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
IPR017974
17,974
Claudin, conserved site
Claudin_CS
Conserved_site
20,552
false
false
This entry represents a conserved region located in an extracellular loop between the first and second transmembrane regions. Zona occludens (ZO), or tight junctions (TJ), are specialised membrane domains found at the most apical region of polarised epithelial and endothelial cells. They create a primary barrier, preve...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01346" ]
[ "CLAUDIN" ]
[ 20552 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-420029", "R-HSA-8935964", "R-HSA-9925563" ]
[ "REACTOME:R-HSA-420029", "REACTOME:R-HSA-8935964", "REACTOME:R-HSA-9925563" ]
3
[ "3x29", "4p79", "5b2g", "6ake", "6akf", "6akg", "6ov2", "6ov3", "7kp4", "7tdm", "7tdn", "8u4v", "8u5b", "9bei", "9cmh", "9cmi" ]
16
[ "PUB00003085", "PUB00003087", "PUB00004927", "PUB00005988", "PUB00009408" ]
[ "9647647", "9786950", "9892664", "10370242", "11283726" ]
[ "Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin.", "A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts.", "Claudin multigene family encoding four-transmembrane domain protein ...
[ 1998, 1998, 1999, 1999, 2001 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "bioreactor metagenome" ]
[ 81, 20470, 1 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 2, 56, 1, 52, 40, 53, 1 ]
7
true
Conserved_site
Claudin, conserved site
Claudin, conserved site
Claudin_CS
1
IPR017975
17,975
Tubulin, conserved site
Tubulin_CS
Conserved_site
64,589
false
false
Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta [ , ]. Within the microtubule lattice, α-β heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta...
[ "GO:0005525", "GO:0007017", "GO:0005874" ]
[ "GTP binding", "microtubule-based process", "microtubule" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS00227" ]
[ "TUBULIN" ]
[ 64589 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-114608", "R-BTA-190840", "R-BTA-2132295", "R-BTA-2467813", "R-BTA-2500257", "R-BTA-2565942", "R-BTA-3371497", "R-BTA-380259", "R-BTA-380270", "R-BTA-380284", "R-BTA-380320", "R-BTA-5610787", "R-BTA-5617833", "R-BTA-5620912", "R-BTA-5620924", "R-BTA-5626467", "R-BTA-5663220", ...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-190840", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-2565942", "REACTOME:R-BTA-3371497", "REACTOME:R-BTA-380259", "REACTOME:R-BTA-380270", "REACTOME:R-BTA-380284", "REACTOME:R-BTA-380320", "REACTOME:R-BT...
233
[ "1ffx", "1ia0", "1jff", "1sa0", "1sa1", "1tub", "1tvk", "1z2b", "1z5v", "1z5w", "2bto", "2btq", "2hxf", "2hxh", "2p4n", "2wbe", "2xrp", "3cb2", "3dco", "3du7", "3e22", "3edl", "3hkb", "3hkc", "3hkd", "3hke", "3iz0", "3j1t", "3j1u", "3j2u", "3j6e", "3j6f"...
784
[ "PUB00000039", "PUB00000721", "PUB00000978", "PUB00002443", "PUB00006112" ]
[ "3896122", "8274140", "2194680", "3680207", "8102497" ]
[ "Molecular biology and genetics of tubulin.", "Gamma-tubulin: the hub of cellular microtubule assemblies.", "Diversity among tubulin subunits: toward what functional end?", "Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.", "Localization of an exchangeable GT...
[ 1985, 1993, 1990, 1987, 1993 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 1007, 739, 62792, 3, 48 ]
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...
[ 46, 19, 33, 24, 93, 36, 4, 35, 66, 4, 4, 131 ]
12
true
Conserved_site
Tubulin, conserved site
Tubulin, conserved site
Tubulin_CS
4
IPR017978
17,978
GPCR family 3, C-terminal
GPCR_3_C
Domain
54,916
false
false
This entry represents the C-terminal region of family 3 GPCR receptor proteins, which contains the seven transmembrane region. The seven TM regions assemble in such a way as to produce a docking pocket into which such molecules as cyclamate and lactisole have been found to bind and consequently confer the taste of swee...
[ "GO:0004930", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PROFILE" ]
[ "PF00003", "PS50259" ]
[ "7tm_3", "G_PROTEIN_RECEP_F3_4" ]
[ 54418, 51934 ]
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-416476", "R-BTA-418594", "R-BTA-420499", "R-CEL-1296041", "R-CEL-418594", "R-CEL-420499", "R-CEL-977444", "R-CEL-997272", "R-DDI-418594", "R-DDI-420499", "R-DDI-977444", "R-DME-418594", "R-DME-420499", "R-DRE-416476", "R-DRE-420499", "R-HSA-1296041", "R-HSA-416476", "R-HSA-4...
[ "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-420499", "REACTOME:R-CEL-1296041", "REACTOME:R-CEL-418594", "REACTOME:R-CEL-420499", "REACTOME:R-CEL-977444", "REACTOME:R-CEL-997272", "REACTOME:R-DDI-418594", "REACTOME:R-DDI-420499", "REACTOME:R-DDI-977444", "REACTOME:R-DME-41...
42
[ "4oo9", "4or2", "5cgc", "5cgd", "6ffh", "6ffi", "6n4x", "6n51", "6n52", "6uo8", "6uo9", "6uoa", "6vjm", "6w2x", "6w2y", "6wiv", "7c7q", "7c7s", "7ca3", "7ca5", "7cum", "7dd5", "7dd6", "7dd7", "7dgd", "7dge", "7dtt", "7dtu", "7dtv", "7dtw", "7e6t", "7e6u"...
152
[ "PUB00004161", "PUB00004309", "PUB00004961", "PUB00007343", "PUB00036049", "PUB00036050", "PUB00044748", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "8255296", "1309649", "8170923", "9292726", "17266540", "10773016", "16076846", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid.", "A family of metabotropic glutamate receptors.", "Fingerprinting G-protein-coupled receptors.", "A new multigene family of putative pheromone receptors.", "Structure, pharmacology and therapeutic prospects o...
[ 1993, 1992, 1994, 1997, 2007, 2000, 2005, 2003, 1994, 2005, 2009, 2006, 2013 ]
13
[]
[ "IPR041946" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "metagenomes" ]
[ 82, 54818, 3, 10, 3 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 19, 162, 34, 92, 292, 253 ]
6
true
Domain
GPCR family 3, C-terminal
GPCR family 3, C-terminal
GPCR_3_C
1
IPR017979
17,979
GPCR, family 3, conserved site
GPCR_3_CS
Conserved_site
30,988
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004930", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE", "PROSITE", "PROSITE" ]
[ "PS00979", "PS00980", "PS00981" ]
[ "G_PROTEIN_RECEP_F3_1", "G_PROTEIN_RECEP_F3_2", "G_PROTEIN_RECEP_F3_3" ]
[ 10995, 13719, 27892 ]
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-416476", "R-BTA-418594", "R-BTA-420499", "R-CEL-418594", "R-CEL-420499", "R-DME-418594", "R-DME-420499", "R-DRE-416476", "R-DRE-420499", "R-HSA-1296041", "R-HSA-416476", "R-HSA-418594", "R-HSA-420499", "R-HSA-6794361", "R-HSA-9717207", "R-HSA-977444", "R-HSA-997272", "R-MMU-...
[ "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-420499", "REACTOME:R-CEL-418594", "REACTOME:R-CEL-420499", "REACTOME:R-DME-418594", "REACTOME:R-DME-420499", "REACTOME:R-DRE-416476", "REACTOME:R-DRE-420499", "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-41...
36
[ "1ewk", "1ewt", "1ewv", "1isr", "1iss", "2e4u", "2e4v", "2e4w", "2e4x", "2e4y", "2e4z", "3ks9", "3lmk", "3mq4", "3sm9", "4oo9", "4or2", "4xaq", "4xar", "4xas", "5c5c", "5cgc", "5cgd", "5cni", "5cnj", "5cnk", "5cnm", "5fbh", "5fbk", "5k5s", "5k5t", "5kzn"...
170
[ "PUB00004161", "PUB00004309", "PUB00004961", "PUB00007343", "PUB00036049", "PUB00036050", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "8255296", "1309649", "8170923", "9292726", "17266540", "10773016", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid.", "A family of metabotropic glutamate receptors.", "Fingerprinting G-protein-coupled receptors.", "A new multigene family of putative pheromone receptors.", "Structure, pharmacology and therapeutic prospects o...
[ 1993, 1992, 1994, 1997, 2007, 2000, 2003, 1994, 2005, 2009, 2006, 2013 ]
12
[]
[]
0
0
null
[ "Eukaryota" ]
[ 30988 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 128, 15, 60, 79, 82 ]
6
true
Conserved_site
GPCR, family 3, conserved site
GPCR, family 3, conserved site
GPCR_3_CS
4
IPR017980
17,980
Metallothionein, family 4, echinoidea/annelida
Metalthion_4_echinoid/annelid
Family
39
false
false
Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05522" ]
[ "Metallothio_6" ]
[ 39 ]
1
[]
[]
[]
0
[ "1qjk", "1qjl" ]
2
[ "PUB00001490", "PUB00003570", "PUB00003571", "PUB00005944", "PUB00078698" ]
[ "2959513", "1779825", "1779826", "2959504", "21633816" ]
[ "Chemistry and biochemistry of metallothionein.", "Overview of metallothionein.", "Definitions and nomenclature of metallothioneins.", "Nomenclature of metallothionein.", "Metallothionein protein evolution: a miniassay." ]
[ 1987, 1991, 1991, 1987, 2011 ]
5
[]
[ "IPR001396" ]
0
1
0
[ "Opisthokonta" ]
[ 39 ]
1
[]
[]
0
true
Family
Metallothionein, family 4, echinoidea/annelida
Metallothionein, family 4, echinoidea/annelida
Metalthion_4_echinoid/annelid
9
IPR017981
17,981
GPCR, family 2-like, 7TM
GPCR_2-like_7TM
Domain
101,834
false
false
This entry represents the transmembrane domain of family 2 GPCR receptor proteins and Frizzled proteins. The secretin-like GPCRs include secretin [ ], calcitonin [ ], parathyroid hormone/parathyroid hormone-related peptides [ ] and vasoactive intestinal peptide [ ], all of which activate adenylyl cyclase and the phosph...
[ "GO:0004888", "GO:0007166", "GO:0016020" ]
[ "transmembrane signaling receptor activity", "cell surface receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROFILE" ]
[ "PS50261" ]
[ "G_PROTEIN_RECEP_F2_4" ]
[ 101834 ]
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-418555", "R-BTA-420092", "R-CEL-4086398", "R-CEL-4086400", "R-CEL-419812", "R-CEL-4608870", "R-CEL-4641262", "R-CEL-4641263", "R-CEL-5140745", "R-CFA-373080", "R-DME-209214", "R-DME-209338", "R-DME-209387", "R-DME-209440", "R-DME-209472", "R-DME-216119", "R-DME-216217", "R-D...
[ "REACTOME:R-BTA-418555", "REACTOME:R-BTA-420092", "REACTOME:R-CEL-4086398", "REACTOME:R-CEL-4086400", "REACTOME:R-CEL-419812", "REACTOME:R-CEL-4608870", "REACTOME:R-CEL-4641262", "REACTOME:R-CEL-4641263", "REACTOME:R-CEL-5140745", "REACTOME:R-CFA-373080", "REACTOME:R-DME-209214", "REACTOME:R-D...
124
[ "4jkv", "4k5y", "4l6r", "4n4w", "4o9r", "4qim", "4qin", "4z9g", "5ee7", "5l7d", "5l7i", "5nx2", "5uz7", "5v56", "5v57", "5vai", "5vew", "5vex", "5xez", "5xf1", "5yqz", "6b3j", "6bd4", "6d32", "6d35", "6e3y", "6fj3", "6kjv", "6kk1", "6kk7", "6lmk", "6lml"...
248
[ "PUB00001208", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "1646711", "1314625", "8170923", "1658940", "1658941", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.", "Fingerprinting G-protein-coupled receptors.", "Expression cloning of an adenylate cyclase-coupled calcitonin receptor.", ...
[ 1991, 1992, 1994, 1991, 1991, 2003, 1994, 2005, 2009, 2006, 2013 ]
11
[]
[ "IPR000539", "IPR000848", "IPR031234", "IPR039125", "IPR047033", "IPR047035", "IPR047037", "IPR047938", "IPR048072" ]
0
9
0
[ "Eukaryota", "Viruses", "bird metagenome" ]
[ 101825, 7, 2 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 5, 15, 577, 66, 246, 200, 4, 2, 286, 7 ]
10
true
Domain
GPCR, family 2-like, 7TM
GPCR, family 2-like, 7TM
GPCR_2-like_7TM
8
IPR017982
17,982
Defensin, insect
Defensin_insect
Family
130
false
false
Insect defensins are a diverse family of anti-bacterial peptides, largely active against Gram-positive bacteria [ , , , , ]. All these peptides range in length from 38 to 51 amino acids. There are six conserved cysteines all involved in intrachain disulphide bonds. A schematic representation of peptides from the arthro...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR00271" ]
[ "DEFENSIN" ]
[ 130 ]
1
[]
[]
[]
0
[ "1ica", "1l4v", "2lld", "2ln4", "2nz3" ]
5
[ "PUB00000525", "PUB00001431", "PUB00001593", "PUB00002559", "PUB00002677", "PUB00004678", "PUB00097946", "PUB00097947", "PUB00097948" ]
[ "8471044", "1425705", "2401368", "2358464", "1761552", "2911573", "23137439", "22542795", "20721297" ]
[ "Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin.", "A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata).", "1H nuclear ma...
[ 1993, 1992, 1990, 1990, 1991, 1989, 2013, 2012, 2009 ]
9
[]
[]
0
0
null
[ "Neoptera" ]
[ 130 ]
1
[]
[]
0
true
Family
Defensin, insect
Defensin, insect
Defensin_insect
4
IPR017983
17,983
GPCR, family 2, secretin-like, conserved site
GPCR_2_secretin-like_CS
Conserved_site
47,835
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004930", "GO:0007186" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE", "PROSITE" ]
[ "PS00649", "PS00650" ]
[ "G_PROTEIN_RECEP_F2_1", "G_PROTEIN_RECEP_F2_2" ]
[ 19171, 43352 ]
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-418555", "R-BTA-420092", "R-CEL-419812", "R-CFA-373080", "R-DRE-419812", "R-DRE-9619665", "R-HSA-163359", "R-HSA-187024", "R-HSA-373080", "R-HSA-381676", "R-HSA-416476", "R-HSA-418555", "R-HSA-419812", "R-HSA-420092", "R-HSA-422085", "R-HSA-5683826", "R-HSA-6798695", "R-HSA-...
[ "REACTOME:R-BTA-418555", "REACTOME:R-BTA-420092", "REACTOME:R-CEL-419812", "REACTOME:R-CFA-373080", "REACTOME:R-DRE-419812", "REACTOME:R-DRE-9619665", "REACTOME:R-HSA-163359", "REACTOME:R-HSA-187024", "REACTOME:R-HSA-373080", "REACTOME:R-HSA-381676", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-41...
42
[ "1u34", "2jnc", "2jnd", "2jod", "2l27", "2qkh", "2x57", "2xdg", "3aqf", "3c4m", "3c59", "3c5t", "3ehs", "3eht", "3ehu", "3h3g", "3iol", "3l2j", "3n7p", "3n7r", "3n7s", "3n93", "3n94", "3n95", "3n96", "4ers", "4hj0", "4l6r", "4lf3", "4rwf", "4rwg", "4zgm"...
256
[ "PUB00001208", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "1646711", "1314625", "8170923", "1658940", "1658941", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.", "Fingerprinting G-protein-coupled receptors.", "Expression cloning of an adenylate cyclase-coupled calcitonin receptor.", ...
[ 1991, 1992, 1994, 1991, 1991, 2003, 1994, 2005, 2009, 2006, 2013 ]
11
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta" ]
[ 4, 47831 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 343, 11, 153, 124, 202 ]
6
true
Conserved_site
GPCR, family 2, secretin-like, conserved site
GPCR, family 2, secretin-like, conserved site
GPCR_2_secretin-like_CS
4
IPR017984
17,984
Chromo domain subgroup
Chromo_dom_subgr
Domain
10,185
false
false
The CHROMO (CHRromatin Organization MOdifier) domain [ , , , ] is a conserved region of around 60 amino acids, originally identified in Drosophila modifiers of variegation. These are proteins that alter the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible condition where ge...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR00504" ]
[ "CHROMODOMAIN" ]
[ 10185 ]
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-73772", "R-CEL-983231", "R-DME-2559580", "R-DME-3108214", "R-DME-3899300", "R-DME-4570464", "R-DME-8939243", "R-DME-8943724", "R-HSA-2559580", "R-HSA-3108214", "R-HSA-3899300", "R-HSA-427389", "R-HSA-4551638", "R-HSA-4570464", "R-HSA-4655427", "R-HSA-73772", "R-HSA-8939243", ...
[ "REACTOME:R-CEL-73772", "REACTOME:R-CEL-983231", "REACTOME:R-DME-2559580", "REACTOME:R-DME-3108214", "REACTOME:R-DME-3899300", "REACTOME:R-DME-4570464", "REACTOME:R-DME-8939243", "REACTOME:R-DME-8943724", "REACTOME:R-HSA-2559580", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-3899300", "REACTOME:R...
29
[ "1ap0", "1guw", "1kna", "1kne", "1pdq", "1pfb", "1q3l", "2d9u", "2dnt", "2dnv", "2k1b", "2k28", "2kvm", "2l11", "2l12", "2l1b", "2m2l", "2mj8", "2rsn", "2rso", "2rvl", "2rvm", "2rvn", "3dm1", "3f2u", "3fdt", "3g7l", "3gv6", "3h91", "3i8z", "3i90", "3i91"...
73
[ "PUB00004399", "PUB00004460", "PUB00004461", "PUB00005519" ]
[ "1708124", "7667093", "7501439", "1982376" ]
[ "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants.", "The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1.", "The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcriptio...
[ 1991, 1995, 1995, 1990 ]
4
[ "IPR023780" ]
[]
1
0
1
[ "Eukaryota", "viral metagenome" ]
[ 10184, 1 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 10, 2, 22, 8, 29, 23, 1, 22, 3 ]
9
true
Domain
Chromo domain subgroup
Chromo domain subgroup
Chromo_dom_subgr
2
IPR017985
17,985
DNA methylase, N-4 cytosine-specific, conserved site
MeTrfase_CN4_CS
Conserved_site
8,505
false
false
Synonym(s): N-4 cytosine-specific DNA methylase, Modification methylase Site-specific DNA-methyltransferase (cytosine-N4-specific) ( ) are enzymes that specifically methylate the amino group at the C-4 position of cytosines in DNA. In prokaryotes, the major role of DNA methylation is to protect host DNA against degrada...
[ "GO:0003677", "GO:0015667", "GO:0009307" ]
[ "DNA binding", "site-specific DNA-methyltransferase (cytosine-N4-specific) activity", "DNA restriction-modification system" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE" ]
[ "PS00093" ]
[ "N4_MTASE" ]
[ 8505 ]
1
[ "EC" ]
[ "2.1.1.113" ]
[ "EC:2.1.1.113" ]
1
[ "1boo", "2zie", "2zif", "2zig", "8s9m", "8s9n", "8s9o" ]
7
[ "PUB00000092" ]
[ "7663118" ]
[ "Structure and function of DNA methyltransferases." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 821, 6678, 243, 177, 586 ]
5
[]
[]
0
true
Conserved_site
DNA methylase, N-4 cytosine-specific, conserved site
DNA methylase, N-4 cytosine-specific, conserved site
MeTrfase_CN4_CS
9
IPR017988
17,988
Ribosome-inactivating protein conserved site
Ribosome_inactivat_prot_CS
Conserved_site
1,073
false
false
null
[ "GO:0030598", "GO:0017148" ]
[ "rRNA N-glycosylase activity", "negative regulation of translation" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00275" ]
[ "SHIGA_RICIN" ]
[ 1073 ]
1
[ "EC" ]
[ "3.2.2.22" ]
[ "EC:3.2.2.22" ]
1
[ "1abr", "1aha", "1ahb", "1ahc", "1apa", "1br5", "1br6", "1bry", "1cf5", "1d6a", "1d8v", "1dm0", "1f8q", "1ggp", "1gik", "1gis", "1giu", "1hwm", "1hwn", "1hwo", "1hwp", "1ifs", "1ift", "1ifu", "1il3", "1il4", "1il5", "1il9", "1j1m", "1j1q", "1j1r", "1j1s"...
268
[ "PUB00000690", "PUB00001175", "PUB00001357", "PUB00003312", "PUB00004654", "PUB00004990" ]
[ "1742358", "2714255", "3276522", "8411176", "3357883", "8066085" ]
[ "Conserved amino acid residues in ribosome-inactivating proteins from plants.", "Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides.", "Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosome...
[ 1991, 1989, 1988, 1993, 1988, 1994 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses" ]
[ 287, 689, 97 ]
3
[ "Zea mays" ]
[ 11 ]
1
true
Conserved_site
Ribosome-inactivating protein conserved site
Ribosome-inactivating protein conserved site
Ribosome_inactivat_prot_CS
8
IPR017989
17,989
Ribosome-inactivating protein type 1/2
Ribosome_inactivat_1/2
Family
1,712
false
false
A number of bacterial and plant toxins act by inhibiting protein synthesis in eukaryotic cells. The toxins of the shiga and ricin family inactivate 60S ribosomal subunits by an N-glycosidic cleavage which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA [ , , ]. Members of the family inclu...
[ "GO:0030598" ]
[ "rRNA N-glycosylase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00396" ]
[ "SHIGARICIN" ]
[ 1712 ]
1
[ "EC" ]
[ "3.2.2.22" ]
[ "EC:3.2.2.22" ]
1
[ "1abr", "1aha", "1ahb", "1ahc", "1apa", "1br5", "1br6", "1bry", "1ce7", "1cf5", "1d6a", "1d8v", "1f8q", "1ggp", "1gik", "1gis", "1giu", "1hwm", "1hwn", "1hwo", "1hwp", "1ifs", "1ift", "1ifu", "1il3", "1il4", "1il5", "1il9", "1j1m", "1j1q", "1j1r", "1j1s"...
290
[ "PUB00000690", "PUB00001175", "PUB00001357", "PUB00003312", "PUB00004654", "PUB00004990" ]
[ "1742358", "2714255", "3276522", "8411176", "3357883", "8066085" ]
[ "Conserved amino acid residues in ribosome-inactivating proteins from plants.", "Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides.", "Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosome...
[ 1991, 1989, 1988, 1993, 1988, 1994 ]
6
[ "IPR001574" ]
[]
1
0
1
[ "Bacteria", "Escherichia phage Lyz12581Vzw", "Eukaryota" ]
[ 156, 1, 1555 ]
3
[ "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 21 ]
2
true
Family
Ribosome-inactivating protein type 1/2
Ribosome-inactivating protein type 1/2
Ribosome_inactivat_1/2
4
IPR017990
17,990
Connexin, conserved site
Connexin_CS
Conserved_site
19,428
false
false
This entry represents a conserved site of connexins. Two sets of nomenclature have been used to identify the connexins. The first, and most commonly used, classifies the connexin molecules according to molecular weight, such as connexin43 (abbreviated to Cx43), indicating a connexin of molecular weight close to 43kDa. ...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PROSITE", "PROSITE" ]
[ "PS00407", "PS00408" ]
[ "CONNEXINS_1", "CONNEXINS_2" ]
[ 17786, 18204 ]
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-112303", "R-BTA-190704", "R-BTA-190840", "R-BTA-190861", "R-BTA-190872", "R-BTA-190873", "R-BTA-191650", "R-BTA-196025", "R-BTA-9013406", "R-CFA-190861", "R-DRE-190840", "R-DRE-190861", "R-DRE-191650", "R-DRE-9013406", "R-GGA-112303", "R-GGA-190861", "R-GGA-190872", "R-HSA-1...
[ "REACTOME:R-BTA-112303", "REACTOME:R-BTA-190704", "REACTOME:R-BTA-190840", "REACTOME:R-BTA-190861", "REACTOME:R-BTA-190872", "REACTOME:R-BTA-190873", "REACTOME:R-BTA-191650", "REACTOME:R-BTA-196025", "REACTOME:R-BTA-9013406", "REACTOME:R-CFA-190861", "REACTOME:R-DRE-190840", "REACTOME:R-DRE-19...
52
[ "2zw3", "3iz1", "3iz2", "5er7", "5era", "6l3t", "6l3u", "6l3v", "6mhq", "6mhy", "6uvr", "6uvs", "6uvt", "7f92", "7f93", "7f94", "7jjp", "7jkc", "7jlw", "7jm9", "7jmc", "7jmd", "7jn0", "7jn1", "7qeo", "7qeq", "7qer", "7qes", "7qet", "7qeu", "7qev", "7qew"...
84
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995 ]
7
[]
[]
0
0
null
[ "Bilateria" ]
[ 19428 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 68, 94, 54, 64 ]
4
true
Conserved_site
Connexin, conserved site
Connexin, conserved site
Connexin_CS
8
IPR017993
17,993
Atrophin-1
Atrophin-1
Family
1,126
false
false
Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxi...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR01222" ]
[ "ATROPHIN" ]
[ 1126 ]
1
[ "REACTOME" ]
[ "R-HSA-8943724" ]
[ "REACTOME:R-HSA-8943724" ]
1
[]
0
[ "PUB00019181", "PUB00019182" ]
[ "9647693", "11264541" ]
[ "Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins.", "Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity." ]
[ 1998, 2001 ]
2
[ "IPR002951" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "uncultured Caudovirales phage" ]
[ 8, 1116, 2 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 3, 4, 5 ]
4
true
Family
Atrophin-1
Atrophin-1
Atrophin-1
2
IPR017994
17,994
P-type trefoil, chordata
P_trefoil_chordata
Family
1,481
false
false
A cysteine-rich domain of approximately forty five amino-acid residues has been found in some extracellular eukaryotic proteins [ , , , ]. It is known as either the 'P', 'trefoil' or 'TFF' domain, and contains six cysteines linked by three disulphide bonds with connectivity 1-5, 2-4, 3-6. This leads to a characteristic...
[]
[]
[]
0
[ "PRINTS", "PANTHER" ]
[ "PR00680", "PTHR13826" ]
[ "PTREFOIL", "" ]
[ 1330, 1415 ]
2
[ "REACTOME" ]
[ "R-HSA-9018519" ]
[ "REACTOME:R-HSA-9018519" ]
1
[ "1e9t", "1hi7", "1pcp", "1pe3", "1pos", "1ps2", "1psp", "2psp", "6v1c", "6v1d", "8cb1", "8cb6" ]
12
[ "PUB00001033", "PUB00001707", "PUB00005012", "PUB00005400" ]
[ "7820556", "9187350", "8518738", "8267796" ]
[ "Trefoil peptides. Coming up clover.", "Rolling in the clover: trefoil factor family (TFF)-domain peptides, cell migration and cancer.", "A trefoil domain in the major rabbit zona pellucida protein.", "The P-domain or trefoil motif: a role in renewal and pathology of mucous epithelia?" ]
[ 1994, 1997, 1993, 1993 ]
4
[]
[]
0
0
null
[ "Ciceribacter ferrooxidans", "Eukaryota" ]
[ 3, 1478 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 7, 8 ]
3
true
Family
P-type trefoil, chordata
P-type trefoil, chordata
P_trefoil_chordata
6
IPR017995
17,995
Homeobox protein, antennapedia type
Homeobox_antennapedia
Family
9,238
false
false
The homeobox is a 60-residue motif first identified in a number of Drosophila homeotic and segmentation proteins, but now known to be well-conserved in many other animals, including vertebrates [ , ]. Proteins containing homeobox domains are likely to play an important role in development - most are known to be sequenc...
[ "GO:0003677", "GO:0003700", "GO:0006355", "GO:0005634" ]
[ "DNA binding", "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "nucleus" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR00025" ]
[ "ANTENNAPEDIA" ]
[ 9238 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-210745", "R-HSA-210747", "R-HSA-5617472", "R-HSA-9830364", "R-HSA-9925561", "R-HSA-9925563", "R-HSA-9937080" ]
[ "REACTOME:R-HSA-210745", "REACTOME:R-HSA-210747", "REACTOME:R-HSA-5617472", "REACTOME:R-HSA-9830364", "REACTOME:R-HSA-9925561", "REACTOME:R-HSA-9925563", "REACTOME:R-HSA-9937080" ]
7
[ "1b8i", "2r5y", "2r5z", "4cyc", "4uut" ]
5
[ "PUB00000591", "PUB00000881", "PUB00005390" ]
[ "2568852", "1358459", "1357790" ]
[ "The structure and function of the homeodomain.", "Vertebrate homeobox gene nomenclature.", "The homeobox in perspective." ]
[ 1989, 1992, 1992 ]
3
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 9238 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 21, 13, 15, 21, 19 ]
6
true
Family
Homeobox protein, antennapedia type
Homeobox protein, antennapedia type
Homeobox_antennapedia
1
IPR017996
17,996
Major royal jelly/yellow-related
MRJP/yellow-related
Family
9,618
false
false
This family describes major royal jelly protein and other yellow-related proteins mostly found in insects. It includes dopaminechrome tautomerase (DPT) which is enconded by the yellow-h gene in Drosophila. DPT catalyzes the conversion of dopaminechrome to 5,6-dihydroxyindole in the eumelanin biosynthetic pathway origin...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF03022", "PR01366", "PTHR10009" ]
[ "MRJP", "ROYALJELLY", "" ]
[ 9412, 2154, 9273 ]
3
[]
[]
[]
0
[ "2qe8", "3q6k", "3q6p", "3q6t", "5yyl", "7asd", "9w1k", "9w2c" ]
8
[ "PUB00006672", "PUB00006678", "PUB00006681", "PUB00032734", "PUB00044651", "PUB00071140", "PUB00079186", "PUB00101888", "PUB00160369" ]
[ "9791542", "10380654", "10441680", "9600888", "11934851", "20656794", "12164780", "34388859", "21795673" ]
[ "A family of major royal jelly proteins of the honeybee Apis mellifera L.", "Molecular characterization of MRJP3, highly polymorphic protein of honeybee (Apis mellifera) royal jelly.", "The family of major royal jelly proteins and its evolution.", "Photoactive yellow protein: a structural prototype for the th...
[ 1998, 1999, 1999, 1998, 2002, 2011, 2002, 2022, 2011 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 9, 3346, 6254, 9 ]
4
[ "Drosophila melanogaster", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 29, 1 ]
2
true
Family
Major royal jelly/yellow-related
Major royal jelly/yellow-related
MRJP/yellow-related
3
IPR017997
17,997
Vinculin
Vinculin
Family
3,568
false
false
Vinculin is an actin filament (F-actin) binding protein involved in cell-matrix adhesion and cell-cell adhesion [ ]. In addition to actin, vinculin interacts with other structural proteins such as talin and alpha-actinins [ ]. Vinculin is a large protein of 116kDa (about a 1000 residues). Structurally the protein consi...
[ "GO:0003779" ]
[ "actin binding" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR46180" ]
[ "" ]
[ 3568 ]
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-114608", "R-CEL-445355", "R-CEL-5674135", "R-CEL-6798695", "R-CEL-9764561", "R-DME-114608", "R-DME-445355", "R-DME-5674135", "R-DME-6798695", "R-DME-9764561", "R-GGA-114608", "R-GGA-445355", "R-GGA-5674135", "R-GGA-6798695", "R-GGA-9764561", "R-HSA-114608", "R-HSA-445355", "...
[ "REACTOME:R-CEL-114608", "REACTOME:R-CEL-445355", "REACTOME:R-CEL-5674135", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-9764561", "REACTOME:R-DME-114608", "REACTOME:R-DME-445355", "REACTOME:R-DME-5674135", "REACTOME:R-DME-6798695", "REACTOME:R-DME-9764561", "REACTOME:R-GGA-114608", "REACTOME:R-G...
50
[ "1qkr", "1rkc", "1rke", "1st6", "1syq", "1t01", "1tr2", "1u6h", "1xwj", "1ydi", "1zvz", "1zw2", "1zw3", "2gdc", "2gww", "2hsq", "2ibf", "3h2u", "3h2v", "3jbi", "3jbk", "3myi", "3rf3", "3s90", "3tj5", "3tj6", "3vf0", "3zdl", "4dj9", "4e17", "4e18", "4ehp"...
51
[ "PUB00000977", "PUB00085941" ]
[ "2112986", "28401269" ]
[ "Vinculin.", "Vinculin in cell-cell and cell-matrix adhesions." ]
[ 1990, 2017 ]
2
[ "IPR006077" ]
[]
1
0
1
[ "Eukaryota", "Pseudomonadati" ]
[ 3563, 5 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 3, 9, 4, 4 ]
6
true
Family
Vinculin
Vinculin
Vinculin
7
IPR017998
17,998
T-complex protein 1
TCP-1
Family
51,760
false
false
Protein folding is generally thought to result solely from properties inherent in the polypeptide primary sequence. However, additional proteins known as molecular chaperones are sometimes required to mediate correct folding and subsequent oligomer assembly [ ]. These chaperones bind to specific protein surfaces, preve...
[ "GO:0140662" ]
[ "ATP-dependent protein folding chaperone" ]
[ "molecular_function" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00304", "PTHR11353" ]
[ "TCOMPLEXTCP1", "" ]
[ 47157, 49391 ]
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-390471", "R-BTA-6798695", "R-BTA-6814122", "R-BTA-9013418", "R-BTA-9013422", "R-CEL-390471", "R-CEL-6798695", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6798695", "R-DDI-6814122", "R-DDI-9013418", "R-DDI-9013422", "R-DME-390471", "R-DME-6814122", "R-GGA-390471", "R-GGA-6814122", ...
[ "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6814122", "REACTOME:R-BTA-9013418", "REACTOME:R-BTA-9013422", "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-6814122", "REACTOME:R...
45
[ "1a6d", "1a6e", "1ass", "1asx", "1e0r", "1gml", "1gn1", "1q2v", "1q3q", "1q3r", "1q3s", "3aq1", "3iyf", "3iyg", "3izh", "3izi", "3izj", "3izk", "3izl", "3izm", "3izn", "3j02", "3j03", "3j1b", "3j1c", "3j1e", "3j1f", "3j3x", "3kfb", "3kfe", "3kfk", "3ko1"...
145
[ "PUB00001821", "PUB00004022", "PUB00004112", "PUB00044610" ]
[ "1487154", "2897629", "1836250", "1348353" ]
[ "Cloning of a cDNA encoding the Tcp-1 (t complex polypeptide 1) homologue of Arabidopsis thaliana.", "Homologous plant and bacterial proteins chaperone oligomeric protein assembly.", "A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.", "Is ...
[ 1992, 1988, 1991, 1992 ]
4
[ "IPR002423" ]
[ "IPR012714", "IPR012715", "IPR012716", "IPR012717", "IPR012718", "IPR012719", "IPR012720", "IPR012721", "IPR012722" ]
1
9
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2774, 969, 47668, 52, 297 ]
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...
[ 29, 12, 18, 12, 77, 70, 8, 41, 46, 8, 8, 120 ]
12
true
Family
T-complex protein 1
T-complex protein 1
TCP-1
7
IPR018000
18,000
Neurotransmitter-gated ion-channel, conserved site
Neurotransmitter_ion_chnl_CS
Conserved_site
76,814
false
false
This entry represents a conserved site based around two highly conserved cysteines in the N-terminal of AchR/GABA/5HT3/Gly receptors. The residues between these two cysteines are also well conserved. In AchR, these cysteine residues have been shown to form a disulphide bond essential to the tertiary structure of the re...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00236" ]
[ "NEUROTR_ION_CHANNEL" ]
[ 76814 ]
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-112314", "R-BTA-629587", "R-BTA-629594", "R-BTA-629597", "R-BTA-977443", "R-CEL-112314", "R-CEL-629587", "R-CEL-629594", "R-CEL-629597", "R-CEL-6798695", "R-CEL-977443", "R-DME-112314", "R-DME-629587", "R-DME-629594", "R-DME-629597", "R-DME-6798695", "R-DME-977443", "R-DRE-1...
[ "REACTOME:R-BTA-112314", "REACTOME:R-BTA-629587", "REACTOME:R-BTA-629594", "REACTOME:R-BTA-629597", "REACTOME:R-BTA-977443", "REACTOME:R-CEL-112314", "REACTOME:R-CEL-629587", "REACTOME:R-CEL-629594", "REACTOME:R-CEL-629597", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-977443", "REACTOME:R-DME-11...
44
[ "2bg9", "2qc1", "3jad", "3jae", "3jaf", "3rhw", "3ri5", "3ria", "3rif", "4aq5", "4aq9", "4bog", "4boi", "4bon", "4boo", "4bor", "4bot", "4cof", "4d01", "4pir", "4tnv", "4tnw", "4uxu", "4uy2", "5bkf", "5bkg", "5cfb", "5fjv", "5hbt", "5hbv", "5kxi", "5o8f"...
393
[ "PUB00002675", "PUB00003455", "PUB00010340", "PUB00044612", "PUB00044613", "PUB00044614", "PUB00044615" ]
[ "1721053", "1846404", "10026168", "18446614", "15383648", "18760291", "15165736" ]
[ "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.", "Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.", "Structural features of the ligand-binding domain of the serotonin 5HT3 receptor.", "Assembly and...
[ 1991, 1991, 1999, 2008, 2004, 2008, 2004 ]
7
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Imitervirales", "metagenomes" ]
[ 84, 76721, 3, 6 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 139, 191, 76, 146, 116, 173 ]
6
true
Conserved_site
Neurotransmitter-gated ion-channel, conserved site
Neurotransmitter-gated ion-channel, conserved site
Neurotransmitter_ion_chnl_CS
1
IPR018002
18,002
Herpesvirus UL45
Herpes_UL45
Family
53
false
false
This family consists several UL45 proteins found in the herpes simplex virus family. The herpes simplex virus UL45 gene encodes an 18kDa virion envelope protein whose function remains unknown. It has been suggested that the 18kDa UL45 gene product is required for efficient growth in the central nervous system at low do...
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF003509" ]
[ "Herpes_UL45" ]
[ 53 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011352" ]
[ "11958453" ]
[ "Mutation of the herpes simplex virus 1 KOS UL45 gene reveals dose dependent effects on central nervous system growth." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Simplexvirus" ]
[ 53 ]
1
[]
[]
0
true
Family
Herpesvirus UL45
Herpesvirus UL45
Herpes_UL45
3
IPR018004
18,004
KilA/APSES-type HTH, DNA-binding
KilA/APSES_HTH
Domain
13,063
false
false
The amino-terminal module of the poxvirus D6R/NIR proteins defines a novel conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses [ ]. Putative proteins with homology to the KilA-N domain have also been identified in Maverick transposable...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF04383", "SM01252" ]
[ "KilA-N", "KilA-N" ]
[ 11741, 12082 ]
2
[]
[]
[]
0
[ "1bm8", "1l3g", "1mb1", "4ux5", "5ybx", "5yc2", "5yca", "6a6w" ]
8
[ "PUB00010111", "PUB00043670" ]
[ "11897024", "17034960" ]
[ "Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors.", "Mavericks, a novel class of giant transposable elements widespread in eukaryotes and related to DNA viruses." ]
[ 2002, 2007 ]
2
[]
[ "IPR017880" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "metagenomes" ]
[ 4251, 8062, 22, 628, 100 ]
5
[ "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)" ]
[ 4, 4, 4 ]
3
true
Domain
KilA/APSES-type HTH, DNA-binding
KilA/APSES-type HTH, DNA-binding
KilA/APSES_HTH
2
IPR018006
18,006
Flagellar FliJ, proteobacteria
Flag_FliJ_proteobac
Family
3,547
false
false
Many flagellar proteins are exported by a flagellum-specific export pathway. Attempts have been made to characterise the apparatus responsible for this process, by designing assays to screen for mutants with export defects [ ]. Experiments involving filament removal from temperature-sensitive flagellar mutants of Salmo...
[ "GO:0003774", "GO:0006935", "GO:0071973", "GO:0009288", "GO:0016020" ]
[ "cytoskeletal motor activity", "chemotaxis", "bacterial-type flagellum-dependent cell motility", "bacterial-type flagellum", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component", "cellular_component" ]
5
[ "PIRSF", "PRINTS" ]
[ "PIRSF019404", "PR01004" ]
[ "FliJ", "FLGFLIJ" ]
[ 3328, 3299 ]
2
[]
[]
[]
0
[ "3ajw", "8ftw", "8ftx" ]
3
[ "PUB00002143" ]
[ "1646201" ]
[ "Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits." ]
[ 1991 ]
1
[ "IPR012823" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 3518, 2, 27 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar FliJ, proteobacteria
Flagellar FliJ, proteobacteria
Flag_FliJ_proteobac
9
IPR018011
18,011
Carbohydrate sulfotransferase 8-10
Carb_sulfotrans_8-10
Family
13,898
false
false
This entry consists of a number of carbohydrate sulphotransferases that transfer sulphate to carbohydrate groups in glycoproteins and glycolipids. These include: Carbohydrate sulphotransferases 8 and 9, which transfer sulphate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O...
[ "GO:0008146", "GO:0016051", "GO:0016020" ]
[ "sulfotransferase activity", "carbohydrate biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PANTHER" ]
[ "PTHR12137" ]
[ "" ]
[ 13898 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.8.2", "R-DRE-2022870", "R-DRE-2022923", "R-DRE-975578", "R-DRE-9939291", "R-HSA-2022870", "R-HSA-2022923", "R-HSA-3595174", "R-HSA-975578", "R-HSA-9939291", "R-MMU-2022870", "R-MMU-2022923", "R-MMU-975578", "R-MMU-9939291", "R-RNO-2022870", "R-RNO-975578", "R-RNO-9939291" ]
[ "EC:2.8.2", "REACTOME:R-DRE-2022870", "REACTOME:R-DRE-2022923", "REACTOME:R-DRE-975578", "REACTOME:R-DRE-9939291", "REACTOME:R-HSA-2022870", "REACTOME:R-HSA-2022923", "REACTOME:R-HSA-3595174", "REACTOME:R-HSA-975578", "REACTOME:R-HSA-9939291", "REACTOME:R-MMU-2022870", "REACTOME:R-MMU-2022923"...
17
[]
0
[ "PUB00033954", "PUB00033955", "PUB00033956", "PUB00033957" ]
[ "11445554", "9478973", "10781601", "11470797" ]
[ "Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans.", "Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion mol...
[ 2001, 1998, 2000, 2001 ]
4
[ "IPR005331" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 3, 1776, 12064, 7, 48 ]
5
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 68, 6, 18, 20, 24 ]
5
true
Family
Carbohydrate sulfotransferase 8-10
Carbohydrate sulfotransferase 8-10
Carb_sulfotrans_8-10
4
IPR018013
18,013
Nucleoside-specific channel-forming protein, Tsx-like
Channel_Tsx-like
Family
5,565
false
false
The tsx gene of Escherichia coli encodes an outer membrane protein, Tsx, which constitutes the receptor for colicin K and Bacteriophage T6, and functions as a substrate-specific channel for nucleosides and deoxy-nucleosides [ ]. The protein contains 294 amino acids, the first 22 of which are characteristic of a bacteri...
[ "GO:0009279" ]
[ "cell outer membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF03502" ]
[ "Channel_Tsx" ]
[ 5565 ]
1
[]
[]
[]
0
[ "1tlw", "1tly", "1tlz" ]
3
[ "PUB00006257" ]
[ "2265760" ]
[ "Analysis of the tsx gene, which encodes a nucleoside-specific channel-forming protein (Tsx) in the outer membrane of Escherichia coli." ]
[ 1990 ]
1
[]
[ "IPR003055" ]
0
1
0
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 5555, 2, 8 ]
3
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Nucleoside-specific channel-forming protein, Tsx-like
Nucleoside-specific channel-forming protein, Tsx-like
Channel_Tsx-like
7
IPR018016
18,016
Nucleoside phosphorylase, conserved site
Nucleoside_phosphorylase_CS
Conserved_site
13,961
false
false
The following phosphorylases are in the same family: Purine nucleoside phosphorylase ( ) (PNP) from most bacteria (gene deoD), which catalyses the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [ ]. Uridine phosphorylase ( ) (UdRPase) from bacteria (gene udp) and mammals, which cat...
[ "GO:0016763" ]
[ "pentosyltransferase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01232" ]
[ "PNP_UDP_1" ]
[ 13961 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.4.2.1", "PWY-4202", "PWY-5532", "PWY-5695", "PWY-6608", "PWY-6609", "PWY-6611", "PWY-6620", "PWY-6627", "PWY-6644", "PWY-7179", "PWY-8440", "R-HSA-73614", "R-HSA-73621", "R-MMU-73614", "R-MMU-73621" ]
[ "EC:2.4.2.1", "METACYC:PWY-4202", "METACYC:PWY-5532", "METACYC:PWY-5695", "METACYC:PWY-6608", "METACYC:PWY-6609", "METACYC:PWY-6611", "METACYC:PWY-6620", "METACYC:PWY-6627", "METACYC:PWY-6644", "METACYC:PWY-7179", "METACYC:PWY-8440", "REACTOME:R-HSA-73614", "REACTOME:R-HSA-73621", "REACT...
16
[ "1a69", "1ecp", "1jds", "1jdt", "1jdu", "1jdv", "1jdz", "1je0", "1je1", "1jp7", "1jpv", "1k3f", "1k9s", "1lx7", "1odi", "1odj", "1odk", "1odl", "1otx", "1oty", "1ou4", "1oum", "1ov6", "1ovg", "1pk7", "1pk9", "1pke", "1pr0", "1pr1", "1pr2", "1pr4", "1pr5"...
189
[ "PUB00000763", "PUB00002872", "PUB00002902" ]
[ "8534998", "7929153", "7744869" ]
[ "Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp.", "Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosph...
[ 1995, 1994, 1995 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctjdk2", "unclassified sequences" ]
[ 763, 11285, 1800, 1, 112 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 1, 2, 7, 13, 4 ]
7
true
Conserved_site
Nucleoside phosphorylase, conserved site
Nucleoside phosphorylase, conserved site
Nucleoside_phosphorylase_CS
2
IPR018020
18,020
Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
OHCU_decarboxylase
Domain
14,179
false
false
The proteins in this entry are OHCU decarboxylase, an enzyme of the purine catabolism that catalyses the conversion of OHCU into S(+)-allantoin [ ]; it is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalysed by urate oxidase ( ) and step two is catalysed by hydroxyisou...
[]
[]
[]
0
[ "PFAM" ]
[ "PF09349" ]
[ "OHCU_decarbox" ]
[ 14179 ]
1
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "4.1.1.97", "PWY-5691", "PWY-7394", "PWY-7849" ]
[ "EC:4.1.1.97", "METACYC:PWY-5691", "METACYC:PWY-7394", "METACYC:PWY-7849" ]
4
[ "2o70", "2o73", "2o74", "2o8i", "2q37", "3o7h", "3o7i", "3o7j", "3o7k", "5uou", "5z5m" ]
11
[ "PUB00042841" ]
[ "16462750" ]
[ "Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes." ]
[ 2006 ]
1
[]
[ "IPR017580", "IPR017595" ]
0
2
0
[ "Bacteria", "Eukaryota", "Halobacteriales", "unclassified sequences" ]
[ 10519, 3548, 41, 71 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 6, 1, 1, 2, 1, 6, 2, 9 ]
8
true
Domain
Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
OHCU_decarboxylase
3
IPR018022
18,022
IPP transferase
IPT
Family
32,769
false
false
This entry represents tRNA dimethylallyltransferase, also known as delta(2)-isopentenylpyrophosphate transferase, IPP transferral and 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. This enzyme catalyses the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladeno...
[ "GO:0052381", "GO:0008033" ]
[ "tRNA dimethylallyltransferase activity", "tRNA processing" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM" ]
[ "MF_00185", "TIGR00174" ]
[ "IPP_trans", "miaA" ]
[ 32105, 31129 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME" ]
[ "2.5.1.75", "PWY-2781", "R-HSA-6782315", "R-HSA-6787450" ]
[ "EC:2.5.1.75", "METACYC:PWY-2781", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-6787450" ]
4
[ "2qgn", "2zm5", "2zxu", "3crm", "3crq", "3crr", "3d3q", "3eph", "3epj", "3epk", "3epl", "3exa", "3foz" ]
13
[ "PUB00075638", "PUB00089916" ]
[ "17062755", "3031456" ]
[ "Roles of Arabidopsis ATP/ADP isopentenyltransferases and tRNA isopentenyltransferases in cytokinin biosynthesis.", "Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae." ]
[ 2006, 1987 ]
2
[ "IPR039657" ]
[ "IPR030666" ]
1
1
0
[ "Bacteria", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences" ]
[ 27066, 5135, 1, 567 ]
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",...
[ 15, 1, 1, 2, 1, 5, 1, 1, 8, 2, 1, 1, 17 ]
13
true
Family
IPP transferase
IPP transferase
IPT
9
IPR018023
18,023
Ribosome maturation protein SBDS, conserved site
Ribosome_mat_SBDS_CS
Conserved_site
3,176
false
false
Proteins identified by this conserved site are involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes in eukaryotes. Together with the EF-2-like GTPase RIA1, they may trigger the GTP-dependent release of TIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosome...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01267" ]
[ "UPF0023" ]
[ 3176 ]
1
[]
[]
[]
0
[ "1p9q", "1t95", "2kdo", "2l9n", "2wbm", "5an9", "5anb", "5anc", "6fsw", "6qkl", "6skg" ]
11
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "bioreactor metagenome" ]
[ 101, 2, 3072, 1 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea ma...
[ 5, 1, 2, 3, 6, 2, 2, 4, 1, 1, 3 ]
11
true
Conserved_site
Ribosome maturation protein SBDS, conserved site
Ribosome maturation protein SBDS, conserved site
Ribosome_mat_SBDS_CS
3
IPR018024
18,024
Cobalamin (vitamin B12) transport protein CbiM
CbiM
Family
3,063
false
false
Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants...
[ "GO:0006824", "GO:0009236", "GO:0016020", "GO:0043190" ]
[ "cobalt ion transport", "cobalamin biosynthetic process", "membrane", "ATP-binding cassette (ABC) transporter complex" ]
[ "biological_process", "biological_process", "cellular_component", "cellular_component" ]
4
[ "HAMAP", "NCBIFAM", "PANTHER", "NCBIFAM" ]
[ "MF_01462", "NF006184", "PTHR43627", "TIGR00123" ]
[ "CbiM", "PRK08319.1", "", "cbiM" ]
[ 2951, 3005, 3063, 2922 ]
4
[ "GP", "GP" ]
[ "GenProp0277", "GenProp1094" ]
[ "GP:GenProp0277", "GP:GenProp1094" ]
2
[ "5x3x", "5x41" ]
2
[ "PUB00009744", "PUB00014672", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00035607", "PUB00056802", "PUB00070131" ]
[ "11215515", "11153269", "12869542", "17163662", "16042605", "12055304", "16352848", "20868747", "23922391" ]
[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.", "B12 trafficking in mammals: A for coenzyme escort service.", "Aerobic syn...
[ 2000, 2001, 2003, 2006, 2005, 2002, 2006, 2010, 2013 ]
9
[ "IPR002751" ]
[]
1
0
1
[ "Bacteria", "Methanobacteriati", "metagenomes" ]
[ 2776, 266, 21 ]
3
[]
[]
0
true
Family
Cobalamin (vitamin B12) transport protein CbiM
Cobalamin (vitamin B12) transport protein CbiM
CbiM
7
IPR018025
18,025
2-hydroxycarboxylate transporter, proteobacteria/firmicutes
2-OHcarbox_trans_Prot/Firm
Family
704
false
false
The 2-hydroxycarboxylate transporter family is a family of secondary transporters found exclusively in the bacterial kingdom. They function in the metabolism of the di- and tricarboxylates malate and citrate, mostly in fermentative pathways involving decarboxylation of malate or oxaloacetate [ ]. The majority of protei...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR00783" ]
[ "ccs" ]
[ 704 ]
1
[]
[]
[]
0
[ "5a1s", "5x9r", "5xar", "5xas", "5xat", "9lsh", "9lsi", "9lsj", "9lsk" ]
9
[ "PUB00034458", "PUB00034459", "PUB00034460", "PUB00044708" ]
[ "8810332", "11566984", "12949159", "16339740" ]
[ "Membrane topology of the sodium ion-dependent citrate carrier of Klebsiella pneumoniae. Evidence for a new structural class of secondary transporters.", "Bacillus subtilis YxkJ is a secondary transporter of the 2-hydroxycarboxylate transporter family that transports L-malate and citrate.", "The Bacillus subtil...
[ 1996, 2001, 2003, 2005 ]
4
[ "IPR004679" ]
[]
1
0
1
[ "Bacteria" ]
[ 704 ]
1
[]
[]
0
true
Family
2-hydroxycarboxylate transporter, proteobacteria/firmicutes
2-hydroxycarboxylate transporter, proteobacteria/firmicutes
2-OHcarbox_trans_Prot/Firm
7
IPR018026
18,026
DNA repair protein Rad4-like
DNA_repair_Rad4-like
Family
1,697
false
false
Mutations in the nucleotide excision repair (NER) pathway can cause the xeroderma pigmentosum skin cancer predisposition syndrome. NER lesions are limited to one DNA strand, but otherwise they are chemically and structurally diverse, being caused by a wide variety of genotoxic chemicals and ultraviolet radiation. The x...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR00605" ]
[ "rad4" ]
[ 1697 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-5696394", "R-DME-5696395", "R-HSA-3108214", "R-HSA-5696394", "R-HSA-5696395", "R-MMU-3108214", "R-MMU-5696394", "R-MMU-5696395", "R-SPO-3108214", "R-SPO-5696395" ]
[ "REACTOME:R-DME-5696394", "REACTOME:R-DME-5696395", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-5696394", "REACTOME:R-HSA-5696395", "REACTOME:R-MMU-3108214", "REACTOME:R-MMU-5696394", "REACTOME:R-MMU-5696395", "REACTOME:R-SPO-3108214", "REACTOME:R-SPO-5696395" ]
10
[ "2qsf", "2qsg", "2qsh", "4yir", "6cfi", "6ubf", "6ug1", "6uin", "7k04", "7m2u", "8ebs", "8ebt", "8ebu", "8ebv", "8ebw", "8ebx", "8eby" ]
17
[ "PUB00007684", "PUB00044171" ]
[ "10915862", "17882165" ]
[ "Nucleotide excision repair in yeast.", "Recognition of DNA damage by the Rad4 nucleotide excision repair protein." ]
[ 2000, 2007 ]
2
[ "IPR004583" ]
[]
1
0
1
[ "Opisthokonta" ]
[ 1697 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 2, 1, 7, 3, 2, 1, 2 ]
7
true
Family
DNA repair protein Rad4-like
DNA repair protein Rad4-like
DNA_repair_Rad4-like
9
IPR018027
18,027
Asn/Gln amidotransferase
Asn/Gln_amidotransferase
Domain
28,095
false
false
The GatB domain, the function of which is uncertain, is associated with aspartyl/glutamyl amidotransferase subunit B and glutamyl amidotransferase subunit E. These are involved in the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) i...
[ "GO:0016884" ]
[ "carbon-nitrogen ligase activity, with glutamine as amido-N-donor" ]
[ "molecular_function" ]
1
[ "PFAM", "SMART" ]
[ "PF02637", "SM00845" ]
[ "GatB_Yqey", "GatB_Yqey" ]
[ 28025, 27536 ]
2
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "6.3.5.-", "PWY-5297", "PWY-7811", "PWY-8229" ]
[ "EC:6.3.5.-", "METACYC:PWY-5297", "METACYC:PWY-7811", "METACYC:PWY-8229" ]
4
[ "1zq1", "2d6f", "2df4", "2dqn", "2f2a", "2g5h", "2g5i", "2hz7", "3al0", "3h0l", "3h0m", "3h0r", "3ip4", "3kfu", "4wj3" ]
15
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1709, 21173, 4644, 6, 563 ]
5
[ "Arabidopsis thaliana", "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 (strain ATCC 204508 / S288c)", "...
[ 3, 1, 2, 2, 3, 1, 2, 5, 1, 1, 5 ]
11
true
Domain
Asn/Gln amidotransferase
Asn/Gln amidotransferase
Asn/Gln_amidotransferase
7
IPR018028
18,028
Catalase, mono-functional, haem-containing
Catalase
Family
44,488
false
false
Catalases ( ) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [ ]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via tra...
[ "GO:0004096", "GO:0020037", "GO:0006979" ]
[ "catalase activity", "heme binding", "response to oxidative stress" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS", "PROFILE", "PANTHER" ]
[ "PR00067", "PS51402", "PTHR11465" ]
[ "CATALASE", "CATALASE_3", "" ]
[ 39425, 44086, 31936 ]
3
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "1.11.1.6", "R-BTA-3299685", "R-BTA-6798695", "R-BTA-9033241", "R-CFA-3299685", "R-CFA-6798695", "R-CFA-9033241", "R-DDI-3299685", "R-DDI-6798695", "R-DDI-9033241", "R-DME-3299685", "R-DME-6798695", "R-DME-9033241", "R-DRE-3299685", "R-DRE-6798695", "R-HSA-3299685", "R-HSA-6798695", ...
[ "EC:1.11.1.6", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-9033241", "REACTOME:R-CFA-3299685", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-9033241", "REACTOME:R-DDI-3299685", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-9033241", "REACTOME:R-DME-3299685", "REACTOME:R-DME-679...
32
[ "1a4e", "1cf9", "1dgb", "1dgf", "1dgg", "1dgh", "1e93", "1f4j", "1gg9", "1gge", "1ggf", "1ggh", "1ggj", "1ggk", "1gwe", "1gwf", "1gwh", "1h6n", "1h7k", "1hbz", "1iph", "1m7s", "1m85", "1mqf", "1nm0", "1p7y", "1p7z", "1p80", "1p81", "1qf7", "1qqw", "1qwl"...
162
[ "PUB00012765", "PUB00015054", "PUB00027249", "PUB00056180" ]
[ "11351128", "14745498", "12557185", "9287428" ]
[ "Mitochondrial catalase and oxidative injury.", "Diversity of structures and properties among catalases.", "Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution.", "Phylogenetic relationships among prokaryotic and eukaryotic catalases." ]
[ 2001, 2004, 2003, 1997 ]
4
[]
[ "IPR024168", "IPR024711", "IPR024712" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Tupanvirus", "unclassified sequences" ]
[ 193, 28997, 15160, 4, 134 ]
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",...
[ 26, 4, 2, 6, 1, 4, 8, 3, 10, 4, 2, 1, 18 ]
13
true
Family
Catalase, mono-functional, haem-containing
Catalase, mono-functional, haem-containing
Catalase
4
IPR018030
18,030
Fimbrial membrane usher, conserved site
Fimbrial_membr_usher_CS
Conserved_site
16,722
false
false
In Gram-negative bacteria the biogenesis of fimbriae (or pili) requires a two- component assembly and transport system which is composed of a periplasmic chaperone (see ) and an outer membrane protein which has been termed a molecular 'usher' [ , , ].
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01151" ]
[ "FIMBRIAL_USHER" ]
[ 16722 ]
1
[]
[]
[]
0
[ "2vqi", "3fcg", "3fip", "3ohn", "3rfz", "4j3o", "6cd2", "6e14", "6e15", "7lhg", "7lhh", "7lhi", "9bog", "9fw9", "9fwb", "9fwz", "9fx8", "9fxb", "9fxs", "9fy9" ]
20
[ "PUB00002237", "PUB00002841", "PUB00005083" ]
[ "7906265", "7909802", "7906046" ]
[ "Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli.", "Chaperone-assisted self-assembly of pili independent of cellular energy.", "Structural and evolutionary relationships between two families of bacterial extracytoplasmic chaperone proteins which function coo...
[ 1994, 1994, 1993 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobellus rubicundus", "metagenomes" ]
[ 16686, 27, 1, 8 ]
4
[ "Escherichia coli (strain K12)" ]
[ 10 ]
1
true
Conserved_site
Fimbrial membrane usher, conserved site
Fimbrial membrane usher, conserved site
Fimbrial_membr_usher_CS
1
IPR018033
18,033
D-aminoacyl-tRNA deacylase, archaeal-type
Deacylase_DtdA_arch-type
Family
1,424
false
false
D-aminoacyl-tRNA deacylases hydrolyse the ester bond between the polynucleotide and the D-amino acid, thereby preventing the accumulation of such mis-acylated and metabolically inactive tRNA molecules. Several aminoacyl-tRNA synthetases have the ability to transfer the D-isomer of their amino acid onto their cognate tR...
[ "GO:0016788", "GO:0051499", "GO:0019478" ]
[ "hydrolase activity, acting on ester bonds", "D-aminoacyl-tRNA deacylase activity", "D-amino acid catabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PIRSF" ]
[ "MF_00562", "PIRSF016210" ]
[ "Deacylase_DtdA", "UCP016210" ]
[ 786, 1002 ]
2
[ "EC" ]
[ "3.1.1.96" ]
[ "EC:3.1.1.96" ]
1
[ "1yqe", "2gfq" ]
2
[ "PUB00045161", "PUB00053895", "PUB00161740" ]
[ "17251192", "16844682", "15215500" ]
[ "GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase.", "Identification in archaea of a novel D-Tyr-tRNATyr deacylase.", "A novel Arabidopsis gene required for ethanol tolerance is conserved among plants and archaea." ]
[ 2007, 2006, 2004 ]
3
[ "IPR007508" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Embryophyta", "unclassified sequences" ]
[ 815, 2, 580, 27 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 5, 7 ]
3
true
Family
D-aminoacyl-tRNA deacylase, archaeal-type
D-aminoacyl-tRNA deacylase, archaeal-type
Deacylase_DtdA_arch-type
7
IPR018034
18,034
KRR1 interacting protein 1
Kri1
Family
4,609
false
false
The budding yeast KRR1-interacting protein 1 (Kri1) is an essential nucleolar protein required for 40S ribosome biogenesis [ ]. This entry also includes Kri1 homologues from animals and plants. Their function is not clear.
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05178", "PTHR14490" ]
[ "Kri1", "" ]
[ 4086, 4583 ]
2
[]
[]
[]
0
[ "9g25", "9g28" ]
2
[ "PUB00010176" ]
[ "11027267" ]
[ "Yeast Krr1p physically and functionally interacts with a novel essential Kri1p, and both proteins are required for 40S ribosome biogenesis in the nucleolus." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 4605, 4 ]
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...
[ 8, 1, 1, 1, 9, 3, 1, 2, 2, 1, 1, 2 ]
12
true
Family
KRR1 interacting protein 1
KRR1 interacting protein 1
Kri1
7
IPR018035
18,035
Flagellar assembly protein FliH/Type III secretion system HrpE
Flagellar_FliH/T3SS_HrpE
Domain
11,990
false
false
This entry represents a region found in the flagellar assembly protein FliH, as well as in type III secretion system protein HrpE. Many flagellar proteins are exported by a flagellum-specific export pathway. Attempts have been made to characterise the apparatus responsible for this process, by designing assays to scree...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02108" ]
[ "FliH" ]
[ 11990 ]
1
[ "GP" ]
[ "GenProp0879" ]
[ "GP:GenProp0879" ]
1
[ "5b0o" ]
1
[ "PUB00002143", "PUB00044769" ]
[ "1646201", "9045830" ]
[ "Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits.", "The hrpA and hrpC operons of Erwinia amylovora encode components of a type III pathway that secretes harpin." ]
[ 1991, 1997 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 11827, 20, 143 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Flagellar assembly protein FliH/Type III secretion system HrpE
Flagellar assembly protein FliH/Type III secretion system HrpE
Flagellar_FliH/T3SS_HrpE
5
IPR018036
18,036
Protein of unknown function DUF429, subgroup
DUF429_subgr
Family
84
false
false
This is a family of uncharacterised proteins.
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF024051" ]
[ "DUF429" ]
[ 84 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[ "IPR007362" ]
[]
1
0
1
[ "Archaea" ]
[ 84 ]
1
[]
[]
0
true
Family
Protein of unknown function DUF429, subgroup
Protein of unknown function DUF429, subgroup
DUF429_subgr
7
IPR018037
18,037
Nitrogen fixation protein FixH, Proteobacterial
FixH_proteobacterial
Family
1,567
false
false
This family consists of several Rhizobium FixH like proteins. It has been suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG [ ]. This entry represents a proteobacterial subgroup of FixH.
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF011386" ]
[ "FixH" ]
[ 1567 ]
1
[]
[]
[]
0
[ "6xkw" ]
1
[ "PUB00011338" ]
[ "2536685" ]
[ "Rhizobium meliloti fixGHI sequence predicts involvement of a specific cation pump in symbiotic nitrogen fixation." ]
[ 1989 ]
1
[ "IPR008620" ]
[]
1
0
1
[ "Bacteria", "Effrenium voratum", "ecological metagenomes" ]
[ 1557, 1, 9 ]
3
[]
[]
0
true
Family
Nitrogen fixation protein FixH, Proteobacterial
Nitrogen fixation protein FixH, Proteobacterial
FixH_proteobacterial
9
IPR018038
18,038
Large ribosomal subunit protein uL30, conserved site
Ribosomal_uL30_CS
Conserved_site
14,131
false
false
Ribosomal protein uL30 is one of the proteins from the large ribosomal subunit. uL30 belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ ], groups bacteria and archaea uL30 (known as L30), yeast mitochondrial uL30m (known as L33), and Drosophila melanogaster, Dictyostelium discoideu...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00634" ]
[ "RIBOSOMAL_L30" ]
[ 14131 ]
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...
69
[ "1bxy", "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1ml5", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo"...
1,606
[ "PUB00004400", "PUB00059244" ]
[ "1549461", "11087857" ]
[ "Yeast ribosomal proteins: XIII. Saccharomyces cerevisiae YL8A gene, interrupted with two introns, encodes a homolog of mammalian L7.", "A nucleolar protein related to ribosomal protein L7 is required for an early step in large ribosomal subunit biogenesis." ]
[ 1992, 2000 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 385, 7243, 6428, 75 ]
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, 2, 2, 1, 6, 8, 1, 6, 9, 4, 3, 15 ]
13
true
Conserved_site
Large ribosomal subunit protein uL30, conserved site
Large ribosomal subunit protein uL30, conserved site
Ribosomal_uL30_CS
3
IPR018039
18,039
Intermediate filament protein, conserved site
IF_conserved
Conserved_site
39,759
false
false
Intermediate filaments (IF) [ ] are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide. IF proteins are members of a very large multigene family of proteins, which has been subdivided in six major subgroups: Type I: Acidic cy...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00226" ]
[ "IF_ROD_1" ]
[ 39759 ]
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-264870", "R-BTA-390522", "R-BTA-438066", "R-BTA-5673001", "R-BTA-6805567", "R-BTA-6809371", "R-BTA-9013422", "R-BTA-9646399", "R-CEL-2559584", "R-CEL-4419969", "R-CEL-9013405", "R-CEL-9035034", "R-CFA-264870", "R-CFA-390522", "R-CFA-6805567", "R-CFA-6809371", "R-CFA-9013422", ...
[ "REACTOME:R-BTA-264870", "REACTOME:R-BTA-390522", "REACTOME:R-BTA-438066", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-6805567", "REACTOME:R-BTA-6809371", "REACTOME:R-BTA-9013422", "REACTOME:R-BTA-9646399", "REACTOME:R-CEL-2559584", "REACTOME:R-CEL-4419969", "REACTOME:R-CEL-9013405", "REACTOME:R...
95
[ "1gk4", "1gk6", "1x8y", "2xv5", "3tnu", "3tyy", "3v4q", "3v4w", "3v5b", "4zry", "6jfv", "6uui", "6yjd", "8rve" ]
14
[ "PUB00001053", "PUB00088643", "PUB00088644" ]
[ "2183847", "12596228", "22869704" ]
[ "Intermediate filaments: structure, assembly and molecular interactions.", "Molecular architecture of intermediate filaments.", "Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly." ]
[ 1990, 2003, 2012 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Metallosphaera hakonensis JCM 8857 = DSM 7519", "ecological metagenomes" ]
[ 69, 39687, 1, 2 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 4, 70, 188, 116, 203 ]
6
true
Conserved_site
Intermediate filament protein, conserved site
Intermediate filament protein, conserved site
IF_conserved
5
IPR018040
18,040
Pectinesterase, Tyr active site
Pectinesterase_Tyr_AS
Active_site
7,439
false
false
Pectinesterase (pectin methylesterase) catalyses the de-esterification of pectin into pectate and methanol. Pectin is one of the main components of the plant cell wall. In plants, pectinesterase plays an important role in cell wall metabolism during fruit ripening. In plant bacterial pathogens such as Erwinia carotovor...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00800" ]
[ "PECTINESTERASE_1" ]
[ 7439 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "3.1.1.11", "PWY-7246", "PWY-7248" ]
[ "EC:3.1.1.11", "METACYC:PWY-7246", "METACYC:PWY-7248" ]
3
[ "1gq8", "1xg2" ]
2
[ "PUB00004997", "PUB00016279", "PUB00016280" ]
[ "1303747", "15722470", "11162105" ]
[ "Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments.", "Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.", "Three-dimensional structure of Erwinia chrysanthemi pectin meth...
[ 1992, 2005, 2001 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "unclassified sequences" ]
[ 603, 6822, 10, 4 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 78, 22, 14 ]
3
true
Active_site
Pectinesterase, Tyr active site
Pectinesterase, Tyr active site
Pectinesterase_Tyr_AS
7
IPR018042
18,042
Aspartate kinase, conserved site
Aspartate_kinase_CS
Conserved_site
39,387
false
false
Aspartate kinase ( ) (AK) catalyzes the first reaction in the aspartate pathway; the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine [ ]. In b...
[ "GO:0004072", "GO:0008652" ]
[ "aspartate kinase activity", "amino acid biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00324" ]
[ "ASPARTOKINASE" ]
[ 39387 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.2.4", "PWY-2941", "PWY-2942", "PWY-5097", "PWY-6160", "PWY-6559", "PWY-6562", "PWY-7153", "PWY-7977", "PWY-8088", "PWY-8179", "PWY-8296" ]
[ "EC:2.7.2.4", "METACYC:PWY-2941", "METACYC:PWY-2942", "METACYC:PWY-5097", "METACYC:PWY-6160", "METACYC:PWY-6559", "METACYC:PWY-6562", "METACYC:PWY-7153", "METACYC:PWY-7977", "METACYC:PWY-8088", "METACYC:PWY-8179", "METACYC:PWY-8296" ]
12
[ "2cdq", "2hmf", "2j0w", "2j0x", "3aaw", "3ab2", "3ab4", "3c1m", "3c1n", "3c20", "3l76", "3tvi", "5yei" ]
13
[ "PUB00002476" ]
[ "2892836" ]
[ "Structure of the yeast HOM3 gene which encodes aspartokinase." ]
[ 1988 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "virus sp. ctr1v16" ]
[ 594, 33770, 4536, 486, 1 ]
5
[ "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" ]
[ 23, 3, 1, 16, 1, 1, 49 ]
7
true
Conserved_site
Aspartate kinase, conserved site
Aspartate kinase, conserved site
Aspartate_kinase_CS
9
IPR018043
18,043
Sodium:galactoside symporter, conserved site
Na/Gal_symport_CS
Conserved_site
7,647
false
false
It has been shown [ ] that integral membrane proteins that mediate the intake of a wide variety of molecules with the concomitant uptake of sodium ions (sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. This collection of sequences represents the...
[ "GO:0022857", "GO:0006814", "GO:0016020" ]
[ "transmembrane transporter activity", "sodium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS00872" ]
[ "NA_GALACTOSIDE_SYMP" ]
[ 7647 ]
1
[]
[]
[]
0
[ "4m64", "8fq9", "8t60" ]
3
[ "PUB00000660" ]
[ "8031825" ]
[ "A functional superfamily of sodium/solute symporters." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "metagenomes" ]
[ 5, 7428, 186, 1, 27 ]
5
[ "Escherichia coli (strain K12)" ]
[ 7 ]
1
true
Conserved_site
Sodium:galactoside symporter, conserved site
Sodium:galactoside symporter, conserved site
Na/Gal_symport_CS
7
IPR018044
18,044
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
Peptidase_S11
Family
46,464
false
false
This group of serine peptidases belong to MEROPS peptidase family S11 (D-Ala-D-Ala carboxypeptidase A family, clan SE). The protein fold of the peptidase domain for members of this family resembles that of D-Ala-D-Ala-carboxypeptidase B, the type example for clan SE. Proteolytic enzymes that exploit serine in their cat...
[ "GO:0009002", "GO:0006508" ]
[ "serine-type D-Ala-D-Ala carboxypeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00725" ]
[ "DADACBPTASE1" ]
[ 46464 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "3.4.16.4", "PWY-5265", "PWY-6471" ]
[ "EC:3.4.16.4", "METACYC:PWY-5265", "METACYC:PWY-6471" ]
3
[ "1es2", "1es3", "1es4", "1es5", "1esi", "1hd8", "1j9m", "1nj4", "1nzo", "1nzu", "1sdn", "1skf", "1tvf", "1xp4", "1z6f", "3a3j", "3beb", "3bec", "3hum", "3hun", "3it9", "3ita", "3itb", "3mfd", "3mzd", "3mze", "3mzf", "4drt", "4k91", "4p0m", "4ppr", "4rye"...
54
[ "PUB00000120", "PUB00000499", "PUB00000522", "PUB00003576" ]
[ "1741619", "1930140", "8439290", "7845208" ]
[ "Serine beta-lactamases and penicillin-binding proteins.", "Amino acid sequence of the penicillin-binding protein/DD-peptidase of Streptomyces K15. Predicted secondary structures of the low Mr penicillin-binding proteins of class A.", "Evolutionary families of peptidases.", "Families of serine peptidases." ]
[ 1991, 1991, 1993, 1994 ]
4
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 45991, 3, 159, 311 ]
4
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Family
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
Peptidase_S11
9
IPR018045
18,045
Sulphate anion transporter, conserved site
S04_transporter_CS
Conserved_site
22,252
false
false
A number of proteins involved in the transport of sulphate across a membrane as well as some yet uncharacterised proteins have been shown [ , ] to be evolutionary related. These proteins are: Neurospora crassa sulphate permease II (gene cys-14). Yeast sulphate permeases (genes SUL1 and SUL2). Rat sulphate anion transpo...
[ "GO:0008271", "GO:1902358" ]
[ "secondary active sulfate transmembrane transporter activity", "sulfate transmembrane transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS01130" ]
[ "SLC26A" ]
[ 22252 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-174362", "R-BTA-427601", "R-CEL-174362", "R-CEL-427601", "R-HSA-174362", "R-HSA-3560792", "R-HSA-427601", "R-HSA-5619046", "R-HSA-5619085", "R-HSA-9662361", "R-MMU-174362", "R-MMU-427601", "R-RNO-174362", "R-RNO-427601", "R-SCE-174362", "R-SCE-427601", "R-SPO-174362", "R-SPO...
[ "REACTOME:R-BTA-174362", "REACTOME:R-BTA-427601", "REACTOME:R-CEL-174362", "REACTOME:R-CEL-427601", "REACTOME:R-HSA-174362", "REACTOME:R-HSA-3560792", "REACTOME:R-HSA-427601", "REACTOME:R-HSA-5619046", "REACTOME:R-HSA-5619085", "REACTOME:R-HSA-9662361", "REACTOME:R-MMU-174362", "REACTOME:R-MMU...
18
[ "7lgu", "7lgw", "7lh2", "7lh3", "7lhv", "7s8x", "7s9a", "7s9b", "7s9c", "7s9d", "7s9e", "7sun", "7v73", "7v74", "7v75", "7wk1", "7wk7", "7wl2", "7wl7", "7wl8", "7wl9", "7wla", "7wlb", "7wle", "7xlm", "7xuh", "7xuj", "7xul", "8hzn", "8iet", "8opq", "8sgw"...
51
[ "PUB00003771", "PUB00005419" ]
[ "7616962", "8140616" ]
[ "Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulphate transporter at the plasma membrane.", "Similarities between a soybean nodulin, Neurospora crassa sulphate permease II and a putative human tumour suppressor." ]
[ 1995, 1994 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "ecological metagenomes", "uncultured Caudovirales phage" ]
[ 5691, 16519, 20, 21, 1 ]
5
[ "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 ...
[ 67, 4, 23, 1, 25, 21, 2, 33, 21, 3, 1, 35 ]
12
true
Conserved_site
Sulphate anion transporter, conserved site
Sulphate anion transporter, conserved site
S04_transporter_CS
4
IPR018046
18,046
Pili assembly chaperone, conserved site
Pili_assmbl_chaperone_CS
Conserved_site
14,318
false
false
Most Gram-negative bacteria possess a supramolecular structure - the pili - on their surface, which mediates attachment to specific receptors. Many interactive subunits are required to assemble pili, but their assembly only takes place after translocation across the cytoplasmic membrane. Periplasmic chaperones assist p...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00635" ]
[ "PILI_CHAPERONE" ]
[ 14318 ]
1
[]
[]
[]
0
[ "1bf8", "1kiu", "1klf", "1l4i", "1n0l", "1p5u", "1p5v", "1pdk", "1qpp", "1qpx", "1qun", "1z9s", "1ze3", "2co6", "2co7", "2j2z", "2j7l", "2os7", "2uy6", "2uy7", "2w07", "2wmp", "2xg4", "2xg5", "3bwu", "3dos", "3dpa", "3dpb", "3dsn", "3f65", "3f6i", "3f6l"...
66
[ "PUB00000121", "PUB00001218", "PUB00001290", "PUB00020121", "PUB00041859", "PUB00098587" ]
[ "1683764", "1348692", "8670884", "2478891", "17082819", "27353649" ]
[ "Chaperone-assisted assembly and molecular architecture of adhesive pili.", "Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.", "Molecular basis of two subfamilies of immunoglobulin-like chaperones.", "Crystal structure of chaperone protein PapD reveals an immuno...
[ 1991, 1992, 1996, 1989, 2006, 2016 ]
6
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 14292, 20, 6 ]
3
[ "Escherichia coli (strain K12)" ]
[ 10 ]
1
true
Conserved_site
Pili assembly chaperone, conserved site
Pili assembly chaperone, conserved site
Pili_assmbl_chaperone_CS
7
IPR018047
18,047
Ammonium transporter, conserved site
Ammonium_transpt_CS
Conserved_site
39,497
false
false
A number of evolutionarily-related proteins have been found to be involved in the transport of ammonium ions across membranes [ , ]. Members of this family include: Saccharomyces cerevisiae ammonium transporters MEP1, MEP2 and MEP3. Arabidopsis thaliana high affinity ammonium transporter (gene AMT1). Corynebacterium gl...
[ "GO:0008519", "GO:0072488", "GO:0016020" ]
[ "ammonium channel activity", "ammonium transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS01219" ]
[ "AMMONIUM_TRANSP" ]
[ 39497 ]
1
[]
[]
[]
0
[ "1u77", "1u7c", "1u7g", "1xqe", "1xqf", "2nmr", "2nop", "2now", "2npc", "2npd", "2npe", "2npg", "2npj", "2npk", "2ns1", "2nuu", "3c1g", "3c1h", "3c1i", "3c1j", "4nh2", "5aex", "5aez", "5af1", "5ah3", "5aid", "5fuf", "6b21", "6ej6", "6ejh", "9cs5" ]
31
[ "PUB00001260", "PUB00002982" ]
[ "8062823", "8621394" ]
[ "Identification of a high affinity NH4+ transporter from plants.", "Functional and genetic characterization of the (methyl)ammonium uptake carrier of Corynebacterium glutamicum." ]
[ 1994, 1996 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 808, 27041, 11067, 581 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "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 / AT...
[ 20, 4, 1, 3, 11, 3, 1, 17 ]
8
true
Conserved_site
Ammonium transporter, conserved site
Ammonium transporter, conserved site
Ammonium_transpt_CS
5
IPR018048
18,048
CXC chemokine, conserved site
Chemokine_CXC_CS
Conserved_site
2,530
false
false
Most members of this family of low-molecular weight proteins seem to have mitogenic, chemotactic or inflammatory activities. They are released by phagocytes, mesenchymal cells and a wide variety of tissue cells, upon exposure to inflammation [ ]. These small cytokines are also called intercrines or chemokines. They are...
[ "GO:0008009", "GO:0006955", "GO:0005576" ]
[ "chemokine activity", "immune response", "extracellular region" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS00471" ]
[ "SMALL_CYTOKINES_CXC" ]
[ 2530 ]
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-375276", "R-BTA-380108", "R-BTA-418594", "R-BTA-6798695", "R-CFA-375276", "R-CFA-380108", "R-CFA-418594", "R-DRE-380108", "R-DRE-418594", "R-GGA-380108", "R-GGA-418594", "R-GGA-6798695", "R-HSA-114608", "R-HSA-140875", "R-HSA-202733", "R-HSA-2559582", "R-HSA-375276", "R-HSA-...
[ "REACTOME:R-BTA-375276", "REACTOME:R-BTA-380108", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-6798695", "REACTOME:R-CFA-375276", "REACTOME:R-CFA-380108", "REACTOME:R-CFA-418594", "REACTOME:R-DRE-380108", "REACTOME:R-DRE-418594", "REACTOME:R-GGA-380108", "REACTOME:R-GGA-418594", "REACTOME:R-GGA-67...
41
[ "1f9p", "1f9q", "1f9r", "1f9s", "1ikl", "1ikm", "1il8", "1ilp", "1ilq", "1lv9", "1mgs", "1mi2", "1msg", "1msh", "1nap", "1o7y", "1o7z", "1o80", "1pfm", "1pfn", "1plf", "1qe6", "1qnk", "1rhp", "1rjt", "1rod", "1tvx", "2il8", "2mgs", "2r3z", "3il8", "3n52"...
74
[ "PUB00001373", "PUB00001646" ]
[ "2523801", "1639201" ]
[ "Purification of granulocyte chemotactic peptide/interleukin-8 reveals N-terminal sequence heterogeneity similar to that of beta-thromboglobulin.", "Interleukin-8, a chemotactic and inflammatory cytokine." ]
[ 1989, 1992 ]
2
[]
[]
0
0
null
[ "Bilateria", "Simian cytomegalovirus (strain Colburn)" ]
[ 2529, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 22, 29, 20 ]
4
true
Conserved_site
CXC chemokine, conserved site
CXC chemokine, conserved site
Chemokine_CXC_CS
8
IPR018049
18,049
Interleukin-7/Interleukin-9, conserved site
IL-7/IL-9_CS
Conserved_site
247
false
false
Interleukin-7 (IL-7) [ ] is a cytokine that serves as a growth factor for early lymphoid cells of both B- and T-cell lineages. Interleukin-9 (IL-9) [ ] is a cytokine that supports IL-2 independent and IL-4 independent growth of helper T-cells.
[ "GO:0005126", "GO:0008083", "GO:0006955", "GO:0005576" ]
[ "cytokine receptor binding", "growth factor activity", "immune response", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PROSITE" ]
[ "PS00255" ]
[ "INTERLEUKIN_7_9" ]
[ 247 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1266695", "R-HSA-1266695", "R-HSA-8985947", "R-MMU-1266695", "R-MMU-8985947", "R-RNO-1266695" ]
[ "REACTOME:R-BTA-1266695", "REACTOME:R-HSA-1266695", "REACTOME:R-HSA-8985947", "REACTOME:R-MMU-1266695", "REACTOME:R-MMU-8985947", "REACTOME:R-RNO-1266695" ]
6
[ "3di2", "3di3", "7ox1", "7ox2", "7ox3", "7ox4", "7ox5", "7ox6", "7xcb" ]
9
[ "PUB00002018", "PUB00003177", "PUB00015241" ]
[ "2663018", "1971295", "15335670" ]
[ "Interleukin 7: effects on early events in lymphopoiesis.", "Human P40/IL-9. Expression in activated CD4+ T cells, genomic organization, and comparison with the mouse gene.", "Hematopoietin sub-family classification based on size, gene organization and sequence homology." ]
[ 1989, 1990, 1993 ]
3
[]
[]
0
0
null
[ "Eutheria", "uncultured bacterium contig00004" ]
[ 246, 1 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 5, 5 ]
3
true
Conserved_site
Interleukin-7/Interleukin-9, conserved site
Interleukin-7/Interleukin-9, conserved site
IL-7/IL-9_CS
7
IPR018050
18,050
Phosphomannose isomerase, type I, conserved site
Pmannose_isomerase-type1_CS
Conserved_site
10,219
false
false
Phosphomannose isomerase (PMI) [ , ] is the enzyme that catalyzes the interconversion of mannose-6-phosphate and fructose-6-phosphate. In eukaryotes, it is involved in the synthesis of GDP-mannose which is a constituent of N- and O-linked glycans as well as GPI anchors. In prokaryotes, it is involved in a variety of pa...
[ "GO:0004476" ]
[ "mannose-6-phosphate isomerase activity" ]
[ "molecular_function" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS00965", "PS00966" ]
[ "PMI_I_1", "PMI_I_2" ]
[ 9838, 6571 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.3.1.8", "PWY-3861", "PWY-3881", "PWY-5659", "PWY-6992", "PWY-7456", "PWY-7586", "R-BTA-446205", "R-CEL-446205", "R-DDI-446205", "R-HSA-4043916", "R-HSA-446205", "R-MMU-446205", "R-RNO-446205", "R-SCE-446205", "R-SPO-446205" ]
[ "EC:5.3.1.8", "METACYC:PWY-3861", "METACYC:PWY-3881", "METACYC:PWY-5659", "METACYC:PWY-6992", "METACYC:PWY-7456", "METACYC:PWY-7586", "REACTOME:R-BTA-446205", "REACTOME:R-CEL-446205", "REACTOME:R-DDI-446205", "REACTOME:R-HSA-4043916", "REACTOME:R-HSA-446205", "REACTOME:R-MMU-446205", "REAC...
16
[ "1pmi", "2wfp", "3h1m", "3h1w", "3h1y", "5nw7", "5zt4", "5zt5", "5zt6", "5zuw", "5zuy", "5zv0", "5zvr", "5zvu", "5zvx" ]
15
[ "PUB00000378", "PUB00001448", "PUB00003929" ]
[ "8260497", "8307007", "8612079" ]
[ "Identification of Cys-150 in the active site of phosphomannose isomerase from Candida albicans.", "Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase.", "The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution." ]
[ 1993, 1994, 1996 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 4512, 5695, 12 ]
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",...
[ 12, 2, 3, 1, 1, 19, 3, 1, 7, 3, 1, 1, 14 ]
13
true
Conserved_site
Phosphomannose isomerase, type I, conserved site
Phosphomannose isomerase, type I, conserved site
Pmannose_isomerase-type1_CS
9
IPR018051
18,051
Surfactant-associated polypeptide, palmitoylation site
SP-C_palmitoylation_site
PTM
281
false
false
This entry represents the palmitoylation site of surfactant associated polypeptide SP-C (also known as Surfactant protein C) and similar mammal proteins. Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a ...
[ "GO:0007585", "GO:0005576" ]
[ "respiratory gaseous exchange by respiratory system", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PROSITE" ]
[ "PS00341" ]
[ "SURFACT_PALMITOYL" ]
[ 281 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-5683826", "R-HSA-5688354", "R-HSA-5688849", "R-HSA-5688890", "R-MMU-5683826", "R-RNO-5683826" ]
[ "REACTOME:R-HSA-5683826", "REACTOME:R-HSA-5688354", "REACTOME:R-HSA-5688849", "REACTOME:R-HSA-5688890", "REACTOME:R-MMU-5683826", "REACTOME:R-RNO-5683826" ]
6
[ "1spf" ]
1
[ "PUB00001605", "PUB00004706" ]
[ "2015882", "2326260" ]
[ "Canine hydrophobic surfactant polypeptide SP-C. A lipopeptide with one thioester-linked palmitoyl group.", "Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups." ]
[ 1991, 1990 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 2, 279 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 2, 4 ]
3
true
PTM
Surfactant-associated polypeptide, palmitoylation site
Surfactant-associated polypeptide, palmitoylation site
SP-C_palmitoylation_site
2
IPR018052
18,052
Aldose 1-epimerase, conserved site
Ald1_epimerase_CS
Conserved_site
11,659
false
false
Aldose 1-epimerase ( ) (mutarotase) is the enzyme responsible for the anomeric interconversion of D-glucose and other aldoses between their alpha- and beta-forms. The sequence of mutarotase from two bacteria, Acinetobacter calcoaceticus and Streptococcus thermophilus is available [ ]. It has also been shown that, on th...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00545" ]
[ "ALDOSE_1_EPIMERASE" ]
[ 11659 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.1.3.3", "PWY-6317", "R-BTA-70370", "R-HSA-70370", "R-HSA-9931929", "R-MMU-70370", "R-RNO-70370", "R-SCE-70370", "R-SPO-70370", "R-SSC-70370" ]
[ "EC:5.1.3.3", "METACYC:PWY-6317", "REACTOME:R-BTA-70370", "REACTOME:R-HSA-70370", "REACTOME:R-HSA-9931929", "REACTOME:R-MMU-70370", "REACTOME:R-RNO-70370", "REACTOME:R-SCE-70370", "REACTOME:R-SPO-70370", "REACTOME:R-SSC-70370" ]
10
[ "1snz", "1so0", "1yga", "1z45" ]
4
[ "PUB00002113" ]
[ "1694527" ]
[ "Carbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-epimerase." ]
[ 1990 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 3, 8903, 2695, 58 ]
4
[ "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)", "Schizosaccharomyces pombe...
[ 2, 3, 1, 4, 3, 1, 5, 3, 1 ]
9
true
Conserved_site
Aldose 1-epimerase, conserved site
Aldose 1-epimerase, conserved site
Ald1_epimerase_CS
7
IPR018053
18,053
Glycoside hydrolase, family 32, active site
Glyco_hydro_32_AS
Active_site
12,691
false
false
It has been shown [ , ] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities: Inulinase ( ) (or inulase) from the fungi Kluyveromyces marxianus (Yeast) (Candida kefyr). Beta-fructofuranosidase ( ), commonly known as invertase in fungi and plants and as sucr...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00609" ]
[ "GLYCOSYL_HYDROL_F32" ]
[ 12691 ]
1
[ "EC", "METACYC" ]
[ "3.2.1.26", "PWY-8314" ]
[ "EC:3.2.1.26", "METACYC:PWY-8314" ]
2
[ "1st8", "1uyp", "1w2t", "1y4w", "1y9g", "1y9m", "2ac1", "2add", "2ade", "2aey", "2aez", "2oxb", "2qqu", "2qqv", "2xqr", "3kf3", "3kf5", "3u75", "4eqv", "6j0t", "6nob", "6nu7", "6nu8", "7bwb", "8beq" ]
25
[ "PUB00000503", "PUB00002122", "PUB00002555" ]
[ "1747104", "2254250", "2113524" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Cloning and sequencing of the sacA gene: characterization of a sucrase from Zymomonas mobilis.", "Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis." ]
[ 1991, 1990, 1990 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "metagenomes" ]
[ 8560, 4002, 101, 28 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 22, 27, 1, 2, 28 ]
5
true
Active_site
Glycoside hydrolase, family 32, active site
Glycoside hydrolase, family 32, active site
Glyco_hydro_32_AS
9
IPR018054
18,054
Chromogranin, conserved site
Chromogranin_CS
Conserved_site
1,919
false
false
Granins (chromogranins or secretogranins) [ ] are a family of acidic proteins present in the secretory granules of a wide variety of endocrine and neuro-endocrine cells. The exact function(s) of these proteins is not yet known but they seem to be the precursors of biologically active peptides and/or they may act as hel...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS00422", "PS00423" ]
[ "GRANINS_1", "GRANINS_2" ]
[ 1763, 919 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-381426", "R-BTA-8957275", "R-HSA-381426", "R-HSA-6803157", "R-HSA-8957275", "R-MMU-381426", "R-MMU-6803157", "R-MMU-8957275", "R-RNO-381426", "R-RNO-6803157", "R-RNO-8957275", "R-SSC-381426", "R-SSC-8957275" ]
[ "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-6803157", "REACTOME:R-HSA-8957275", "REACTOME:R-MMU-381426", "REACTOME:R-MMU-6803157", "REACTOME:R-MMU-8957275", "REACTOME:R-RNO-381426", "REACTOME:R-RNO-6803157", "REACTOME:R-RNO-8957275", "REACTOME:R-...
13
[]
0
[ "PUB00005374" ]
[ "2053134" ]
[ "The granin (chromogranin/secretogranin) family." ]
[ 1991 ]
1
[]
[]
0
0
null
[ "Bacteria", "Halorientalis brevis", "Opisthokonta" ]
[ 42, 1, 1876 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 9, 8, 21 ]
4
true
Conserved_site
Chromogranin, conserved site
Chromogranin, conserved site
Chromogranin_CS
6
IPR018056
18,056
Kringle, conserved site
Kringle_CS
Conserved_site
18,153
false
false
Kringles are autonomous structural domains, found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity [ , , ]. Kringle domains [ , , ] are characterised...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00021" ]
[ "KRINGLE_1" ]
[ 18153 ]
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-6798695", "R-BTA-75205", "R-CEL-5140745", "R-CFA-114608", "R-CFA-1257604", "R-CFA-5673001", "R-CFA-6806942", "R-CFA-6807004", "R-CFA-6811558", "R-CFA-8851805", "R-CFA-8851907", "R-CFA-8865999", "R-CFA-8874081", "R-CFA-8875513", "R-CFA-8875555", "R-CFA-8875656", "R-...
[ "EC:3.4.21", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-75205", "REACTOME:R-CEL-5140745", "REACTOME:R-CFA-114608", "REACTOME:R-CFA-1257604", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-6806942", "REACTOME:R-CFA-6807004", "REACTOME:R-CFA-6811558", "REACTOME:R-CFA-8851805", "REACTOME:R-CFA-8851907"...
132
[ "1a0h", "1b2i", "1bht", "1cea", "1ceb", "1gmn", "1gmo", "1gp9", "1hpj", "1hpk", "1i5k", "1i71", "1jfn", "1kdu", "1ki0", "1kiv", "1krn", "1nk1", "1nl1", "1nl2", "1pk2", "1pk4", "1pkr", "1pmk", "1pml", "1tpk", "1urk", "2doh", "2doi", "2fd6", "2feb", "2hpp"...
134
[ "PUB00000803", "PUB00001541", "PUB00001620", "PUB00002414", "PUB00003257", "PUB00003400" ]
[ "3891096", "6373375", "1879523", "3886654", "2157850", "3131537" ]
[ "Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules.", "Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases.", "Evolutionary origin of numerous kringles in human and simian apolip...
[ 1985, 1984, 1991, 1985, 1990, 1987 ]
6
[]
[]
0
0
null
[ "Enterobacteriaceae", "Eukaryota", "viral metagenome" ]
[ 2, 18148, 3 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 32, 3, 75, 42, 68 ]
6
true
Conserved_site
Kringle, conserved site
Kringle, conserved site
Kringle_CS
9
IPR018057
18,057
Deoxyribonuclease I, active site
Deoxyribonuclease-1_AS
Active_site
2,557
false
false
This entry represents the first conserved active site containing a histidine residue [ ]. Deoxyribonuclease I (DNase I) ( ) [ ] is a vertebrate enzyme which catalyzes the endonucleolytic cleavage of double-stranded DNA to 5'- phosphodinucleotide and 5'-phosphooligonucleotide end-products. DNase I is an enzyme involved ...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00919" ]
[ "DNASE_I_1" ]
[ 2557 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.21", "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695" ]
[ "EC:3.1.21", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695" ]
4
[ "1atn", "1dnk", "2a3z", "2a40", "2a41", "2a42", "2d1k", "2dnj", "3cjc", "3dni", "3w3d", "4awn", "7kiu", "7nxv", "7nzm", "9fju", "9fjy", "9nb9" ]
18
[ "PUB00001239", "PUB00003994", "PUB00004018", "PUB00004077", "PUB00004719" ]
[ "8428592", "3713845", "3352748", "2395459", "2251263" ]
[ "Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death).", "Structure of DNase I at 2.0 A resolution suggests a mechanism for binding to and cutting DNA.", "Structure refined to 2A of a nicked DNA octanucleotide complex with DNase I.", ...
[ 1993, 1986, 1988, 1990, 1990 ]
5
[]
[]
0
0
null
[ "Vertebrata" ]
[ 2557 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 12, 12, 16 ]
4
true
Active_site
Deoxyribonuclease I, active site
Deoxyribonuclease I, active site
Deoxyribonuclease-1_AS
8
IPR018060
18,060
AraC-like, DNA binding HTH domain
HTH_AraC
Domain
499,894
false
false
Many bacterial transcription regulation proteins bind DNA through a 'helix-turn-helix' (HTH) motif. One major subfamily of these proteins [ , ] is related to the arabinose operon regulatory protein AraC [ , . Except for celD [ ], all of these proteins seem to be positive transcriptional factors. Although the sequences ...
[ "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
[ "PFAM", "PFAM", "PROFILE", "SMART" ]
[ "PF00165", "PF12833", "PS01124", "SM00342" ]
[ "HTH_AraC", "HTH_18", "HTH_ARAC_FAMILY_2", "HTH_ARAC" ]
[ 1872, 492388, 499463, 492435 ]
4
[ "GP", "GP", "GP", "GP" ]
[ "GenProp0052", "GenProp0292", "GenProp0457", "GenProp0458" ]
[ "GP:GenProp0052", "GP:GenProp0292", "GP:GenProp0457", "GP:GenProp0458" ]
4
[ "1bl0", "1d5y", "1u8b", "1wpk", "1xs9", "1zgw", "2k9s", "3gbg", "3lsg", "3mkl", "3mn2", "3oio", "3oou", "3w6v", "4fe4", "4fe7", "4mlo", "5chh", "5nla", "5suw", "5sux", "6p7r", "6p7t", "6pb9", "6swi", "6xiu", "6xiv", "7bef", "7beg", "7r3w", "7vwy", "7vwz"...
41
[ "PUB00001933", "PUB00003566", "PUB00004444", "PUB00004817" ]
[ "2179047", "2314271", "8451183", "8516313" ]
[ "Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12.", "Finding protein similarities with nucleotide sequence databases.", "The XylS/AraC family of regulators.", "Functional domains of the AraC protein." ]
[ 1990, 1990, 1993, 1993 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]
[ 39, 496323, 1345, 3, 58, 2126 ]
6
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 7, 38, 1 ]
3
true
Domain
AraC-like, DNA binding HTH domain
AraC-like, DNA binding HTH domain
HTH_AraC
2
IPR018061
18,061
Retropepsins
Retropepsins
Domain
369,237
false
false
This group of aspartic peptidases belong to the peptidase clan AA. The clan includes the single domain aspartic proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses) which are active as homodimers. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C...
[]
[]
[]
0
[ "PFAM" ]
[ "PF00077" ]
[ "RVP" ]
[ 369237 ]
1
[ "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.7.-", "2.7.7.49", "2.7.7.7", "3.1.26", "3.4.23", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179", "R-HSA-162585"...
[ "EC:2.7.7.-", "EC:2.7.7.49", "EC:2.7.7.7", "EC:3.1.26", "EC:3.4.23", "METACYC:PWY-6322", "METACYC:PWY-6626", "METACYC:PWY-6749", "METACYC:PWY-6955", "METACYC:PWY-6998", "METACYC:PWY-7127", "METACYC:PWY-7419", "METACYC:PWY-7529", "METACYC:PWY-7706", "METACYC:PWY-7719", "METACYC:PWY-7735...
35
[ "1a30", "1a8g", "1a8k", "1a94", "1a9m", "1aaq", "1aid", "1ajv", "1ajx", "1axa", "1az5", "1b11", "1b6j", "1b6k", "1b6l", "1b6m", "1b6p", "1bai", "1bdl", "1bdq", "1bdr", "1bv7", "1bv9", "1bve", "1bvg", "1bwa", "1bwb", "1c6x", "1c6y", "1c6z", "1c70", "1cpi"...
960
[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00032703", "PUB00041573", "PUB00042504", "PUB00048142", "PUB00065205", "PUB00066803", "PUB00076754", "PUB00076784", "PUB00076785", "PUB00076786", "PUB00076788", "PUB000767...
[ "2194475", "1851433", "8439290", "6795036", "10331925", "11566868", "10864493", "8841139", "17010377", "2682266", "18597783", "23254940", "21765428", "16395329", "4912600", "10497172", "21751400", "15831103", "9311808" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Gastric proteinases--structure, function, evolution and mechanism of action.", "Crystal structure of the hy...
[ 1990, 1991, 1993, 1981, 1999, 2001, 2000, 1996, 2006, 1989, 2008, 2013, 2011, 2006, 1970, 1999, 2011, 2005, 1997 ]
19
[ "IPR001995" ]
[ "IPR034170" ]
1
1
0
[ "Bacteria", "Eukaryota", "Methanomicrobia", "Viruses", "ecological metagenomes" ]
[ 72, 6662, 2, 362495, 6 ]
5
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 3, 20, 17, 1 ]
5
true
Domain
Retropepsins
Retropepsins
Retropepsins
7
IPR018062
18,062
HTH domain AraC-type, conserved site
HTH_AraC-typ_CS
Conserved_site
243,087
false
false
Many bacterial transcription regulation proteins bind DNA through a 'helix-turn-helix' (HTH) motif. One major subfamily of these proteins [ , ] is related to the arabinose operon regulatory protein AraC [ , . Except for celD [ ], all of these proteins seem to be positive transcriptional factors. Although the sequences ...
[ "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" ]
[ "PS00041" ]
[ "HTH_ARAC_FAMILY_1" ]
[ 243087 ]
1
[]
[]
[]
0
[ "1bl0", "1d5y", "1u8b", "1wpk", "1xs9", "1zgw", "2k9s", "3gbg", "3mkl", "3mn2", "3oio", "4fe4", "4fe7", "4mlo", "5suw", "5sux", "6p7r", "6p7t", "6pb9", "6swi", "6xiu", "6xiv", "7bef", "7beg", "7r3w", "7vwy", "7vwz", "7w5w", "7w5x", "7w5y", "8vrq", "8vst"...
35
[ "PUB00001933", "PUB00003566", "PUB00004444", "PUB00004817" ]
[ "2179047", "2314271", "8451183", "8516313" ]
[ "Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12.", "Finding protein similarities with nucleotide sequence databases.", "The XylS/AraC family of regulators.", "Functional domains of the AraC protein." ]
[ 1990, 1990, 1993, 1993 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "unclassified sequences" ]
[ 241941, 202, 10, 7, 927 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 4, 31, 1 ]
3
true
Conserved_site
HTH domain AraC-type, conserved site
HTH domain AraC-type, conserved site
HTH_AraC-typ_CS
8
IPR018063
18,063
SAM-dependent methyltransferase RsmI, conserved site
SAM_MeTrfase_RsmI_CS
Conserved_site
19,494
false
false
Several uncharacterised proteins have been shown to share regions of similarities, including Escherichia coli hypothetical protein yraL, and HI1654, the corresponding Haemophilus influenzae protein; Bacillus subtilis hypothetical protein yabC; Helicobacter pylori hypothetical protein HP0552; Mycoplasma genitalium and M...
[ "GO:0008168" ]
[ "methyltransferase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01296" ]
[ "RSMI" ]
[ 19494 ]
1
[ "EC" ]
[ "2.1.1.198" ]
[ "EC:2.1.1.198" ]
1
[ "3kwp", "5hw4", "9pzg" ]
3
[ "PUB00054204" ]
[ "19965768" ]
[ "Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA." ]
[ 2010 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 18413, 693, 388 ]
3
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 3, 1, 3, 7 ]
4
true
Conserved_site
SAM-dependent methyltransferase RsmI, conserved site
SAM-dependent methyltransferase RsmI, conserved site
SAM_MeTrfase_RsmI_CS
5
IPR018065
18,065
Large ribosomal subunit protein eL34, conserved site
Ribosomal_eL34_CS
Conserved_site
5,063
false
false
This entry represents the conserved site of large ribosomal subunit protein eL34. A number of eukaryotic and archaebacterial ribosomal proteins belong to the eL34 family. These include, vertebrate eL34, mosquito eL34 (known as L31) [ ], plant eL34 [ ], yeast putative ribosomal protein YIL052c and archaebacterial eL34.
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01145" ]
[ "RIBOSOMAL_L34E" ]
[ 5063 ]
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-DRE-156827", "R-DRE-1799339", "R-DRE-72689", "R-DRE-975956", "R-DRE-975957", "R-HSA-156827", "R-HSA-156902", "R-HSA-1799339", "R-HSA-192823", "R-HSA-2408557", "R-HSA-6791226", "R-HSA-72689", "R-HSA-72706", "R-HSA-72764", "R-HSA-9010553", "R-HSA-9633012", "R-HSA-975956", "R-HSA-9...
[ "REACTOME:R-DRE-156827", "REACTOME:R-DRE-1799339", "REACTOME:R-DRE-72689", "REACTOME:R-DRE-975956", "REACTOME:R-DRE-975957", "REACTOME:R-HSA-156827", "REACTOME:R-HSA-156902", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-192823", "REACTOME:R-HSA-2408557", "REACTOME:R-HSA-6791226", "REACTOME:R-HSA-...
32
[ "3j6x", "3j6y", "3j77", "3j78", "3j79", "3j7o", "3j7p", "3j7q", "3j7r", "3j92", "3jag", "3jah", "3jai", "3jaj", "3jan", "3jbn", "3jbo", "3jbp", "3jct", "4adx", "4d5y", "4d67", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u", "4u4y", "4u4z"...
535
[ "PUB00000669", "PUB00004568" ]
[ "8049275", "8075394" ]
[ "Mosquito ribosomal protein rpL31 resembles rat rpL34: cDNA and deduced amino acid sequence.", "Developmental and environmental regulation of two ribosomal protein genes in tobacco." ]
[ 1994, 1994 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota" ]
[ 167, 63, 4833 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 9, 1, 3, 3, 1, 3, 1, 5, 5, 2, 2, 24 ]
12
true
Conserved_site
Large ribosomal subunit protein eL34, conserved site
Large ribosomal subunit protein eL34, conserved site
Ribosomal_eL34_CS
2
IPR018066
18,066
Tubby, C-terminal, conserved site
Tubby_C_CS
Conserved_site
10,119
false
false
Tubby, an autosomal recessive mutation, mapping to mouse chromosome 7, was recently found to be the result of a splicing defect in a novel gene with unknown function. This mutation maps to the tub gene [ , ]. The mouse tubby mutation is the cause of maturity-onset obesity, insulin resistance and sensory deficits. By co...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS01200", "PS01201" ]
[ "TUB_1", "TUB_2" ]
[ 9337, 7764 ]
2
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-5610787", "R-HSA-5610787", "R-MMU-5610787" ]
[ "REACTOME:R-CEL-5610787", "REACTOME:R-HSA-5610787", "REACTOME:R-MMU-5610787" ]
3
[ "1c8z", "1i7e", "1s31", "2fim", "3c5n", "8fh3" ]
6
[ "PUB00000932", "PUB00004232", "PUB00007281", "PUB00014197" ]
[ "8612280", "8606774", "10591637", "14708010" ]
[ "Identification and characterization of the mouse obesity gene tubby: a member of a novel gene family.", "A candidate gene for the mouse mutation tubby.", "Implication of tubby proteins as transcription factors by structure-based functional analysis.", "Tubby proteins: the plot thickens." ]
[ 1996, 1996, 1999, 2004 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 10119 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 36, 1, 29, 1, 17, 13, 26, 18, 57 ]
9
true
Conserved_site
Tubby, C-terminal, conserved site
Tubby, C-terminal, conserved site
Tubby_C_CS
7
IPR018067
18,067
Protein phosphatase 2A regulatory subunit PR55, conserved site
PP2A_PR55_CS
Conserved_site
12,013
false
false
Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase implicated in many cellular processes, including the regulation of metabolic enzymes and proteins involved in signal transduction [ , ]. PP2A is a trimer composed of a 36kDa catalytic subunit, a 65kDa regulatory subunit (subunit A) and a variable third sub...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS01024", "PS01025" ]
[ "PR55_1", "PR55_2" ]
[ 11355, 9658 ]
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-DDI-69231", "R-DDI-69273", "R-DME-209155", "R-DME-209190", "R-DME-209214", "R-DME-209360", "R-DME-209396", "R-DME-209413", "R-DME-209440", "R-DME-209461", "R-DME-2995383", "R-DME-432553", "R-DME-432620", "R-DME-69231", "R-DME-69273", "R-DME-975957", "R-HSA-2465910", "R-HSA-29953...
[ "REACTOME:R-DDI-69231", "REACTOME:R-DDI-69273", "REACTOME:R-DME-209155", "REACTOME:R-DME-209190", "REACTOME:R-DME-209214", "REACTOME:R-DME-209360", "REACTOME:R-DME-209396", "REACTOME:R-DME-209413", "REACTOME:R-DME-209440", "REACTOME:R-DME-209461", "REACTOME:R-DME-2995383", "REACTOME:R-DME-4325...
36
[ "3dw8", "8so0", "8ttb", "8twe", "8uo5", "9c6b", "9c7t", "9mzw", "9n0y", "9n0z" ]
10
[ "PUB00000344", "PUB00003499" ]
[ "1849734", "1370560" ]
[ "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform.", "The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little ...
[ 1991, 1992 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 12013 ]
1
[ "Arabidopsis thaliana", "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 (strain ATCC 204508 / S288c)", "...
[ 13, 11, 3, 13, 15, 2, 7, 27, 1, 1, 34 ]
11
true
Conserved_site
Protein phosphatase 2A regulatory subunit PR55, conserved site
Protein phosphatase 2A regulatory subunit PR55, conserved site
PP2A_PR55_CS
8
IPR018070
18,070
Neuromedin U, amidation site
Neuromedin-U_amidation-site
PTM
558
false
false
Neuromedin U (NmU) [ , ] is a vertebrate peptide which stimulates uterine smooth muscle contraction and causes selective vasoconstriction. Like most other active peptides, it is proteolytically processed from a larger precursor protein. The mature peptides are 8 (NmU-8) to 25 (NmU-25) residues long and C-terminally ami...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00967" ]
[ "NMU" ]
[ 558 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-375276", "R-HSA-416476", "R-HSA-418594", "R-MMU-375276", "R-MMU-416476", "R-MMU-418594", "R-RNO-375276", "R-RNO-416476", "R-RNO-418594" ]
[ "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-418594" ]
9
[ "7w53", "7w55", "7w56", "7w57", "7xk8" ]
5
[ "PUB00000026", "PUB00005078" ]
[ "3239891", "1455013" ]
[ "The distribution and biological effects of neuromedins B and U.", "The purification and sequence analysis of an avian neuromedin U." ]
[ 1988, 1992 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 2, 556 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 6, 7 ]
3
true
PTM
Neuromedin U, amidation site
Neuromedin U, amidation site
Neuromedin-U_amidation-site
2
IPR018071
18,071
Omega-atracotoxin, conserved site
Omega-atracotox_CS
Conserved_site
34
false
false
This entry consists of several Hadronyche versuta (Blue mountains funnel-web spider) specific omega-atracotoxin proteins. Omega-Atracotoxin-Hv1a is an insect-specific neurotoxin whose phylogenetic specificity derives from its ability to antagonise insect, but not vertebrate, voltage-gated calcium channels. Two spatiall...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS60016" ]
[ "OMEGA_ACTX_1" ]
[ 34 ]
1
[]
[]
[]
0
[ "1axh", "1hvw" ]
2
[ "PUB00012336" ]
[ "11313356" ]
[ "Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Arthropoda" ]
[ 34 ]
1
[]
[]
0
true
Conserved_site
Omega-atracotoxin, conserved site
Omega-atracotoxin, conserved site
Omega-atracotox_CS
3
IPR018072
18,072
Conotoxin, alpha-type, conserved site
Conotoxin_a-typ_CS
Conserved_site
297
false
false
Conotoxin consists of several alpha conotoxin precursor proteins from a number of Conus species. Cone snail toxins, conotoxins, are small peptides with disulphide connectivity, that target ion-channels or G-protein coupled receptors. Based on the number and pattern of disulphide bonds and biological activities, conotox...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS60014" ]
[ "ALPHA_CONOTOXIN" ]
[ 297 ]
1
[]
[]
[]
0
[ "1a0m", "1akg", "1b45", "1dg2", "1hje", "1k64", "1m2c", "1mii", "1mtq", "1mxn", "1mxp", "1not", "1pen", "1qmw", "1ul2", "1xga", "1xgb", "1xgc", "1zlc", "2ajw", "2ak0", "2gcz", "2h8s", "2i28", "2jur", "2jus", "2jut", "2lz5", "2md6", "2mdq", "2ns3", "4ez1"...
54
[ "PUB00013117", "PUB00016617", "PUB00016622", "PUB00017021", "PUB00017022" ]
[ "3196703", "11478951", "10988292", "2410412", "1390774" ]
[ "Phylogenetic specificity of cholinergic ligands: alpha-conotoxin SI.", "Cone venom--from accidental stings to deliberate injection.", "lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus.", "Conus ge...
[ 1988, 2001, 2000, 1985, 1992 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 10, 287 ]
2
[]
[]
0
true
Conserved_site
Conotoxin, alpha-type, conserved site
Conotoxin, alpha-type, conserved site
Conotoxin_a-typ_CS
5
IPR018073
18,073
Proteinase inhibitor I25, cystatin, conserved site
Prot_inh_cystat_CS
Conserved_site
9,111
false
false
Cystatins are cysteine proteinase inhibitors belonging to MEROPS inhibitor family I25, clan IH [ , , ]. They mainly inhibit peptidases belonging to peptidase families C1 (papain family) and C13 (legumain family). The cystatin family includes: The Type 1 cystatins, which are intracellular cystatins that are present in t...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00287" ]
[ "CYSTATIN" ]
[ 9111 ]
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-381426", "R-BTA-6798695", "R-BTA-8957275", "R-DDI-6798695", "R-HSA-114608", "R-HSA-140837", "R-HSA-375276", "R-HSA-381426", "R-HSA-416476", "R-HSA-418594", "R-HSA-6798695", "R-HSA-6809371", "R-HSA-8957275", "R-HSA-977225", "R-MMU-381426", "R-MMU-6798695", "R-MMU-6809371", "R...
[ "REACTOME:R-BTA-381426", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8957275", "REACTOME:R-DDI-6798695", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140837", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA...
28
[ "1a67", "1a90", "1cew", "1cyu", "1cyv", "1dvc", "1dvd", "1eqk", "1g96", "1gd3", "1gd4", "1n9j", "1nb3", "1nb5", "1r4c", "1rn7", "1roa", "1stf", "1tij", "1yvb", "2l4v", "2mzv", "2oct", "3gax", "3ima", "3k9m", "3kfq", "3kse", "3l0r", "3lh4", "3mwz", "3ps8"...
55
[ "PUB00001614", "PUB00003412", "PUB00014312" ]
[ "1855589", "2107324", "14587292" ]
[ "The cystatins: protein inhibitors of cysteine proteinases.", "Evolution of proteins of the cystatin superfamily.", "Cystatins." ]
[ 1991, 1990, 2003 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Haloterrigena salina JCM 13891", "Viruses", "viral metagenome" ]
[ 150, 8943, 1, 16, 1 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 18, 6, 2, 17, 24, 15, 43, 33 ]
8
true
Conserved_site
Proteinase inhibitor I25, cystatin, conserved site
Proteinase inhibitor I25, cystatin, conserved site
Prot_inh_cystat_CS
5
IPR018074
18,074
Ubiquitin-activating enzyme E1, conserved site
UBQ-activ_enz_E1_CS
Conserved_site
3,701
false
false
Ubiquitin-activating enzyme (E1 enzyme) [ , ] activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine resi...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00536" ]
[ "UBIQUITIN_ACTIVAT_1" ]
[ 3701 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.2.1.45", "PWY-7511", "R-BTA-8866652", "R-BTA-983168", "R-DDI-1169408", "R-DDI-8866652", "R-DDI-936440", "R-DDI-983168", "R-DDI-9909505", "R-HSA-3065676", "R-HSA-3065678", "R-HSA-8866652", "R-HSA-983168", "R-MMU-3065676", "R-MMU-3065678", "R-MMU-8866652", "R-MMU-983168", "R-RNO-8...
[ "EC:6.2.1.45", "METACYC:PWY-7511", "REACTOME:R-BTA-8866652", "REACTOME:R-BTA-983168", "REACTOME:R-DDI-1169408", "REACTOME:R-DDI-8866652", "REACTOME:R-DDI-936440", "REACTOME:R-DDI-983168", "REACTOME:R-DDI-9909505", "REACTOME:R-HSA-3065676", "REACTOME:R-HSA-3065678", "REACTOME:R-HSA-8866652", ...
21
[ "1y8q", "1y8r", "3cmm", "3kyc", "3kyd", "4nnj", "4p22", "5l6h", "5l6i", "5l6j", "5tr4", "6cwy", "6cwz", "6dc6", "6nya", "6xog", "6xoh", "6xoi", "6zhs", "6zht", "6zhu", "6zqh", "7k5j", "7zh9", "9dqb", "9drj", "9qgg", "9qgi", "9qgr" ]
29
[ "PUB00000623", "PUB00002725", "PUB00002915", "PUB00005373" ]
[ "1647207", "1634524", "7629121", "1656558" ]
[ "Genetic analysis of the ubiquitin system.", "Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis.", "An essential yeast gene encoding a homolog of ubiquitin-activating enzyme.", "The ubiquitin pathway for protein degradation." ]
[ 1991, 1992, 1995, 1991 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Klosneuvirinae" ]
[ 3696, 5 ]
2
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]
[ 7, 2, 3, 9, 5, 10, 13, 1, 46 ]
9
true
Conserved_site
Ubiquitin-activating enzyme E1, conserved site
Ubiquitin-activating enzyme E1, conserved site
UBQ-activ_enz_E1_CS
5
IPR018075
18,075
Ubiquitin-activating enzyme E1
UBQ-activ_enz_E1
Family
7,973
false
false
The post-translational attachment of ubiquitin ( ) to proteins (ubiquitinylation) alters the function, location or trafficking of a protein, or targets it to the 26S proteasome for degradation [ , , ]. Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activatin...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR01408" ]
[ "Ube1" ]
[ 7973 ]
1
[ "EC", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTO...
[ "6.2.1.45", "GenProp1754", "PWY-7511", "R-BTA-8866652", "R-BTA-983168", "R-DDI-1169408", "R-DDI-8866652", "R-DDI-936440", "R-DDI-983168", "R-DDI-9909505", "R-HSA-1169408", "R-HSA-168928", "R-HSA-5656169", "R-HSA-8866652", "R-HSA-936440", "R-HSA-983168", "R-HSA-9909505", "R-MMU-1169...
[ "EC:6.2.1.45", "GP:GenProp1754", "METACYC:PWY-7511", "REACTOME:R-BTA-8866652", "REACTOME:R-BTA-983168", "REACTOME:R-DDI-1169408", "REACTOME:R-DDI-8866652", "REACTOME:R-DDI-936440", "REACTOME:R-DDI-983168", "REACTOME:R-DDI-9909505", "REACTOME:R-HSA-1169408", "REACTOME:R-HSA-168928", "REACTOME...
28
[ "3cmm", "4ii2", "4ii3", "4nnj", "5knl", "5l6h", "5l6i", "5l6j", "5tr4", "5um6", "6dc6", "6nya", "6o82", "6o83", "6zhs", "6zht", "6zhu", "6zqh", "7k5j", "7pvn", "7pyv", "7sol", "7zh9", "8oif", "8se9", "8sea", "8seb", "8sv8", "9b5c", "9b5d", "9b5e", "9b5f"...
65
[ "PUB00015619", "PUB00015620", "PUB00015621", "PUB00015625" ]
[ "15454246", "14998368", "15556404", "15196553" ]
[ "The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.", "Getting into position: the catalytic mechanisms of protein ubiquitylation.", "Polyubiquitin chains: polymeric protein signals.", "The novel functions of ubiquitination in signaling." ]
[ 2004, 2004, 2004, 2004 ]
4
[ "IPR000011" ]
[]
1
0
1
[ "Eukaryota", "Klosneuvirinae", "metagenomes" ]
[ 7963, 7, 3 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 7, 3, 5, 3, 6, 7, 1, 11, 17, 1, 1, 48 ]
12
true
Family
Ubiquitin-activating enzyme E1
Ubiquitin-activating enzyme E1
UBQ-activ_enz_E1
6
IPR018077
18,077
Glycoside hydrolase, family 25 subgroup
Glyco_hydro_fam25_subgr
Family
14,378
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 [ ,...
[]
[]
[]
0
[ "SMART" ]
[ "SM00641" ]
[ "Glyco_25" ]
[ 14378 ]
1
[ "EC" ]
[ "3.2.1.17" ]
[ "EC:3.2.1.17" ]
1
[ "1h09", "1jfx", "1oba", "2ixu", "2ixv", "2j8f", "2j8g", "2wag", "2x8r", "4krt", "4kru", "6zm8", "6zmv" ]
13
[ "PUB00000503", "PUB00001811", "PUB00002378", "PUB00004870", "PUB00005266" ]
[ "1747104", "1916274", "567645", "7624375", "8535779" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes.", "The N,O-diacetylmuramidase of Chalaropsis species. Identificaiton of aspartyl and glutamy...
[ 1991, 1991, 1978, 1995, 1995 ]
5
[ "IPR002053" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 4, 13190, 911, 227, 46 ]
5
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1, 1 ]
2
true
Family
Glycoside hydrolase, family 25 subgroup
Glycoside hydrolase, family 25 subgroup
Glyco_hydro_fam25_subgr
1
IPR018078
18,078
DNA-binding, RecF, conserved site
DNA-binding_RecF_CS
Conserved_site
21,164
false
false
All proteins in this family, including RecF, for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. RecF is involved in DNA metabolism and is required for recombinational DNA repair and for induction of the SOS...
[ "GO:0003697", "GO:0005524", "GO:0006281" ]
[ "single-stranded DNA binding", "ATP binding", "DNA repair" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE", "PROSITE" ]
[ "PS00617", "PS00618" ]
[ "RECF_1", "RECF_2" ]
[ 17706, 19008 ]
2
[]
[]
[]
0
[ "2o5v", "5z67", "5z68", "5z69" ]
4
[ "PUB00003768", "PUB00004414" ]
[ "7898435", "1542576" ]
[ "Nucleotide sequence of the recF gene cluster from Staphylococcus aureus and complementation analysis in Bacillus subtilis recF mutants.", "Sequence and complementation analysis of recF genes from Escherichia coli, Salmonella typhimurium, Pseudomonas putida and Bacillus subtilis: evidence for an essential phospha...
[ 1995, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 4, 20704, 44, 1, 411 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Conserved_site
DNA-binding, RecF, conserved site
DNA-binding, RecF, conserved site
DNA-binding_RecF_CS
9
IPR018079
18,079
Small ribosomal subunit protein uS4, conserved site
Ribosomal_uS4_CS
Conserved_site
49,478
false
false
Ribosomal protein uS4 is one of the proteins from the small ribosomal subunit. In Escherichia coli, uS4 is known to bind directly to 16S ribosomal RNA. Mutations in uS4 have been shown to increase translational error frequencies. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities ...
[ "GO:0019843" ]
[ "rRNA binding" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00632" ]
[ "RIBOSOMAL_S4" ]
[ 49478 ]
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-6791226", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", ...
[ "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...
98
[ "1c05", "1c06", "1eg0", "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qd7", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo"...
1,810
[ "PUB00003681", "PUB00004390" ]
[ "1729612", "2041737" ]
[ "NAM9 nuclear suppressor of mitochondrial ochre mutations in Saccharomyces cerevisiae codes for a protein homologous to S4 ribosomal proteins from chloroplasts, bacteria, and eucaryotes.", "Yeast ribosomal proteins: XII. YS11 of Saccharomyces cerevisiae is a homologue to E. coli S4 according to the gene analysis....
[ 1992, 1991 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctNZc11", "unclassified sequences" ]
[ 580, 21108, 27403, 1, 386 ]
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, 1, 1, 3, 1, 5, 5, 2, 8, 4, 3, 3, 8 ]
13
true
Conserved_site
Small ribosomal subunit protein uS4, conserved site
Small ribosomal subunit protein uS4, conserved site
Ribosomal_uS4_CS
3
IPR018080
18,080
Band 7/stomatin-like, conserved site
Band_7/stomatin-like_CS
Conserved_site
13,513
false
false
Stomatin is also known as erythrocyte membrane protein band 7.2b. It is a 31kDa membrane protein [ ], and was named after the rare human disease: haemolytic anaemia hereditary stomatocytosis. The protein contains a single hydrophobic domain, close to the N terminus, and is phosphorylated [ ]. Stomatin is believed to be...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01270" ]
[ "BAND_7" ]
[ 13513 ]
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-2672351", "R-CEL-373753", "R-CEL-6798695", "R-CEL-8980692", "R-CEL-9013026", "R-CEL-9013406", "R-CEL-9013407", "R-DME-2672351", "R-DME-373753", "R-DME-6798695", "R-DME-8980692", "R-DME-9013026", "R-DME-9013406", "R-DME-9013407", "R-HSA-2672351", "R-HSA-373753", "R-HSA-6798695"...
[ "REACTOME:R-CEL-2672351", "REACTOME:R-CEL-373753", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8980692", "REACTOME:R-CEL-9013026", "REACTOME:R-CEL-9013406", "REACTOME:R-CEL-9013407", "REACTOME:R-DME-2672351", "REACTOME:R-DME-373753", "REACTOME:R-DME-6798695", "REACTOME:R-DME-8980692", "REACTOME:...
31
[ "2rpb", "3bk6", "4fvf", "4fvg", "4fvj", "7wh3", "8gn9", "8z5g", "9oh9" ]
9
[ "PUB00002046", "PUB00002047" ]
[ "9147127", "9088993" ]
[ "Stomatin.", "Quinoline antimalarials: mechanisms of action and resistance." ]
[ 1997, 1997 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 255, 8982, 4181, 95 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 29, 10, 11, 1, 6, 4, 6 ]
7
true
Conserved_site
Band 7/stomatin-like, conserved site
Band 7/stomatin-like, conserved site
Band_7/stomatin-like_CS
2
IPR018081
18,081
Anaphylatoxin, complement system
Anaphylatoxin_comp_syst
Homologous_superfamily
5,473
false
false
Complement components C3, C4 and C5 are large glycoproteins that have important functions in the immune response and host defence [ ]. They have a wide variety of biological activities and are proteolytically activated by cleavage at a specific site, forming a-and b-fragments [ ]. A-fragments form distinct structural d...
[]
[]
[]
0
[ "SSF" ]
[ "SSF47686" ]
[ "" ]
[ 5473 ]
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-173736", "R-BTA-174577", "R-BTA-198933", "R-BTA-375276", "R-BTA-381426", "R-BTA-418594", "R-BTA-6798695", "R-BTA-8957275", "R-BTA-977606", "R-HSA-166663", "R-HSA-166665", "R-HSA-173736", "R-HSA-174577", "R-HSA-198933", "R-HSA-375276", "R-HSA-381426", "R-HSA-418594", "R-HSA-6...
[ "REACTOME:R-BTA-173736", "REACTOME:R-BTA-174577", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8957275", "REACTOME:R-BTA-977606", "REACTOME:R-HSA-166663", "REACTOME:R-HSA-166665", "REACTOME:R-HSA-1...
43
[ "1c5a", "1cfa", "1kjs", "2a73", "3cu7", "3hqa", "3hqb", "3kls", "3km9", "3prx", "3pvm", "4e0s", "4hw5", "4hwj", "4i6o", "4p39", "4p3a", "4p3b", "4uu9", "4wb2", "4wb3", "5b4p", "5hcc", "5hcd", "5hce", "5i5k", "5jpm", "5jpn", "6jv7", "6jv8", "6rqj", "6ru5"...
57
[ "PUB00001343", "PUB00002512", "PUB00003181" ]
[ "3081348", "2777798", "1431125" ]
[ "C5a fragment of bovine complement. Purification, bioassays, amino-acid sequence and other structural studies.", "Sequence of the gene for murine complement component C4.", "Primary structure of cobra complement component C3." ]
[ 1986, 1989, 1992 ]
3
[]
[]
0
0
null
[ "Chitinophaga agrisoli", "Eumetazoa" ]
[ 1, 5472 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 16, 22, 17, 17 ]
4
true
Homologous_superfamily
Anaphylatoxin, complement system
Anaphylatoxin, complement system
Anaphylatoxin_comp_syst
5
IPR018082
18,082
AmbAllergen
AmbAllergen
Family
11,534
false
false
Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-alpha-D-mann-4-enuronosyl groups at their non-reducing ends. The protein is maximally expressed late in pollen development....
[]
[]
[]
0
[ "PRINTS" ]
[ "PR00807" ]
[ "AMBALLERGEN" ]
[ 11534 ]
1
[ "EC" ]
[ "4.2.2.2" ]
[ "EC:4.2.2.2" ]
1
[ "1pxz", "6fi2", "9buj" ]
3
[ "PUB00002041", "PUB00003179", "PUB00004536", "PUB00004560", "PUB00085875" ]
[ "7920021", "1717566", "1983191", "1421152", "25978036" ]
[ "Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI.", "Complete sequence of the allergen Amb alpha II. Recombinant expression and reactivity with T cells from ragweed allergic patients.", "Molecular and genetic characterization of two pollen-expresse...
[ 1994, 1991, 1990, 1992, 2015 ]
5
[ "IPR045032" ]
[]
1
0
1
[ "Aureococcus anophagefferens virus", "Bacteria", "Eukaryota", "Ignisphaera aggregans", "metagenomes" ]
[ 1, 231, 11284, 4, 14 ]
5
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 119, 32, 65 ]
3
true
Family
AmbAllergen
AmbAllergen
AmbAllergen
7
IPR018083
18,083
Sterol reductase, conserved site
Sterol_reductase_CS
Conserved_site
9,816
false
false
The following enzymes belong to a conserved family of sterol reductases which act by reducing double bonds [ , ]: Fungal delta(14)-sterol reductase ( ) (C-14 sterol reductase) (gene ERG24 in budding yeast), an enzyme of ergosterol biosynthesis. Mammalian (TM7SF2) and plant delta(14)-sterol reductases. Fungal delta(24(2...
[ "GO:0016628" ]
[ "oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor" ]
[ "molecular_function" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS01017", "PS01018" ]
[ "STEROL_REDUCT_1", "STEROL_REDUCT_2" ]
[ 8072, 7860 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "1.3.1", "R-BTA-6807047", "R-BTA-6807062", "R-DRE-6807047", "R-DRE-6807062", "R-HSA-191273", "R-HSA-2426168", "R-HSA-2995383", "R-HSA-6807047", "R-HSA-6807062", "R-HSA-8980692", "R-HSA-9013106", "R-HSA-9013148", "R-HSA-9013149", "R-HSA-9013404", "R-HSA-9013405", "R-HSA-9013408", "R...
[ "EC:1.3.1", "REACTOME:R-BTA-6807047", "REACTOME:R-BTA-6807062", "REACTOME:R-DRE-6807047", "REACTOME:R-DRE-6807062", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-2426168", "REACTOME:R-HSA-2995383", "REACTOME:R-HSA-6807047", "REACTOME:R-HSA-6807062", "REACTOME:R-HSA-8980692", "REACTOME:R-HSA-9013106...
45
[ "4quv", "9l5r", "9l5s", "9l5t" ]
4
[ "PUB00001844", "PUB00018010" ]
[ "8125337", "9878250" ]
[ "The identification of a gene family in the Saccharomyces cerevisiae ergosterol biosynthesis pathway.", "The human lamin B receptor/sterol reductase multigene family." ]
[ 1994, 1998 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 70, 9746 ]
2
[ "Arabidopsis thaliana", "Danio rerio", "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)", "Schizosaccharomyces pombe (st...
[ 9, 5, 24, 16, 2, 8, 13, 2, 2, 12 ]
10
true
Conserved_site
Sterol reductase, conserved site
Sterol reductase, conserved site
Sterol_reductase_CS
6
IPR018085
18,085
Uracil-DNA glycosylase, active site
Ura-DNA_Glyclase_AS
Active_site
25,538
false
false
Uracil-DNA glycosylase (UNG) [ ] is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved [ ] ...
[ "GO:0016799", "GO:0006281" ]
[ "hydrolase activity, hydrolyzing N-glycosyl compounds", "DNA repair" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00130" ]
[ "U_DNA_GLYCOSYLASE" ]
[ 25538 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.2.2.27", "R-DDI-110329", "R-DDI-110357", "R-HSA-110328", "R-HSA-110329", "R-HSA-110357", "R-HSA-9609690", "R-HSA-9821002", "R-MMU-110329", "R-MMU-110357", "R-SCE-110329", "R-SPO-110329" ]
[ "EC:3.2.2.27", "REACTOME:R-DDI-110329", "REACTOME:R-DDI-110357", "REACTOME:R-HSA-110328", "REACTOME:R-HSA-110329", "REACTOME:R-HSA-110357", "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-9821002", "REACTOME:R-MMU-110329", "REACTOME:R-MMU-110357", "REACTOME:R-SCE-110329", "REACTOME:R-SPO-110329" ]
12
[ "1akz", "1emh", "1emj", "1eug", "1eui", "1flz", "1lau", "1lqg", "1lqj", "1lqm", "1okb", "1q3f", "1ssp", "1udg", "1udh", "1udi", "1ugh", "1uug", "1yuo", "2boo", "2eug", "2hxm", "2j8x", "2jhq", "2owq", "2oxm", "2oyt", "2ssp", "2uug", "2zhx", "3a7n", "3cxm"...
140
[ "PUB00000054", "PUB00000916", "PUB00001176", "PUB00004202", "PUB00004423", "PUB00004816" ]
[ "3052275", "7697717", "2555154", "7845459", "8332455", "8389453" ]
[ "DNA repair enzymes.", "Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis.", "Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme.", "The structural basis of specific base-excision repair by uracil-DNA ...
[ 1988, 1995, 1989, 1995, 1993, 1993 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 13, 20306, 4325, 603, 291 ]
5
[ "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)", "Schizosaccharomyces ...
[ 14, 1, 14, 4, 1, 4, 3, 1, 1, 8 ]
10
true
Active_site
Uracil-DNA glycosylase, active site
Uracil-DNA glycosylase, active site
Ura-DNA_Glyclase_AS
3
IPR018086
18,086
NADH:ubiquinone oxidoreductase, subunit 1, conserved site
NADH_UbQ_OxRdtase_su1_CS
Conserved_site
77,965
false
false
This entry represents subunit 1 NADH:ubiquinone oxidoreductase [ ]. Among the many polypeptide subunits that make up complex I, there are fifteen which are located in the membrane part, seven of which are encoded by the mitochondrial and chloroplast genomes of most species. The most conserved of these organelle-encoded...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS00667", "PS00668" ]
[ "COMPLEX1_ND1_1", "COMPLEX1_ND1_2" ]
[ 63313, 70138 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "7.1.1.-", "R-CEL-5419276", "R-DME-5419276", "R-DME-611105", "R-DME-6799198", "R-DRE-611105", "R-GGA-5419276", "R-GGA-611105", "R-GGA-6799198", "R-HSA-5419276", "R-HSA-611105", "R-HSA-6799198", "R-HSA-9837999", "R-MMU-5419276", "R-MMU-611105", "R-MMU-6799198", "R-RNO-5419276", "R-R...
[ "EC:7.1.1.-", "REACTOME:R-CEL-5419276", "REACTOME:R-DME-5419276", "REACTOME:R-DME-611105", "REACTOME:R-DME-6799198", "REACTOME:R-DRE-611105", "REACTOME:R-GGA-5419276", "REACTOME:R-GGA-611105", "REACTOME:R-GGA-6799198", "REACTOME:R-HSA-5419276", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198"...
19
[ "4he8", "4hea", "4wz7", "5gpn", "5gup", "5lc5", "5ldw", "5ldx", "5lnk", "5o31", "5xtc", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6gcs", "6h8k", "6hum", "6i0d", "6i1p", "6khi", "6khj", "6l7o", "6l7p", "6nbq", "6nbx", "6nby", "6q8o", "6q8w", "6q8x", "6q9b"...
327
[ "PUB00001392", "PUB00003309", "PUB00005074", "PUB00043561", "PUB00045437" ]
[ "2029890", "7690854", "1470679", "10940377", "18394423" ]
[ "The respiratory-chain NADH dehydrogenase (complex I) of mitochondria.", "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I.", "The NADH:ubiquinone oxi...
[ 1991, 1993, 1992, 2000, 2008 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 305, 17846, 59301, 513 ]
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",...
[ 12, 3, 1, 11, 3, 969, 8, 1, 4, 6, 4 ]
11
true
Conserved_site
NADH:ubiquinone oxidoreductase, subunit 1, conserved site
NADH:ubiquinone oxidoreductase, subunit 1, conserved site
NADH_UbQ_OxRdtase_su1_CS
1
IPR018087
18,087
Glycoside hydrolase, family 5, conserved site
Glyco_hydro_5_CS
Conserved_site
17,295
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:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00659" ]
[ "GLYCOSYL_HYDROL_F5" ]
[ 17295 ]
1
[ "EC", "EC", "METACYC" ]
[ "3.2.1", "3.2.1.4", "PWY-6788" ]
[ "EC:3.2.1", "EC:3.2.1.4", "METACYC:PWY-6788" ]
3
[ "1a3h", "1cec", "1cz1", "1e5j", "1ece", "1edg", "1egz", "1eqc", "1eqp", "1g01", "1g0c", "1h11", "1h2j", "1h4p", "1h5v", "1hf6", "1lf1", "1ocq", "1qhz", "1qi0", "1qi2", "1tvn", "1tvp", "1vrx", "1w3k", "1w3l", "2a3h", "2ckr", "2cks", "2jep", "2jeq", "2osw"...
139
[ "PUB00000503", "PUB00001778", "PUB00004870", "PUB00004956", "PUB00005266" ]
[ "1747104", "2806912", "7624375", "1677466", "8535779" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Cellulase families revealed by hydrophobic cluster analysis.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Cellulase EGZ of Erwinia chrysanthemi: struct...
[ 1991, 1989, 1995, 1991, 1995 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 115, 10254, 11, 6820, 95 ]
5
[ "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 21, 4, 1, 20 ]
4
true
Conserved_site
Glycoside hydrolase, family 5, conserved site
Glycoside hydrolase, family 5, conserved site
Glyco_hydro_5_CS
1
IPR018088
18,088
Chalcone/stilbene synthase, active site
Chalcone/stilbene_synthase_AS
Active_site
5,816
false
false
Chalcone synthases (CHS) ( ) and stilbene synthases (STS) (formerly known as resveratrol synthases) are related plant enzymes, members of the plant polyketide synthase superfamily. CHS is an important enzyme in flavonoid biosynthesis and STS is a key enzyme in stilbene-type phyloalexin biosynthesis. Both enzymes cataly...
[ "GO:0016746", "GO:0009058" ]
[ "acyltransferase activity", "biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00441" ]
[ "CHALCONE_SYNTH" ]
[ 5816 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.3.1", "2.3.1.74", "PWY-5135", "PWY-6316", "PWY-6515", "PWY-6787", "PWY-7397", "PWY-7897" ]
[ "EC:2.3.1", "EC:2.3.1.74", "METACYC:PWY-5135", "METACYC:PWY-6316", "METACYC:PWY-6515", "METACYC:PWY-6787", "METACYC:PWY-7397", "METACYC:PWY-7897" ]
8
[ "1bi5", "1bq6", "1cgk", "1cgz", "1d6h", "1d6i", "1ee0", "1i86", "1i88", "1i89", "1i8b", "1jwx", "1qlv", "1u0u", "1u0v", "1u0w", "1xes", "1xet", "1z1e", "1z1f", "2p0u", "3awj", "3awk", "3tsy", "3wd7", "4wum", "4yjy", "5uc5", "6dx7", "6dx9", "6dxa", "6dxb"...
56
[ "PUB00002705", "PUB00072442", "PUB00095149" ]
[ "2033084", "2184816", "21909286" ]
[ "The role of cysteines in polyketide synthases. Site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways.", "Stilbene and chalcone synthases: related enzymes with key functions in plant-specific pathways.", "Chalcone synthase and its functions in plan...
[ 1991, 1990, 2011 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 404, 5412 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 23, 2, 9 ]
3
true
Active_site
Chalcone/stilbene synthase, active site
Chalcone/stilbene synthase, active site
Chalcone/stilbene_synthase_AS
7
IPR018089
18,089
Orotidine 5'-phosphate decarboxylase, active site
OMPdecase_AS
Active_site
25,473
false
false
Orotidine 5'-phosphate decarboxylase (OMPdecase) [ , ] catalyses the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofu...
[ "GO:0004590", "GO:0006207" ]
[ "orotidine-5'-phosphate decarboxylase activity", "'de novo' pyrimidine nucleobase biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00156" ]
[ "OMPDECASE" ]
[ 25473 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.1.1.23", "PWY-5686", "PWY-7790", "PWY-7791", "R-DDI-500753", "R-DME-500753", "R-HSA-500753", "R-MMU-500753" ]
[ "EC:4.1.1.23", "METACYC:PWY-5686", "METACYC:PWY-7790", "METACYC:PWY-7791", "REACTOME:R-DDI-500753", "REACTOME:R-DME-500753", "REACTOME:R-HSA-500753", "REACTOME:R-MMU-500753" ]
8
[ "1dbt", "1dqw", "1dqx", "1dv7", "1dvj", "1eix", "1jjk", "1km1", "1km2", "1km3", "1l2u", "1lol", "1loq", "1lor", "1los", "1lp6", "1vqt", "1x1z", "2aqw", "2cz5", "2czd", "2cze", "2czf", "2e6y", "2eaw", "2f84", "2fds", "2ffc", "2guu", "2jgy", "2p1f", "2q8l"...
205
[ "PUB00002768", "PUB00003724" ]
[ "1730672", "2835631" ]
[ "The orotidine-5'-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family.", "Sequence analysis of the DdPYR5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases." ]
[ 1992, 1988 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Marseillevirus LCMAC103", "unclassified sequences" ]
[ 592, 19970, 4449, 1, 461 ]
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, 7, 3, 1, 5, 5, 1, 1, 12 ]
12
true
Active_site
Orotidine 5'-phosphate decarboxylase, active site
Orotidine 5'-phosphate decarboxylase, active site
OMPdecase_AS
7
IPR018090
18,090
Pyrimidine-nucleoside phosphorylase, bacterial/eukaryotic
Pyrmidine_PPas_bac/euk
Family
14,337
false
false
Two highly similar activities are represented in this group: thymidine phosphorylase (TP, gene deoA, ) and pyrimidine-nucleoside phosphorylase (PyNP, gene pdp, ). Both are dimeric enzymes that function in the salvage pathway to catalyse the reversible phosphorolysis of pyrimidine nucleosides to the free base and sugar ...
[ "GO:0016154", "GO:0006213" ]
[ "pyrimidine-nucleoside phosphorylase activity", "pyrimidine nucleoside metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "NCBIFAM" ]
[ "TIGR02644" ]
[ "Y_phosphoryl" ]
[ 14337 ]
1
[ "EC", "GP", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.4.2.4", "GenProp1410", "GenProp1631", "PWY-7181", "R-HSA-73614", "R-HSA-73621", "R-MMU-73614", "R-MMU-73621", "R-RNO-73614", "R-RNO-73621" ]
[ "EC:2.4.2.4", "GP:GenProp1410", "GP:GenProp1631", "METACYC:PWY-7181", "REACTOME:R-HSA-73614", "REACTOME:R-HSA-73621", "REACTOME:R-MMU-73614", "REACTOME:R-MMU-73621", "REACTOME:R-RNO-73614", "REACTOME:R-RNO-73621" ]
10
[ "1azy", "1brw", "1otp", "1tpt", "2dsj", "2j0f", "2tpt", "2wk5", "2wk6", "3h5q", "4ead", "4eaf", "4lhm", "4x46", "4xr5", "4yek", "4yyy", "5ep8", "5ey3", "5oln", "7m7k" ]
21
[ "PUB00010722", "PUB00010723", "PUB00010724" ]
[ "9310231", "9698549", "9817849" ]
[ "Platelet-derived endothelial cell growth factor thymidine phosphorylase in tumour growth and response to therapy.", "Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase.", "The crystal structure of pyrimidine nucleoside phosphorylase in a closed...
[ 1997, 1998, 1998 ]
3
[ "IPR000053" ]
[ "IPR013465" ]
1
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]
[ 13522, 613, 8, 194 ]
4
[ "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 3, 1, 2 ]
5
true
Family
Pyrimidine-nucleoside phosphorylase, bacterial/eukaryotic
Pyrimidine-nucleoside phosphorylase, bacterial/eukaryotic
Pyrmidine_PPas_bac/euk
4
IPR018091
18,091
Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site
PEP_carboxykin_GTP_CS
Conserved_site
11,297
false
false
This entry represents a conserved site found in GTP-utilising phosphoenolpyruvate carboxykinase enzymes. An essential cysteine residue has been proposed [ ] to be implicated in the catalytic mechanism; this residue is located in the central part of PEPCK and is in the centre of a perfectly conserved region.
[ "GO:0004613" ]
[ "phosphoenolpyruvate carboxykinase (GTP) activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00505" ]
[ "PEPCK_GTP" ]
[ 11297 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.1.1.32", "PWY-7383", "R-DDI-70263", "R-DME-70263", "R-GGA-352875", "R-HSA-2161541", "R-HSA-381340", "R-HSA-70263", "R-HSA-9615017", "R-HSA-9632974", "R-MMU-70263", "R-RNO-70263", "R-SSC-70263" ]
[ "EC:4.1.1.32", "METACYC:PWY-7383", "REACTOME:R-DDI-70263", "REACTOME:R-DME-70263", "REACTOME:R-GGA-352875", "REACTOME:R-HSA-2161541", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-70263", "REACTOME:R-HSA-9615017", "REACTOME:R-HSA-9632974", "REACTOME:R-MMU-70263", "REACTOME:R-RNO-70263", "REACTOME...
13
[ "1khb", "1khe", "1khf", "1khg", "1m51", "1nhx", "2faf", "2fah", "2gmv", "2qew", "2qey", "2qf1", "2qf2", "2qzy", "2rk7", "2rk8", "2rka", "2rkd", "2rke", "2zci", "3dt2", "3dt4", "3dt7", "3dtb", "3moe", "3mof", "3moh", "4gmm", "4gmu", "4gmw", "4gmz", "4gnl"...
85
[ "PUB00002529" ]
[ "2909519" ]
[ "Cysteine 288: an essential hyperreactive thiol of cytosolic phosphoenolpyruvate carboxykinase (GTP)." ]
[ 1989 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Yasminevirus sp. GU-2018", "metagenomes" ]
[ 60, 6838, 4210, 1, 188 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 2, 3, 9, 11, 8 ]
6
true
Conserved_site
Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site
Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site
PEP_carboxykin_GTP_CS
3
IPR018093
18,093
BCCT transporter, conserved site
BCCT_CS
Conserved_site
14,545
false
false
These prokaryotic transport proteins belong to a family known as BCCT (for Betaine / Carnitine / Choline Transporters) and are specific for compounds containing a quaternary nitrogen atom. The BCCT proteins contain 12 transmembrane regions and are energized by proton symport. They contain a conserved region with four t...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01303" ]
[ "BCCT" ]
[ 14545 ]
1
[]
[]
[]
0
[ "2wit", "2wsw", "2wsx", "3hfx", "3p03", "4ain", "4c7r", "4doj", "4llh", "4m8j", "8ybq", "8ybr", "9gkk" ]
13
[ "PUB00002302" ]
[ "8752321" ]
[ "Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 14132, 124, 247, 42 ]
4
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Conserved_site
BCCT transporter, conserved site
BCCT transporter, conserved site
BCCT_CS
8
IPR018094
18,094
Thymidylate kinase
Thymidylate_kinase
Family
29,479
false
false
Thymidylate kinase ( ; dTMP kinase) catalyses the phosphorylation of thymidine 5'-monophosphate (dTMP) to form thymidine 5'-diphosphate (dTDP) in the presence of ATP and magnesium: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate Thymidylate kinase is an ubiquitous enzyme of about 25 Kd and is important in...
[ "GO:0004798", "GO:0005524", "GO:0006233" ]
[ "dTMP kinase activity", "ATP binding", "dTDP biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM" ]
[ "MF_00165", "TIGR00041" ]
[ "Thymidylate_kinase", "DTMP_kinase" ]
[ 28558, 26895 ]
2
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.4.9", "GenProp1264", "GenProp1494", "GenProp1617", "GenProp1621", "PWY-6545", "PWY-7184", "PWY-7187", "PWY-7197", "PWY-7198", "PWY-7210", "R-CEL-499943", "R-DDI-499943", "R-DME-499943", "R-DRE-499943", "R-HSA-499943", "R-MMU-499943", "R-PFA-499943", "R-SCE-499943", "R-SPO-...
[ "EC:2.7.4.9", "GP:GenProp1264", "GP:GenProp1494", "GP:GenProp1617", "GP:GenProp1621", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7187", "METACYC:PWY-7197", "METACYC:PWY-7198", "METACYC:PWY-7210", "REACTOME:R-CEL-499943", "REACTOME:R-DDI-499943", "REACTOME:R-DME-499943", "REACTO...
20
[ "1e2d", "1e2e", "1e2f", "1e2g", "1e2q", "1e98", "1e99", "1e9a", "1e9b", "1e9c", "1e9d", "1e9e", "1e9f", "1g3u", "1gsi", "1gtv", "1mrn", "1mrs", "1n5i", "1n5j", "1n5k", "1n5l", "1nmx", "1nmy", "1nmz", "1nn0", "1nn1", "1nn3", "1nn5", "1tmk", "1w2g", "1w2h"...
117
[ "PUB00016913" ]
[ "8024690" ]
[ "Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1020, 23006, 4715, 205, 533 ]
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",...
[ 9, 1, 2, 2, 1, 3, 1, 1, 3, 4, 1, 1, 4 ]
13
true
Family
Thymidylate kinase
Thymidylate kinase
Thymidylate_kinase
9
IPR018095
18,095
Thymidylate kinase, conserved site
Thymidylate_kin_CS
Conserved_site
19,934
false
false
Thymidylate kinase ( ; dTMP kinase) catalyses the phosphorylation of thymidine 5'-monophosphate (dTMP) to form thymidine 5'-diphosphate (dTDP) in the presence of ATP and magnesium: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate Thymidylate kinase is an ubiquitous enzyme of about 25 Kd and is important in...
[ "GO:0004798", "GO:0005524", "GO:0006233" ]
[ "dTMP kinase activity", "ATP binding", "dTDP biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE" ]
[ "PS01331" ]
[ "THYMIDYLATE_KINASE" ]
[ 19934 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.4.9", "PWY-6545", "PWY-7184", "PWY-7187", "PWY-7197", "PWY-7198", "PWY-7210", "R-CEL-499943", "R-DDI-499943", "R-DME-499943", "R-DRE-499943", "R-HSA-499943", "R-MMU-499943", "R-PFA-499943", "R-SCE-499943", "R-SPO-499943" ]
[ "EC:2.7.4.9", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7187", "METACYC:PWY-7197", "METACYC:PWY-7198", "METACYC:PWY-7210", "REACTOME:R-CEL-499943", "REACTOME:R-DDI-499943", "REACTOME:R-DME-499943", "REACTOME:R-DRE-499943", "REACTOME:R-HSA-499943", "REACTOME:R-MMU-499943", "REACT...
16
[ "1e2d", "1e2e", "1e2f", "1e2g", "1e2q", "1e98", "1e99", "1e9a", "1e9b", "1e9c", "1e9d", "1e9e", "1e9f", "1g3u", "1gsi", "1gtv", "1mrn", "1mrs", "1n5i", "1n5j", "1n5k", "1n5l", "1nmx", "1nmy", "1nmz", "1nn0", "1nn1", "1nn3", "1nn5", "1tmk", "1w2g", "1w2h"...
106
[ "PUB00016913" ]
[ "8024690" ]
[ "Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 342, 14916, 4231, 111, 334 ]
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",...
[ 9, 1, 1, 2, 1, 4, 2, 1, 3, 5, 1, 1, 15 ]
13
true
Conserved_site
Thymidylate kinase, conserved site
Thymidylate kinase, conserved site
Thymidylate_kin_CS
4
IPR018096
18,096
Interleukin-4/interleukin-13, conserved site
IL-4/IL-13_CS
Conserved_site
385
false
false
Interleukin-4 (IL-4) [ ] is a cytokine that plays a central role in the control and regulation of the immune and inflammatory system. IL-4 is a participant in several B-cell activation processes. It also stimulates other cell types such as T cells or mast cells. IL-4 is a glycoprotein of 110 to 131 residues. It contain...
[ "GO:0005126", "GO:0006955", "GO:0005576" ]
[ "cytokine receptor binding", "immune response", "extracellular region" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PROSITE" ]
[ "PS00838" ]
[ "INTERLEUKIN_4_13" ]
[ 385 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6785807", "R-CFA-6785807", "R-HSA-6785807", "R-HSA-9012546", "R-MMU-6785807", "R-RNO-6785807", "R-SSC-6785807" ]
[ "REACTOME:R-BTA-6785807", "REACTOME:R-CFA-6785807", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9012546", "REACTOME:R-MMU-6785807", "REACTOME:R-RNO-6785807", "REACTOME:R-SSC-6785807" ]
7
[ "1bbn", "1bcn", "1cyl", "1ga3", "1hij", "1hik", "1iar", "1ijz", "1ik0", "1iti", "1itl", "1itm", "1rcb", "2b8u", "2b8x", "2b8y", "2b8z", "2b90", "2b91", "2cyk", "2d48", "2int", "3bpl", "3bpn", "3bpo", "3g6d", "3l5w", "3l5x", "3lb6", "3qb7", "4i77", "4ps4"...
42
[ "PUB00000107", "PUB00000339", "PUB00004143" ]
[ "1693082", "1993171", "8096327" ]
[ "Lymphokine control of in vivo immunoglobulin isotype selection.", "Disulfide assignments in recombinant mouse and human interleukin 4.", "Interleukin-13 is a new human lymphokine regulating inflammatory and immune responses." ]
[ 1990, 1991, 1993 ]
3
[]
[]
0
0
null
[ "Bilateria" ]
[ 385 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 3, 5 ]
3
true
Conserved_site
Interleukin-4/interleukin-13, conserved site
Interleukin-4/interleukin-13, conserved site
IL-4/IL-13_CS
5
IPR018097
18,097
EGF-like calcium-binding, conserved site
EGF_Ca-bd_CS
Conserved_site
177,624
false
false
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown [ , , , , ] to be present in a large number of membrane-bound and extracellular, mostly animal, proteins. Many of these proteins require calcium for their biological function, and a calcium-binding site has been found at...
[ "GO:0005509" ]
[ "calcium ion binding" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01187" ]
[ "EGF_CA" ]
[ 177624 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-114608", "R-BTA-140834", "R-BTA-140837", "R-BTA-140875", "R-BTA-1474228", "R-BTA-1566948", "R-BTA-159740", "R-BTA-159763", "R-BTA-159782", "R-BTA-1971475", "R-BTA-2022870", "R-BTA-2022923", "R-BTA-2024101", "R-BTA-202733", "R-BTA-2129379", "R-BTA-216083", "R-BTA-2173789", "R...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-140834", "REACTOME:R-BTA-140837", "REACTOME:R-BTA-140875", "REACTOME:R-BTA-1474228", "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-159740", "REACTOME:R-BTA-159763", "REACTOME:R-BTA-159782", "REACTOME:R-BTA-1971475", "REACTOME:R-BTA-2022870", "REACTOME:R-BTA...
371
[ "1apo", "1apq", "1aut", "1bf9", "1c5m", "1ccf", "1dan", "1dva", "1dx5", "1edm", "1emn", "1emo", "1ezq", "1f0r", "1f0s", "1f7e", "1f7m", "1fak", "1fax", "1ff7", "1ffm", "1g2l", "1g2m", "1hj7", "1hz8", "1i0u", "1ioe", "1iqe", "1iqf", "1iqg", "1iqh", "1iqi"...
272
[ "PUB00000923", "PUB00001555", "PUB00002741", "PUB00003983", "PUB00004321", "PUB00004609", "PUB00004964" ]
[ "7606779", "3282918", "1527084", "6607417", "2288911", "6334307", "3534958" ]
[ "The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions.", "Structure and function of epidermal growth factor-like regions in proteins.", "How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of...
[ 1995, 1988, 1992, 1984, 1990, 1984, 1986 ]
7
[]
[]
0
0
null
[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "metagenomes" ]
[ 151, 1, 177466, 6 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 105, 79, 480, 93, 512, 304, 245, 468, 142 ]
9
true
Conserved_site
EGF-like calcium-binding, conserved site
EGF-like calcium-binding, conserved site
EGF_Ca-bd_CS
1
IPR018098
18,098
Small ribosomal subunit protein eS24 conserved site
Ribosomal_eS24_CS
Conserved_site
7,256
false
false
This conserved site is found in eS24 ribosomal proteins from eukaryotes and archaebacteria. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growin...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00529" ]
[ "RIBOSOMAL_S24E" ]
[ 7256 ]
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-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72695", "R-DDI-72702", "R-DDI-72706", "R-DDI-975956", "R-DDI-975957", ...
[ "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-DDI-156827", "REACTOME:R-DDI-179933...
74
[ "1xn9", "1ywx", "2g1d", "2v94", "3j16", "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"...
607
[ "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", "Eukaryota", "Halopseudomonas pelagia", "ecological metagenomes" ]
[ 463, 6790, 1, 2 ]
4
[ "Arabidopsis thaliana", "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 (strain ATCC 204508 / S288c)", "...
[ 5, 3, 1, 5, 8, 1, 9, 16, 2, 2, 19 ]
11
true
Conserved_site
Small ribosomal subunit protein eS24 conserved site
Small ribosomal subunit protein eS24 conserved site
Ribosomal_eS24_CS
6
IPR018099
18,099
Purine phosphorylase, family 2, conserved site
Purine_phosphorylase-2_CS
Conserved_site
14,376
false
false
This entry consists of purine nucleoside phosphorylase ( ) (PNP) that catalyses the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [ ], 6-oxopurine nucleoside phosphorylase ( ) that is a purine nucleoside phosphorylase specific for 6-oxopurine nucleosides [ , ], 5'-methylthioadenos...
[ "GO:0016763" ]
[ "pentosyltransferase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01240" ]
[ "PNP_MTAP_2" ]
[ 14376 ]
1
[ "EC", "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "2.4.2", "2.4.2.28", "PWY-6756", "PWY-8130", "R-BTA-1237112", "R-CEL-1237112", "R-DME-1237112", "R-DRE-1237112", "R-HSA-1237112", "R-HSA-6798695", "R-HSA-74217", "R-HSA-74259", "R-HSA-8950505", "R-HSA-9735763", "R-HSA-9755088", "R-MMU-1237112", "R-MMU-6798695", "R-MMU-74217", "R-...
[ "EC:2.4.2", "EC:2.4.2.28", "METACYC:PWY-6756", "METACYC:PWY-8130", "REACTOME:R-BTA-1237112", "REACTOME:R-CEL-1237112", "REACTOME:R-DME-1237112", "REACTOME:R-DRE-1237112", "REACTOME:R-HSA-1237112", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-74217", "REACTOME:R-HSA-74259", "REACTOME:R-HSA-89505...
30
[ "1a9o", "1a9p", "1a9q", "1a9r", "1a9s", "1a9t", "1b8n", "1b8o", "1c3x", "1cb0", "1cg6", "1fxu", "1g2o", "1i80", "1k27", "1lv8", "1lvu", "1m73", "1n3i", "1pbn", "1pf7", "1pwy", "1qe5", "1rct", "1rfg", "1rr6", "1rsz", "1rt9", "1sd1", "1sd2", "1ula", "1ulb"...
128
[ "PUB00002280", "PUB00002584", "PUB00060784", "PUB00060785", "PUB00060789", "PUB00060790" ]
[ "7559336", "2104852", "2108157", "3091600", "17419725", "21683167" ]
[ "Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli.", "Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.", "Physicochemical and immunological studies on mammalian 5'-deoxy-5'-methylthioad...
[ 1995, 1990, 1990, 1986, 2007, 2011 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 353, 8718, 5077, 228 ]
4
[ "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)", ...
[ 1, 45, 3, 1, 14, 6, 1, 6, 2, 1 ]
10
true
Conserved_site
Purine phosphorylase, family 2, conserved site
Purine phosphorylase, family 2, conserved site
Purine_phosphorylase-2_CS
1
IPR018101
18,101
Translation elongation factor Ts, conserved site
Transl_elong_Ts_CS
Conserved_site
27,347
false
false
This entry represents EF-Tu (EF1A) proteins found primarily in bacteria, mitochondria and chloroplasts.
[ "GO:0003746", "GO:0006414" ]
[ "translation elongation factor activity", "translational elongation" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE", "PROSITE" ]
[ "PS01126", "PS01127" ]
[ "EF_TS_1", "EF_TS_2" ]
[ 21710, 23792 ]
2
[ "REACTOME" ]
[ "R-HSA-5389840" ]
[ "REACTOME:R-HSA-5389840" ]
1
[ "1aip", "1efu", "1tfe", "1xb2", "2cp9", "3agp", "3agq", "3avt", "3avu", "3avv", "3avw", "3avx", "3avy", "3mmp", "3vnu", "3vnv", "4fwt", "4pc1", "4pc2", "4pc3", "4pc6", "4pc7", "4q7j", "4r71", "7vmx" ]
25
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Haloferax", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 23134, 3716, 3, 493, 1 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 10, 1, 1, 1, 1, 9, 7, 4, 6, 16 ]
10
true
Conserved_site
Translation elongation factor Ts, conserved site
Translation elongation factor Ts, conserved site
Transl_elong_Ts_CS
8
IPR018102
18,102
Small ribosomal subunit protein uS11, conserved site
Ribosomal_uS11_CS
Conserved_site
41,471
false
false
Ribosomal protein uS11 [ ] plays an essential role in selecting the correct tRNA in protein biosynthesis. It is located on the large lobe of the small ribosomal subunit. On the basis of sequence similarities, uS11 belongs to a family of bacterial, archaeal and eukaryotic ribosomal proteins. This entry represents a smal...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00054" ]
[ "RIBOSOMAL_S11" ]
[ 41471 ]
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-6791226", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-6791226", "R-DDI-72689", "R-DDI-72695", "R-DDI-72702", "R-DDI-72706", "R-DDI-975956",...
[ "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-6791226", "REACTOME:R-CEL-72649", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72695", "REACTOME:R-CEL-72702", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-156827", "REACTOME:R-DDI-179933...
85
[ "1fjg", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1x18", "1xmo", "1xmq", "1xnq", "1xnr", "2e5l"...
1,856
[ "PUB00001562", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "3191988", "11297922", "11290319", "11114498" ]
[ "Amino acid sequences of ribosomal proteins S11 from Bacillus stearothermophilus and S19 from Halobacterium marismortui. Comparison of the ribosomal protein S11 family.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal pr...
[ 1988, 2001, 2001, 2000 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 858, 21826, 18364, 423 ]
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",...
[ 14, 1, 2, 3, 1, 5, 7, 1, 8, 7, 2, 2, 27 ]
13
true
Conserved_site
Small ribosomal subunit protein uS11, conserved site
Small ribosomal subunit protein uS11, conserved site
Ribosomal_uS11_CS
4
IPR018103
18,103
Translationally controlled tumour protein, conserved site
Translation_control_tumour_CS
Conserved_site
4,864
false
false
The translationally controlled tumor proteins (TCTPs, such as p21, p23 and histamine releasing factor (HRF)) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in a variety of cellular functions, including microtubule stabilization, cell cycle, apoptosis, and cytokine rele...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS01002", "PS01003" ]
[ "TCTP_1", "TCTP_2" ]
[ 3800, 3761 ]
2
[]
[]
[]
0
[ "1h6q", "1h7y", "1yz1", "2hr9", "2kwb", "2loy", "3ebm", "3p3k", "5o9k", "5o9l", "5o9m", "6izb", "6ize" ]
13
[ "PUB00007168", "PUB00084252", "PUB00084253", "PUB00084254" ]
[ "11473261", "19262129", "18274553", "23085438" ]
[ "Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.", "To cease or to proliferate: new insights into TCTP function from a Drosophila study.", "TCTP protects from apoptotic cell death by antagonizing bax function.", "Molecular interaction of artemisinin with translationa...
[ 2001, 2007, 2008, 2013 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 14, 4850 ]
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...
[ 7, 1, 1, 3, 12, 2, 1, 3, 8, 1, 1, 15 ]
12
true
Conserved_site
Translationally controlled tumour protein, conserved site
Translationally controlled tumour protein, conserved site
Translation_control_tumour_CS
9
IPR018104
18,104
Translation initiation factor 1A (eIF-1A), conserved site
TIF_eIF-1A_CS
Conserved_site
6,566
false
false
Eukaryotic translation initiation factor A (eIF-1A) (formerly known as eiF-4C) is a protein that seems to be required for maximal rate of protein biosynthesis. It enhances ribosome dissociation into subunits and stabilises the binding of the initiator Met-tRNA to 40S ribosomal subunits [ ]. The archaea possess an eIF-1...
[ "GO:0003743", "GO:0006413" ]
[ "translation initiation factor activity", "translational initiation" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS01262" ]
[ "IF1A" ]
[ 6566 ]
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-DDI-156827", "R-DDI-72689", "R-DDI-72695", "R-DDI-72702", "R-HSA-156827", "R-HSA-72649", "R-HSA-72689", "R-HSA-72695", "R-HSA-72702", "R-HSA-72706", "R-MMU-156827", "R-MMU-72649", "R-MMU-72689", "R-MMU-72695", "R-MMU-72702", "R-MMU-72706", "R-RNO-156827", "R-RNO-72649", "R-RNO...
[ "REACTOME:R-DDI-156827", "REACTOME:R-DDI-72689", "REACTOME:R-DDI-72695", "REACTOME:R-DDI-72702", "REACTOME:R-HSA-156827", "REACTOME:R-HSA-72649", "REACTOME:R-HSA-72689", "REACTOME:R-HSA-72695", "REACTOME:R-HSA-72702", "REACTOME:R-HSA-72706", "REACTOME:R-MMU-156827", "REACTOME:R-MMU-72649", "...
32
[ "1d7q", "1jt8", "2oqk", "3j80", "3j81", "3jam", "3jap", "3wbk", "3zjy", "4bts", "4kzy", "4kzz", "4mno", "4uer", "5jb3", "5jbh", "6fyx", "6fyy", "6gsm", "6gsn", "6sw9", "6swc", "6swd", "6swe", "6yal", "6yam", "6ybw", "6zce", "6zmw", "6zp4", "6zu9", "7a09"...
66
[ "PUB00002919" ]
[ "7559407" ]
[ "Characterization of yeast translation initiation factor 1A and cloning of its essential gene." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Archaea", "Eukaryota", "Oceanibaculum indicum", "Sylvanvirus sp.", "ecological metagenomes" ]
[ 1096, 5451, 2, 1, 16 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea ma...
[ 7, 1, 2, 2, 5, 18, 4, 8, 1, 1, 8 ]
11
true
Conserved_site
Translation initiation factor 1A (eIF-1A), conserved site
Translation initiation factor 1A (eIF-1A), conserved site
TIF_eIF-1A_CS
3
IPR018105
18,105
Translationally controlled tumour protein
Translational_control_tumour_p
Family
6,195
false
false
Mammalian translationally controlled tumour protein (TCTP) (or P23) is a protein which has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour [ , ], but which is also expressed in normal cells. The physiological function of TCTP is still not known. It was first id...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF00838", "PR01653", "PTHR11991" ]
[ "TCTP", "TCTPROTEIN", "" ]
[ 6189, 5349, 5931 ]
3
[]
[]
[]
0
[ "1h6q", "1h7y", "1txj", "1yz1", "2hr9", "2kwb", "2loy", "3ebm", "3p3k", "5o9k", "5o9l", "5o9m", "6izb", "6ize", "6j2y" ]
15
[ "PUB00000270", "PUB00000677", "PUB00004349", "PUB00004553", "PUB00006584", "PUB00007167", "PUB00007168" ]
[ "2479380", "9655922", "3357792", "1623194", "8091862", "10951206", "11473261" ]
[ "The growth-related protein P23 of the Ehrlich ascites tumor: translational control, cloning and primary structure.", "Identification of heavy metal induced changes in the expression patterns of the translationally controlled tumour protein (TCTP) in the earthworm Lumbricus rubellus1.", "Nucleotide sequence of ...
[ 1989, 1998, 1988, 1992, 1994, 2000, 2001 ]
7
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 21, 6174 ]
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...
[ 9, 1, 1, 3, 14, 2, 1, 3, 8, 1, 1, 17 ]
12
true
Family
Translationally controlled tumour protein
Translationally controlled tumour protein
Translational_control_tumour_p
8
IPR018107
18,107
Sodium:dicarboxylate symporter, conserved site
Na-dicarboxylate_symporter_CS
Conserved_site
30,714
false
false
It has been shown [ ] that integral membrane proteins that mediate the uptake of a wide variety of molecules with the concomitant uptake of sodium ions (sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. One of these families is known as the sodiu...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS00713", "PS00714" ]
[ "NA_DICARBOXYL_SYMP_1", "NA_DICARBOXYL_SYMP_2" ]
[ 22403, 27353 ]
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-210455", "R-BTA-210500", "R-BTA-352230", "R-BTA-425393", "R-BTA-9013149", "R-BTA-9013406", "R-BTA-9013407", "R-BTA-9013423", "R-CEL-210455", "R-CEL-210500", "R-CEL-352230", "R-CEL-425393", "R-CEL-9013149", "R-CEL-9013406", "R-CEL-9013407", "R-CEL-9013423", "R-HSA-210455", "R...
[ "REACTOME:R-BTA-210455", "REACTOME:R-BTA-210500", "REACTOME:R-BTA-352230", "REACTOME:R-BTA-425393", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013407", "REACTOME:R-BTA-9013423", "REACTOME:R-CEL-210455", "REACTOME:R-CEL-210500", "REACTOME:R-CEL-352230", "REACTOME:R-CEL...
42
[ "1xfh", "2nwl", "2nww", "2nwx", "3v8f", "3v8g", "4izm", "4ky0", "4oye", "4oyf", "4x2s", "5cfy", "5dwy", "5e9s", "5llm", "5llu", "5lm4", "5mju", "6bat", "6bau", "6bav", "6bmi", "6gct", "6mp6", "6mpb", "6r7r", "6rvx", "6rvy", "6s3q", "6uwf", "6uwl", "6v8g"...
114
[ "PUB00000660", "PUB00004137", "PUB00004138", "PUB00004767" ]
[ "8031825", "1448170", "1280334", "1279699" ]
[ "A functional superfamily of sodium/solute symporters.", "Cloning and expression of a rat brain L-glutamate transporter.", "Primary structure and functional characterization of a high-affinity glutamate transporter.", "Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate tra...
[ 1994, 1992, 1992, 1992 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 177, 17174, 13267, 96 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 32, 8, 2, 66, 36, 54 ]
7
true
Conserved_site
Sodium:dicarboxylate symporter, conserved site
Sodium:dicarboxylate symporter, conserved site
Na-dicarboxylate_symporter_CS
5
IPR018108
18,108
Mitochondrial carrier protein, transmembrane region
MCP_transmembrane
Repeat
214,295
false
false
This entry represents the transmembrane region in mitochondrial carrier proteins. A variety of substrate carrier proteins involved in energy transfer are found in the inner mitochondrial membrane or are integral to the membranes of other eukaryotic organelles such as the peroxisome [ , , , , ]. Such proteins include: A...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF00153", "PS50920" ]
[ "Mito_carr", "SOLCAR" ]
[ 213619, 210746 ]
2
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp1413", "R-BTA-1268020", "R-BTA-166187", "R-BTA-167826", "R-BTA-196819", "R-BTA-352230", "R-BTA-425393", "R-BTA-428643", "R-BTA-71064", "R-BTA-83936", "R-BTA-9837999", "R-BTA-9856872", "R-CEL-1614517", "R-CEL-200425", "R-CEL-428643", "R-CEL-8963693", "R-CEL-9856872", "R-DDI-...
[ "GP:GenProp1413", "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-166187", "REACTOME:R-BTA-167826", "REACTOME:R-BTA-196819", "REACTOME:R-BTA-352230", "REACTOME:R-BTA-425393", "REACTOME:R-BTA-428643", "REACTOME:R-BTA-71064", "REACTOME:R-BTA-83936", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9856872", ...
136
[ "1okc", "2c3e", "2lck", "4c9g", "4c9h", "4c9j", "4c9q", "6gci", "7w5z", "8b6h", "8bqs", "8g8w", "8gym", "8gzu", "8hbv", "8hbw", "8j1n", "9fzq" ]
18
[ "PUB00001005", "PUB00001675", "PUB00003301", "PUB00005084", "PUB00005351", "PUB00005407", "PUB00029479", "PUB00101069" ]
[ "8325039", "8206158", "8487299", "8140286", "2158156", "8291088", "14603310", "21785437" ]
[ "The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships.", "Mitochondrial carrier proteins.", "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential.", "Expansion of the mitochondrial carrie...
[ 1993, 1994, 1993, 1993, 1990, 1993, 2003, 2011 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halorutilus salinus", "Viruses", "metagenomes" ]
[ 162, 213995, 1, 71, 66 ]
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...
[ 269, 49, 158, 119, 270, 169, 40, 202, 237, 34, 24, 409 ]
12
true
Repeat
Mitochondrial carrier protein, transmembrane region
Mitochondrial carrier protein, transmembrane region
MCP_transmembrane
2
IPR018109
18,109
Folylpolyglutamate synthetase, conserved site
Folylpolyglutamate_synth_CS
Conserved_site
43,738
false
false
Folylpolyglutamate synthase (FPGS) is an ATP-dependent enzyme that is responsible for the addition of a polyglutamate tail to folate and folate derivatives [ ]. It plays a key role in the retention of the intracellular folate pool. In some bacteria, such as Escherichia coli, the addition of L-glutamate to dihydropteroa...
[ "GO:0004326", "GO:0005524", "GO:0009396" ]
[ "tetrahydrofolylpolyglutamate synthase activity", "ATP binding", "folic acid-containing compound biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE", "PROSITE" ]
[ "PS01011", "PS01012" ]
[ "FOLYLPOLYGLU_SYNT_1", "FOLYLPOLYGLU_SYNT_2" ]
[ 28965, 25290 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.2", "R-CEL-196757", "R-DDI-196757", "R-HSA-196757", "R-MMU-196757", "R-SCE-196757", "R-SPO-196757" ]
[ "EC:6.3.2", "REACTOME:R-CEL-196757", "REACTOME:R-DDI-196757", "REACTOME:R-HSA-196757", "REACTOME:R-MMU-196757", "REACTOME:R-SCE-196757", "REACTOME:R-SPO-196757" ]
7
[ "1fgs", "1jbv", "1jbw", "1o5z", "1w78", "1w7k", "2gc5", "2gc6", "2gca", "2gcb", "2vor", "2vos", "3n2a", "3nrs", "3pyz", "3qcz", "4bub", "6vr7", "7wac", "7wad", "7wae", "7waf", "8f5d" ]
23
[ "PUB00006413", "PUB00032198" ]
[ "9618466", "15705579" ]
[ "Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase.", "Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy." ]
[ 1998, 2005 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 371, 33752, 8869, 1, 745 ]
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",...
[ 22, 1, 1, 3, 1, 6, 3, 2, 9, 7, 3, 1, 49 ]
13
true
Conserved_site
Folylpolyglutamate synthetase, conserved site
Folylpolyglutamate synthetase, conserved site
Folylpolyglutamate_synth_CS
4