",
"R-DME-2142789",
"R-DRE-2142789",
"R-HSA-2142789",
"R-MMU-2142789",
"R-RNO-2142789",
"R-SCE-2142789",
"R-SPO-2142789",
"R-XTR-2142789"
] | [
"EC:1.14.15.45",
"EC:1.14.15.46",
"REACTOME:R-BTA-2142789",
"REACTOME:R-CEL-2142789",
"REACTOME:R-DME-2142789",
"REACTOME:R-DRE-2142789",
"REACTOME:R-HSA-2142789",
"REACTOME:R-MMU-2142789",
"REACTOME:R-RNO-2142789",
"REACTOME:R-SCE-2142789",
"REACTOME:R-SPO-2142789",
"REACTOME:R-XTR-2142789"
] | 12 | [
"4k22",
"4n9x"
] | 2 | [
"PUB00013761",
"PUB00013779",
"PUB00013809",
"PUB00013831",
"PUB00013834",
"PUB00013848"
] | [
"1339425",
"365223",
"11153266",
"12721307",
"10802164",
"11583838"
] | [
"Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone.",
"Alternative hydroxylases for the aerobic and anaerobic biosynthesis of ubiquinone in Escherichia coli.",
"Biosynthesis of menaquinone (vitamin K2... | [
1992,
1978,
2001,
2003,
2000,
2001
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
14066,
4275,
127
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
9,
1,
4,
1,
3,
2,
2,
1,
4,
3,
1,
1,
10
] | 13 | true | Conserved_site | Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site | Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site | Ubi_Hdrlase_CS | 6 |
IPR018170 | 18,170 | Aldo/keto reductase, conserved site | Aldo/ket_reductase_CS | Conserved_site | 90,859 | false | false | This entry represents three conserved sites found in members of the aldo/keto reductase family. The third site, located in the C-terminal, is centered on a lysine residue whose chemical modification, in aldose and aldehyde reductases, affect the catalytic efficiency. The aldo-keto reductase family includes a number of ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS00062",
"PS00063",
"PS00798"
] | [
"ALDOKETO_REDUCTASE_2",
"ALDOKETO_REDUCTASE_3",
"ALDOKETO_REDUCTASE_1"
] | [
74641,
43455,
61865
] | 3 | [
"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-156590",
"R-BTA-193368",
"R-BTA-193775",
"R-BTA-193807",
"R-BTA-2162123",
"R-BTA-5365859",
"R-BTA-5661270",
"R-BTA-975634",
"R-BTA-9757110",
"R-DDI-156590",
"R-DDI-193144",
"R-DDI-193368",
"R-DDI-193775",
"R-DDI-193807",
"R-DDI-196108",
"R-DDI-2162123",
"R-DDI-53658... | [
"EC:1.1.1",
"REACTOME:R-BTA-156590",
"REACTOME:R-BTA-193368",
"REACTOME:R-BTA-193775",
"REACTOME:R-BTA-193807",
"REACTOME:R-BTA-2162123",
"REACTOME:R-BTA-5365859",
"REACTOME:R-BTA-5661270",
"REACTOME:R-BTA-975634",
"REACTOME:R-BTA-9757110",
"REACTOME:R-DDI-156590",
"REACTOME:R-DDI-193144",
"... | 113 | [
"1a80",
"1abn",
"1ads",
"1ae4",
"1afs",
"1ah0",
"1ah3",
"1ah4",
"1az1",
"1az2",
"1c9w",
"1cwn",
"1dla",
"1ef3",
"1eko",
"1el3",
"1frb",
"1hqt",
"1hw6",
"1iei",
"1ihi",
"1j96",
"1jez",
"1k8c",
"1lwi",
"1m9h",
"1mar",
"1mi3",
"1mrq",
"1mzr",
"1pwl",
"1pwm"... | 427 | [
"PUB00002548",
"PUB00002605",
"PUB00002751",
"PUB00005156",
"PUB00015049"
] | [
"2498333",
"2105951",
"1447221",
"1621098",
"10884227"
] | [
"The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.",
"Sequence analysis of bovine lens aldose reductase.",
"The crystal structure of the aldose reductase.NADPH binary complex.",
"An unlikely sugar substrate site in the 1.65 A structure of the ... | [
1989,
1990,
1992,
1992,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1642,
40613,
48230,
9,
365
] | 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",... | [
57,
11,
16,
16,
2,
36,
51,
7,
62,
95,
6,
4,
103
] | 13 | true | Conserved_site | Aldo/keto reductase, conserved site | Aldo/keto reductase, conserved site | Aldo/ket_reductase_CS | 2 |
IPR018171 | 18,171 | Peptidyl-tRNA hydrolase, conserved site | Pept_tRNA_hydro_CS | Conserved_site | 29,396 | false | false | This entry represents two conserved regions that each contain an histidine. The first of these regions is located in the N-terminal part of the protein, the other in the central part. Peptidyl-tRNA hydrolase ( ) (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-... | [
"GO:0004045"
] | [
"peptidyl-tRNA hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS01195",
"PS01196"
] | [
"PEPT_TRNA_HYDROL_1",
"PEPT_TRNA_HYDROL_2"
] | [
24060,
25026
] | 2 | [
"EC"
] | [
"3.1.1.29"
] | [
"EC:3.1.1.29"
] | 1 | [
"1ryb",
"1rym",
"1ryn",
"2jrc",
"2lgj",
"2mjl",
"2naf",
"2pth",
"2z2i",
"2z2j",
"2z2k",
"3kjz",
"3kk0",
"3nea",
"3ofv",
"3p2j",
"3tck",
"3tcn",
"3td2",
"3td6",
"3v2i",
"3vjr",
"4dhw",
"4djj",
"4erx",
"4fno",
"4fop",
"4fot",
"4fyj",
"4hoy",
"4iko",
"4jc4"... | 81 | [
"PUB00001213",
"PUB00001861",
"PUB00005030",
"PUB00062567",
"PUB00106491"
] | [
"1833189",
"8635758",
"8563640",
"22923517",
"26508479"
] | [
"Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis.",
"Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of Escherichia coli.",
"New protein functions in yeast chromosome VIII.",
"Structural basis for the substrate recognition and catalysis of peptidyl-tR... | [
1991,
1996,
1995,
2012,
2015
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_66_E06"
] | [
24808,
4084,
1,
502,
1
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"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 (strain ATCC 204508 / S288c)... | [
20,
2,
1,
2,
1,
1,
7,
4,
1,
1,
24
] | 11 | true | Conserved_site | Peptidyl-tRNA hydrolase, conserved site | Peptidyl-tRNA hydrolase, conserved site | Pept_tRNA_hydro_CS | 7 |
IPR018176 | 18,176 | Tryptophanase, conserved site | Tryptophanase_CS | Conserved_site | 1,500 | false | false | Tryptophanase (tryptophan indole-lyase, TNase) ( ) and tyrosine phenol-lyase (TPL) ( ) are related pyridoxal-phosphate dependent homotetrameric enzymes that catalyse the reversible hydrolytic cleavage of L-tryptophan or L-tyrosine to indole or phenol, respectively, and ammonium pyruvate. These two enzymes are very simi... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00853"
] | [
"BETA_ELIM_LYASE"
] | [
1500
] | 1 | [
"EC"
] | [
"4.1.99.1"
] | [
"EC:4.1.99.1"
] | 1 | [
"1ax4",
"1c7g",
"1tpl",
"2c44",
"2ez1",
"2ez2",
"2oqx",
"2tpl",
"2v0y",
"2v1p",
"2vlf",
"2vlh",
"2ycn",
"2ycp",
"2yct",
"2yhk",
"4up2",
"4w1y",
"4w4h",
"5d8g",
"5w19",
"5w1b",
"6dur",
"6dvx",
"6dxv",
"6dyt",
"6dz5",
"6ecg",
"6mls",
"6mme",
"6mo3",
"6mpd"... | 46 | [
"PUB00014799"
] | [
"12686128"
] | [
"Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
40,
1411,
34,
15
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Tryptophanase, conserved site | Tryptophanase, conserved site | Tryptophanase_CS | 7 |
IPR018177 | 18,177 | L-lactate dehydrogenase, active site | L-lactate_DH_AS | Active_site | 15,518 | false | false | NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes functions as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these ac... | [
"GO:0004459"
] | [
"L-lactate dehydrogenase (NAD+) activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00064"
] | [
"L_LDH"
] | [
15518
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.27",
"PWY-5031",
"PWY-5481",
"PWY-6901",
"PWY-8086",
"R-BTA-70268",
"R-BTA-9861718",
"R-CEL-70268",
"R-DME-70268",
"R-DME-9861718",
"R-DRE-70268",
"R-DRE-9861718",
"R-GGA-373920",
"R-GGA-70268",
"R-HSA-70268",
"R-HSA-9861718",
"R-MMU-70268",
"R-MMU-9861718",
"R-RNO-70268",... | [
"EC:1.1.1.27",
"METACYC:PWY-5031",
"METACYC:PWY-5481",
"METACYC:PWY-6901",
"METACYC:PWY-8086",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-9861718",
"REACTOME:R-CEL-70268",
"REACTOME:R-DME-70268",
"REACTOME:R-DME-9861718",
"REACTOME:R-DRE-70268",
"REACTOME:R-DRE-9861718",
"REACTOME:R-GGA-373920"... | 22 | [
"1a5z",
"1ez4",
"1hye",
"1hyg",
"1hyh",
"1i0z",
"1i10",
"1ldb",
"1ldm",
"1ldn",
"1llc",
"1lld",
"1lth",
"1t2f",
"1v6a",
"1y6j",
"2e37",
"2ldb",
"2ldx",
"2v65",
"2v6b",
"2v6m",
"2v7p",
"2x0i",
"2x0j",
"2xxb",
"2xxj",
"2zqy",
"2zqz",
"3d0o",
"3d4p",
"3h3f"... | 146 | [
"PUB00013812"
] | [
"11021970"
] | [
"Analysis and prediction of functional sub-types from protein sequence alignments."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Panine betaherpesvirus 2",
"metagenomes"
] | [
157,
8887,
6438,
1,
35
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (stra... | [
6,
2,
9,
3,
22,
23,
1,
8,
19,
1,
8
] | 11 | true | Active_site | L-lactate dehydrogenase, active site | L-lactate dehydrogenase, active site | L-lactate_DH_AS | 4 |
IPR018181 | 18,181 | Heat shock protein 70, conserved site | Heat_shock_70_CS | Conserved_site | 117,355 | false | false | Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding regio... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS00297",
"PS00329",
"PS01036"
] | [
"HSP70_1",
"HSP70_2",
"HSP70_3"
] | [
78683,
94080,
95354
] | 3 | [
"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-3371453",
"R-BTA-3371497",
"R-BTA-3371568",
"R-BTA-3371571",
"R-BTA-450408",
"R-BTA-6798695",
"R-BTA-6799198",
"R-BTA-72163",
"R-BTA-8856828",
"R-BTA-8876725",
"R-BTA-888590",
"R-BTA-983170",
"R-BTA-9833482",
"R-BTA-9837999",
"R-BTA-9841251",
"R-BTA-9865881",
"R-BTA-9909505",
... | [
"REACTOME:R-BTA-3371453",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-3371568",
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-450408",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6799198",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-8876725",
"REACTOME:R-BTA-888590",
"REACTOME:R-... | 163 | [
"1atr",
"1ats",
"1ba0",
"1ba1",
"1bup",
"1dkg",
"1hjo",
"1hpm",
"1hx1",
"1kax",
"1kay",
"1kaz",
"1nga",
"1ngb",
"1ngc",
"1ngd",
"1nge",
"1ngf",
"1ngg",
"1ngh",
"1ngi",
"1ngj",
"1qqm",
"1qqn",
"1qqo",
"1s3x",
"1xqs",
"1yuw",
"2bup",
"2e88",
"2e8a",
"2kho"... | 257 | [
"PUB00000712",
"PUB00000809",
"PUB00000958",
"PUB00001766",
"PUB00004019",
"PUB00004070"
] | [
"2686623",
"2944601",
"9476895",
"2841196",
"3282176",
"2143562"
] | [
"Essential roles of 70kDa heat inducible proteins.",
"Speculations on the functions of the major heat shock and glucose-regulated proteins.",
"The Hsp70 and Hsp60 chaperone machines.",
"The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization.",
"Heat-shock proteins. Coming in from... | [
1989,
1986,
1998,
1988,
1988,
1990
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
850,
54819,
60007,
621,
1058
] | 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",... | [
53,
12,
23,
30,
5,
125,
60,
5,
79,
49,
13,
7,
150
] | 13 | true | Conserved_site | Heat shock protein 70, conserved site | Heat shock protein 70, conserved site | Heat_shock_70_CS | 9 |
IPR018185 | 18,185 | Gas vesicle C repeat | Gas_vesicle_C_repeat | Repeat | 147 | false | false | Gas vesicles are small, hollow, gas filled protein structures found in several cyanobacterial and archaebacterial microorganisms [ ]. They allow the positioning of the bacteria at the favorable depth for growth. Gas vesicles are hollow cylindrical tubes, closed by a hollow, conical cap at each end. Both the conical end... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00235"
] | [
"GAS_VESICLE_C"
] | [
147
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000481"
] | [
"2513809"
] | [
"Gas vesicle proteins."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Cyanophyceae"
] | [
147
] | 1 | [] | [] | 0 | true | Repeat | Gas vesicle C repeat | Gas vesicle C repeat | Gas_vesicle_C_repeat | 8 |
IPR018186 | 18,186 | Transcription factor, T-box, conserved site | TF_T-box_CS | Conserved_site | 20,309 | false | false | Transcription factors of the T-box family are required both for early cell-fate decisions, such as those necessary for formation of the basic vertebrate body plan, for differentiation and organogenesis [ ] and also have been associated to multiple aspects of development and in adult terminal cell-type differentiation i... | [
"GO:0003700",
"GO:0006355",
"GO:0005634"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS01264",
"PS01283"
] | [
"TBOX_2",
"TBOX_1"
] | [
17947,
16644
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-2032785",
"R-CEL-9856649",
"R-DME-9856649",
"R-DRE-2032785",
"R-GGA-2032785",
"R-HSA-2032785",
"R-HSA-5578768",
"R-HSA-8953750",
"R-HSA-9733709",
"R-HSA-9754189",
"R-HSA-9758919",
"R-HSA-9793380",
"R-HSA-9796292",
"R-HSA-9823730",
"R-HSA-9824272",
"R-HSA-9825892",
"R-HSA-98278... | [
"REACTOME:R-CEL-2032785",
"REACTOME:R-CEL-9856649",
"REACTOME:R-DME-9856649",
"REACTOME:R-DRE-2032785",
"REACTOME:R-GGA-2032785",
"REACTOME:R-HSA-2032785",
"REACTOME:R-HSA-5578768",
"REACTOME:R-HSA-8953750",
"REACTOME:R-HSA-9733709",
"REACTOME:R-HSA-9754189",
"REACTOME:R-HSA-9758919",
"REACTOM... | 24 | [
"1h6f",
"1xbr",
"2x6u",
"2x6v",
"4a04",
"4s0h",
"5bqd",
"5flv",
"5qrf",
"5qrg",
"5qrh",
"5qri",
"5qrj",
"5qrk",
"5qrl",
"5qrm",
"5qrn",
"5qro",
"5qrp",
"5qrq",
"5qrr",
"5qrs",
"5qrt",
"5qru",
"5qrv",
"5qrw",
"5qrx",
"5qry",
"5qrz",
"5qs0",
"5qs1",
"5qs2"... | 65 | [
"PUB00000739",
"PUB00001985",
"PUB00003895",
"PUB00004265",
"PUB00005531",
"PUB00006158",
"PUB00007157",
"PUB00099960",
"PUB00099961"
] | [
"9504043",
"9503012",
"7920656",
"9349824",
"9196325",
"9395282",
"12093383",
"29726930",
"28057261"
] | [
"The T-box gene family.",
"A combined analysis of genomic and primary protein structure defines the phylogenetic relationship of new members if the T-box family.",
"An ancient family of embryonically expressed mouse genes sharing a conserved protein motif with the T locus.",
"Crystallographic structure of the... | [
1998,
1998,
1994,
1997,
1997,
1997,
2002,
2018,
2017
] | 9 | [] | [] | 0 | 0 | null | [
"Cohnella phaseoli",
"Opisthokonta",
"bird metagenome"
] | [
1,
20307,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
99,
20,
47,
47,
52
] | 6 | true | Conserved_site | Transcription factor, T-box, conserved site | Transcription factor, T-box, conserved site | TF_T-box_CS | 1 |
IPR018187 | 18,187 | Asp/Glu racemase, active site 1 | Asp/Glu_racemase_AS_1 | Active_site | 25,161 | false | false | Aspartate racemase ( ) and glutamate racemase ( ) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity [ ]. Glutamate racemase, which interconverts L-glutamate into D-glutamate, is required for the biosynthesis of peptidoglycan and some peptide-based antibiotics such ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00923"
] | [
"ASP_GLU_RACEMASE_1"
] | [
25161
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"5.1.1.3",
"PWY-6386",
"PWY-6387"
] | [
"EC:5.1.1.3",
"METACYC:PWY-6386",
"METACYC:PWY-6387"
] | 3 | [
"1b73",
"1b74",
"1jfl",
"1zuw",
"2gzm",
"2jfn",
"2jfo",
"2jfp",
"2jfq",
"2jfu",
"2jfv",
"2jfw",
"2jfx",
"2jfy",
"2jfz",
"2vvt",
"2w4i",
"3hfr",
"3ist",
"3isv",
"3ojc",
"3s7z",
"3s81",
"3uhf",
"3uho",
"3uhp",
"4b1f",
"5ell",
"5elm",
"5evc",
"5hj7",
"5hqt"... | 42 | [
"PUB00000380"
] | [
"8385993"
] | [
"Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctjdk2",
"metagenomes"
] | [
69,
24620,
120,
1,
351
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Active_site | Asp/Glu racemase, active site 1 | Asp/Glu racemase, active site 1 | Asp/Glu_racemase_AS_1 | 6 |
IPR018188 | 18,188 | Ribonuclease T2, His active site 1 | RNase_T2_His_AS_1 | Active_site | 13,407 | false | false | The fungal ribonucleases T2 from Aspergillus oryzae, M from Aspergillus saitoi and Rh from Rhizopeus niveus are structurally and functionally related 30 Kd glycoproteins [ ] that cleave the 3'-5' internucleotide linkage of RNA via a nucleotide 2',3'-cyclic phosphate intermediates ( ). Two histidines residues have been ... | [
"GO:0003723",
"GO:0033897"
] | [
"RNA binding",
"ribonuclease T2 activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00530"
] | [
"RNASE_T2_1"
] | [
13407
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.6.1.19",
"R-CEL-6798695",
"R-DDI-6798695",
"R-DRE-6798695",
"R-HSA-6798695",
"R-MMU-6798695",
"R-SCE-6798695"
] | [
"EC:4.6.1.19",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DRE-6798695",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695",
"REACTOME:R-SCE-6798695"
] | 7 | [
"1bk7",
"1bol",
"1dix",
"1ioo",
"1iqq",
"1iyb",
"1j1f",
"1j1g",
"1uca",
"1ucc",
"1ucd",
"1ucg",
"1v9h",
"1vcz",
"1vd1",
"1vd3",
"2ea1",
"2pqx",
"2pqy",
"2z70",
"3d3z",
"3t0o",
"3tbj"
] | 23 | [
"PUB00001381",
"PUB00001640",
"PUB00002342"
] | [
"2298207",
"1633875",
"2229029"
] | [
"Identification of two essential histidine residues of ribonuclease T2 from Aspergillus oryzae.",
"Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus.",
"Primary structure of a base non-specific and adenylic acid preferential ribonuclease from Aspergillus sai... | [
1990,
1992,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
4316,
9052,
6,
33
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"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 ... | [
24,
1,
7,
1,
7,
3,
1,
18,
5,
1,
20
] | 11 | true | Active_site | Ribonuclease T2, His active site 1 | Ribonuclease T2, His active site 1 | RNase_T2_His_AS_1 | 7 |
IPR018189 | 18,189 | Phosphoglucose isomerase, conserved site | Phosphoglucose_isomerase_CS | Conserved_site | 32,428 | false | false | Phosphoglucose isomerase ( ) (PGI) [ , ] is a dimeric enzyme that catalyses the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. PGI is involved in different pathways: in most higher organisms it is involved in glycolysis; in mammals it is involved in gluconeogenesis; in plants in carbohydrate ... | [
"GO:0004347",
"GO:0006094",
"GO:0006096"
] | [
"glucose-6-phosphate isomerase activity",
"gluconeogenesis",
"glycolytic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00174",
"PS00765"
] | [
"P_GLUCOSE_ISOMERASE_2",
"P_GLUCOSE_ISOMERASE_1"
] | [
29930,
27946
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.3.1.9",
"PWY-3801",
"PWY-5054",
"PWY-5384",
"PWY-5514",
"PWY-5659",
"PWY-6142",
"PWY-621",
"PWY-622",
"PWY-6981",
"PWY-6992",
"PWY-7238",
"PWY-7347",
"PWY-7385",
"PWY-8013",
"R-BTA-5628897",
"R-BTA-6798695",
"R-BTA-70171",
"R-BTA-70263",
"R-DDI-5628897",
"R-DDI-6798695",
... | [
"EC:5.3.1.9",
"METACYC:PWY-3801",
"METACYC:PWY-5054",
"METACYC:PWY-5384",
"METACYC:PWY-5514",
"METACYC:PWY-5659",
"METACYC:PWY-6142",
"METACYC:PWY-621",
"METACYC:PWY-622",
"METACYC:PWY-6981",
"METACYC:PWY-6992",
"METACYC:PWY-7238",
"METACYC:PWY-7347",
"METACYC:PWY-7385",
"METACYC:PWY-801... | 51 | [
"1b0z",
"1c7q",
"1c7r",
"1dqr",
"1g98",
"1gzd",
"1gzv",
"1hm5",
"1hox",
"1iat",
"1iri",
"1jiq",
"1jlh",
"1koj",
"1n8t",
"1nuh",
"1q50",
"1t10",
"1u0e",
"1u0f",
"1u0g",
"1xtb",
"1zzg",
"2cvp",
"2cxn",
"2cxo",
"2cxp",
"2cxq",
"2cxr",
"2cxs",
"2cxt",
"2cxu"... | 76 | [
"PUB00003422",
"PUB00004511",
"PUB00006445",
"PUB00006471",
"PUB00011130"
] | [
"1593646",
"6115414",
"10318897",
"10653639",
"10770936"
] | [
"Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase.",
"Glucose-6-phosphate isomerase.",
"The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.",
"Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that mo... | [
1992,
1981,
1999,
2000,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
348,
24251,
7487,
342
] | 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",... | [
8,
2,
5,
1,
1,
6,
2,
1,
13,
4,
1,
1,
18
] | 13 | true | Conserved_site | Phosphoglucose isomerase, conserved site | Phosphoglucose isomerase, conserved site | Phosphoglucose_isomerase_CS | 2 |
IPR018191 | 18,191 | 4-oxalocrotonate tautomerase | 4-OT | Family | 5,851 | false | false | This entry represents 4-Oxalocrotonate tautomerase (4-OT, also known as 2-hydroxymuconate tautomerase) from bacteria and some archaeal species. It is an enzyme that converts 2-hydroxymuconate to the α-β-unsaturated ketone, 2-oxo-3-hexenedioate [ ]. This enzyme forms part of a bacterial metabolic pathway that oxidativel... | [
"GO:0016853"
] | [
"isomerase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00013",
"cd00491"
] | [
"taut",
"4Oxalocrotonate_Tautomerase"
] | [
5850,
1594
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"5.3.2.-",
"GenProp0708",
"PWY-5642",
"PWY-6550"
] | [
"EC:5.3.2.-",
"GP:GenProp0708",
"METACYC:PWY-5642",
"METACYC:PWY-6550"
] | 4 | [
"1bjp",
"1otf",
"2fm7",
"2op8",
"2opa",
"2orm",
"2x4k",
"3m20",
"3m21",
"4faz",
"4fdx",
"4ota",
"4otb",
"4otc",
"4x19",
"4x1c",
"5cln",
"5clo",
"5tig",
"6bgn",
"6fps",
"6ghw",
"6ogm",
"7puo",
"7xuy"
] | 25 | [
"PUB00007676",
"PUB00019310",
"PUB00066780"
] | [
"12051677",
"8547259",
"1339435"
] | [
"The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a beta-alpha-beta structural motif.",
"Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases.",
"4-Oxalocrotonate tautomerase, an enzyme composed of 6... | [
2002,
1996,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Opisthokonta",
"Sym plasmid",
"unclassified sequences"
] | [
35,
5751,
4,
1,
60
] | 5 | [] | [] | 0 | true | Family | 4-oxalocrotonate tautomerase | 4-oxalocrotonate tautomerase | 4-OT | 2 |
IPR018192 | 18,192 | Small ribosomal subunit protein uS5, N-terminal, conserved site | Ribosomal_uS5_N_CS | Conserved_site | 33,203 | false | false | Ribosomal protein uS5 is one of the proteins from the small ribosomal subunit, and is a protein of 166 to 254 amino-acid residues. In Escherichia coli, S5 is known to be important in the assembly and function of the 30S ribosomal subunit. Mutations in S5 have been shown to increase translational error frequencies. It b... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00585"
] | [
"RIBOSOMAL_S5"
] | [
33203
] | 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-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-6791226",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CEL-9937383",
"R-DDI-156827",
"R-DDI-... | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-6791226",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL... | 115 | [
"1dv4",
"1eg0",
"1fjg",
"1fka",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1pkp",
"1qd7",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo"... | 1,812 | [
"PUB00003665"
] | [
"2247072"
] | [
"Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
832,
21919,
10076,
376
] | 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",... | [
23,
2,
1,
3,
1,
13,
13,
1,
8,
19,
2,
2,
17
] | 13 | true | Conserved_site | Small ribosomal subunit protein uS5, N-terminal, conserved site | Small ribosomal subunit protein uS5, N-terminal, conserved site | Ribosomal_uS5_N_CS | 3 |
IPR018193 | 18,193 | Glycerate kinase, flavodoxin-like fold | Glyc_kinase_flavodox-like_fold | Homologous_superfamily | 20,404 | false | false | Proteins in this entry include glycerate kinase 2 ( ), which catalyses the phosphorylation of (R)-glycerate to 3-phospho-(R)-glycerate in the presence of ATP. These proteins consist of two different α/β domains: domain 1 has a flavodoxin-like fold, while domain 2 has a restriction enzyme-like fold (domain 2 is inserted... | [
"GO:0008887",
"GO:0031388"
] | [
"glycerate kinase activity",
"organic acid phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.1510.10"
] | [
""
] | [
20404
] | 1 | [] | [] | [] | 0 | [
"1to6",
"3cwc"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"unclassified sequences"
] | [
19653,
501,
1,
249
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Homologous_superfamily | Glycerate kinase, flavodoxin-like fold | Glycerate kinase, flavodoxin-like fold | Glyc_kinase_flavodox-like_fold | 1 |
IPR018194 | 18,194 | Nickel-dependent hydrogenase, large subunit, nickel binding site | Ni-dep_hyd_lsu_Ni_BS | Binding_site | 9,769 | false | false | Hydrogenases are enzymes that catalyse the reversible oxidation of hydrogen and are important in anaerobic metabolism. There are various types of metal-containing hydrogenases and can be broadly divided into three groups: Fe ('iron only') hydrogenases; Ni-Fe hydrogenases; and Ni-Fe-Se hydrogenases [ ]. The [NiFe] and [... | [
"GO:0008901",
"GO:0016151"
] | [
"ferredoxin hydrogenase activity",
"nickel cation binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00507",
"PS00508"
] | [
"NI_HGENASE_L_1",
"NI_HGENASE_L_2"
] | [
7725,
7276
] | 2 | [
"EC"
] | [
"1.12.99"
] | [
"EC:1.12.99"
] | 1 | [
"1cc1",
"1e3d",
"1frf",
"1frv",
"1h2a",
"1h2r",
"1ubh",
"1ubj",
"1ubk",
"1ubl",
"1ubm",
"1ubo",
"1ubr",
"1ubt",
"1ubu",
"1wuh",
"1wui",
"1wuj",
"1wuk",
"1wul",
"1yq9",
"1yqw",
"1yrq",
"2frv",
"2wpn",
"3ayx",
"3ayz",
"3cur",
"3cus",
"3h3x",
"3myr",
"3rgw"... | 173 | [
"PUB00001739",
"PUB00002102",
"PUB00004672",
"PUB00020978",
"PUB00099872"
] | [
"3078655",
"2180913",
"2521386",
"7854413",
"24778258"
] | [
"The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio.",
"Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames.",
"Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases... | [
1988,
1990,
1989,
1995,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1129,
8372,
22,
246
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Binding_site | Nickel-dependent hydrogenase, large subunit, nickel binding site | Nickel-dependent hydrogenase, large subunit, nickel binding site | Ni-dep_hyd_lsu_Ni_BS | 5 |
IPR018195 | 18,195 | Transferrin family, iron binding site | Transferrin_Fe_BS | Binding_site | 4,388 | false | false | Transferrins are a family of eukaryotic iron-binding glycoproteins that share the common function of controlling the level of free iron in biological fluids [ ]. The transferrin family currently includes: Blood serotransferrin (siderophilin). Milk lactotransferrin (lactoferrin). Egg white ovotransferrin (conalbumin). M... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS00205",
"PS00206",
"PS00207"
] | [
"TRANSFERRIN_LIKE_1",
"TRANSFERRIN_LIKE_2",
"TRANSFERRIN_LIKE_3"
] | [
3789,
3727,
3008
] | 3 | [
"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-6798695",
"R-BTA-6799990",
"R-BTA-6803157",
"R-DME-114608",
"R-DME-381426",
"R-DME-6798695",
"R-DME-6799990",
"R-DME-8957275",
"R-DME-917937",
"R-HSA-114608",
"R-HSA-1222449",
"R-HSA-163125",
"R-HSA-381426",
"R-HSA-6798695",
"R-HSA-6799990",
"R-HSA-6803157",
"R-HSA-8856825",
... | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6799990",
"REACTOME:R-BTA-6803157",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-381426",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-6799990",
"REACTOME:R-DME-8957275",
"REACTOME:R-DME-917937",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-1222449",
"REACTOME:R-... | 47 | [
"1a8e",
"1a8f",
"1aiv",
"1aov",
"1b0l",
"1b1x",
"1b3e",
"1b7u",
"1b7z",
"1biy",
"1bka",
"1blf",
"1bp5",
"1btj",
"1cb6",
"1ce2",
"1d3k",
"1d4n",
"1dot",
"1dsn",
"1dtg",
"1dtz",
"1eh3",
"1f9b",
"1fck",
"1fqe",
"1fqf",
"1gv8",
"1gvc",
"1h43",
"1h44",
"1h45"... | 195 | [
"PUB00001349",
"PUB00003252"
] | [
"3032619",
"2585506"
] | [
"Iron transport and storage.",
"Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 A resolution."
] | [
1987,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"gut metagenome"
] | [
7,
4378,
2,
1
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
7,
32,
19,
23
] | 5 | true | Binding_site | Transferrin family, iron binding site | Transferrin family, iron binding site | Transferrin_Fe_BS | 3 |
IPR018197 | 18,197 | Glycerate kinase, restriction-enzyme-like fold | Glycerate_kinase_RE-like | Homologous_superfamily | 19,878 | false | false | Glycerate kinase 2 ( ) catalyses the phosphorylation of (R)-glycerate to 3-phospho-(R)-glycerate in the presence of ATP. These proteins consist of two different α/β domains: domain 1 has a flavodoxin-like fold, while domain 2 has a restriction enzyme-like fold (domain 2 is inserted into domain 1). | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.50.10350"
] | [
""
] | [
19878
] | 1 | [] | [] | [] | 0 | [
"1to6",
"3cwc"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"metagenomes"
] | [
19184,
486,
1,
207
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Homologous_superfamily | Glycerate kinase, restriction-enzyme-like fold | Glycerate kinase, restriction-enzyme-like fold | Glycerate_kinase_RE-like | 4 |
IPR018199 | 18,199 | Small ribosomal subunit protein eS4, N-terminal, conserved site | Ribosomal_eS4_N_CS | Conserved_site | 5,648 | false | false | A number of eukaryotic and archaeal ribosomal proteins can be grouped on the basis of sequence similarities. One of these families includes small ribosomal subunit protein eS4 from archaea and eukaryotes. Small ribosomal subunit protein eS4A from yeast is also known as S7/YS6; archaeal members are also known as S4e; an... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00528"
] | [
"RIBOSOMAL_S4E"
] | [
5648
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R-CEL-975956",
... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-179933... | 115 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r"... | 587 | [
"PUB00000844",
"PUB00080279"
] | [
"2124517",
"24524803"
] | [
"Homologous ribosomal protein genes on the human X and Y chromosomes: escape from X inactivation and possible implications for Turner syndrome.",
"A new system for naming ribosomal proteins."
] | [
1990,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Pseudomonadota",
"ecological metagenomes"
] | [
539,
5104,
3,
2
] | 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... | [
11,
1,
1,
2,
10,
4,
1,
8,
7,
2,
3,
19
] | 12 | true | Conserved_site | Small ribosomal subunit protein eS4, N-terminal, conserved site | Small ribosomal subunit protein eS4, N-terminal, conserved site | Ribosomal_eS4_N_CS | 3 |
IPR018200 | 18,200 | Ubiquitin specific protease, conserved site | USP_CS | Conserved_site | 130,036 | false | false | Protein ubiquitination is a reversible posttranslational modification that affects a large number of cellular processes, including protein degradation, trafficking, cell signalling, and the DNA damage response. Ubiquitination is reversible, and dedicated deubiquitinases exist that hydrolyse isopeptide bonds. Ubiquitin-... | [
"GO:0004843"
] | [
"cysteine-type deubiquitinase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00972",
"PS00973"
] | [
"USP_1",
"USP_2"
] | [
106689,
112634
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.19.12",
"R-BTA-168638",
"R-BTA-5357786",
"R-BTA-5357905",
"R-BTA-5357956",
"R-BTA-5689880",
"R-BTA-8948751",
"R-BTA-9010553",
"R-BTA-936440",
"R-BTA-9758274",
"R-CEL-1169408",
"R-CEL-5689880",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-8866652",
"R-CEL-8948747",
... | [
"EC:3.4.19.12",
"REACTOME:R-BTA-168638",
"REACTOME:R-BTA-5357786",
"REACTOME:R-BTA-5357905",
"REACTOME:R-BTA-5357956",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8948751",
"REACTOME:R-BTA-9010553",
"REACTOME:R-BTA-936440",
"REACTOME:R-BTA-9758274",
"REACTOME:R-CEL-1169408",
"REACTOME:R-CEL-5689... | 149 | [
"1nb8",
"1nbf",
"1vjv",
"2ayn",
"2ayo",
"2f1z",
"2gfo",
"2hd5",
"2ibi",
"2vhf",
"2y5b",
"2y6e",
"3i3t",
"3ihp",
"3m99",
"3mhh",
"3mhs",
"3mtn",
"3n3k",
"3nhe",
"3v6c",
"3v6e",
"4fip",
"4fjc",
"4fk5",
"4m5w",
"4m5x",
"4w4u",
"4wa6",
"4zux",
"5a5b",
"5cht"... | 179 | [
"PUB00003577",
"PUB00072483"
] | [
"7845226",
"19734957"
] | [
"Families of cysteine peptidases.",
"Dissection of USP catalytic domains reveals five common insertion points."
] | [
1994,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
47,
129654,
116,
219
] | 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... | [
128,
44,
224,
41,
228,
150,
13,
116,
202,
16,
14,
319
] | 12 | true | Conserved_site | Ubiquitin specific protease, conserved site | Ubiquitin specific protease, conserved site | USP_CS | 3 |
IPR018201 | 18,201 | Beta-ketoacyl synthase, active site | Ketoacyl_synth_AS | Active_site | 113,871 | false | false | This entry represents the active site of beta-ketoacyl synthases from bacteria and eukaryotes. Fatty acid synthases (FASs) and polyketide synthases (PKSs) are closely related and have a common evolutionary history. FASs and PKSs share a similar enzymatic domain structure in which acyl transferase (AT), ketosynthase (KS... | [
"GO:0004315",
"GO:0006633"
] | [
"3-oxoacyl-[acyl-carrier-protein] synthase activity",
"fatty acid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00606"
] | [
"KS3_1"
] | [
113871
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"2.3.1",
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
... | [
"EC:2.3.1",
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"... | 235 | [
"1b3n",
"1dd8",
"1e5m",
"1fj4",
"1fj8",
"1g5x",
"1h4f",
"1j3n",
"1kas",
"1ox0",
"1oxh",
"1tqy",
"1w0i",
"2alm",
"2aq7",
"2aqb",
"2buh",
"2bui",
"2byw",
"2byx",
"2byy",
"2byz",
"2bz3",
"2bz4",
"2c9h",
"2cdh",
"2gfw",
"2gfy",
"2gqd",
"2hg4",
"2iwy",
"2iwz"... | 190 | [
"PUB00000791",
"PUB00001171",
"PUB00001385",
"PUB00001394",
"PUB00019762",
"PUB00103749",
"PUB00103750",
"PUB00103751",
"PUB00103752"
] | [
"3076376",
"2583128",
"2209605",
"2050137",
"9482715",
"21830247",
"26784357",
"30007436",
"23249187"
] | [
"beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue.",
"Structure and deduced function of the granaticin-producing polyketide synthase gene cluster of Streptomyces violaceoruber Tu22.",
"The multifunctional 6-methylsalicylic... | [
1988,
1989,
1990,
1991,
1998,
2011,
2016,
2018,
2013
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
28,
82470,
30571,
802
] | 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",... | [
13,
5,
11,
9,
2,
5,
6,
9,
12,
4,
2,
1,
37
] | 13 | true | Active_site | Beta-ketoacyl synthase, active site | Beta-ketoacyl synthase, active site | Ketoacyl_synth_AS | 2 |
IPR018202 | 18,202 | Serine carboxypeptidase, serine active site | Ser_caboxypep_ser_AS | Active_site | 37,704 | false | false | All known carboxypeptidases are either metallo carboxypeptidases or serine carboxypeptidases ( and ). The catalytic activity of the serine carboxypeptidases, like that of the trypsin family serine proteases, is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which is... | [
"GO:0004185"
] | [
"serine-type carboxypeptidase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00131"
] | [
"CARBOXYPEPT_SER_SER"
] | [
37704
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.16",
"R-CEL-2132295",
"R-CEL-6798695",
"R-HSA-2132295",
"R-HSA-4085001",
"R-HSA-4341670",
"R-HSA-6798695",
"R-HSA-9840310",
"R-MMU-2132295",
"R-MMU-4085001",
"R-MMU-6798695",
"R-MMU-9840310"
] | [
"EC:3.4.16",
"REACTOME:R-CEL-2132295",
"REACTOME:R-CEL-6798695",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-4085001",
"REACTOME:R-HSA-4341670",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9840310",
"REACTOME:R-MMU-2132295",
"REACTOME:R-MMU-4085001",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-98403... | 12 | [
"1ac5",
"1bcr",
"1bcs",
"1ivy",
"1whs",
"1wht",
"1wpx",
"1ysc",
"3sc2",
"4az0",
"4az3",
"4ci9",
"4cia",
"4cib",
"4mws",
"4mwt",
"6wia",
"7kdv"
] | 18 | [
"PUB00000792",
"PUB00001667",
"PUB00002027",
"PUB00002615",
"PUB00002648",
"PUB00003678",
"PUB00004727",
"PUB00094584"
] | [
"2639682",
"8224168",
"1587609",
"2324088",
"1907282",
"1549128",
"1961751",
"12967708"
] | [
"Primary structure of carboxypeptidase III from malted barley.",
"The primary structure of carboxypeptidase S1 from Penicillium janthinellum.",
"Cloning and characterization of transcripts showing virulence-related gene expression in Naegleria fowleri.",
"Structure of wheat serine carboxypeptidase II at 3.5-A... | [
1989,
1993,
1992,
1990,
1991,
1992,
1991,
2003
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cafeteriavirus-dependent mavirus",
"Eukaryota",
"Methanomicrobia",
"metagenomes"
] | [
1288,
1,
36395,
4,
16
] | 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... | [
137,
8,
3,
5,
25,
10,
4,
111,
18,
3,
2,
210
] | 12 | true | Active_site | Serine carboxypeptidase, serine active site | Serine carboxypeptidase, serine active site | Ser_caboxypep_ser_AS | 4 |
IPR018203 | 18,203 | GDP dissociation inhibitor | GDP_dissociation_inhibitor | Family | 14,094 | false | false | null | [
"GO:0005092",
"GO:0007264"
] | [
"GDP-dissociation inhibitor activity",
"small GTPase-mediated signal transduction"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00996",
"PR00891",
"PTHR11787"
] | [
"GDI",
"RABGDIREP",
""
] | [
13111,
13083,
13442
] | 3 | [
"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-8876198",
"R-CEL-6803205",
"R-CEL-8873719",
"R-CEL-8876198",
"R-DME-6803205",
"R-DME-8873719",
"R-DME-8876198",
"R-HSA-6798695",
"R-HSA-6803205",
"R-HSA-8873719",
"R-HSA-8876198",
"R-MMU-6798695",
"R-MMU-6803205",
"R-MMU-8873719",
"R-MMU-8876198",
"R-RNO-6798695",
"R-RNO-68032... | [
"REACTOME:R-BTA-8876198",
"REACTOME:R-CEL-6803205",
"REACTOME:R-CEL-8873719",
"REACTOME:R-CEL-8876198",
"REACTOME:R-DME-6803205",
"REACTOME:R-DME-8873719",
"REACTOME:R-DME-8876198",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6803205",
"REACTOME:R-HSA-8873719",
"REACTOME:R-HSA-8876198",
"REACTOM... | 27 | [
"1d5t",
"1gnd",
"1ltx",
"1lv0",
"1ukv",
"1vg0",
"1vg9",
"2bcg",
"3cph",
"3cpi",
"3cpj",
"3p1w",
"6c87"
] | 13 | [
"PUB00000785",
"PUB00001266",
"PUB00004235"
] | [
"7585614",
"7957092",
"8609986"
] | [
"Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens.",
"Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes.",
"Structure and mutational analysis of Rab GDP-dissociation ... | [
1995,
1994,
1996
] | 3 | [] | [
"IPR000806",
"IPR001738",
"IPR017230"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Thermococcus sibiricus (strain DSM 12597 / MM 739)",
"metagenomes"
] | [
326,
13757,
1,
10
] | 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... | [
14,
4,
7,
3,
23,
19,
2,
14,
23,
2,
2,
84
] | 12 | true | Family | GDP dissociation inhibitor | GDP dissociation inhibitor | GDP_dissociation_inhibitor | 8 |
IPR018204 | 18,204 | Tryptophan synthase, alpha chain, active site | Trp_synthase_alpha_AS | Active_site | 25,200 | false | false | Tryptophan synthase ( ) catalyses the last step in the biosynthesis of tryptophan: the conversion of indoleglycerol phosphate and serine, to tryptophan and glyceraldehyde 3-phosphate [ , ]. Tryptophan synthetase has two functional domains: the alpha chain for the aldol cleavage of indoleglycerol phosphate to indole and... | [
"GO:0004834"
] | [
"tryptophan synthase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00167"
] | [
"TRP_SYNTHASE_ALPHA"
] | [
25200
] | 1 | [
"EC"
] | [
"4.2.1.20"
] | [
"EC:4.2.1.20"
] | 1 | [
"1a50",
"1a5s",
"1bks",
"1c29",
"1c8v",
"1c9d",
"1cw2",
"1cx9",
"1fuy",
"1geq",
"1k3u",
"1k7e",
"1k7f",
"1k7x",
"1k8x",
"1k8y",
"1k8z",
"1kfb",
"1kfc",
"1kfe",
"1kfj",
"1kfk",
"1qop",
"1qoq",
"1rd5",
"1tjp",
"1tjr",
"1ttp",
"1ttq",
"1ubs",
"1ujp",
"1v7y"... | 173 | [
"PUB00000116",
"PUB00000769",
"PUB00004683",
"PUB00014824"
] | [
"2679363",
"1366510",
"2734310",
"2521855"
] | [
"Evolution of a biosynthetic pathway: the tryptophan paradigm.",
"The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.",
"A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana.",
"Nucleotide sequence of the N... | [
1989,
1990,
1989,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
685,
20932,
3124,
459
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
8,
1,
1,
7,
1,
1,
37
] | 7 | true | Active_site | Tryptophan synthase, alpha chain, active site | Tryptophan synthase, alpha chain, active site | Trp_synthase_alpha_AS | 6 |
IPR018206 | 18,206 | Electron transfer flavoprotein subunit alpha, conserved site | ETF_asu_C_CS | Conserved_site | 22,497 | false | false | This entry represents the conserved site of the C-terminal domain of the alpha subunit of both Group I and Group II electron transfer flavoproteins. Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They ca... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00696"
] | [
"ETF_ALPHA"
] | [
22497
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-611105",
"R-DDI-611105",
"R-HSA-611105",
"R-MMU-611105",
"R-RNO-611105",
"R-SCE-611105",
"R-SPO-611105"
] | [
"REACTOME:R-CEL-611105",
"REACTOME:R-DDI-611105",
"REACTOME:R-HSA-611105",
"REACTOME:R-MMU-611105",
"REACTOME:R-RNO-611105",
"REACTOME:R-SCE-611105",
"REACTOME:R-SPO-611105"
] | 7 | [
"1efp",
"1efv",
"1o94",
"1o95",
"1o96",
"1o97",
"1t9g",
"2a1t",
"2a1u",
"3clr",
"3cls",
"3clt",
"3clu",
"5ol2"
] | 14 | [
"PUB00004879",
"PUB00004936",
"PUB00005086",
"PUB00024527",
"PUB00033231",
"PUB00033232"
] | [
"8962055",
"2326318",
"8525056",
"10026281",
"8599534",
"12567183"
] | [
"Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.",
"Biosynthesis, molecular cloning and sequencing of electron transfer flavoprotein.",
"Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF-alpha and ETF-beta.",
"Crystal structure... | [
1996,
1990,
1995,
1999,
1996,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
278,
18366,
3578,
275
] | 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",... | [
2,
1,
1,
2,
2,
11,
1,
1,
1,
4,
1,
1,
3
] | 13 | true | Conserved_site | Electron transfer flavoprotein subunit alpha, conserved site | Electron transfer flavoprotein subunit alpha, conserved site | ETF_asu_C_CS | 5 |
IPR018207 | 18,207 | Haem oxygenase conserved site | Haem_oxygenase_CS | Conserved_site | 3,132 | false | false | Haem oxygenase ( ) (HO) [ ] is the microsomal enzyme that, in animals, carries out the oxidation of haem, it cleaves the haem ring at the alpha-methene bridge to form biliverdin and carbon monoxide [ ]. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. In mammals there are three isozymes of hae... | [
"GO:0004392"
] | [
"heme oxygenase (decyclizing) activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00593"
] | [
"HEME_OXYGENASE"
] | [
3132
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"1.14.14.18",
"PWY-5874",
"R-BTA-189483",
"R-BTA-917937",
"R-BTA-9609523",
"R-BTA-9707564",
"R-BTA-9707587",
"R-HSA-189483",
"R-HSA-6785807",
"R-HSA-6798695",
"R-HSA-844456",
"R-HSA-8980692",
"R-HSA-917937",
"R-HSA-9609523",
"R-HSA-9660826",
"R-HSA-9707564",
"R-HSA-9707587",
"R-HSA... | [
"EC:1.14.14.18",
"METACYC:PWY-5874",
"REACTOME:R-BTA-189483",
"REACTOME:R-BTA-917937",
"REACTOME:R-BTA-9609523",
"REACTOME:R-BTA-9707564",
"REACTOME:R-BTA-9707587",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-844456",
"REACTOME:R-HSA-8980692",
... | 38 | [
"1dve",
"1dvg",
"1irm",
"1ivj",
"1iw0",
"1iw1",
"1ix3",
"1ix4",
"1j02",
"1j2c",
"1n3u",
"1n45",
"1ni6",
"1oyk",
"1oyl",
"1oze",
"1ozl",
"1ozr",
"1ozw",
"1s13",
"1s8c",
"1t5p",
"1twn",
"1twr",
"1ubb",
"1ulx",
"1v8x",
"1vgi",
"1we1",
"1wnv",
"1wnw",
"1wnx"... | 86 | [
"PUB00001493",
"PUB00002314",
"PUB00002451",
"PUB00004905",
"PUB00005160"
] | [
"3290025",
"9006041",
"3032976",
"9326680",
"8093563"
] | [
"Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications.",
"Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin.",
"N... | [
1988,
1997,
1987,
1997,
1993
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"freshwater metagenome"
] | [
597,
2534,
1
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
15,
7,
8
] | 4 | true | Conserved_site | Haem oxygenase conserved site | Haem oxygenase conserved site | Haem_oxygenase_CS | 2 |
IPR018208 | 18,208 | Glycoside hydrolase family 11, active site 1 | GH11_AS_1 | Active_site | 4,897 | false | false | The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases ( ), cellobiohydrolases ( ) (exoglucanases), or xylanases ( ) [ , ]. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be c... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00776"
] | [
"GH11_1"
] | [
4897
] | 1 | [
"EC"
] | [
"3.2.1.8"
] | [
"EC:3.2.1.8"
] | 1 | [
"1axk",
"1bcx",
"1bk1",
"1bvv",
"1c5h",
"1c5i",
"1enx",
"1f5j",
"1h1a",
"1h4g",
"1hix",
"1hv1",
"1igo",
"1m4w",
"1pvx",
"1qh6",
"1qh7",
"1red",
"1ree",
"1ref",
"1t6g",
"1te1",
"1ukr",
"1xnb",
"1xnc",
"1xnd",
"1xnk",
"1xxn",
"1xyn",
"1xyo",
"1xyp",
"1yna"... | 158 | [
"PUB00000117",
"PUB00000503",
"PUB00000519",
"PUB00001778",
"PUB00003608"
] | [
"2252383",
"1747104",
"1359880",
"2806912",
"1886523"
] | [
"Molecular biology of cellulose degradation.",
"A classification of glycosyl hydrolases based on amino acid sequence similarities.",
"Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus.",
"Cellulase families revealed by hydrophobic cluster analysis.",
"Domains in... | [
1990,
1991,
1992,
1989,
1991
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
1888,
2887,
29,
93
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Active_site | Glycoside hydrolase family 11, active site 1 | Glycoside hydrolase family 11, active site 1 | GH11_AS_1 | 9 |
IPR018209 | 18,209 | Pyruvate kinase, active site | Pyrv_Knase_AS | Active_site | 32,437 | false | false | Pyruvate kinase ( ) (PK) catalyses the final step in glycolysis [ , ], the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP: ADP + phosphoenolpyruvate = ATP + pyruvate The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activ... | [
"GO:0004743",
"GO:0006096"
] | [
"pyruvate kinase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00110"
] | [
"PYRUVATE_KINASE"
] | [
32437
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",... | [
"2.7.1.40",
"PWY-1042",
"PWY-2221",
"PWY-5484",
"PWY-5723",
"PWY-6886",
"PWY-6901",
"PWY-7003",
"PWY-7218",
"PWY-7383",
"PWY-8004",
"PWY-8404",
"R-CFA-70171",
"R-CFA-70268",
"R-DDI-6798695",
"R-DDI-70171",
"R-DDI-70268",
"R-DDI-9861718",
"R-DME-6798695",
"R-DME-70171",
"R-DME... | [
"EC:2.7.1.40",
"METACYC:PWY-1042",
"METACYC:PWY-2221",
"METACYC:PWY-5484",
"METACYC:PWY-5723",
"METACYC:PWY-6886",
"METACYC:PWY-6901",
"METACYC:PWY-7003",
"METACYC:PWY-7218",
"METACYC:PWY-7383",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"REACTOME:R-CFA-70171",
"REACTOME:R-CFA-70268",
"REAC... | 49 | [
"1a3w",
"1a3x",
"1a49",
"1a5u",
"1aqf",
"1e0t",
"1e0u",
"1f3w",
"1f3x",
"1pkl",
"1pkm",
"1pkn",
"1pky",
"1t5a",
"1zjh",
"2e28",
"2g50",
"2vgb",
"2vgf",
"2vgg",
"2vgi",
"3bjf",
"3bjt",
"3e0v",
"3e0w",
"3eoe",
"3g2g",
"3gg8",
"3gqy",
"3gr4",
"3h6o",
"3hqn"... | 190 | [
"PUB00000569",
"PUB00014134",
"PUB00014243",
"PUB00024392",
"PUB00100069"
] | [
"2379684",
"11960989",
"12798932",
"10751408",
"29748232"
] | [
"Isoenzymes of pyruvate kinase.",
"Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.",
"Pyruvate kinase: current status of regulatory and functional properties.",
"The allosteric regulation of pyruvate kinase.",
"An allostatic mechanism for M2 p... | [
1990,
2002,
2003,
2000,
2018
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctNmW2",
"unclassified sequences"
] | [
237,
19945,
11932,
1,
322
] | 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",... | [
37,
8,
9,
5,
2,
17,
7,
1,
27,
14,
2,
1,
43
] | 13 | true | Active_site | Pyruvate kinase, active site | Pyruvate kinase, active site | Pyrv_Knase_AS | 8 |
IPR018211 | 18,211 | Alcohol dehydrogenase, iron-type, conserved site | ADH_Fe_CS | Conserved_site | 50,648 | false | false | Alcohol dehydrogenase ( ) (ADH) catalyses the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD. Currently three, structurally and catalytically, different types of alcohol dehydrogenases are known: Zinc-containing 'long-chain' alcohol dehydrogenases. Insect-type, or 'short-chain' al... | [
"GO:0016491",
"GO:0046872"
] | [
"oxidoreductase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00060",
"PS00913"
] | [
"ADH_IRON_2",
"ADH_IRON_1"
] | [
29722,
43461
] | 2 | [
"EC",
"REACTOME"
] | [
"1.1.1",
"R-CEL-880009"
] | [
"EC:1.1.1",
"REACTOME:R-CEL-880009"
] | 2 | [
"1jpu",
"1jq5",
"1jqa",
"1kq3",
"1oj7",
"1rrm",
"1ta9",
"1vlj",
"2bi4",
"2bl4",
"3bfj",
"3owo",
"3ox4",
"3uhj",
"3zdr",
"4fr2",
"4mca",
"4qgs",
"5br4",
"5xn8",
"5yvm",
"5yvr",
"5yvs",
"5zxl",
"6ahc",
"6csj",
"6jko",
"6jkp",
"6l1k",
"6scg",
"6sci",
"6tqh"... | 64 | [
"PUB00001606",
"PUB00002060",
"PUB00002085",
"PUB00002196",
"PUB00002203",
"PUB00002240",
"PUB00003722",
"PUB00160956"
] | [
"2015910",
"3584063",
"2661535",
"1644761",
"1385386",
"8132480",
"2823079",
"36928033"
] | [
"Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE.",
"Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis.",
"Similarity of Escherichia coli propanediol oxidoreductase (fucO product) an... | [
1991,
1987,
1989,
1992,
1992,
1994,
1987,
2023
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctMCY8",
"unclassified sequences"
] | [
418,
48184,
1659,
1,
386
] | 5 | [
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
7,
1,
3
] | 4 | true | Conserved_site | Alcohol dehydrogenase, iron-type, conserved site | Alcohol dehydrogenase, iron-type, conserved site | ADH_Fe_CS | 1 |
IPR018212 | 18,212 | Sodium/solute symporter, conserved site | Na/solute_symporter_CS | Conserved_site | 33,991 | false | false | Sodium/substrate symport (or co-transport) is a widespread mechanism of solute transport across cytoplasmic membranes of pro-and eukaryotic cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gra... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00456",
"PS00457"
] | [
"NA_SOLUT_SYMP_1",
"NA_SOLUT_SYMP_2"
] | [
24436,
20308
] | 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-189200",
"R-CFA-429593",
"R-DRE-189200",
"R-HSA-189200",
"R-HSA-196780",
"R-HSA-199220",
"R-HSA-209968",
"R-HSA-425397",
"R-HSA-428643",
"R-HSA-429593",
"R-HSA-5619096",
"R-HSA-5656364",
"R-HSA-5658208",
"R-HSA-8981373",
"R-MMU-189200",
"R-MMU-196780",
"R-MMU-199220",
"R-MMU... | [
"REACTOME:R-BTA-189200",
"REACTOME:R-CFA-429593",
"REACTOME:R-DRE-189200",
"REACTOME:R-HSA-189200",
"REACTOME:R-HSA-196780",
"REACTOME:R-HSA-199220",
"REACTOME:R-HSA-209968",
"REACTOME:R-HSA-425397",
"REACTOME:R-HSA-428643",
"REACTOME:R-HSA-429593",
"REACTOME:R-HSA-5619096",
"REACTOME:R-HSA-56... | 31 | [
"2xq2",
"3dh4",
"7sl8",
"7sla",
"7uuy",
"7uuz",
"7uv0",
"7vsi",
"7wmv",
"7yni",
"7ynj",
"7ynk",
"8hb0",
"8hdh",
"8hez",
"8hg7",
"8hin",
"9kkq",
"9kkw",
"9kl0",
"9kmn"
] | 21 | [
"PUB00000660",
"PUB00005080",
"PUB00009984"
] | [
"8031825",
"1965458",
"12354616"
] | [
"A functional superfamily of sodium/solute symporters.",
"The Na+/pantothenate symporter (PanF) of Escherichia coli is homologous to the Na+/proline symporter (PutP) of E. coli and the Na+/glucose symporters of mammals.",
"The sodium/substrate symporter family: structural and functional features."
] | [
1994,
1990,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Biquartavirus",
"Eukaryota",
"unclassified sequences"
] | [
476,
24226,
4,
9106,
179
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
4,
14,
29,
38
] | 5 | true | Conserved_site | Sodium/solute symporter, conserved site | Sodium/solute symporter, conserved site | Na/solute_symporter_CS | 9 |
IPR018214 | 18,214 | Glutamyl-tRNA reductase, conserved site | GluRdtase_CS | Conserved_site | 17,178 | false | false | Delta-aminolevulinic acid (ALA) is the obligatory precursor for the synthesis of all tetrapyrroles including porphyrin derivatives such as chlorophyll and heme. ALA can be synthesized via two different pathways: the Shemin (or C4) pathway which involves the single step condensation of succinyl-CoA and glycine and which... | [
"GO:0008883"
] | [
"glutamyl-tRNA reductase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00747"
] | [
"GLUTR"
] | [
17178
] | 1 | [
"EC",
"METACYC"
] | [
"1.2.1.70",
"PWY-5188"
] | [
"EC:1.2.1.70",
"METACYC:PWY-5188"
] | 2 | [
"1gpj",
"4n7r",
"5che",
"5yjl"
] | 4 | [
"PUB00005387"
] | [
"1502723"
] | [
"Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
701,
14844,
1428,
205
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
2,
13
] | 4 | true | Conserved_site | Glutamyl-tRNA reductase, conserved site | Glutamyl-tRNA reductase, conserved site | GluRdtase_CS | 2 |
IPR018215 | 18,215 | ClpP, Ser active site | ClpP_Ser_AS | Active_site | 39,235 | false | false | Clp is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin [ ]. It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP [ ], although the P subunit alone does possess ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00381"
] | [
"CLP_PROTEASE_SER"
] | [
39235
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.92",
"R-BTA-9837999",
"R-CEL-9837999",
"R-HSA-9837999",
"R-MMU-9837999"
] | [
"EC:3.4.21.92",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-9837999",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-9837999"
] | 5 | [
"1tg6",
"1tyf",
"1y7o",
"1yg6",
"1yg8",
"2fzs",
"2zl0",
"2zl2",
"3hln",
"3ktg",
"3kth",
"3kti",
"3ktj",
"3ktk",
"3mt6",
"3p2l",
"3q7h",
"3qwd",
"3st9",
"3sta",
"3tt6",
"3tt7",
"3v5e",
"4emm",
"4emp",
"4jct",
"4mxi",
"4ryf",
"4u0g",
"5c90",
"5dkp",
"5dl1"... | 170 | [
"PUB00002564"
] | [
"2197275"
] | [
"Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
21438,
17329,
5,
11,
452
] | 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",... | [
11,
1,
1,
3,
1,
2,
3,
1,
17,
2,
38
] | 11 | true | Active_site | ClpP, Ser active site | ClpP, Ser active site | ClpP_Ser_AS | 2 |
IPR018216 | 18,216 | Cathelicidin, conserved site | Cathelicidin_CS | Conserved_site | 733 | false | false | Cathelicidins are antimicrobial peptides and, together with defensins, form a large group of cationic peptides with amphipathic properties, and are part of the innate immune system in many vertebrates. These peptides exert antimicrobial activity against a wide range of microorganisms such as bacteria, enveloped viruses... | [
"GO:0006952",
"GO:0005576"
] | [
"defense response",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00946",
"PS00947"
] | [
"CATHELICIDINS_1",
"CATHELICIDINS_2"
] | [
478,
698
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6798695",
"R-BTA-6803157",
"R-HSA-6798695",
"R-HSA-6803157",
"R-MMU-6798695",
"R-MMU-6803157"
] | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6803157",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6803157",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-6803157"
] | 6 | [
"1kwi",
"1lxe",
"1n5h",
"1n5p",
"1pfp",
"4eyc"
] | 6 | [
"PUB00001695",
"PUB00048248",
"PUB00095113"
] | [
"7589491",
"18818205",
"23065264"
] | [
"Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain.",
"Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles.",
"Cathelicidins: family of antimicrobial peptides. A review."
] | [
1995,
2008,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Euteleostomi",
"Nostoc"
] | [
731,
2
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
5
] | 3 | true | Conserved_site | Cathelicidin, conserved site | Cathelicidin, conserved site | Cathelicidin_CS | 5 |
IPR018218 | 18,218 | Scorpion long chain toxin | Scorpion_toxinL | Family | 615 | false | false | Scorpion toxins, which may be mammal or insect specific, bind to sodium channels, inhibiting the inactivation of activated channels and blocking neuronal transmission. The complete covalent structure of the toxins has been deduced: it comprises around 66 amino acid residues and is cross-linked by four disulphide bridge... | [
"GO:0019871",
"GO:0090729",
"GO:0005576"
] | [
"sodium channel inhibitor activity",
"toxin activity",
"extracellular region"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00285"
] | [
"SCORPNTOXIN"
] | [
615
] | 1 | [] | [] | [] | 0 | [
"1aho",
"1b3c",
"1b7d",
"1bmr",
"1chz",
"1cn2",
"1djt",
"1dq7",
"1fh3",
"1i6f",
"1i6g",
"1jza",
"1jzb",
"1kv0",
"1lqh",
"1lqi",
"1lqq",
"1nh5",
"1npi",
"1nra",
"1nrb",
"1omy",
"1ptx",
"1seg",
"1sn1",
"1sn4",
"1snb",
"1t1t",
"1t7a",
"1t7b",
"1t7e",
"1vna"... | 69 | [
"PUB00000473",
"PUB00001584",
"PUB00005313",
"PUB00095081",
"PUB00097254"
] | [
"2930463",
"2311768",
"6845379",
"30678116",
"27130039"
] | [
"Purification and N-terminal partial sequence of anti-epilepsy peptide from venom of the scorpion Buthus martensii Karsch.",
"Primary structure of scorpion anti-insect toxins isolated from the venom of Leiurus quinquestriatus quinquestriatus.",
"Covalent structure of toxins I and II from the scorpion Buthus occ... | [
1989,
1990,
1983,
2019,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Arthropoda"
] | [
615
] | 1 | [] | [] | 0 | true | Family | Scorpion long chain toxin | Scorpion long chain toxin | Scorpion_toxinL | 4 |
IPR018219 | 18,219 | Thiol peroxidase conserved site | Tpx_CS | Conserved_site | 9,742 | false | false | Escherichia coli protein Tpx [ ] is an antioxidant protein with a thiol peroxidase activity. It acts as an antioxidant enzyme by removing peroxides within the catalase-and peroxidase-deficient periplasmic space of E. coli. It is a small protein of 18kDa whose sequence is well conserved in other bacterial species. | [
"GO:0016684"
] | [
"oxidoreductase activity, acting on peroxide as acceptor"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01265"
] | [
"TPX"
] | [
9742
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"1.11.1.24",
"R-HSA-1222538",
"R-HSA-1222541"
] | [
"EC:1.11.1.24",
"REACTOME:R-HSA-1222538",
"REACTOME:R-HSA-1222541"
] | 3 | [
"1psq",
"1q98",
"1qxh",
"1xvq",
"1y25",
"2jsy",
"2jsz",
"2xpd",
"2xpe",
"2yjh",
"2yzh",
"3hvs",
"3hvv",
"3i43",
"3p7x",
"3zrd",
"3zre",
"4af2",
"4je1",
"6udg",
"8xvw",
"8zwt",
"8zxu",
"9f5v"
] | 24 | [
"PUB00002933"
] | [
"7499381"
] | [
"Thioredoxin-linked \"thiol peroxidase\" from periplasmic space of Escherichia coli."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
9636,
17,
89
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Thiol peroxidase conserved site | Thiol peroxidase conserved site | Tpx_CS | 9 |
IPR018220 | 18,220 | Adenylosuccinate synthase, GTP-binding site | Adenylosuccin_syn_GTP-bd | Binding_site | 30,717 | false | false | Adenylosuccinate synthetase ( ) plays an important role in purine biosynthesis, by catalysing the GTP-dependent conversion of IMP and aspartic acid to AMP. Adenylosuccinate synthetase has been characterised from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozyme... | [
"GO:0005525"
] | [
"GTP binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01266"
] | [
"ADENYLOSUCCIN_SYN_1"
] | [
30717
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.4.4",
"PWY-7219",
"R-BTA-73817",
"R-CEL-73817",
"R-DDI-73817",
"R-DME-73817",
"R-DRE-73817",
"R-GGA-421203",
"R-HSA-73817",
"R-MMU-73817",
"R-PFA-73817",
"R-SCE-73817",
"R-SPO-73817",
"R-SSC-73817",
"R-XTR-73817"
] | [
"EC:6.3.4.4",
"METACYC:PWY-7219",
"REACTOME:R-BTA-73817",
"REACTOME:R-CEL-73817",
"REACTOME:R-DDI-73817",
"REACTOME:R-DME-73817",
"REACTOME:R-DRE-73817",
"REACTOME:R-GGA-421203",
"REACTOME:R-HSA-73817",
"REACTOME:R-MMU-73817",
"REACTOME:R-PFA-73817",
"REACTOME:R-SCE-73817",
"REACTOME:R-SPO-7... | 15 | [
"1ade",
"1adi",
"1cg0",
"1cg3",
"1cg4",
"1ch8",
"1cib",
"1dj2",
"1dj3",
"1gim",
"1gin",
"1hon",
"1hoo",
"1hop",
"1iwe",
"1j4b",
"1juy",
"1kjx",
"1kkb",
"1kkf",
"1ksz",
"1lny",
"1lon",
"1loo",
"1mez",
"1mf0",
"1mf1",
"1nht",
"1p9b",
"1qf4",
"1qf5",
"1son"... | 52 | [
"PUB00003352",
"PUB00006296",
"PUB00006475"
] | [
"7490761",
"8244965",
"10669609"
] | [
"Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli.",
"Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains.",
"Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis tha... | [
1995,
1993,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
788,
23072,
6340,
25,
492
] | 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",... | [
5,
1,
4,
2,
1,
3,
6,
1,
4,
8,
1,
1,
5
] | 13 | true | Binding_site | Adenylosuccinate synthase, GTP-binding site | Adenylosuccinate synthase, GTP-binding site | Adenylosuccin_syn_GTP-bd | 1 |
IPR018221 | 18,221 | Glycoside hydrolase family 9, His active site | Glyco_hydro_9_His_AS | Active_site | 12,945 | false | false | The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases, cellobiohydrolases (exoglucanases), or xylanases [ , ]. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified in... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00592"
] | [
"GH9_2"
] | [
12945
] | 1 | [
"EC",
"METACYC"
] | [
"3.2.1.4",
"PWY-6788"
] | [
"EC:3.2.1.4",
"METACYC:PWY-6788"
] | 2 | [
"1clc",
"1g87",
"1ga2",
"1js4",
"1k72",
"1kfg",
"1rq5",
"1tf4",
"1ut9",
"2xfg",
"2yik",
"3ez8",
"3gzk",
"3h2w",
"3h3k",
"3rx5",
"3rx7",
"3rx8",
"3tf4",
"3x17",
"4cj0",
"4cj1",
"4tf4",
"4zg8",
"4zh5",
"5e2j",
"5gxx",
"5gxy",
"5gxz",
"5gy0",
"5gy1",
"6dht"... | 38 | [
"PUB00000117",
"PUB00000503",
"PUB00000511",
"PUB00001778",
"PUB00002631",
"PUB00003608",
"PUB00092589"
] | [
"2252383",
"1747104",
"1637316",
"2806912",
"2037583",
"1886523",
"29914107"
] | [
"Molecular biology of cellulose degradation.",
"A classification of glycosyl hydrolases based on amino acid sequence similarities.",
"Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.",
"Cellulase families revealed by hydrophobic cluster analysis.",
"... | [
1990,
1991,
1992,
1989,
1991,
1991,
2018
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Haloarculaceae",
"unclassified sequences"
] | [
1921,
10948,
6,
70
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
114,
51,
94
] | 3 | true | Active_site | Glycoside hydrolase family 9, His active site | Glycoside hydrolase family 9, His active site | Glyco_hydro_9_His_AS | 4 |
IPR018222 | 18,222 | Nuclear transport factor 2, eukaryote | Nuclear_transport_factor_2_euk | Domain | 26,062 | false | false | Ran ( ) is an evolutionary conserved member of the Ras superfamily of small GTPases that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Import receptors bind their cargos in the cytoplasm where the concentration of RanGTP is low and release their cargos in the nucleus where the concent... | [] | [] | [] | 0 | [
"PROFILE",
"CDD"
] | [
"PS50177",
"cd00780"
] | [
"NTF2_DOMAIN",
"NTF2"
] | [
26029,
18203
] | 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-159227",
"R-BTA-159230",
"R-BTA-159231",
"R-BTA-159236",
"R-CEL-159236",
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-GGA-159236",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"R-HSA-9705671",
"R-MMU-159227",
"R-MMU-159230",
"R-MMU-15... | [
"REACTOME:R-BTA-159227",
"REACTOME:R-BTA-159230",
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-CEL-159236",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-GGA-159236",
"REACTOME:R-HSA-159227",
"REACTOME:R-HSA-159... | 27 | [
"1ar0",
"1ask",
"1gy5",
"1gy6",
"1gy7",
"1gyb",
"1jb2",
"1jb4",
"1jb5",
"1jkg",
"1jn5",
"1of5",
"1oun",
"1q40",
"1qma",
"1u5o",
"1zo2",
"1zx2",
"2qiy",
"3nv0",
"3q90",
"3ujm",
"4fcj",
"4fcm",
"4iia",
"4wp5",
"4wwu",
"4wyk",
"4x2h",
"4x2m",
"4x2o",
"4xm4"... | 55 | [
"PUB00006684",
"PUB00006685",
"PUB00007086",
"PUB00018170"
] | [
"11129791",
"10930458",
"12019565",
"11073998"
] | [
"Insights into the molecular mechanism of nuclear trafficking using nuclear transport factor 2 (NTF2).",
"The interaction between Ran and NTF2 is required for cell cycle progression.",
"Regulation of nuclear import and export by the GTPase Ran.",
"TAP (NXF1) belongs to a multigene family of putative RNA expor... | [
2000,
2000,
2002,
2000
] | 4 | [
"IPR002075"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Natrialbaceae",
"Viruses",
"metagenomes"
] | [
91,
25952,
3,
11,
5
] | 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... | [
73,
7,
24,
18,
53,
28,
4,
22,
35,
3,
4,
82
] | 12 | true | Domain | Nuclear transport factor 2, eukaryote | Nuclear transport factor 2, eukaryote | Nuclear_transport_factor_2_euk | 2 |
IPR018223 | 18,223 | Argininosuccinate synthase, conserved site | Arginosuc_synth_CS | Conserved_site | 28,439 | false | false | Argininosuccinate synthase ( ) (AS) is a urea cycle enzyme that catalyses the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate [ , ]. In humans, a defect in the AS gene causes citrullinemia, a genetic disease characterised ... | [
"GO:0004055",
"GO:0005524",
"GO:0006526"
] | [
"argininosuccinate synthase activity",
"ATP binding",
"L-arginine biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00564",
"PS00565"
] | [
"ARGININOSUCCIN_SYN_1",
"ARGININOSUCCIN_SYN_2"
] | [
27768,
25433
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.4.5",
"PWY-4983",
"PWY-4984",
"PWY-5",
"PWY-5154",
"PWY-7400",
"R-BTA-70635",
"R-HSA-70635",
"R-MMU-70635"
] | [
"EC:6.3.4.5",
"METACYC:PWY-4983",
"METACYC:PWY-4984",
"METACYC:PWY-5",
"METACYC:PWY-5154",
"METACYC:PWY-7400",
"REACTOME:R-BTA-70635",
"REACTOME:R-HSA-70635",
"REACTOME:R-MMU-70635"
] | 9 | [
"1j1z",
"1j20",
"1j21",
"1k92",
"1k97",
"1kh1",
"1kh2",
"1kh3",
"1kor",
"1kp2",
"1kp3",
"1vl2",
"2nz2",
"4nzp",
"4u7j",
"4xfj",
"5us8",
"6e5y",
"6xnq",
"7k5z"
] | 20 | [
"PUB00001799",
"PUB00002066"
] | [
"2123815",
"3133361"
] | [
"Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals.",
"Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina bark... | [
1990,
1988
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
822,
22640,
2,
4433,
542
] | 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... | [
4,
1,
1,
1,
8,
3,
2,
3,
3,
1,
1,
10
] | 12 | true | Conserved_site | Argininosuccinate synthase, conserved site | Argininosuccinate synthase, conserved site | Arginosuc_synth_CS | 5 |
IPR018224 | 18,224 | Ependymin, conserved site | Ependymin_CS | Conserved_site | 178 | false | false | Ependymins are secretory proteins found predominantly in the cerebrospinal fluid of teleost fish [ , ]. A bound form of the glycoproteins is associated with the extracellular matrix, probably with collagen fibrils, that may be the functional form of ependymins [ ]. The proteins bind calcium via N-linked sialic acid res... | [
"GO:0005509",
"GO:0007160",
"GO:0005576"
] | [
"calcium ion binding",
"cell-matrix adhesion",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00898",
"PS00899"
] | [
"EPENDYMIN_1",
"EPENDYMIN_2"
] | [
153,
147
] | 2 | [] | [] | [] | 0 | [
"6e7o",
"6e8n",
"6jld"
] | 3 | [
"PUB00000027",
"PUB00002045",
"PUB00003426"
] | [
"1831964",
"8005346",
"8350351"
] | [
"Ependymin, a brain extracellular glycoprotein, and CNS plasticity.",
"Ependymins and their potential role in neuroplasticity and regeneration: calcium-binding meningeal glycoproteins of the cerebrospinal fluid and extracellular matrix.",
"Molecular analysis of ependymins from the cerebrospinal fluid of the ord... | [
1991,
1994,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
178
] | 1 | [
"Danio rerio",
"Homo sapiens"
] | [
1,
4
] | 2 | true | Conserved_site | Ependymin, conserved site | Ependymin, conserved site | Ependymin_CS | 1 |
IPR018225 | 18,225 | Transaldolase, active site | Transaldolase_AS | Active_site | 33,762 | false | false | Transaldolase ( ) catalyses the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together with transketolase, provides a link between the glycolytic and pentose-phosphate pathways. Transaldo... | [
"GO:0005975"
] | [
"carbohydrate metabolic process"
] | [
"biological_process"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00958",
"PS01054"
] | [
"TRANSALDOLASE_2",
"TRANSALDOLASE_1"
] | [
22002,
31906
] | 2 | [
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.2.1.2",
"PWY-1861",
"PWY-5723",
"R-DDI-163754",
"R-DDI-71336",
"R-DME-163754",
"R-DME-71336",
"R-HSA-163754",
"R-HSA-6791055",
"R-HSA-6791462",
"R-HSA-71336",
"R-HSA-8950505",
"R-HSA-9818028",
"R-MMU-163754",
"R-MMU-71336",
"R-RNO-163754",
"R-RNO-71336",
"R-SCE-163754",
"R-SCE... | [
"EC:2.2.1.2",
"METACYC:PWY-1861",
"METACYC:PWY-5723",
"REACTOME:R-DDI-163754",
"REACTOME:R-DDI-71336",
"REACTOME:R-DME-163754",
"REACTOME:R-DME-71336",
"REACTOME:R-HSA-163754",
"REACTOME:R-HSA-6791055",
"REACTOME:R-HSA-6791462",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-8950505",
"REACTOME:R-H... | 23 | [
"1f05",
"1i2n",
"1i2o",
"1i2p",
"1i2q",
"1i2r",
"1l6w",
"1onr",
"1ucw",
"1vpx",
"1wx0",
"2cwn",
"2e1d",
"3clm",
"3cq0",
"3cwn",
"3hjz",
"3igx",
"3kof",
"3m16",
"3r5e",
"3r8r",
"3s0c",
"3s1u",
"3s1v",
"3s1w",
"3s1x",
"3te9",
"3tk7",
"3tkf",
"3tno",
"3upb"... | 67 | [
"PUB00005649"
] | [
"8109173"
] | [
"Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
164,
27327,
120,
5739,
412
] | 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",... | [
3,
1,
1,
2,
4,
5,
2,
2,
2,
9,
2,
1,
8
] | 13 | true | Active_site | Transaldolase, active site | Transaldolase, active site | Transaldolase_AS | 3 |
IPR018226 | 18,226 | Barwin, conserved site | Barwin_CS | Conserved_site | 1,313 | false | false | Barwin is a basic protein isolated from aqueous extracts of barley seeds. It is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges [ , ]. Comparative analysis shows the sequence to be highly similar to a 122 amino acid stretch in the C-terminal of the products of... | [
"GO:0042742",
"GO:0050832"
] | [
"defense response to bacterium",
"defense response to fungus"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00771",
"PS00772"
] | [
"BARWIN_1",
"BARWIN_2"
] | [
1130,
841
] | 2 | [] | [] | [] | 0 | [
"1bw3",
"1bw4",
"4jp6",
"4jp7",
"7ksn"
] | 5 | [
"PUB00000371",
"PUB00000372"
] | [
"1390663",
"1390664"
] | [
"Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes.",
"Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy."
] | [
1992,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1313
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
11,
6
] | 3 | true | Conserved_site | Barwin, conserved site | Barwin, conserved site | Barwin_CS | 6 |
IPR018228 | 18,228 | Deoxyribonuclease, TatD-related, conserved site | DNase_TatD-rel_CS | Conserved_site | 39,455 | false | false | This family of proteins are related to a large superfamily of metalloenzymes [ ]. TatD, a member of this family has been shown experimentally to be a DNase enzyme [ ]. Allantoinase , N-isopropylammelide isopropyl amidohydrolase and the SCN1 protein from fission yeast belong to this family. | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS01090",
"PS01091",
"PS01137"
] | [
"TATD_2",
"TATD_3",
"TATD_1"
] | [
16577,
24084,
22619
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-381038",
"R-MMU-168638",
"R-MMU-450302",
"R-MMU-450321",
"R-MMU-5689896"
] | [
"REACTOME:R-HSA-381038",
"REACTOME:R-MMU-168638",
"REACTOME:R-MMU-450302",
"REACTOME:R-MMU-450321",
"REACTOME:R-MMU-5689896"
] | 5 | [
"1xwy",
"1yix",
"1zzm",
"2gzx",
"2xio",
"3e2v",
"3icj",
"3igh",
"3rcm",
"4p5u",
"4pe8",
"6l25",
"8efg"
] | 13 | [
"PUB00004994",
"PUB00007123"
] | [
"9144792",
"10747959"
] | [
"An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.",
"TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export."
] | [
1997,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
368,
31644,
6869,
16,
558
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
12,
6,
2,
2,
3,
8,
20,
4,
13,
3,
49
] | 11 | true | Conserved_site | Deoxyribonuclease, TatD-related, conserved site | Deoxyribonuclease, TatD-related, conserved site | DNase_TatD-rel_CS | 2 |
IPR018229 | 18,229 | Rhodopsin, retinal binding site | Rhodopsin_retinal_BS | Binding_site | 3,736 | false | false | The bacterial opsins are retinal-binding proteins that provide light-dependent ion transport and sensory functions to a family of halophilic bacteria [ , ]. They are integral membrane proteins believed to contain seven transmembrane (TM) domains, the last of which contains the attachment point for retinal (a conserved ... | [
"GO:0005216",
"GO:0006811",
"GO:0016020"
] | [
"monoatomic ion channel activity",
"monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00327",
"PS00950"
] | [
"BACTERIAL_OPSIN_RET",
"BACTERIAL_OPSIN_1"
] | [
1271,
3545
] | 2 | [] | [] | [] | 0 | [
"1ap9",
"1at9",
"1bct",
"1bm1",
"1brd",
"1brr",
"1brx",
"1c3w",
"1c8r",
"1c8s",
"1cwq",
"1dze",
"1e0p",
"1e12",
"1f4z",
"1f50",
"1fbb",
"1fbk",
"1gu8",
"1gue",
"1h2s",
"1h68",
"1iw6",
"1iw9",
"1ixf",
"1jgj",
"1jv7",
"1kg8",
"1kg9",
"1kgb",
"1kme",
"1l0m"... | 292 | [
"PUB00001180",
"PUB00005349",
"PUB00044796",
"PUB00044876",
"PUB00044877",
"PUB00044878"
] | [
"2591367",
"2468194",
"1247534",
"17067849",
"10393943",
"15274618"
] | [
"Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor.",
"Two pumps, one principle: light-driven ion transport in halobacteria.",
"Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site.",
"Seeing the rainbow: light sensing in fungi... | [
1989,
1989,
1976,
2006,
1999,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
666,
803,
1799,
5,
463
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Binding_site | Rhodopsin, retinal binding site | Rhodopsin, retinal binding site | Rhodopsin_retinal_BS | 8 |
IPR018230 | 18,230 | BUD31/G10-related, conserved site | BUD31/G10-rel_CS | Conserved_site | 3,751 | false | false | A Xenopus protein known as G10 [ ] and alternatively as BUD31-homologue has been found to be highly conserved in a wide range of eukaryotic species. The function of G10 is still unknown. G10 is a protein of about 17 to 18kDa (143 to 157 residues) which is hydrophilic and whose C-terminal half is rich in cysteines and c... | [
"GO:0005634"
] | [
"nucleus"
] | [
"cellular_component"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00997",
"PS00998"
] | [
"G10_1",
"G10_2"
] | [
3380,
2355
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-72163",
"R-CEL-72163",
"R-DRE-72163",
"R-HSA-72163",
"R-MMU-72163",
"R-RNO-72163"
] | [
"REACTOME:R-BTA-72163",
"REACTOME:R-CEL-72163",
"REACTOME:R-DRE-72163",
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-RNO-72163"
] | 6 | [
"2my1",
"5gm6",
"5gmk",
"5lj3",
"5lj5",
"5lqw",
"5mps",
"5mq0",
"5mqf",
"5wsg",
"5xjc",
"5y88",
"5ylz",
"5yzg",
"5z56",
"5z57",
"6bk8",
"6exn",
"6ff4",
"6ff7",
"6icz",
"6id0",
"6id1",
"6j6g",
"6j6h",
"6j6n",
"6j6q",
"6qdv",
"6zym",
"7aav",
"7abf",
"7abg"... | 58 | [
"PUB00001892"
] | [
"2568313"
] | [
"Poly(A) elongation during Xenopus oocyte maturation is required for translational recruitment and is mediated by a short sequence element."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3751
] | 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... | [
2,
1,
2,
1,
2,
1,
1,
5,
2,
1,
5
] | 11 | true | Conserved_site | BUD31/G10-related, conserved site | BUD31/G10-related, conserved site | BUD31/G10-rel_CS | 4 |
IPR018232 | 18,232 | Glycoside hydrolase, family 37, conserved site | Glyco_hydro_37_CS | Conserved_site | 11,476 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004555",
"GO:0005991"
] | [
"alpha,alpha-trehalase activity",
"trehalose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00927",
"PS00928"
] | [
"TREHALASE_1",
"TREHALASE_2"
] | [
8164,
10759
] | 2 | [
"EC",
"REACTOME"
] | [
"3.2.1.28",
"R-HSA-189085"
] | [
"EC:3.2.1.28",
"REACTOME:R-HSA-189085"
] | 2 | [
"2jf4",
"2jg0",
"2jjb",
"2wyn",
"5jta",
"5m4a",
"5n6n",
"5nis",
"5z66",
"5z6h",
"7e9u",
"7e9x",
"7eaw"
] | 13 | [
"PUB00002824",
"PUB00004870",
"PUB00005266"
] | [
"8444853",
"7624375",
"8535779"
] | [
"Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1993,
1995,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
4726,
6709,
29,
12
] | 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",... | [
5,
4,
2,
7,
2,
2,
3,
2,
3,
4,
2,
1,
7
] | 13 | true | Conserved_site | Glycoside hydrolase, family 37, conserved site | Glycoside hydrolase, family 37, conserved site | Glyco_hydro_37_CS | 8 |
IPR018233 | 18,233 | Calsequestrin, conserved site | Calsequestrin_CS | Conserved_site | 1,690 | false | false | Calsequestrin is the principal calcium-binding protein present in the sarcoplasmic reticulum of cardiac and skeletal muscle [ ]. It is a highly acidic protein that is able to bind over 40 calcium ions and acts as an internal calcium store in muscle. Sequence analysis has suggested that calcium is not bound in distinct ... | [
"GO:0005509"
] | [
"calcium ion binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00863",
"PS00864"
] | [
"CALSEQUESTRIN_1",
"CALSEQUESTRIN_2"
] | [
871,
1544
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2672351",
"R-HSA-5578775",
"R-MMU-2672351",
"R-MMU-5578775",
"R-RNO-2672351",
"R-RNO-5578775"
] | [
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-5578775",
"REACTOME:R-MMU-2672351",
"REACTOME:R-MMU-5578775",
"REACTOME:R-RNO-2672351",
"REACTOME:R-RNO-5578775"
] | 6 | [
"1a8y",
"2vaf",
"3trp",
"3trq",
"3uom",
"3us3",
"3v1w",
"5crd",
"5cre",
"5crg",
"5crh",
"5kn0",
"5kn1",
"5kn2",
"5kn3",
"6owv",
"6oww",
"7f05",
"8f48"
] | 19 | [
"PUB00000289",
"PUB00002488",
"PUB00002682"
] | [
"3427023",
"3379055",
"1985907"
] | [
"Characterization of cardiac calsequestrin.",
"Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning.",
"Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calseque... | [
1987,
1988,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1690
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
8,
10
] | 3 | true | Conserved_site | Calsequestrin, conserved site | Calsequestrin, conserved site | Calsequestrin_CS | 9 |
IPR018234 | 18,234 | GTP cyclohydrolase I, conserved site | GTP_CycHdrlase_I_CS | Conserved_site | 26,865 | false | false | GTP cyclohydrolase I ( ) catalyses the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP [ ]. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. The comparison of the sequenc... | [
"GO:0003934",
"GO:0046654"
] | [
"GTP cyclohydrolase I activity",
"tetrahydrofolate biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00859",
"PS00860"
] | [
"GTP_CYCLOHYDROL_1_1",
"GTP_CYCLOHYDROL_1_2"
] | [
25019,
22853
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.4.16",
"PWY-5663",
"PWY-6147",
"PWY-6703",
"PWY-6983",
"PWY-7442",
"PWY-7852",
"R-CEL-1474151",
"R-DDI-1474151",
"R-DME-1474151",
"R-HSA-1474151",
"R-MMU-1474151",
"R-RNO-1474151",
"R-SCE-1474151",
"R-SPO-1474151"
] | [
"EC:3.5.4.16",
"METACYC:PWY-5663",
"METACYC:PWY-6147",
"METACYC:PWY-6703",
"METACYC:PWY-6983",
"METACYC:PWY-7442",
"METACYC:PWY-7852",
"REACTOME:R-CEL-1474151",
"REACTOME:R-DDI-1474151",
"REACTOME:R-DME-1474151",
"REACTOME:R-HSA-1474151",
"REACTOME:R-MMU-1474151",
"REACTOME:R-RNO-1474151",
... | 15 | [
"1a8r",
"1a9c",
"1fb1",
"1fbx",
"1gtp",
"1is7",
"1is8",
"1n3r",
"1n3s",
"1n3t",
"1wm9",
"1wpl",
"1wuq",
"1wur",
"4du6",
"4uqf",
"6z80",
"6z85",
"6z86",
"6z87",
"6z88",
"6z89",
"7ala",
"7alb",
"7alc",
"7alq",
"9p8z"
] | 27 | [
"PUB00000247",
"PUB00022220"
] | [
"7542887",
"12559918"
] | [
"Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers.",
"Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I."
] | [
1995,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
160,
21352,
4766,
82,
505
] | 5 | [
"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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
... | [
2,
2,
4,
1,
5,
3,
1,
5,
1,
1
] | 10 | true | Conserved_site | GTP cyclohydrolase I, conserved site | GTP cyclohydrolase I, conserved site | GTP_CycHdrlase_I_CS | 3 |
IPR018235 | 18,235 | Bacterial luciferase, conserved site | Bacterial_luciferase_CS | Conserved_site | 589 | false | false | The enzyme responsible for bioluminescence in motile Gram-negative luminous bacteria is bacterial luciferase [ , , ] ( ), which catalyses the oxidation the oxidation of reduced riboflavin phosphate (FMNH2) and a long chain fatty aldehyde with the emission of blue green light (490 nm). Luciferase is a heterodimeric enzy... | [
"GO:0047646"
] | [
"alkanal monooxygenase (FMN-linked) activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00494"
] | [
"BACTERIAL_LUCIFERASE"
] | [
589
] | 1 | [
"EC",
"METACYC"
] | [
"1.14.14.3",
"PWY-7723"
] | [
"EC:1.14.14.3",
"METACYC:PWY-7723"
] | 2 | [
"1brl",
"1bsl",
"1fvp",
"1luc",
"1nfp",
"1xkj",
"3fgc",
"4j2p",
"6fri"
] | 9 | [
"PUB00001517",
"PUB00028001",
"PUB00028002"
] | [
"8370470",
"1560772",
"2030669"
] | [
"Bacterial bioluminescence: organization, regulation, and application of the lux genes.",
"Evolutionary origins of bacterial bioluminescence.",
"Molecular biology of bacterial bioluminescence."
] | [
1993,
1992,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
589
] | 1 | [] | [] | 0 | true | Conserved_site | Bacterial luciferase, conserved site | Bacterial luciferase, conserved site | Bacterial_luciferase_CS | 8 |
IPR018236 | 18,236 | SAICAR synthetase, conserved site | SAICAR_synthetase_CS | Conserved_site | 28,093 | false | false | Phosphoribosylaminoimidazole-succinocarboxamide synthase ( ) (SAICAR synthetase) catalyses the seventh step in the de novo purine biosynthetic pathway; the ATP-dependent conversion of 5'-phosphoribosyl-5-aminoimidazole-4-carboxylic acid and aspartic acid to SAICAR [ , ]. In bacteria (purC), fungi (ADE1) and plants (Pur... | [
"GO:0004639",
"GO:0006164"
] | [
"phosphoribosylaminoimidazolesuccinocarboxamide synthase activity",
"purine nucleotide biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS01057",
"PS01058"
] | [
"SAICAR_SYNTHETASE_1",
"SAICAR_SYNTHETASE_2"
] | [
22146,
24167
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.2.6",
"PWY-6123",
"PWY-6124",
"PWY-7234",
"R-CEL-73817",
"R-DME-73817",
"R-GGA-419140",
"R-HSA-73817",
"R-MMU-73817",
"R-RNO-73817"
] | [
"EC:6.3.2.6",
"METACYC:PWY-6123",
"METACYC:PWY-6124",
"METACYC:PWY-7234",
"REACTOME:R-CEL-73817",
"REACTOME:R-DME-73817",
"REACTOME:R-GGA-419140",
"REACTOME:R-HSA-73817",
"REACTOME:R-MMU-73817",
"REACTOME:R-RNO-73817"
] | 10 | [
"1a48",
"1kut",
"1obd",
"1obg",
"2cnq",
"2cnu",
"2cnv",
"2gqr",
"2gqs",
"2h31",
"2ywv",
"2yzl",
"2z02",
"3kre",
"3nua",
"3r9r",
"3u54",
"3u55",
"4fe2",
"4fgr",
"4ja0",
"4nye",
"4o7l",
"4o7n",
"4o7r",
"4o7s",
"4o7t",
"4o7v",
"4o7w",
"4o7y",
"4o7z",
"4o81"... | 51 | [
"PUB00004940",
"PUB00070198"
] | [
"1574589",
"15641804"
] | [
"De novo purine nucleotide biosynthesis.",
"Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase."
] | [
1992,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
447,
22268,
4772,
50,
556
] | 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",... | [
3,
1,
3,
2,
1,
4,
1,
1,
3,
6,
1,
1,
6
] | 13 | true | Conserved_site | SAICAR synthetase, conserved site | SAICAR synthetase, conserved site | SAICAR_synthetase_CS | 1 |
IPR018237 | 18,237 | Myelin proteolipid protein PLP, conserved site | Myelin_PLP_CS | Conserved_site | 4,654 | false | false | The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction [ ]. Myelin proteolipid protein (PLP or lipophilin) [ ] is the major myelin protein from the central nervous system (CNS). It probably plays an import... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00575",
"PS01004"
] | [
"MYELIN_PLP_1",
"MYELIN_PLP_2"
] | [
4148,
4025
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000360",
"PUB00000749",
"PUB00002447",
"PUB00003190",
"PUB00004311"
] | [
"1281423",
"1722981",
"2435734",
"1711121",
"8398137"
] | [
"Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP.",
"Evolution of the myelin integral membrane proteins of the central nervous system.",
"Complete amino acid sequence of PO protein i... | [
1992,
1991,
1987,
1991,
1993
] | 5 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
4654
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
24,
11,
21
] | 4 | true | Conserved_site | Myelin proteolipid protein PLP, conserved site | Myelin proteolipid protein PLP, conserved site | Myelin_PLP_CS | 6 |
IPR018238 | 18,238 | Glycoside hydrolase, family 14, conserved site | Glyco_hydro_14_CS | Conserved_site | 4,105 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0016161",
"GO:0000272"
] | [
"beta-amylase activity",
"polysaccharide catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00506",
"PS00679"
] | [
"BETA_AMYLASE_1",
"BETA_AMYLASE_2"
] | [
3615,
2064
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.2.1.2",
"PWY-6724",
"PWY-842"
] | [
"EC:3.2.1.2",
"METACYC:PWY-6724",
"METACYC:PWY-842"
] | 3 | [
"1b1y",
"1b90",
"1b9z",
"1bfn",
"1btc",
"1bya",
"1byb",
"1byc",
"1byd",
"1fa2",
"1itc",
"1j0y",
"1j0z",
"1j10",
"1j11",
"1j12",
"1j18",
"1q6c",
"1q6d",
"1q6e",
"1q6f",
"1q6g",
"1uko",
"1ukp",
"1v3h",
"1v3i",
"1vem",
"1ven",
"1veo",
"1vep",
"1wdp",
"1wdq"... | 51 | [
"PUB00001450",
"PUB00002337",
"PUB00002354",
"PUB00004870",
"PUB00005062",
"PUB00005234",
"PUB00005266"
] | [
"8174545",
"2474529",
"1491009",
"7624375",
"2464171",
"2457058",
"8535779"
] | [
"Residues essential for catalytic activity of soybean beta-amylase.",
"Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase.",
"Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the ... | [
1994,
1989,
1992,
1995,
1988,
1988,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
205,
3900
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
25,
16,
36
] | 3 | true | Conserved_site | Glycoside hydrolase, family 14, conserved site | Glycoside hydrolase, family 14, conserved site | Glyco_hydro_14_CS | 1 |
IPR018239 | 18,239 | NAD-dependent DNA ligase, active site | DNA_ligase_AS | Active_site | 23,845 | false | false | DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalyzing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination. There are two forms of DNA ligase: one requires ATP ( ), the oth... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01055"
] | [
"DNA_LIGASE_N1"
] | [
23845
] | 1 | [
"EC"
] | [
"6.5.1.2"
] | [
"EC:6.5.1.2"
] | 1 | [
"1ta8",
"1tae",
"1v9p",
"1zau",
"2owo",
"3ba8",
"3ba9",
"3baa",
"3bab",
"3bac",
"3jsl",
"3jsn",
"3pn1",
"3sgi",
"3uq8",
"4cc5",
"4cc6",
"4eeq",
"4efb",
"4efe",
"4glw",
"4glx",
"4lh6",
"4lh7",
"4uco",
"4ucr",
"4ucs",
"4uct",
"4ucu",
"4ucv",
"4ufz",
"5fpo"... | 39 | [
"PUB00001728",
"PUB00002786",
"PUB00004738",
"PUB00044797"
] | [
"1526462",
"8390989",
"1988940",
"8760897"
] | [
"Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis.",
"Guanylate kinase of Escherichia coli K-12.",
"Location of the active site for enzyme-adenylate formation in DNA ligases.",
"Identification of essential residues in Thermus thermophilus DNA ligase."
] | [
1992,
1993,
1991,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
158,
23139,
117,
12,
419
] | 5 | [
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
2,
1
] | 2 | true | Active_site | NAD-dependent DNA ligase, active site | NAD-dependent DNA ligase, active site | DNA_ligase_AS | 2 |
IPR018240 | 18,240 | Clathrin adaptor, mu subunit, conserved site | Clathrin_mu_CS | Conserved_site | 16,512 | false | false | This entry represents the mu subunit of various clathrin adaptors (AP1, AP2 and AP3) [ ]. The mu subunit regulates the coupling of clathrin lattices with particular membrane proteins by self-phosphorylation via a mechanism that is still unclear [ ]. The mu subunit possesses a highly conserved N-terminal domain of aroun... | [
"GO:0006886",
"GO:0016192",
"GO:0030131"
] | [
"intracellular protein transport",
"vesicle-mediated transport",
"clathrin adaptor complex"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00990",
"PS00991"
] | [
"CLAT_ADAPTOR_M_1",
"CLAT_ADAPTOR_M_2"
] | [
13980,
12354
] | 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-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-8856825",
"R-BTA-8856828",
"R-BTA-8866427",
"R-BTA-8964038",
"R-CEL-190873",
"R-CEL-196025",
"R... | [
"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... | 117 | [
"1bw8",
"1bxx",
"1h6e",
"1hes",
"1i31",
"1w63",
"2bp5",
"2jkr",
"2jkt",
"2pr9",
"2vgl",
"2xa7",
"3h85",
"3l81",
"3ml6",
"4emz",
"4en2",
"4hmy",
"4ikn",
"4mdr",
"4p6z",
"4uqi",
"5c7z",
"5fpi",
"5wrk",
"5wrl",
"5wrm",
"6bnt",
"6cm9",
"6cri",
"6d83",
"6d84"... | 81 | [
"PUB00001404",
"PUB00025539"
] | [
"1761056",
"11583591"
] | [
"The medium chains of the mammalian clathrin-associated proteins have a homolog in yeast.",
"Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T-lymphocyte antigen 4 and CD28."
] | [
1991,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
16512
] | 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... | [
21,
5,
19,
4,
49,
22,
3,
14,
32,
3,
2,
30
] | 12 | true | Conserved_site | Clathrin adaptor, mu subunit, conserved site | Clathrin adaptor, mu subunit, conserved site | Clathrin_mu_CS | 9 |
IPR018241 | 18,241 | Anion exchange, conserved site | Anion_exchange_CS | Conserved_site | 5,008 | false | false | Bicarbonate (HCO 3 - ) transport mechanisms are the principal regulators of pH in animal cells. Such transport also plays a vital role in acid-base movements in the stomach, pancreas, intestine, kidney, reproductive organs and the central nervous system. Functional studies have suggested four different HCO 3 - transpor... | [
"GO:0005452",
"GO:0006820",
"GO:0016020"
] | [
"solute:inorganic anion antiporter activity",
"monoatomic anion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00219",
"PS00220"
] | [
"ANION_EXCHANGER_1",
"ANION_EXCHANGER_2"
] | [
3397,
4246
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1237044",
"R-HSA-1247673",
"R-HSA-425381",
"R-HSA-5619050",
"R-MMU-1237044",
"R-MMU-1247673",
"R-MMU-425381",
"R-RNO-1237044",
"R-RNO-1247673",
"R-RNO-425381"
] | [
"REACTOME:R-HSA-1237044",
"REACTOME:R-HSA-1247673",
"REACTOME:R-HSA-425381",
"REACTOME:R-HSA-5619050",
"REACTOME:R-MMU-1237044",
"REACTOME:R-MMU-1247673",
"REACTOME:R-MMU-425381",
"REACTOME:R-RNO-1237044",
"REACTOME:R-RNO-1247673",
"REACTOME:R-RNO-425381"
] | 10 | [
"4yzf",
"7tvz",
"7tw0",
"7tw1",
"7tw2",
"7tw3",
"7tw5",
"7tw6",
"7ty4",
"7ty6",
"7ty7",
"7ty8",
"7tya",
"7uz3",
"7uzu",
"7uzv",
"7v07",
"7v0k",
"7v0m",
"7v0t",
"7v0u",
"7v0y",
"7v19",
"8crq",
"8crr",
"8crt",
"8cs9",
"8csl",
"8csv",
"8csy",
"8ct3",
"8cte"... | 55 | [
"PUB00005997",
"PUB00005998",
"PUB00005999",
"PUB00006000",
"PUB00006023",
"PUB00018713"
] | [
"2289848",
"2042971",
"9491367",
"10353704",
"9235899",
"9261985"
] | [
"Molecular biology of the anion exchanger gene family.",
"The band 3-related anion exchanger (AE) gene family.",
"The structure and function of band 3 (AE1): recent developments (review).",
"The association between familial distal renal tubular acidosis and mutations in the red cell anion exchanger (band 3, A... | [
1990,
1991,
1997,
1998,
1997,
1997
] | 6 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
5008
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
33,
19,
22,
17
] | 4 | true | Conserved_site | Anion exchange, conserved site | Anion exchange, conserved site | Anion_exchange_CS | 3 |
IPR018243 | 18,243 | Neuromodulin, palmitoylation site | Neuromodulin_palmitoyl_site | PTM | 403 | false | false | This entry represents the N-terminal in Neuromodulin which contains two cysteine residues that are palmitoylated and are responsible for the attachment of the protein to the membrane. Neuromodulin (also known as growth-associated protein 43 or GAP-43) is a component of the motile growth cones. It is membrane protein wh... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00412"
] | [
"NEUROMODULIN_1"
] | [
403
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-373760",
"R-HSA-373760",
"R-MMU-373760",
"R-RNO-373760"
] | [
"REACTOME:R-BTA-373760",
"REACTOME:R-HSA-373760",
"REACTOME:R-MMU-373760",
"REACTOME:R-RNO-373760"
] | 4 | [] | 0 | [
"PUB00000128",
"PUB00004062",
"PUB00004299",
"PUB00004303"
] | [
"2648946",
"2158629",
"3272162",
"2641999"
] | [
"Axonal growth-associated proteins.",
"G0 is a major growth cone protein subject to regulation by GAP-43.",
"Human GAP-43: its deduced amino acid sequence and chromosomal localization in mouse and human.",
"Selective conservation of GAP-43 structure in vertebrate evolution."
] | [
1989,
1990,
1988,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
403
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
1,
4
] | 4 | true | PTM | Neuromodulin, palmitoylation site | Neuromodulin, palmitoylation site | Neuromodulin_palmitoyl_site | 8 |
IPR018244 | 18,244 | Allergen V5/Tpx-1-related, conserved site | Allrgn_V5/Tpx1_CS | Conserved_site | 26,176 | false | false | The cysteine-rich secretory proteins (Crisp) are predominantly found in the mammalian male reproductive tract as well as in the venom of reptiles. This family includes mammalian testis-specific protein (Tpx-1), also known as cysteine-rich secretory protein 2 (CRISP2) [ ]; venom allergen 5 from vespid wasps and venom al... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS01009",
"PS01010"
] | [
"CRISP_1",
"CRISP_2"
] | [
19964,
15440
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6798695",
"R-CEL-6798695",
"R-HSA-1989781",
"R-HSA-6798695",
"R-MMU-6798695"
] | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-6798695",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695"
] | 5 | [
"1cfe",
"1qnx",
"1rc9",
"1smb",
"1u53",
"1wvr",
"1xta",
"1xx5",
"2dda",
"2ddb",
"2epf",
"2giz",
"2vzn",
"3mz8",
"3nt8",
"3q2r",
"3q2u",
"4aiw",
"4ly5",
"4nui",
"4nuk",
"4nun",
"4nuo",
"5ete",
"5jys",
"6imf"
] | 26 | [
"PUB00001206",
"PUB00001948",
"PUB00003182",
"PUB00033277",
"PUB00068002",
"PUB00068003",
"PUB00092777",
"PUB00093389"
] | [
"2026137",
"2613236",
"8454859",
"16339766",
"18342304",
"18222185",
"23148443",
"20608917"
] | [
"Differential targeting of the tobacco PR-1 pathogenesis-related proteins to the extracellular space and vacuoles of crystal idioblasts.",
"Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene.",
"Sequence analysis and antigenic cross-reactivity of a venom ... | [
1991,
1989,
1993,
2006,
2008,
2008,
2012,
2011
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosocosmicus",
"Eukaryota",
"Tupanvirus",
"metagenomes"
] | [
777,
6,
25365,
6,
22
] | 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... | [
52,
13,
20,
7,
25,
24,
2,
61,
31,
3,
31
] | 11 | true | Conserved_site | Allergen V5/Tpx-1-related, conserved site | Allergen V5/Tpx-1-related, conserved site | Allrgn_V5/Tpx1_CS | 2 |
IPR018245 | 18,245 | Gonadotropin, beta subunit, conserved site | Gonadotropin_bsu_CS | Conserved_site | 3,352 | false | false | The crystal structures of four growth factors; nerve growth factor, transforming growth factor-beta, platelet-derived growth factor, and human chorionic gonadotropin from four separate superfamilies revealed that these proteins are structurally related and share a common overall topology [ ]. These proteins show very l... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00261",
"PS00689"
] | [
"GLYCO_HORMONE_BETA_1",
"GLYCO_HORMONE_BETA_2"
] | [
3127,
2442
] | 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-193048",
"R-BTA-193993",
"R-BTA-209822",
"R-BTA-209968",
"R-BTA-375281",
"R-BTA-418555",
"R-BTA-8866910",
"R-BTA-975578",
"R-GGA-209822",
"R-GGA-209968",
"R-GGA-375281",
"R-GGA-418555",
"R-HSA-193048",
"R-HSA-193993",
"R-HSA-209822",
"R-HSA-209968",
"R-HSA-375281",
"R-HSA-41... | [
"REACTOME:R-BTA-193048",
"REACTOME:R-BTA-193993",
"REACTOME:R-BTA-209822",
"REACTOME:R-BTA-209968",
"REACTOME:R-BTA-375281",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-8866910",
"REACTOME:R-BTA-975578",
"REACTOME:R-GGA-209822",
"REACTOME:R-GGA-209968",
"REACTOME:R-GGA-375281",
"REACTOME:R-GGA-41... | 42 | [
"1fl7",
"1hcn",
"1hrp",
"1qfw",
"1xwd",
"4ay9",
"4mqw",
"6p57",
"7fig",
"7fih",
"7fii",
"7t9i",
"7utz",
"7xw5",
"8i2g"
] | 15 | [
"PUB00000033",
"PUB00000091",
"PUB00000517",
"PUB00000890",
"PUB00001089",
"PUB00004177"
] | [
"6267989",
"7663117",
"1445230",
"8490958",
"7583638",
"8202136"
] | [
"Glycoprotein hormones: structure and function.",
"The cystine-knot growth-factor superfamily.",
"Molecular structures of glycoprotein hormones and functions of their carbohydrate components.",
"A structural superfamily of growth factors containing a cystine knot motif.",
"Cystine knots.",
"Crystal struct... | [
1981,
1995,
1992,
1993,
1995,
1994
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Ethanoperedens thermophilum",
"Eukaryota",
"Myoviridae sp. ctj3P51"
] | [
178,
1,
3172,
1
] | 4 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
23,
8,
12
] | 4 | true | Conserved_site | Gonadotropin, beta subunit, conserved site | Gonadotropin, beta subunit, conserved site | Gonadotropin_bsu_CS | 3 |
IPR018246 | 18,246 | AP endonuclease 2, zinc binding site | AP_endonuc_F2_Zn_BS | Binding_site | 16,425 | false | false | Cellular DNA is spontaneously and continuously damaged by environmental and internal factors such as X-rays, UV light and agents such as the antitumor drugs bleomycin and neocarzinostatin or those that generate oxygen radicals. Apurinic/apyrimidinic (AP) sites can form spontaneously or as highly cytotoxic intermediates... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS00729",
"PS00730",
"PS00731"
] | [
"AP_NUCLEASE_F2_1",
"AP_NUCLEASE_F2_2",
"AP_NUCLEASE_F2_3"
] | [
8722,
14263,
12596
] | 3 | [
"EC"
] | [
"3.1.21.2"
] | [
"EC:3.1.21.2"
] | 1 | [
"1qtw",
"1qum",
"1xp3",
"2nq9",
"2nqh",
"2nqj",
"2x7v",
"2x7w",
"3aal",
"3aam",
"4hno",
"4k1g",
"5zhz",
"6khy",
"6ki3",
"8axy",
"8edd",
"8pkb",
"8rly"
] | 19 | [
"PUB00000730",
"PUB00002671",
"PUB00003837",
"PUB00004710",
"PUB00017986",
"PUB00048372",
"PUB00052615"
] | [
"7661852",
"1720775",
"8446028",
"1693433",
"10458614",
"18408731",
"17242363"
] | [
"Structure and function of apurinic/apyrimidinic endonucleases.",
"Metalloenzymes in DNA repair. Escherichia coli endonuclease IV and Saccharomyces cerevisiae Apn1.",
"Nucleotide sequence of the first cosmid from the Mycobacterium leprae genome project: structure and function of the Rif-Str regions.",
"Yeast ... | [
1995,
1991,
1993,
1990,
1999,
2008,
2007
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
586,
13107,
2332,
72,
328
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"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,
5,
1,
1,
1,
1
] | 6 | true | Binding_site | AP endonuclease 2, zinc binding site | AP endonuclease 2, zinc binding site | AP_endonuc_F2_Zn_BS | 6 |
IPR018247 | 18,247 | EF-Hand 1, calcium-binding site | EF_Hand_1_Ca_BS | Binding_site | 531,631 | false | false | This entry represents the complete EF-hand loop as well as the first residue which follows the loop and which seem to always be hydrophobic. Interestingly, positions 1 (X), 3 (Y) and 12 (-Z) are the most conserved. The 6th residue in an EF-hand loop is, in most cases a Gly, but the number of exceptions to this 'rule' h... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00018"
] | [
"EF_HAND_1"
] | [
531631
] | 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-111447",
"R-BTA-114508",
"R-BTA-114608",
"R-BTA-1474228",
"R-BTA-1483166",
"R-BTA-163560",
"R-BTA-1855204",
"R-BTA-2025928",
"R-BTA-2160916",
"R-BTA-2514859",
"R-BTA-2565942",
"R-BTA-2871809",
"R-BTA-3000178",
"R-BTA-3000497",
"R-BTA-3108214",
"R-BTA-354192",
"R-BTA-380259",
... | [
"REACTOME:R-BTA-111447",
"REACTOME:R-BTA-114508",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-163560",
"REACTOME:R-BTA-1855204",
"REACTOME:R-BTA-2025928",
"REACTOME:R-BTA-2160916",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-2565942",
"REACTOME:R-... | 735 | [
"1a03",
"1a29",
"1a2x",
"1a75",
"1ahr",
"1aj4",
"1aj5",
"1ak8",
"1alv",
"1alw",
"1ap4",
"1aui",
"1avs",
"1b1g",
"1b4c",
"1b7t",
"1b8c",
"1b8l",
"1b8r",
"1b9a",
"1bjf",
"1blq",
"1bmo",
"1boc",
"1bod",
"1bu3",
"1c07",
"1c7v",
"1c7w",
"1cb1",
"1cdl",
"1cdm"... | 1,568 | [
"PUB00004973",
"PUB00023349",
"PUB00081528",
"PUB00081532",
"PUB00081536"
] | [
"7553064",
"9228939",
"8848832",
"7656053",
"10591109"
] | [
"Calcium-binding proteins 1: EF-hands.",
"EF-hands embrace.",
"Calcium binding and conformational response in EF-hand proteins.",
"Signal transduction versus buffering activity in Ca(2+)-binding proteins.",
"Diversity of conformational states and changes within the EF-hand protein superfamily."
] | [
1995,
1997,
1996,
1994,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1974,
61420,
465783,
898,
1556
] | 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",... | [
645,
156,
912,
228,
1,
672,
539,
21,
371,
752,
13,
13,
1017
] | 13 | true | Binding_site | EF-Hand 1, calcium-binding site | EF-Hand 1, calcium-binding site | EF_Hand_1_Ca_BS | 5 |
IPR018250 | 18,250 | Neuregulin-1 | NRG1 | Family | 2,086 | false | false | Neuregulins (NRG) are a sub-family of EGF-like molecules that have been shown to play multiple essential roles in vertebrate embryogenesis including: cardiac development, Schwann cell and oligodendrocyte differentiation, some aspects of neuronal development, as well as the formation of neuromuscular synapses [ , ]. Inc... | [
"GO:0005102",
"GO:0007399"
] | [
"signaling receptor binding",
"nervous system development"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR01089"
] | [
"NEUREGULIN"
] | [
2086
] | 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-1227986",
"R-HSA-1236394",
"R-HSA-1250196",
"R-HSA-1250342",
"R-HSA-1250347",
"R-HSA-1251985",
"R-HSA-1257604",
"R-HSA-1306955",
"R-HSA-1358803",
"R-HSA-1963640",
"R-HSA-1963642",
"R-HSA-2219530",
"R-HSA-5673001",
"R-HSA-6785631",
"R-HSA-6811558",
"R-HSA-8847993",
"R-HSA-88637... | [
"REACTOME:R-HSA-1227986",
"REACTOME:R-HSA-1236394",
"REACTOME:R-HSA-1250196",
"REACTOME:R-HSA-1250342",
"REACTOME:R-HSA-1250347",
"REACTOME:R-HSA-1251985",
"REACTOME:R-HSA-1257604",
"REACTOME:R-HSA-1306955",
"REACTOME:R-HSA-1358803",
"REACTOME:R-HSA-1963640",
"REACTOME:R-HSA-1963642",
"REACTOM... | 35 | [] | 0 | [
"PUB00003030",
"PUB00004316",
"PUB00004928",
"PUB00009788",
"PUB00091025"
] | [
"9804837",
"9208852",
"9892702",
"12145742",
"12821646"
] | [
"Sensory and motor neuron-derived factor is a transmembrane heregulin that is expressed on the plasma membrane with the active domain exposed to the extracellular environment.",
"Neuregulins and their receptors: a versatile signaling module in organogenesis and oncogenesis.",
"Failure of spinal cord oligodendro... | [
1998,
1997,
1999,
2002,
2003
] | 5 | [
"IPR040180"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
2086
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
22,
19,
30
] | 3 | true | Family | Neuregulin-1 | Neuregulin-1 | NRG1 | 1 |
IPR018251 | 18,251 | Crustacean neurohormone, conserved site | Crust_neurhormone_CS | Conserved_site | 966 | false | false | Arthropod express a family of neuropeptides [ ] which so far consist of the following types of neurohormones: Crustacean hyperglycemic hormone (CHH). CHH is primarily involved in blood sugar regulation, but also plays a role in the control of molting and reproduction. Molt-inhibiting hormone (MIH). MIH inhibits Y-organ... | [
"GO:0005184",
"GO:0005576"
] | [
"neuropeptide hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS01250"
] | [
"CHH_MIH_GIH"
] | [
966
] | 1 | [] | [] | [] | 0 | [
"1j0t",
"5b5i",
"5xs1"
] | 3 | [
"PUB00009750"
] | [
"8590372"
] | [
"Molecular biology of neurohormone precursors in the eyestalk of Crustacea."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
966
] | 1 | [
"Caenorhabditis elegans",
"Drosophila melanogaster"
] | [
1,
4
] | 2 | true | Conserved_site | Crustacean neurohormone, conserved site | Crustacean neurohormone, conserved site | Crust_neurhormone_CS | 4 |
IPR018252 | 18,252 | Annexin repeat, conserved site | Annexin_repeat_CS | Conserved_site | 23,912 | false | false | Annexins [ , , , , , , , ] are a group of calcium-binding proteins that associate reversibly with membranes. They bind to phospholipid bilayers in the presence of micromolar free calcium concentration. The binding is specific for calcium and for acidic phospholipids. Annexins have been claimed to be involved in cytoske... | [
"GO:0005509",
"GO:0005544"
] | [
"calcium ion binding",
"calcium-dependent phospholipid binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00223"
] | [
"ANNEXIN_1"
] | [
23912
] | 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-6798695",
"R-BTA-75205",
"R-BTA-9860927",
"R-CFA-6798695",
"R-CFA-75205",
"R-CFA-9860927",
"R-DDI-114608",
"R-DDI-6798695",
"R-DME-114608",
"R-DME-6798695",
"R-DME-9860927",
"R-GGA-114608",
"R-GGA-6798695",
"R-GGA-75205",
"R-GGA-9860927",
"R-HSA-114608",
"R-HSA-416476",
"R-H... | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-75205",
"REACTOME:R-BTA-9860927",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-75205",
"REACTOME:R-CFA-9860927",
"REACTOME:R-DDI-114608",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-9860927",
"REACTOME:R-GG... | 40 | [
"1a8a",
"1a8b",
"1aei",
"1aii",
"1ain",
"1ala",
"1ann",
"1anw",
"1anx",
"1aow",
"1avc",
"1avh",
"1avr",
"1axn",
"1bc0",
"1bc1",
"1bc3",
"1bcw",
"1bcy",
"1bcz",
"1bo9",
"1dk5",
"1dm5",
"1g5n",
"1hak",
"1hm6",
"1hvd",
"1hve",
"1hvf",
"1hvg",
"1i4a",
"1m9i"... | 111 | [
"PUB00000296",
"PUB00000662",
"PUB00000969",
"PUB00001198",
"PUB00001395",
"PUB00005347",
"PUB00005527",
"PUB00093767",
"PUB00093770"
] | [
"2973805",
"8155692",
"2659190",
"2147412",
"1646719",
"2539661",
"8091504",
"27071553",
"28422051"
] | [
"Ca2+-dependent phospholipid- (and membrane-) binding proteins.",
"Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins.",
"The annexin family of calcium-binding proteins. Review article.",
"The crystal and molecular structure o... | [
1988,
1994,
1989,
1990,
1991,
1989,
1994,
2016,
2017
] | 9 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
6,
23906
] | 2 | [
"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"
] | [
24,
4,
45,
5,
104,
56,
2,
17,
69,
33
] | 10 | true | Conserved_site | Annexin repeat, conserved site | Annexin repeat, conserved site | Annexin_repeat_CS | 6 |
IPR018253 | 18,253 | DnaJ domain, conserved site | DnaJ_domain_CS | Conserved_site | 144,134 | false | false | null | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00636"
] | [
"DNAJ_1"
] | [
144134
] | 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-3371453",
"R-BTA-3371497",
"R-BTA-3371568",
"R-BTA-3371571",
"R-BTA-5687128",
"R-BTA-6798695",
"R-BTA-888590",
"R-BTA-9841251",
"R-DDI-3371497",
"R-DDI-6798695",
"R-DME-6798695",
"R-DME-888590",
"R-HSA-3371453",
"R-HSA-3371497",
"R-HSA-3371568",
"R-HSA-3371571",
"R-HSA-381038"... | [
"REACTOME:R-BTA-3371453",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-3371568",
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-5687128",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-888590",
"REACTOME:R-BTA-9841251",
"REACTOME:R-DDI-3371497",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DME-6798695",
"REACTOME... | 43 | [
"1bq0",
"1bqz",
"1hdj",
"1xbl",
"2ctp",
"2ctr",
"2ctw",
"2cug",
"2dmx",
"2dn9",
"2ej7",
"2kqx",
"2lgw",
"2lo1",
"2m6y",
"2n04",
"2n05",
"2och",
"2qsa",
"3lz8",
"3ucs",
"4j7z",
"4rwu",
"4wb7",
"5nro",
"5vso",
"5y88",
"6byr",
"6d6x",
"6iws",
"6jzb",
"6n3q"... | 67 | [
"PUB00003367",
"PUB00005384",
"PUB00020790",
"PUB00033831",
"PUB00033832"
] | [
"8764403",
"1585456",
"15170475",
"11395418",
"12454054"
] | [
"NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.",
"A module of the DnaJ heat shock proteins found in malaria parasites.",
"The J-protein family: modulating protein assembly, disassembly and translocation.",
"Folding of newly translated proteins in vivo: the r... | [
1996,
1992,
2004,
2001,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
513,
38111,
104408,
139,
963
] | 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",... | [
231,
17,
65,
54,
2,
89,
67,
17,
142,
104,
16,
14,
284
] | 13 | true | Conserved_site | DnaJ domain, conserved site | DnaJ domain, conserved site | DnaJ_domain_CS | 2 |
IPR018254 | 18,254 | Large ribosomal subunit protein uL29, conserved site | Ribosomal_uL29_CS | Conserved_site | 20,136 | false | false | Ribosomal protein uL29 is one of the proteins from the large ribosomal subunit. uL29 belongs to a family of ribosomal proteins of 63 to 138 amino-acid residues which, on the basis of sequence similarities, groups: Red algal uL29. Bacterial uL29. Mammalian uL29 (known as L35) Caenorhabditis elegans uL29 (known as L35) (... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00579"
] | [
"RIBOSOMAL_L29"
] | [
20136
] | 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-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-97595... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 82 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1r73",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk"... | 1,649 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00079483",
"PUB00080476"
] | [
"11297922",
"11290319",
"11114498",
"10937990",
"12756233"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The structural basis of ribosome activity in peptide bond synthesis.",
"Interplay of signal recognition particle and trigger factor at L23 near the nascent ch... | [
2001,
2001,
2000,
2000,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
649,
16626,
2628,
233
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
13,
1,
1,
3,
1,
2,
1,
7,
2,
1
] | 10 | true | Conserved_site | Large ribosomal subunit protein uL29, conserved site | Large ribosomal subunit protein uL29, conserved site | Ribosomal_uL29_CS | 1 |
IPR018255 | 18,255 | Large ribosomal subunit protein uL16, conserved site, eukaryota/archaea | Ribosomal_uL16_CS_euk_arc | Conserved_site | 6,497 | false | false | This entry represents a conserved site found in the central region of the large ribosomal subunit protein uL16 from archaea and eukaryotes (in the latter were previously known as L10) [ , ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS01257"
] | [
"RIBOSOMAL_L10E"
] | [
6497
] | 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-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-97595... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 76 | [
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1yhq",
"1yi2",
"1yij",
"1yit",
"1yj9",
"1yjn",
"1yjw",
"2otj",
"2otl",
"2pa2",
"2qa4",
"2qex",
"3cc2",
"3cc4",
"3cc7",
"3cce",
"3ccj",
"3ccl",
"3ccm"... | 525 | [
"PUB00000257",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279"
] | [
"8780716",
"11297922",
"11290319",
"11114498",
"24524803"
] | [
"The primary structure of rat ribosomal protein L10: relationship to a Jun-binding protein and to a putative Wilms' tumor suppressor.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A new system for namin... | [
1996,
2001,
2001,
2000,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Picornavirales sp.",
"unclassified sequences"
] | [
700,
5,
5773,
1,
18
] | 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... | [
10,
1,
2,
2,
7,
5,
1,
8,
3,
1,
2,
16
] | 12 | true | Conserved_site | Large ribosomal subunit protein uL16, conserved site, eukaryota/archaea | Large ribosomal subunit protein uL16, conserved site, eukaryota/archaea | Ribosomal_uL16_CS_euk_arc | 4 |
IPR018257 | 18,257 | Large ribosomal subunit protein bL19, conserved site | Ribosomal_bL19_CS | Conserved_site | 20,805 | false | false | This entry represents a conserved region found at the C-terminal of the large ribosomal subunit protein bL19 from bacteria Red algal chloroplast (bL19c) and cyanelle [ , , ]. In Escherichia coli, bL19 is known to be located at the 30S-50S ribosomal subunit interface [ ] and may play a role in the structure and function... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS01015"
] | [
"RIBOSOMAL_L19"
] | [
20805
] | 1 | [] | [] | [] | 0 | [
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3j3v",
"3j3w",
"3j5l",
"3j7z",
"3j8g",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce",
"3jcj"... | 1,124 | [
"PUB00000273",
"PUB00001241",
"PUB00002697",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279"
] | [
"339951",
"8262035",
"1985969",
"11297922",
"11290319",
"11114498",
"24524803"
] | [
"Primary structure of protein L19 from the large subunit of Escherichia coli ribosomes.",
"Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein.",
"Cloning, sequencing, and overexpression of genes for ribosomal proteins from Bacillus stearothermophilus.",
"Atomic ... | [
1978,
1993,
1991,
2001,
2001,
2000,
2014
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
19839,
2,
557,
407
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Conserved_site | Large ribosomal subunit protein bL19, conserved site | Large ribosomal subunit protein bL19, conserved site | Ribosomal_bL19_CS | 5 |
IPR018258 | 18,258 | Large ribosomal subunit protein bL21, conserved site | Ribosomal_bL21_CS | Conserved_site | 19,081 | false | false | This entry represents the Large ribosomal subunit protein bL21 found in bacteria and eukaryotic organelles such as chloroplast and mitochondria. In Escherichia coli, bL21 is known to bind to the 23S rRNA in the presence of bL20. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities, ... | [
"GO:0003723",
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"RNA binding",
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PROSITE"
] | [
"PS01169"
] | [
"RIBOSOMAL_L21"
] | [
19081
] | 1 | [] | [] | [] | 0 | [
"2j28",
"2rdo",
"3bbx",
"3iy9",
"3j3v",
"3j3w",
"3j5l",
"3j7z",
"3j8g",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce",
"3jcj",
"3jcn",
"4csu",
"4u1u",
"4u1v",
"4u20",
"4u24",
"4u25",
"4u26",
"4u27",
"4uy8",
"4v4h",
"4v4q",
"4v50",
"4v52"... | 766 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
17066,
1742,
273
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
1,
5,
18
] | 4 | true | Conserved_site | Large ribosomal subunit protein bL21, conserved site | Large ribosomal subunit protein bL21, conserved site | Ribosomal_bL21_CS | 3 |
IPR018259 | 18,259 | Large ribosomal subunit protein eL21, conserved site | Ribosomal_eL21_CS | Conserved_site | 6,153 | false | false | The eL21 family contains proteins from a number of eukaryotic and archaebacterial organisms which include mammalian eL21, Entamoeba histolytica eL21, Caenorhabditis elegans eL21 (C14B9.7), Saccharomyces cerevisiae (Baker's yeast) eL21 (URP1) and Haloarcula marismortui eL21 (HL31). Ribosomes are the particles that catal... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS01171"
] | [
"RIBOSOMAL_L21E"
] | [
6153
] | 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-156827",
"R-CEL-1799339",
"R-CEL-72689",
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"R-CEL-975957",
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"R-HSA-156827",
"R-HSA-156902",
"R-HSA-1799339",
"R-HSA-192823",
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"R-HSA-679... | [
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"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72706",
"REACTOME:R-DDI-975956",
"REACTOME:R-DDI-97595... | 51 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 660 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
651,
8,
5480,
14
] | 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,
1,
1,
1,
5,
2,
1,
6,
14,
2,
2,
16
] | 12 | true | Conserved_site | Large ribosomal subunit protein eL21, conserved site | Large ribosomal subunit protein eL21, conserved site | Ribosomal_eL21_CS | 5 |
IPR018260 | 18,260 | Large ribosomal subunit protein uL22, conserved site | Ribosomal_uL22_CS | Conserved_site | 35,262 | false | false | Ribosomal protein uL22 is one of the proteins from the large ribosomal subunit. In Escherichia coli, uL22 is known to bind 23S rRNA [ ]. It belongs to a family of ribosomal proteins which includes: bacterial uL22; algal and plant chloroplast uL22 (in legumes uL22 is encoded in the nucleus instead of the chloroplast); c... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00464"
] | [
"RIBOSOMAL_L22"
] | [
35262
] | 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-156827",
"R-CEL-1799339",
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"R-CEL-975956",
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"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",
"R-DME-975956",
"R-DME-975957",
"R-HSA-156827",
"R-HSA-156902",
"R-HSA-1799339",
"R-HSA-192823",
"R-HSA-2408557",
"R-HSA-679... | [
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
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"REACTOME:R-DME-1799339",
"REACTOME:R-DME-72689",
"REACTOME:R-DME-72706",
"REACTOME:R-DME-975956",
"REACTOME:R-DME-97595... | 51 | [
"1bxe",
"1ffk",
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"1jj2",
"1jzx",
"1jzy",
"1jzz",
"1k01",
"1k73",
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"1k9m",
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"1kd1",
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"1m1k",
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"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4"... | 1,806 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00028498"
] | [
"11297922",
"11290319",
"11114498",
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"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution."
] | [
2001,
2001,
2000,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
394,
17575,
17012,
281
] | 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",... | [
9,
1,
1,
2,
1,
9,
5,
1,
7,
9,
2,
2,
28
] | 13 | true | Conserved_site | Large ribosomal subunit protein uL22, conserved site | Large ribosomal subunit protein uL22, conserved site | Ribosomal_uL22_CS | 5 |
IPR018261 | 18,261 | Large ribosomal subunit protein bL27, conserved site | Ribosomal_bL27_CS | Conserved_site | 25,260 | false | false | Large ribosomal subunit protein bL27 (known as L27) is a protein from the large (50S) subunit; it is essential for ribosome function, but its exact role is unclear. It belongs to a family of ribosomal proteins, examples of which are found in bacteria, chloroplasts of plants and red algae and the mitochondria of fungi (... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00831"
] | [
"RIBOSOMAL_L27"
] | [
25260
] | 1 | [] | [] | [] | 0 | [
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1v8q",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"1y69",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
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"3j5l",
"3j6b",
"3j7z",
"3j8g",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce"... | 1,128 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
21849,
3005,
406
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
10,
1,
7,
1,
1,
11
] | 6 | true | Conserved_site | Large ribosomal subunit protein bL27, conserved site | Large ribosomal subunit protein bL27, conserved site | Ribosomal_bL27_CS | 1 |
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