LiteFold/InterPro · Datasets at Hugging Face

IPR004066

4,066

Lysophosphatidic acid receptor EDG-4

LPA_rcpt_EDG4

Family

187

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:0070915", "GO:0007186", "GO:0016020" ]

[ "lysophosphatidic acid receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS" ]

[ "PR01528" ]

[ "EDG4RECEPTOR" ]

[ 187 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "273", "R-HSA-416476", "R-HSA-418594", "R-HSA-419408", "R-MMU-416476", "R-MMU-418594", "R-MMU-419408" ]

[ "IUPHAR:273", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-419408", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-MMU-419408" ]

7

[]

0

[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00007103", "PUB00007104", "PUB00007190", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]

[ "2111655", "2830256", "8386361", "8170923", "11264467", "10603487", "11093753", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]

[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "Lysophospholipid receptors.", "Life on the edg.", "Lysophosphatidic acid receptors.", ...

[ 1990, 1988, 1993, 1994, 2001, 1999, 2000, 2003, 1994, 2005, 2009, 2006, 2013 ]

13

[ "IPR004065" ]

[]

1

0

1

[ "Amniota" ]

[ 187 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 2, 2 ]

3

true

Family

Lysophosphatidic acid receptor EDG-4

LPA_rcpt_EDG4

1

IPR004067

4,067

CC chemokine receptor 6

Chemokine_CCR6

Family

225

false

Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...

[ "GO:0016493", "GO:0006935", "GO:0006955", "GO:0007186", "GO:0016020" ]

[ "C-C chemokine receptor activity", "chemotaxis", "immune response", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]

5

[ "PRINTS" ]

[ "PR01529" ]

[ "CHEMOKINER6" ]

[ 225 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "63", "R-HSA-1461957", "R-HSA-380108", "R-HSA-418594", "R-MMU-1461957", "R-MMU-380108", "R-MMU-418594" ]

[ "IUPHAR:63", "REACTOME:R-HSA-1461957", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-1461957", "REACTOME:R-MMU-380108", "REACTOME:R-MMU-418594" ]

7

[ "6wwz" ]

1

[ "PUB00007326", "PUB00009401", "PUB00064589", "PUB00064621", "PUB00064622", "PUB00064688", "PUB00064689", "PUB00064690", "PUB00064691", "PUB00064692", "PUB00067945", "PUB00067946", "PUB00095353", "PUB00095354" ]

[ "9169459", "11544102", "10714678", "10601351", "9500790", "9886385", "9294137", "17486092", "10521347", "19249008", "9689100", "7592998", "20068036", "25122636" ]

[ "Identification of CCR6, the specific receptor for a novel lymphocyte-directed CC chemokine LARC.", "Chemokine receptors.", "Chemokines: a new classification system and their role in immunity.", "Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells."...

[ 1997, 2001, 2000, 1999, 1998, 1999, 1997, 2007, 1999, 2009, 1998, 1995, 2010, 2014 ]

14

[ "IPR000355" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 225 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 3, 2 ]

3

true

Family

CC chemokine receptor 6

Chemokine_CCR6

7

IPR004068

4,068

CC chemokine receptor 8

Chemokine_CCR8

Family

152

false

Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...

[ "GO:0016493", "GO:0006935", "GO:0006955", "GO:0007186", "GO:0007204", "GO:0016020" ]

[ "C-C chemokine receptor activity", "chemotaxis", "immune response", "G protein-coupled receptor signaling pathway", "positive regulation of cytosolic calcium ion concentration", "membrane" ]

[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]

6

[ "PRINTS" ]

[ "PR01530" ]

[ "CHEMOKINER8" ]

[ 152 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "65", "R-HSA-380108", "R-HSA-418594", "R-MMU-380108", "R-MMU-418594" ]

[ "IUPHAR:65", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-380108", "REACTOME:R-MMU-418594" ]

5

[ "8kfx", "8kfy", "8kfz", "8xml" ]

4

[ "PUB00009401", "PUB00064589", "PUB00064621", "PUB00064622", "PUB00064705", "PUB00064706", "PUB00064707", "PUB00064708", "PUB00064710", "PUB00064711", "PUB00064713", "PUB00064714", "PUB00064715", "PUB00067945", "PUB00067946" ]

[ "11544102", "10714678", "10601351", "9500790", "9211859", "10540332", "10910894", "10419462", "9521068", "14576057", "11340325", "10611408", "12055238", "9689100", "7592998" ]

[ "Chemokine receptors.", "Chemokines: a new classification system and their role in immunity.", "Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.", "Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocyte...

[ 2001, 2000, 1999, 1998, 1997, 1999, 2000, 1999, 1998, 2004, 2001, 1999, 2002, 1998, 1995 ]

15

[ "IPR000355" ]

[]

1

0

1

[ "Theria" ]

[ 152 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 3, 2 ]

3

true

Family

CC chemokine receptor 8

Chemokine_CCR8

3

IPR004069

4,069

CC chemokine receptor 9

Chemokine_CCR9

Family

198

false

Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...

[ "GO:0016493", "GO:0006935", "GO:0006955", "GO:0007186", "GO:0016020" ]

[ "C-C chemokine receptor activity", "chemotaxis", "immune response", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]

5

[ "PRINTS" ]

[ "PR01531" ]

[ "CHEMOKINER9" ]

[ 198 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "66", "R-HSA-380108", "R-HSA-418594", "R-MMU-380108", "R-MMU-418594" ]

[ "IUPHAR:66", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-380108", "REACTOME:R-MMU-418594" ]

5

[ "5lwe" ]

1

[ "PUB00009401", "PUB00018819", "PUB00064589", "PUB00064621", "PUB00064622", "PUB00064715", "PUB00064718", "PUB00064720", "PUB00064721", "PUB00064722", "PUB00064723", "PUB00067945", "PUB00067946", "PUB00067947" ]

[ "11544102", "10229797", "10714678", "10601351", "9500790", "12055238", "10498628", "11159507", "16253981", "11046037", "11487533", "9689100", "7592998", "15623660" ]

[ "Chemokine receptors.", "Cutting edge: identification of the orphan chemokine receptor GPR-9-6 as CCR9, the receptor for the chemokine TECK.", "Chemokines: a new classification system and their role in immunity.", "Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal...

[ 2001, 1999, 2000, 1999, 1998, 2002, 1999, 2001, 2006, 2000, 2001, 1998, 1995, 2004 ]

14

[ "IPR000355" ]

[]

1

0

1

[ "Theria" ]

[ 198 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 2, 3 ]

3

true

Family

CC chemokine receptor 9

Chemokine_CCR9

2

IPR004070

4,070

CXC chemokine receptor 3

Chemokine_CXCR3

Family

513

false

Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...

[ "GO:0016494", "GO:0002685", "GO:0006935", "GO:0006954", "GO:0007186", "GO:0016020" ]

[ "C-X-C chemokine receptor activity", "regulation of leukocyte migration", "chemotaxis", "inflammatory response", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]

6

[ "PRINTS" ]

[ "PR01532" ]

[ "CXCCHMKINER3" ]

[ 513 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "70", "R-BTA-380108", "R-BTA-418594", "R-HSA-380108", "R-HSA-418594", "R-MMU-380108", "R-MMU-418594", "R-RNO-380108", "R-RNO-418594" ]

[ "IUPHAR:70", "REACTOME:R-BTA-380108", "REACTOME:R-BTA-418594", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-380108", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-380108", "REACTOME:R-RNO-418594" ]

9

[ "8hnk", "8hnl", "8hnm", "8hnn", "8k2w", "8k2x", "8xxy", "8xxz", "8xyi", "8xyk", "8y0h", "8y0n" ]

12

[ "PUB00007328", "PUB00007329", "PUB00007330", "PUB00007331", "PUB00009401", "PUB00028909", "PUB00063238", "PUB00064589", "PUB00064621", "PUB00064622", "PUB00064677", "PUB00064860", "PUB00064861", "PUB00064862", "PUB00064863", "PUB00064864", "PUB00064865", "PUB00064867", "PUB000648...

[ "9625760", "9660793", "9064356", "11310833", "11544102", "12173928", "10233762", "10714678", "10601351", "9500790", "10699158", "12750173", "11085753", "10525042", "15254596", "12415259", "17538187", "9466968", "16127166", "10605606", "9987599", "17600132", "12884299", ...

[ "Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3.", "Binding and functional properties of recombinant and endogenous CXCR3 chemokine receptors.", "Chemokine receptor specific for I...

[ 1998, 1998, 1996, 2001, 2001, 2002, 1999, 2000, 1999, 1998, 2000, 2003, 2000, 1999, 2004, 2002, 2007, 1998, 2005, 2000, 1999, 2007, 2003, 1998, 1995 ]

25

[ "IPR000355" ]

[]

1

0

1

[ "Gnathostomata" ]

[ 513 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 3, 1, 2 ]

4

true

Family

CXC chemokine receptor 3

Chemokine_CXCR3

7

IPR004072

4,072

Vomeronasal receptor, type 1

Vmron_rcpt_1

Family

7,844

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:0016503", "GO:0007186", "GO:0016020" ]

[ "pheromone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PFAM", "PRINTS", "PANTHER" ]

[ "PF03402", "PR01534", "PTHR24062" ]

[ "V1R", "VOMERONASL1R", "" ]

[ 7841, 5308, 7676 ]

3

[]

0

[]

0

[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00007338", "PUB00007339", "PUB00007340", "PUB00007341", "PUB00007342", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]

[ "2111655", "2830256", "8386361", "8170923", "11163270", "10531049", "10548735", "11116092", "10973240", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]

[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "A novel family of candidate pheromone receptors in mammals.", "The vomeronasal organ.", ...

[ 1990, 1988, 1993, 1994, 2000, 1999, 1999, 2000, 2000, 2003, 1994, 2005, 2009, 2006, 2013 ]

15

[]

0

null

[ "Bilateria" ]

[ 7844 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 10, 342, 121 ]

4

true

Family

Vomeronasal receptor, type 1

Vmron_rcpt_1

5

IPR004073

4,073

GPCR, family 3, vomeronasal receptor, type 2

GPCR_3_vmron_rcpt_2

Family

13,811

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

[ "PRINTS" ]

[ "PR01535" ]

[ "VOMERONASL2R" ]

[ 13811 ]

1

[]

0

[]

0

[ "PUB00004161", "PUB00004309", "PUB00004961", "PUB00007338", "PUB00007339", "PUB00007343", "PUB00007344", "PUB00007345", "PUB00036049", "PUB00036050", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]

[ "8255296", "1309649", "8170923", "11163270", "10531049", "9292726", "9560249", "10433261", "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 novel family of candidate pheromone receptors in mammals.", "The vomeronasal organ.", "A new multigene fam...

[ 1993, 1992, 1994, 2000, 1999, 1997, 1998, 1999, 2007, 2000, 2003, 1994, 2005, 2009, 2006, 2013 ]

16

[ "IPR000337" ]

[]

1

0

1

[ "Vertebrata" ]

[ 13811 ]

1

[ "Danio rerio", "Mus musculus", "Rattus norvegicus" ]

[ 69, 274, 151 ]

3

true

Family

GPCR, family 3, vomeronasal receptor, type 2

GPCR_3_vmron_rcpt_2

6

IPR004074

4,074

Interleukin-1 receptor type I/II

IL-1_rcpt_I/II-typ

Family

5,243

false

Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif...

[ "GO:0004908" ]

[ "interleukin-1 receptor activity" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR01536" ]

[ "INTRLKN1R12F" ]

[ 5243 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...

[ "3.2.2.6", "PWY-5381", "R-HSA-1257604", "R-HSA-388844", "R-HSA-6783783", "R-HSA-6811558", "R-HSA-9007892", "R-HSA-9008059", "R-HSA-9012546", "R-HSA-9014826", "R-HSA-9014843", "R-HSA-9020702", "R-HSA-9679191", "R-MMU-1257604", "R-MMU-388844", "R-MMU-6811558", "R-MMU-9007892", "R-MMU...

[ "EC:3.2.2.6", "METACYC:PWY-5381", "REACTOME:R-HSA-1257604", "REACTOME:R-HSA-388844", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-6811558", "REACTOME:R-HSA-9007892", "REACTOME:R-HSA-9008059", "REACTOME:R-HSA-9012546", "REACTOME:R-HSA-9014826", "REACTOME:R-HSA-9014843", "REACTOME:R-HSA-9020702", ...

28

[ "1g0y", "1ira", "1itb", "3o4o", "3wo3", "3wo4", "4dep", "4gaf", "4kc3", "4r6u", "4yfd", "5vi4", "6u6u", "9eth", "9eti" ]

15

[ "PUB00003281", "PUB00004697", "PUB00007346", "PUB00007347", "PUB00007348", "PUB00007349", "PUB00007350", "PUB00007351" ]

[ "1738162", "2602367", "2969618", "8702856", "1833184", "1826022", "1339315", "9062194" ]

[ "beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.", "Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.", "cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.", ...

[ 1992, 1989, 1988, 1996, 1991, 1991, 1992, 1997 ]

8

[ "IPR015621" ]

[ "IPR004076", "IPR004077", "IPR004078" ]

1

3

0

[ "Chordopoxvirinae", "Deuterostomia" ]

[ 114, 5129 ]

2

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 31, 25, 22, 37 ]

4

true

Family

Interleukin-1 receptor type I/II

IL-1_rcpt_I/II-typ

4

IPR004076

4,076

Interleukin-1 receptor type 1

IL-1_rcpt_I-typ

Family

1,279

false

Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif...

[ "GO:0004909" ]

[ "interleukin-1, type I, activating receptor activity" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR01538" ]

[ "INTRLEUKN1R1" ]

[ 1279 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.2.2.6", "PWY-5381", "R-HSA-6783783", "R-HSA-9007892", "R-HSA-9014826", "R-HSA-9020702", "R-HSA-9679191", "R-MMU-9007892", "R-MMU-9014826", "R-MMU-9020702", "R-RNO-9020702" ]

[ "EC:3.2.2.6", "METACYC:PWY-5381", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-9007892", "REACTOME:R-HSA-9014826", "REACTOME:R-HSA-9020702", "REACTOME:R-HSA-9679191", "REACTOME:R-MMU-9007892", "REACTOME:R-MMU-9014826", "REACTOME:R-MMU-9020702", "REACTOME:R-RNO-9020702" ]

11

[ "1g0y", "1ira", "1itb", "4dep", "4gaf" ]

5

[ "PUB00003281", "PUB00004697", "PUB00007346", "PUB00007347", "PUB00007348", "PUB00007349", "PUB00007350", "PUB00007351" ]

[ "1738162", "2602367", "2969618", "8702856", "1833184", "1826022", "1339315", "9062194" ]

[ "beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.", "Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.", "cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.", ...

[ 1992, 1989, 1988, 1996, 1991, 1991, 1992, 1997 ]

8

[ "IPR004074" ]

[]

1

0

1

[ "Tetrapoda" ]

[ 1279 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 14, 6, 15 ]

3

true

Family

Interleukin-1 receptor type 1

IL-1_rcpt_I-typ

8

IPR004077

4,077

Interleukin-1 receptor type II

IL-1_rcpt_II-typ

Family

838

false

Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif...

[ "GO:0004910" ]

[ "interleukin-1, type II, blocking receptor activity" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR01539" ]

[ "INTRLEUKN1R2" ]

[ 838 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "69", "R-HSA-388844", "R-HSA-6783783", "R-HSA-9020702", "R-MMU-388844", "R-MMU-9020702", "R-RNO-9020702" ]

[ "IUPHAR:69", "REACTOME:R-HSA-388844", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-9020702", "REACTOME:R-MMU-388844", "REACTOME:R-MMU-9020702", "REACTOME:R-RNO-9020702" ]

7

[ "3o4o" ]

1

[ "PUB00003281", "PUB00004697", "PUB00007346", "PUB00007347", "PUB00007348", "PUB00007349", "PUB00007350" ]

[ "1738162", "2602367", "2969618", "8702856", "1833184", "1826022", "1339315" ]

[ "beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.", "Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.", "cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.", ...

[ 1992, 1989, 1988, 1996, 1991, 1991, 1992 ]

7

[ "IPR004074" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 838 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 4, 6, 8 ]

3

true

Family

Interleukin-1 receptor type II

IL-1_rcpt_II-typ

5

IPR004078

4,078

Interleukin-1 binding protein

IL-1-bd

Family

133

false

Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif...

[ "GO:0019966", "GO:0044003" ]

[ "interleukin-1 binding", "symbiont-mediated perturbation of host process" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS" ]

[ "PR01540" ]

[ "INTRLEUKN1BP" ]

[ 133 ]

1

[]

0

[]

0

[ "PUB00003281", "PUB00004697", "PUB00007346", "PUB00007347", "PUB00007348", "PUB00007349", "PUB00007350" ]

[ "1738162", "2602367", "2969618", "8702856", "1833184", "1826022", "1339315" ]

[ "beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.", "Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.", "cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.", ...

[ 1992, 1989, 1988, 1996, 1991, 1991, 1992 ]

7

[ "IPR004074" ]

[]

1

0

1

[ "Chordopoxvirinae" ]

[ 133 ]

1

[]

0

true

Family

Interleukin-1 binding protein

IL-1-bd

8

IPR004079

4,079

Gonadoliberin I precursor

Gonadoliberin_I_precursor

Family

666

false

Reproduction is controlled in humans by the hypothalamic-pituitary-gonadal axis [ ]. A key molecule in this control circuit is the decapeptide luteinising hormone releasing hormone (LHRH), also termed gonadotropin-releasing hormone (GnRH). GnRH is produced by hypothalamic neurones, secreted in a pulsatile manner into t...

[ "GO:0005183" ]

[ "gonadotropin hormone-releasing hormone activity" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR01541" ]

[ "GONADOLIBRNI" ]

[ 666 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-GGA-375281", "R-GGA-416476", "R-HSA-375281", "R-HSA-416476", "R-MMU-375281", "R-MMU-416476", "R-RNO-375281", "R-RNO-416476", "R-SSC-375281", "R-SSC-416476" ]

[ "REACTOME:R-GGA-375281", "REACTOME:R-GGA-416476", "REACTOME:R-HSA-375281", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375281", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375281", "REACTOME:R-RNO-416476", "REACTOME:R-SSC-375281", "REACTOME:R-SSC-416476" ]

10

[]

0

[ "PUB00007352" ]

[ "6090951" ]

[ "Characterization of cDNA for precursor of human luteinizing hormone releasing hormone." ]

[ 1984 ]

1

[ "IPR019792" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 666 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 4, 3 ]

3

true

Family

Gonadoliberin I precursor

Gonadoliberin_I_precursor

6

IPR004080

4,080

Foot-and-mouth disease virus VP1 coat

FMDV_VP1_coat

Domain

11,599

false

The complete nucleotide sequence of cDNA coding for the structural capsid polypeptides of Foot-and-mouth disease virus (FMDV) has been determined. The FMDV capsid is composed of 60 icosahedral units, each of which comprises one copy each of proteins VP1, VP2, VP3 and VP4 [ ]. Specific enzymatic cleavages in vivo yield ...

[ "GO:0005198", "GO:0019028" ]

[ "structural molecule activity", "viral capsid" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR01542" ]

[ "FMDVP1COAT" ]

[ 11599 ]

1

[ "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.7.7.48", "3.4.22.28", "3.4.22.46", "3.6.1.15", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210" ]

[ "EC:2.7.7.48", "EC:3.4.22.28", "EC:3.4.22.46", "EC:3.6.1.15", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210" ]

9

[ "1bbt", "1fmd", "1fod", "1qgc", "1qqp", "1zba", "1zbe", "2wzr", "4gh4", "4iv1", "4iv3", "5ac9", "5aca", "5d8a", "5ddj", "5ne4", "5ned", "5nej", "5nem", "5ner", "5net", "5neu", "5owx", "5oyi", "7d3k", "7d3l", "7d3m", "7d3r", "7dss", "7dst", "7eno", "7enp"...

45

[ "PUB00007353", "PUB00007354" ]

[ "6282711", "2537470" ]

[ "The nucleotide sequence of cDNA coding for the structural proteins of foot-and-mouth disease virus.", "The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution." ]

[ 1982, 1989 ]

2

[ "IPR001676" ]

[]

1

0

1

[ "Foot-and-mouth disease virus" ]

[ 11599 ]

1

[]

0

true

Domain

Foot-and-mouth disease virus VP1 coat

FMDV_VP1_coat

2

IPR004082

4,082

Protein OBERON

OBERON

Family

2,518

false

This entry represents a plant specific protein family, OBERON (OBE), also known as ptyvirus VPg-interacting protein (PVIP). In Arabidopsis, there are four OBEs, OBE1-4. OBE1 together with OBE2 are required for the maintenance and/or establishment of both the shoot and root meristems, probably by controlling the express...

[]

0

[ "PRINTS", "PANTHER" ]

[ "PR01544", "PTHR21736" ]

[ "ARATH130DUF", "" ]

[ 2355, 2504 ]

2

[]

0

[]

0

[ "PUB00067922", "PUB00067923", "PUB00067924", "PUB00092785" ]

[ "18403411", "19392692", "14963126", "30194869" ]

[ "The Arabidopsis OBERON1 and OBERON2 genes encode plant homeodomain finger proteins and are required for apical meristem maintenance.", "Arabidopsis plant homeodomain finger proteins operate downstream of auxin accumulation in specifying the vasculature and primary root meristem.", "A cysteine-rich plant protei...

[ 2008, 2009, 2004, 2018 ]

4

[]

0

null

[ "Eukaryota" ]

[ 2518 ]

1

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 15, 11, 19 ]

3

true

Family

Protein OBERON

OBERON

2

IPR004083

4,083

Regulatory associated protein of TOR

Raptor

Family

7,325

false

This family consists of Raptor (regulatory associated protein of TOR) and its orthologs which includes Kog1p of Saccharomyces cerevisiae (Baker's yeast), a highly conserved 150kDa TOR-binding protein [ , , ]. The target-of-rapamycin (TOR) proteins are protein kinases that were first identified in S. cerevisiae through ...

[ "GO:0031929", "GO:0031931" ]

[ "TOR signaling", "TORC1 complex" ]

[ "biological_process", "cellular_component" ]

2

[ "PANTHER" ]

[ "PTHR12848" ]

[ "" ]

[ 7325 ]

1

[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "GenProp2030", "R-DDI-1632852", "R-DDI-165159", "R-DDI-166208", "R-DDI-3371571", "R-DDI-380972", "R-DDI-5628897", "R-DDI-8943724", "R-DDI-9639288", "R-HSA-1632852", "R-HSA-165159", "R-HSA-166208", "R-HSA-3371571", "R-HSA-380972", "R-HSA-5628897", "R-HSA-8943724", "R-HSA-9639288", "...

[ "GP:GenProp2030", "REACTOME:R-DDI-1632852", "REACTOME:R-DDI-165159", "REACTOME:R-DDI-166208", "REACTOME:R-DDI-3371571", "REACTOME:R-DDI-380972", "REACTOME:R-DDI-5628897", "REACTOME:R-DDI-8943724", "REACTOME:R-DDI-9639288", "REACTOME:R-HSA-1632852", "REACTOME:R-HSA-165159", "REACTOME:R-HSA-1662...

29

[ "5h64", "5wbi", "5wbj", "5wbk", "5wbl", "6bcu", "6bcx", "6sb0", "6sb2", "6u62", "6zpn", "7owg", "7pea", "7peb", "7pec", "7pqh", "7ux2", "7uxc", "7uxh", "8era", "8rch", "8rck", "8rcn", "9ed4", "9f42", "9f43", "9f44", "9f45" ]

28

[ "PUB00000893", "PUB00015259", "PUB00015260", "PUB00015261", "PUB00015263" ]

[ "8387896", "12150925", "12150926", "12408816", "15450605" ]

[ "Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression.", "mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery.", "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action.", ...

[ 1993, 2002, 2002, 2002, 2004 ]

5

[]

0

null

[ "Eukaryota", "marine sediment metagenome" ]

[ 7324, 1 ]

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...

[ 15, 5, 11, 3, 6, 10, 1, 4, 5, 1, 1, 65 ]

12

true

Family

Regulatory associated protein of TOR

Raptor

6

IPR004084

4,084

Meiosis-specific protein Spo11

Meiosis_Spo11

Domain

284

false

Spo11 is a meiosis-specific protein that is responsible for the initiation of recombination during the early stages of meiosis through the formation of DNA double-strand breaks (DSBs) by a type II DNA topoisomerase-like activity [ , ]. These DSBs initiate homologous recombination, which is required for chromosomal segr...

[ "GO:0003677", "GO:0007131" ]

[ "DNA binding", "reciprocal meiotic recombination" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF03533" ]

[ "SPO11_like" ]

[ 284 ]

1

[ "REACTOME" ]

[ "R-HSA-912446" ]

[ "REACTOME:R-HSA-912446" ]

1

[]

0

[ "PUB00007203", "PUB00007204", "PUB00020805", "PUB00083725" ]

[ "10534401", "10622720", "11805049", "26917763" ]

[ "Cloning, characterization, and localization of mouse and human SPO11.", "Differential gene expression of mammalian SPO11/TOP6A homologs during meiosis.", "Functional interactions between SPO11 and REC102 during initiation of meiotic recombination in Saccharomyces cerevisiae.", "A DNA topoisomerase VI-like co...

[ 1999, 1999, 2002, 2016 ]

4

[]

0

null

[ "Sarcopterygii" ]

[ 284 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 1, 1 ]

3

true

Domain

Meiosis-specific protein Spo11

Meiosis_Spo11

3

IPR004085

4,085

DNA topoisomerase VI, subunit A

TopoVI_A

Family

1,882

false

This entry represents subunit A of topoisomerase VI, a type IIB topoisomerase found predominantly in archaea, but also in a few eukayotes, such as the plant Arabidopsis thaliana [ ]. This enzyme assembles as a heterotetramer, consisting of two A subunits required for DNA cleavage and two B subunits required for ATP hyd...

[ "GO:0003677", "GO:0003918", "GO:0006265", "GO:0005694" ]

[ "DNA binding", "DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity", "DNA topological change", "chromosome" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP", "PRINTS" ]

[ "MF_00132", "PR01552" ]

[ "Top6A", "TPISMRASE6A" ]

[ 1446, 1868 ]

2

[ "EC" ]

[ "5.6.2.2" ]

[ "EC:5.6.2.2" ]

1

[ "1d3y", "2q2e", "2zbk" ]

3

[ "PUB00005437", "PUB00007202", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00020795", "PUB00020804" ]

[ "7770916", "10545127", "11395412", "12596227", "12042765", "7980433", "12618182" ]

[ "The mechanisms of DNA topoisomerases.", "Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11.", "DNA topoisomerases: structure, function, and mechanism.", "Phylogenomics of type II DNA topoisomerases.", "Cellular roles of DNA topoisomerases...

[ 1995, 1999, 2001, 2003, 2002, 1994, 2003 ]

7

[ "IPR002815" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 976, 88, 772, 46 ]

4

[ "Arabidopsis thaliana", "Drosophila melanogaster", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 3, 1, 3, 4 ]

4

true

Family

DNA topoisomerase VI, subunit A

TopoVI_A

1

IPR004086

4,086

P pili tip fibrillum PapE protein, Enterobacteriaceae

P_pili_tip_fibrillum_PapE

Family

45

false

The Gram-negative pathogen Escherichia coli causes several common bacterial illnesses in humans, including diarrhoea, neonatal meningitidis and urinary tract infections. Attachment to host tissues is essential for successful invasion, and requires interaction between a bacterial adhesive protein and its target receptor...

[ "GO:0007155", "GO:0009289" ]

[ "cell adhesion", "pilus" ]

[ "biological_process", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR01555" ]

[ "FIMBRIALPAPE" ]

[ 45 ]

1

[]

0

[ "1n0l", "1n12" ]

2

[ "PUB00007359", "PUB00007360", "PUB00007361", "PUB00007362" ]

[ "1348107", "7816100", "2895103", "8917515" ]

[ "P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips.", "Structural polymorphism of bacterial adhesion pili.", "Structure and antigenic properties of the tip-located P pilus proteins of uropathogenic Escherichia coli.", "Development of pilus organelle subassemblies in vi...

[ 1992, 1995, 1988, 1996 ]

4

[]

0

null

[ "Enterobacteriaceae" ]

[ 45 ]

1

[]

0

true

Family

P pili tip fibrillum PapE protein, Enterobacteriaceae

P_pili_tip_fibrillum_PapE

8

IPR004088

4,088

K Homology domain, type 1

KH_dom_type_1

Domain

134,823

false

The K homology (KH) domain was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. It is a domain of around 70 amino acids that is present in a wide variety of quite diverse nucleic acid-binding proteins [ ]. It has been shown to bind RNA [ , ]. Like many other RNA-binding motifs, KH motifs...

[ "GO:0003723" ]

[ "RNA binding" ]

[ "molecular_function" ]

1

[ "PFAM", "PFAM" ]

[ "PF00013", "PF15985" ]

[ "KH_1", "KH_6" ]

[ 126809, 8014 ]

2

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "2.7.7.8", "PDOC50084", "R-BTA-429958", "R-BTA-450385", "R-BTA-450513", "R-BTA-450604", "R-BTA-4570464", "R-BTA-6791226", "R-BTA-72163", "R-BTA-72203", "R-BTA-9930044", "R-CEL-429958", "R-CEL-450385", "R-CEL-450513", "R-CEL-450604", "R-CEL-6791226", "R-CEL-72163", "R-CEL-72203", ...

[ "EC:2.7.7.8", "PROSITEDOC:PDOC50084", "REACTOME:R-BTA-429958", "REACTOME:R-BTA-450385", "REACTOME:R-BTA-450513", "REACTOME:R-BTA-450604", "REACTOME:R-BTA-4570464", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72163", "REACTOME:R-BTA-72203", "REACTOME:R-BTA-9930044", "REACTOME:R-CEL-429958", "RE...

79

[ "1dt4", "1dtj", "1e3h", "1e3p", "1ec6", "1j4w", "1j5k", "1khm", "1tua", "1vig", "1vih", "1we8", "1wvn", "1x4m", "1x4n", "1ztg", "1zzi", "1zzj", "1zzk", "2ann", "2anr", "2axy", "2ba0", "2cpq", "2cte", "2ctf", "2ctj", "2ctk", "2ctl", "2ctm", "2dgr", "2e3u"...

122

[ "PUB00005188", "PUB00005961", "PUB00005962", "PUB00007305" ]

[ "8036511", "9302998", "10369774", "11160884" ]

[ "Conserved structures and diversity of functions of RNA-binding proteins.", "The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome.", "High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcrip...

[ 1994, 1997, 1999, 2001 ]

4

[ "IPR004087" ]

[ "IPR047226", "IPR047228", "IPR047274", "IPR047275", "IPR047276", "IPR047368", "IPR047369", "IPR047370", "IPR047371", "IPR047372", "IPR047373", "IPR047374", "IPR047375", "IPR047381", "IPR047382", "IPR047424", "IPR047440", "IPR047496", "IPR047538", "IPR047553", "IPR047554", "...

1

27

0

[ "Archaea", "Bacteria", "Eukaryota", "Nucleocytoviricota", "unclassified sequences" ]

[ 1487, 35880, 96698, 5, 753 ]

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",...

[ 151, 38, 159, 82, 1, 198, 160, 6, 78, 158, 6, 4, 266 ]

13

true

Domain

K Homology domain, type 1

KH_dom_type_1

1

IPR004089

4,089

Methyl-accepting chemotaxis protein (MCP) signalling domain

MCPsignal_dom

Domain

218,781

false

Methyl-accepting chemotaxis proteins (MCPs) are a family of bacterial receptors that mediate chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behaviour [ ]. Environmental diversity gives rise to diversity in bacterial signall...

[ "GO:0007165", "GO:0016020" ]

[ "signal transduction", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PROFILE", "SMART" ]

[ "PF00015", "PS50111", "SM00283" ]

[ "MCPsignal", "CHEMOTAXIS_TRANSDUC_2", "MA" ]

[ 216309, 218336, 211200 ]

3

[ "PROSITEDOC" ]

[ "PDOC00465" ]

[ "PROSITEDOC:PDOC00465" ]

1

[ "1qu7", "2ch7", "3g67", "3g6b", "3ja6", "3ur1", "3zx6", "4jpb", "6s18", "6s1a", "6s1k", "6s33", "6s37", "6s38", "6s3b", "8c5v", "8gl3" ]

17

[ "PUB00042592", "PUB00042593", "PUB00129171", "PUB00129172", "PUB00163243" ]

[ "16359703", "17299051", "20738376", "20411245", "37772839" ]

[ "Changing the specificity of a bacterial chemoreceptor.", "Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors.", "Sensing of environmental signals: classification of chemoreceptors according to the size of their ligand binding regions.", "Ba...

[ 2006, 2007, 2010, 2010, 2023 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 3862, 212546, 737, 22, 1614 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 3, 5, 1 ]

3

true

Domain

Methyl-accepting chemotaxis protein (MCP) signalling domain

MCPsignal_dom

1

IPR004090

4,090

Chemotaxis methyl-accepting receptor

Chemotax_Me-accpt_rcpt

Family

117,706

false

Methyl-accepting chemotaxis proteins (MCPs) are a family of bacterial receptors that mediate chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behaviour [ ]. Environmental diversity gives rise to diversity in bacterial signall...

[ "GO:0004888", "GO:0006935", "GO:0007165", "GO:0016020" ]

[ "transmembrane signaling receptor activity", "chemotaxis", "signal transduction", "membrane" ]

[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]

4

[ "PRINTS" ]

[ "PR00260" ]

[ "CHEMTRNSDUCR" ]

[ 117706 ]

1

[]

0

[ "1qu7", "2ch7", "3ja6", "3ur1", "3zx6", "4jpb", "6s18", "6s1a", "6s1k", "6s33", "6s37", "6s38", "6s3b", "8c5v" ]

14

[ "PUB00042592", "PUB00042593" ]

[ "16359703", "17299051" ]

[ "Changing the specificity of a bacterial chemoreceptor.", "Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors." ]

[ 2006, 2007 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 2717, 114012, 2, 147, 828 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]

[ 2, 5 ]

2

true

Family

Chemotaxis methyl-accepting receptor

Chemotax_Me-accpt_rcpt

2

IPR004091

4,091

Chemotaxis methyl-accepting receptor, methyl-accepting site

Chemotax_Me-accpt_rcpt_Me-site

PTM

6,644

false

Methyl-accepting chemotaxis proteins (MCPs) are a family of bacterial receptors that mediate chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behaviour [ ]. Environmental diversity gives rise to diversity in bacterial signall...

[]

0

[ "PROSITE" ]

[ "PS00538" ]

[ "CHEMOTAXIS_TRANSDUC_1" ]

[ 6644 ]

1

[ "PROSITEDOC" ]

[ "PDOC00465" ]

[ "PROSITEDOC:PDOC00465" ]

1

[ "1qu7", "3zx6", "6s1k", "8c5v" ]

4

[ "PUB00042592", "PUB00042593" ]

[ "16359703", "17299051" ]

[ "Changing the specificity of a bacterial chemoreceptor.", "Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors." ]

[ 2006, 2007 ]

2

[]

0

null

[ "Opisthokonta", "Pseudomonadota" ]

[ 12, 6632 ]

2

[ "Escherichia coli (strain K12)" ]

[ 4 ]

1

true

PTM

Chemotaxis methyl-accepting receptor, methyl-accepting site

Chemotax_Me-accpt_rcpt_Me-site

1

IPR004092

4,092

Mbt repeat domain

Mbt

Domain

17,252

false

The function of the malignant brain tumor (MBT) repeat is unknown, but is found in a number of nuclear proteins involved in transcriptional repression. The repeat contains a completely conserved glutamate at its amino terminus that may be important for function. The crystal structure of the two MBT repeats of human SCM...

[ "GO:0006355", "GO:0005634" ]

[ "regulation of DNA-templated transcription", "nucleus" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PROFILE", "SMART" ]

[ "PF02820", "PS51079", "SM00561" ]

[ "MBT", "MBT", "MBT" ]

[ 17184, 16214, 16246 ]

3

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC51079", "R-DME-2559580", "R-DME-3108214", "R-DME-3899300", "R-DME-4551638", "R-DME-4570464", "R-DME-8939243", "R-DME-8943724", "R-DME-8953750", "R-HSA-2559580", "R-HSA-3108214", "R-HSA-3899300", "R-HSA-4551638", "R-HSA-4570464", "R-HSA-4655427", "R-HSA-6804760", "R-HSA-8939243",...

[ "PROSITEDOC:PDOC51079", "REACTOME:R-DME-2559580", "REACTOME:R-DME-3108214", "REACTOME:R-DME-3899300", "REACTOME:R-DME-4551638", "REACTOME:R-DME-4570464", "REACTOME:R-DME-8939243", "REACTOME:R-DME-8943724", "REACTOME:R-DME-8953750", "REACTOME:R-HSA-2559580", "REACTOME:R-HSA-3108214", "REACTOME:...

34

[ "1oi1", "1oyx", "1oz2", "1oz3", "1wjq", "1wjr", "1wjs", "2biv", "2eqm", "2jtf", "2p0k", "2pqw", "2r57", "2r58", "2r5a", "2r5m", "2rhi", "2rhu", "2rhx", "2rhy", "2rhz", "2ri2", "2ri3", "2ri5", "2rjc", "2rjd", "2rje", "2rjf", "2vyt", "3cey", "3f70", "3feo"...

54

[ "PUB00014895" ]

[ "12952983" ]

[ "Crystal structure of the malignant brain tumor (MBT) repeats in Sex Comb on Midleg-like 2 (SCML2)." ]

[ 2003 ]

1

[]

0

null

[ "Eukaryota" ]

[ 17252 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 67, 7, 48, 47, 43 ]

6

true

Domain

Mbt repeat domain

Mbt

4

IPR004093

4,093

Staphylokinase

SAK

Family

302

false

This entry represents staphylokinases. Staphylokinase (also known as SAK) from Staphylococcus aureus is a virulence factor due to its interaction with plasminogen and alpha-defensins in the hosts. The binding of staphylokinase to plasminogen results in the formation of active plasmin, a proteolytic enzyme facilitating ...

[ "GO:0031639", "GO:0005576" ]

[ "plasminogen activation", "extracellular region" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF02821" ]

[ "Staphylokinase" ]

[ 302 ]

1

[]

0

[ "1bml", "1bui", "1c4p", "1c76", "1c77", "1c78", "1c79", "1l4d", "1l4z", "1qqr", "1ssn", "2sak" ]

12

[ "PUB00020378", "PUB00070733", "PUB00070734" ]

[ "9145104", "16111912", "23801604" ]

[ "Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential.", "Staphylococcus aureus: Staphylokinase.", "Staphylokinase promotes the establishment of Staphylococcus aureus skin infections while decreasing disease severity." ]

[ 1997, 2006, 2013 ]

3

[]

0

null

[ "Bacillota", "Caudoviricetes" ]

[ 285, 17 ]

2

[]

0

true

Family

Staphylokinase

SAK

2

IPR004094

4,094

Antistasin-like domain

Antistasin-like

Domain

3,604

false

Antistatin is a small, disulphide cross-linked serine protease inhibitor isolated from the salivary glands of the Mexican leech. It is a potent anticoagulant by virtue of its ability to inhibit factor Xa in the coagulation cascade. Antistatin also exhibits a strong antimetastatic activity. It contains internal repeats ...

[ "GO:0004867" ]

[ "serine-type endopeptidase inhibitor activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE" ]

[ "PF02822", "PS51252" ]

[ "Antistasin", "ANTISTASIN" ]

[ 3489, 3414 ]

2

[ "PROSITEDOC" ]

[ "PDOC51252" ]

[ "PROSITEDOC:PDOC51252" ]

1

[ "1bx7", "1bx8", "1c9p", "1c9t", "1eja", "1hia", "1skz", "3bg4", "5ubm" ]

9

[ "PUB00014231", "PUB00068105", "PUB00068106", "PUB00068107" ]

[ "10512718", "1516699", "15013771", "16523290" ]

[ "Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system.", "The primitive metazoan Hydra expresses antistasin, a serine protease inhibitor of vertebrate blood coagulation: cDNA cloning, cellular localisation and developmental regul...

[ 1999, 1992, 2004, 2006 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "viral metagenome" ]

[ 26, 3573, 5 ]

3

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 5, 7, 3, 2, 2, 4 ]

6

true

Domain

Antistasin-like domain

Antistasin-like

8

IPR004096

4,096

4-vinyl reductase, 4VR

V4R

Domain

5,057

false

Central cellular functions such as metabolism, solute transport and signal transduction are regulated, in part, via binding of small molecules by specialised domains. The 4-vinyl reductase (4VR) domain is a predicted small molecular binding domain, that may bind to hydrocarbons [ ]. Proteins that contain this domain in...

[]

0

[ "PFAM", "SMART" ]

[ "PF02830", "SM00989" ]

[ "V4R", "V4R" ]

[ 3508, 5019 ]

2

[]

0

[ "2osd", "2oso", "5fru", "5frv", "5frw", "5frx", "5fry", "5frz", "5fs0", "5kbe", "5kbg", "5kbh", "5kbi", "6iy8", "7vqf" ]

15

[ "PUB00007364", "PUB00083146" ]

[ "11292341", "9023219" ]

[ "Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains.", "Expression, inducer spectrum, domain structure, and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus NCIB8250." ]

[ 2001, 1997 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 588, 4419, 9, 41 ]

4

[]

0

true

Domain

4-vinyl reductase, 4VR

V4R

8

IPR004097

4,097

DHHA2 domain

DHHA2

Domain

12,512

false

This domain is called DHHA2 since it is often associated with the DHH domain ( ) and is diagnostic of DHH subfamily 2 members [ ]. The domain is about 120 residues long and contains a conserved DXK motif at its amino terminus. It is present in inorganic pyrophosphatases and in exopolyphosphatase of Saccharomyces cerevi...

[ "GO:0016462", "GO:0005737" ]

[ "pyrophosphatase activity", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM", "SMART" ]

[ "PF02833", "SM01131" ]

[ "DHHA2", "DHHA2" ]

[ 12490, 11733 ]

2

[ "EC", "METACYC", "METACYC" ]

[ "3.6.1.1", "PWY-7805", "PWY-7807" ]

[ "EC:3.6.1.1", "METACYC:PWY-7805", "METACYC:PWY-7807" ]

3

[ "1i74", "1k20", "1k23", "1wpm", "1wpp", "2eb0", "2enx", "2haw", "2iw4", "2qb6", "2qb7", "2qb8", "4rpa", "6ll7", "6ll8" ]

15

[ "PUB00005478" ]

[ "9478130" ]

[ "A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease." ]

[ 1998 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 163, 7285, 5003, 61 ]

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)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain ...

[ 1, 1, 3, 9, 3, 1, 3, 1, 1 ]

9

true

Domain

DHHA2 domain

DHHA2

8

IPR004098

4,098

Prp18

Domain

5,653

false

The splicing factor Prp18 is required for the second step of pre-mRNA splicing. PRP18 appears to be primarily associated with the U5 snRNP. The structure of a large fragment of the Saccharomyces cerevisiae Prp18 is known [ ]. This fragment is fully active in yeast splicing in vitro and includes the sequences of Prp18 t...

[ "GO:0008380", "GO:0005681" ]

[ "RNA splicing", "spliceosomal complex" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF02840" ]

[ "Prp18" ]

[ 5653 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-72163", "R-DRE-72163", "R-HSA-72163", "R-MMU-72163", "R-RNO-72163" ]

[ "REACTOME:R-BTA-72163", "REACTOME:R-DRE-72163", "REACTOME:R-HSA-72163", "REACTOME:R-MMU-72163", "REACTOME:R-RNO-72163" ]

5

[ "1dvk", "5mps", "5mq0", "5wsg", "5ylz", "6bk8", "6exn", "7b9v", "9dtr" ]

9

[ "PUB00007365" ]

[ "10737784" ]

[ "Crystal structure of the functional domain of the splicing factor Prp18." ]

[ 2000 ]

1

[]

0

null

[ "Eukaryota" ]

[ 5653 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 8, 1, 2, 1, 4, 3, 1, 11, 4, 1, 1, 25 ]

12

true

Domain

Prp18

3

IPR004099

4,099

Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain

Pyr_nucl-diS_OxRdtase_dimer

Domain

122,840

false

This entry represents a dimerisation domain that is usually found at the C-terminal of both class I and class II oxidoreductases, as well as in NADH oxidases and peroxidases [ , , ].

[]

0

[ "PFAM" ]

[ "PF02852" ]

[ "Pyr_redox_dim" ]

[ 122840 ]

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-204174", "R-BTA-3299685", "R-BTA-499943", "R-BTA-5263617", "R-BTA-5362517", "R-BTA-5628897", "R-BTA-6783984", "R-BTA-70895", "R-BTA-9837999", "R-BTA-9853506", "R-BTA-9858328", "R-BTA-9859138", "R-BTA-9861559", "R-CEL-204174", "R-CEL-3299685", "R-CEL-499943", "R-CEL-5263617", ...

[ "REACTOME:R-BTA-204174", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-499943", "REACTOME:R-BTA-5263617", "REACTOME:R-BTA-5362517", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-6783984", "REACTOME:R-BTA-70895", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9853506", "REACTOME:R-BTA-9858328", "REACTOME:R-...

102

[ "1aog", "1bhy", "1bwc", "1bzl", "1dnc", "1dxl", "1ebd", "1f8w", "1fea", "1feb", "1fec", "1ger", "1ges", "1get", "1geu", "1gra", "1grb", "1gre", "1grf", "1grg", "1grh", "1grt", "1gsn", "1gxf", "1h6v", "1jeh", "1joa", "1k4q", "1lpf", "1lvl", "1mo9", "1mok"...

318

[ "PUB00024128", "PUB00027392", "PUB00037266" ]

[ "11090282", "12390015", "7766608" ]

[ "Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase.", "Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.", "Crystallographic analyses of NADH peroxidase Cys42Ala and ...

[ 2000, 2002, 1995 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]

[ 2468, 98958, 19883, 3, 4, 1524 ]

6

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 25, 5, 9, 4, 4, 30, 23, 2, 22, 22, 3, 2, 41 ]

13

true

Domain

Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain

Pyr_nucl-diS_OxRdtase_dimer

4

IPR004100

4,100

ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain

ATPase_F1/V1/A1_a/bsu_N

Domain

129,786

false

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...

[ "GO:0046034", "GO:1902600" ]

[ "ATP metabolic process", "proton transmembrane transport" ]

[ "biological_process", "biological_process" ]

2

[ "PFAM" ]

[ "PF02874" ]

[ "ATP-synt_ab_N" ]

[ 129786 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...

[ "7.1.2.2", "PWY-7980", "R-BTA-1222556", "R-BTA-77387", "R-BTA-917977", "R-BTA-9639288", "R-BTA-983712", "R-CEL-1222556", "R-CEL-1268020", "R-CEL-163210", "R-CEL-77387", "R-CEL-8949613", "R-CEL-917977", "R-CEL-9639288", "R-CEL-983712", "R-CEL-9837999", "R-CFA-1268020", "R-CFA-163210...

[ "EC:7.1.2.2", "METACYC:PWY-7980", "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-917977", "REACTOME:R-BTA-9639288", "REACTOME:R-BTA-983712", "REACTOME:R-CEL-1222556", "REACTOME:R-CEL-1268020", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-77387", "REACTOME:R-CEL-8949613", "REAC...

80

[ "1bmf", "1cow", "1e1q", "1e1r", "1e79", "1efr", "1fx0", "1h8e", "1h8h", "1kmh", "1mab", "1nbm", "1ohh", "1qo1", "1sky", "1vdz", "1w0j", "1w0k", "2c61", "2ck3", "2f43", "2hld", "2jdi", "2jiz", "2jj1", "2jj2", "2qe7", "2r9v", "2rkw", "2v7q", "2w6e", "2w6f"...

510

[ "PUB00004187", "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020609", "PUB00020611", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]

[ "8065448", "11309608", "15473999", "15078220", "15629643", "12745923", "20450191", "18937357", "1385979", "9741106" ]

[ "Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.", "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechan...

[ 1994, 2001, 2004, 2004, 2005, 2003, 2010, 2008, 1992, 1998 ]

10

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1932, 64055, 62589, 1210 ]

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",...

[ 43, 5, 6, 16, 2, 33, 12, 4, 38, 22, 4, 4, 57 ]

13

true

Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain

ATPase_F1/V1/A1_a/bsu_N

6

IPR004101

4,101

Mur ligase, C-terminal

Mur_ligase_C

Domain

143,392

false

This entry represents the C-terminal domain from all four stage 2 Mur enzymes: UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanine-D-glutamate ligase (MurD), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (Mur...

[ "GO:0016881", "GO:0009058" ]

[ "acid-amino acid ligase activity", "biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF02875" ]

[ "Mur_ligase_C" ]

[ 143392 ]

1

[ "EC" ]

[ "6.3.2" ]

[ "EC:6.3.2" ]

1

[ "1e0d", "1e8c", "1eeh", "1fgs", "1gg4", "1gqq", "1gqy", "1j6u", "1jbv", "1jbw", "1o5z", "1p31", "1p3d", "1uag", "1w78", "1w7k", "2am1", "2am2", "2f00", "2gc5", "2gc6", "2gca", "2gcb", "2jff", "2jfg", "2jfh", "2uag", "2uuo", "2uup", "2vor", "2vos", "2vtd"...

136

[ "PUB00008020", "PUB00035788", "PUB00035789", "PUB00035790", "PUB00035791", "PUB00035792", "PUB00101154" ]

[ "9652408", "17139082", "17427948", "16595662", "16322581", "16934839", "18974047" ]

[ "Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin).", "Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC).", "Targeted molecular dynamics simulation studies of...

[ 1998, 2006, 2007, 2006, 2005, 2006, 2008 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]

[ 551, 138063, 1822, 2, 2954 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 6, 3, 3 ]

4

true

Domain

Mur ligase, C-terminal

Mur_ligase_C

6

IPR004102

4,102

Poly(ADP-ribose) polymerase, regulatory domain

Poly(ADP-ribose)pol_reg_dom

Domain

9,978

false

Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The regulatory domain of the polymerase is alm...

[ "GO:0003950" ]

[ "NAD+ poly-ADP-ribosyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE" ]

[ "PF02877", "PS51060" ]

[ "PARP_reg", "PARP_ALPHA_HD" ]

[ 9047, 9875 ]

2

[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "2.4.2.-", "2.4.2.30", "PWY-5381", "PWY-5800", "PWY-6148", "PWY-6720", "PWY-7018", "PWY-7025", "PWY-7450", "PWY-7817", "PWY-7981", "PDOC51059", "R-CEL-5696394", "R-CEL-5696395", "R-CEL-5696400", "R-DME-110362", "R-DME-2173795", "R-DME-3108214", "R-DME-5685939", "R-DME-5696394",...

[ "EC:2.4.2.-", "EC:2.4.2.30", "METACYC:PWY-5381", "METACYC:PWY-5800", "METACYC:PWY-6148", "METACYC:PWY-6720", "METACYC:PWY-7018", "METACYC:PWY-7025", "METACYC:PWY-7450", "METACYC:PWY-7817", "METACYC:PWY-7981", "PROSITEDOC:PDOC51059", "REACTOME:R-CEL-5696394", "REACTOME:R-CEL-5696395", "RE...

52

[ "1a26", "1efy", "1gs0", "1pax", "1uk0", "1uk1", "1wok", "2paw", "2pax", "2rcw", "2rd6", "3c49", "3c4h", "3ce0", "3fhb", "3gjw", "3gn7", "3kcz", "3kjd", "3l3l", "3l3m", "3pax", "4dqy", "4gv0", "4gv2", "4gv4", "4gv7", "4hhy", "4hhz", "4l6s", "4l6z", "4l70"...

119

[ "PUB00013997" ]

[ "9521710" ]

[ "Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling." ]

[ 1998 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 5, 89, 9857, 19, 8 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 19, 4, 6, 1, 14, 12, 1, 9, 9, 21 ]

10

true

Domain

Poly(ADP-ribose) polymerase, regulatory domain

Poly(ADP-ribose)pol_reg_dom

7

IPR004103

4,103

Polysaccharide lyase family 8, C-terminal

Lyase_8_C

Domain

4,285

false

Proteins containing this domain consist of a group of secreted bacterial lyase enzymes capable of acting on hyaluronan (hyaluronate lyase, ) and chondroitin (chondroitin AC lyase, ) in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen [ , ]. This domain is almost always ass...

[ "GO:0016829", "GO:0005576" ]

[ "lyase activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM" ]

[ "PF02884" ]

[ "Lyase_8_C" ]

[ 4285 ]

1

[ "EC", "METACYC" ]

[ "4.2.2.1", "PWY-7645" ]

[ "EC:4.2.2.1", "METACYC:PWY-7645" ]

2

[ "1c82", "1cb8", "1egu", "1f1s", "1f9g", "1hm2", "1hm3", "1hmu", "1hmw", "1i8q", "1j0m", "1j0n", "1loh", "1lxk", "1lxm", "1n7n", "1n7o", "1n7p", "1n7q", "1n7r", "1ojm", "1ojn", "1ojo", "1ojp", "1rw9", "1rwa", "1rwc", "1rwf", "1rwg", "1rwh", "1w3y", "1x1h"...

46

[ "PUB00014309", "PUB00014311" ]

[ "14523022", "10329169" ]

[ "Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action.", "Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes." ]

[ 2003, 1999 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Halomicrobium mukohataei", "Medusavirus stheno T3", "metagenomes" ]

[ 3709, 557, 3, 1, 15 ]

5

[]

0

true

Domain

Polysaccharide lyase family 8, C-terminal

Lyase_8_C

8

IPR004104

4,104

Gfo/Idh/MocA-like oxidoreductase, C-terminal

Gfo/Idh/MocA-like_OxRdtase_C

Domain

35,775

false

This entry represents a domain found C-terminal in Gfo/Idh/MocA family of proteins. In general, the Gfo/Idh/MocA protein family members are enzymes that catalyse various different chemical reactions such as oxidation and reduction of carbohydrates, oxidation of trans-dihydrodiols, reduction of biliverdin, and hydrolysa...

[]

0

[ "PFAM" ]

[ "PF02894" ]

[ "GFO_IDH_MocA_C" ]

[ 35775 ]

1

[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC" ]

[ "1.1.1.18", "GenProp1271", "GenProp1286", "GenProp1468", "GenProp1534", "PWY-5940", "PWY-7237", "PWY-7241" ]

[ "EC:1.1.1.18", "GP:GenProp1271", "GP:GenProp1286", "GP:GenProp1468", "GP:GenProp1534", "METACYC:PWY-5940", "METACYC:PWY-7237", "METACYC:PWY-7241" ]

8

[ "1evj", "1h6a", "1h6b", "1h6c", "1h6d", "1ofg", "1ryd", "1rye", "3dty", "3e82", "3ec7", "3f4l", "3fd8", "3fhl", "3gdo", "3gfg", "3hnp", "3i23", "3kux", "3mz0", "3nt2", "3nt4", "3nt5", "3nto", "3ntq", "3ntr", "3o9z", "3oa0", "3oa2", "3q2i", "3q2k", "4l8v"...

59

[ "PUB00094646" ]

[ "26749496" ]

[ "Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases." ]

[ 2016 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 331, 29064, 5962, 2, 416 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "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)",...

[ 5, 2, 4, 2, 7, 1, 2, 16 ]

8

true

Domain

Gfo/Idh/MocA-like oxidoreductase, C-terminal

Gfo/Idh/MocA-like_OxRdtase_C

8

IPR004105

4,105

Histidine kinase CheA-like, homodimeric domain

CheA-like_dim

Domain

22,728

false

Signal transducing histidine kinases are the key elements in two-component signal transduction systems, which control complex processes such as the initiation of development in microorganisms [ , ]. Examples of histidine kinases are EnvZ, which plays a central role in osmoregulation [ ], and CheA, which plays a central...

[ "GO:0000155", "GO:0004673", "GO:0000160", "GO:0006935", "GO:0005737" ]

[ "phosphorelay sensor kinase activity", "protein histidine kinase activity", "phosphorelay signal transduction system", "chemotaxis", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "PFAM", "SMART" ]

[ "PF02895", "SM01231" ]

[ "H-kinase_dim", "H-kinase_dim" ]

[ 19595, 22675 ]

2

[ "EC", "GP" ]

[ "2.7.13.3", "GenProp1147" ]

[ "EC:2.7.13.3", "GP:GenProp1147" ]

2

[ "1b3q", "3ja6", "4xiv", "6s1k", "6y1y", "8c5v" ]

6

[ "PUB00000966", "PUB00007866", "PUB00011096", "PUB00013246", "PUB00013247", "PUB00013562", "PUB00013563", "PUB00020801" ]

[ "9989504", "11406410", "10966457", "8868347", "10426948", "8029829", "1482126", "11145881" ]

[ "Structure of CheA, a signal-transducing histidine kinase.", "Histidine kinases and response regulator proteins in two-component signaling systems.", "Two-component signal transduction.", "Protein aspartate phosphatases control the output of two-component signal transduction systems.", "Solution structure o...

[ 1999, 2001, 2000, 1996, 1999, 1994, 1992, 2000 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 535, 21922, 23, 248 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Histidine kinase CheA-like, homodimeric domain

CheA-like_dim

6

IPR004106

4,106

Peptidase S9, N-terminal domain superfamily

Peptidase_S9_N_sf

Homologous_superfamily

35,529

false

This superfamily represents the β-propeller domain found at the N-terminal of prolyl oligopeptidases, including acylamino-acid-releasing enzyme (also known as acylaminoacyl peptidase). The prolyl oligopeptidase family consist of a number of evolutionary related peptidases whose catalytic activity seems to be provided b...

[ "GO:0004252", "GO:0006508" ]

[ "serine-type endopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "SSF" ]

[ "SSF50993" ]

[ "" ]

[ 35529 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.4.21", "R-BTA-6798695", "R-BTA-72764", "R-HSA-6798695", "R-HSA-72764", "R-MMU-6798695", "R-MMU-72764", "R-RNO-6798695", "R-RNO-72764", "R-SCE-6791226" ]

[ "EC:3.4.21", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-72764", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-72764", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-72764", "REACTOME:R-RNO-6798695", "REACTOME:R-RNO-72764", "REACTOME:R-SCE-6791226" ]

10

[ "1e5t", "1e8m", "1e8n", "1h2w", "1h2x", "1h2y", "1h2z", "1o6f", "1o6g", "1qfm", "1qfs", "1uoo", "1uop", "1uoq", "1ve6", "1ve7", "1vz2", "1vz3", "1yr2", "2bkl", "2hu5", "2hu7", "2hu8", "2qr5", "2qzp", "2xdw", "2xe4", "3ddu", "3eq7", "3eq8", "3eq9", "3iuj"...

138

[ "PUB00020062", "PUB00068074", "PUB00162571" ]

[ "9695945", "23085164", "40269455" ]

[ "Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.", "Coupled motions during dynamics reveal a tunnel toward the active site regulated by the N-terminal α-helix in an acylaminoacyl peptidase.", "Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging....

[ 1998, 2012, 2025 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 198, 23539, 11459, 6, 327 ]

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",...

[ 35, 1, 6, 7, 1, 15, 10, 1, 14, 20, 1, 54 ]

12

true

Homologous_superfamily

Peptidase S9, N-terminal domain superfamily

Peptidase_S9_N_sf

2

IPR004107

4,107

Integrase, SAM-like, N-terminal

Integrase_SAM-like_N

Domain

100,886

false

Proteins containing this domain cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment [ , ]. The phage integrase N-terminal SAM-like domain is almost always found with the signature that...

[ "GO:0003677", "GO:0015074" ]

[ "DNA binding", "DNA integration" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PFAM", "PFAM" ]

[ "PF02899", "PF13495", "PF14659" ]

[ "Phage_int_SAM_1", "Phage_int_SAM_4", "Phage_int_SAM_3" ]

[ 63640, 13994, 23264 ]

3

[]

0

[ "1a0p", "1p7d", "1z19", "1z1b", "1z1g", "2a3v", "2kd1", "2khq", "2kiw", "2kkp", "2oxo", "3lys", "4a8e", "5hxy", "5j0n", "9i5v" ]

16

[ "PUB00004261", "PUB00005224" ]

[ "9288963", "9082984" ]

[ "Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse.", "Flexibility in DNA recombination: structure of the lambda integrase catalytic core." ]

[ 1997, 1997 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "other sequences", "unclassified sequences" ]

[ 1593, 96234, 365, 903, 3, 1788 ]

6

[ "Danio rerio", "Escherichia coli (strain K12)", "Mus musculus" ]

[ 5, 3, 1 ]

3

true

Domain

Integrase, SAM-like, N-terminal

Integrase_SAM-like_N

6

IPR004108

4,108

Iron hydrogenase, large subunit, C-terminal

Fe_hydrogenase_lsu_C

Domain

15,653

false

Proteins containing this domain may be involved in the mechanism of biological hydrogen activation and contain 4FE-4S clusters. They can use molecular hydrogen for the reduction of a variety of substances. This domain consists of two intertwined α/β subdomains with FE-S cluster located at the interface between these su...

[]

0

[ "PFAM" ]

[ "PF02906" ]

[ "Fe_hyd_lg_C" ]

[ 15653 ]

1

[ "GP", "REACTOME" ]

[ "GenProp1353", "R-HSA-2564830" ]

[ "GP:GenProp1353", "REACTOME:R-HSA-2564830" ]

2

[ "1c4a", "1c4c", "1e08", "1feh", "1gx7", "1hfe", "2n0s", "3c8y", "3lx4", "4r0v", "4xdc", "4xdd", "5byq", "5byr", "5bys", "5la3", "5oef", "6gl6", "6gly", "6glz", "6gm0", "6gm1", "6gm2", "6gm3", "6gm4", "6gm5", "6gm6", "6gm7", "6gm8", "6h63", "6n59", "6n6p"...

70

[ "PUB00023853", "PUB00103926" ]

[ "10529166", "20418861" ]

[ "Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum.", "Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG)." ]

[ 1999, 2010 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "virus sp. ctHJb31" ]

[ 10, 8386, 6703, 553, 1 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 4, 1, 3, 3, 18, 3, 1, 4, 9, 1, 1, 9 ]

12

true

Domain

Iron hydrogenase, large subunit, C-terminal

Fe_hydrogenase_lsu_C

3

IPR004111

4,111

Tetracycline repressor TetR, C-terminal

Repressor_TetR_C

Domain

33,714

false

This entry represents the C-terminal domain found in the tetracycline transcriptional repressor TetR, which binds to the Tet(A) gene to repress its expression in the absence of tetracycline [ ]. Tet(A) is a membrane-associated efflux protein that exports tetracycline from the cell before it can attach to ribosomes and ...

[ "GO:0045892" ]

[ "negative regulation of DNA-templated transcription" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF02909" ]

[ "TetR_C_1" ]

[ 33714 ]

1

[]

0

[ "1a6i", "1bjz", "1ork", "1qpi", "1z0x", "2fj1", "2g7g", "2g7l", "2hxi", "2hxo", "2ns7", "2ns8", "2o7o", "2opt", "2tct", "2trt", "2vke", "2vkv", "2vpr", "2x6o", "2x9d", "2xb5", "2xgc", "2xgd", "2xge", "2xpu", "2xpv", "2xpw", "2xrl", "2y2z", "2y30", "2y31"...

85

[ "PUB00003347", "PUB00005182" ]

[ "7707374", "8153629" ]

[ "The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance.", "Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance." ]

[ 1995, 1994 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes", "plasmids" ]

[ 33637, 4, 71, 2 ]

4

[ "Arabidopsis thaliana" ]

[ 1 ]

1

true

Domain

Tetracycline repressor TetR, C-terminal

Repressor_TetR_C

5

IPR004113

4,113

FAD-binding oxidoreductase/transferase, type 4, C-terminal

FAD-bd_oxidored_4_C

Domain

76,245

false

This entry represents a domain found in a group of type 4 FAD-binding oxidoreductase/transferases and similar proteins from all cellular organisms, including D-2-hydroxyglutarate dehydrogenase from humans [ ] and Escherichia coli [ ], Alkyldihydroxyacetonephosphate synthase from Caenorhabditis elegans and D-2-hydroxygl...

[ "GO:0003824", "GO:0050660" ]

[ "catalytic activity", "flavin adenine dinucleotide binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF02913" ]

[ "FAD-oxidase_C" ]

[ 76245 ]

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-880009", "R-CEL-75896", "R-DME-75896", "R-DME-9033241", "R-DRE-1268020", "R-DRE-880009", "R-HSA-1268020", "R-HSA-75896", "R-HSA-880009", "R-HSA-9033241", "R-HSA-9033500", "R-HSA-9837999", "R-MMU-1268020", "R-MMU-75896", "R-MMU-880009", "R-MMU-9033241", "R-MMU-9837999", "R-RN...

[ "REACTOME:R-BTA-880009", "REACTOME:R-CEL-75896", "REACTOME:R-DME-75896", "REACTOME:R-DME-9033241", "REACTOME:R-DRE-1268020", "REACTOME:R-DRE-880009", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-75896", "REACTOME:R-HSA-880009", "REACTOME:R-HSA-9033241", "REACTOME:R-HSA-9033500", "REACTOME:R-HSA-9...

23

[ "1ahu", "1ahv", "1ahz", "1dii", "1diq", "1dzn", "1e0y", "1e8f", "1e8g", "1e8h", "1qlt", "1qlu", "1vao", "1w1j", "1w1k", "1w1l", "1w1m", "1wve", "1wvf", "2uuu", "2uuv", "2vao", "3pm9", "4bby", "4bc7", "4bc9", "4bca", "5adz", "5ae1", "5ae2", "5ae3", "5fxd"...

85

[ "PUB00019533", "PUB00103958", "PUB00103959", "PUB00103960" ]

[ "9141139", "36144368", "26774271", "33431826" ]

[ "Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.", "Revealing a New Family of D-2-Hydroxyglutarate Dehydrogenases in Escherichia coli and Pantoea ananatis Encoded by ydiJ.", "Saccharomyces cerevisiae Forms D-2-Hydro...

[ 1997, 2022, 2016, 2021 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Yasminevirus sp. GU-2018", "unclassified sequences" ]

[ 1500, 58026, 15637, 2, 1, 1079 ]

6

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 8, 5, 6, 5, 3, 19, 10, 4, 3, 17, 3, 1, 18 ]

13

true

Domain

FAD-binding oxidoreductase/transferase, type 4, C-terminal

FAD-bd_oxidored_4_C

7

IPR004114

4,114

THUMP domain

THUMP_dom

Domain

33,636

false

The THUMP domain (named after THioUridine synthases, RNA Methylases and Pseudouridine synthases) is a module of approximately 110 amino acid residues involved in RNA metabolism. It is found in enzymes responsible for various RNA modifications, including methylation, pseudouridylation, thiouridylation, deamination, and ...

[ "GO:0003723" ]

[ "RNA binding" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE", "SMART" ]

[ "PF02926", "PS51165", "SM00981" ]

[ "THUMP", "THUMP", "THUMP" ]

[ 32721, 31714, 30406 ]

3

[ "PROSITEDOC", "REACTOME" ]

[ "PDOC51165", "R-HSA-6790901" ]

[ "PROSITEDOC:PDOC51165", "REACTOME:R-HSA-6790901" ]

2

[ "1vbk", "2c5s", "2dir", "3g8q", "3k0b", "3ldg", "3ldu", "3tlj", "3tm4", "3tm5", "3tma", "3v8v", "3v97", "4kr6", "4kr7", "4kr9", "5e71", "5e72", "6zxv", "6zxw", "6zxy" ]

21

[ "PUB00007072", "PUB00039897", "PUB00100797", "PUB00100798", "PUB00100799", "PUB00154188" ]

[ "11295541", "16343540", "16687654", "22362734", "17010378", "36833309" ]

[ "THUMP--a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases.", "Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain.", "THUMP from archaeal tRNA:m22G10 methyltransferase, a genuine autonomously fol...

[ 2001, 2006, 2006, 2012, 2006, 2023 ]

6

[]

[ "IPR041730", "IPR049962" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 2033, 24540, 6783, 12, 268 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 3, 2, 8, 1, 2, 9, 5, 1, 7, 11, 1, 1, 8 ]

13

true

Domain

THUMP domain

THUMP_dom

9

IPR004115

4,115

GAD-like domain superfamily

GAD-like_sf

Homologous_superfamily

32,221

false

This superfamily represents a 2 layer α/β insertion domain found in the glutamyl-tRNA amidotransferase subunit E and some aspartyl tRNA ligases [ , ], and in hypothetical protein PH0730 ( ).

[ "GO:0004812", "GO:0005524", "GO:0005737" ]

[ "aminoacyl-tRNA ligase activity", "ATP binding", "cytoplasm" ]

[ "molecular_function", "molecular_function", "cellular_component" ]

3

[ "CATHGENE3D", "SSF" ]

[ "G3DSA:3.30.1360.30", "SSF55261" ]

[ "", "" ]

[ 31987, 29381 ]

2

[ "EC", "REACTOME" ]

[ "6.1.1", "R-HSA-379726" ]

[ "EC:6.1.1", "REACTOME:R-HSA-379726" ]

2

[ "1c0a", "1efw", "1eqr", "1g51", "1il2", "1l0w", "1zq1", "2d6f", "2p8t", "4ah6", "4o2d", "4rmf", "4wj3", "4wj4", "5w25", "6hhv", "6hhw", "6hhx", "6sjc", "6wom", "7ap4" ]

21

[ "PUB00021841", "PUB00040197" ]

[ "11566892", "16809540" ]

[ "The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.", "Structural basis of RNA-dependent recruitment of glutamine to the genetic code." ]

[ 2001, 2006 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Microviridae sp. ctRQq14", "unclassified sequences" ]

[ 1217, 25635, 4738, 1, 630 ]

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",...

[ 6, 1, 1, 2, 1, 10, 3, 1, 5, 6, 1, 1, 6 ]

13

true

Homologous_superfamily

GAD-like domain superfamily

GAD-like_sf

1

IPR004116

4,116

Amelogenin

Family

929

false

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth. They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix...

[ "GO:0007275", "GO:0031012" ]

[ "multicellular organism development", "extracellular matrix" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PRINTS", "PANTHER", "SMART" ]

[ "PF02948", "PR01757", "PTHR46794", "SM00818" ]

[ "Amelogenin", "AMELOGENIN", "", "Amelogenin" ]

[ 926, 740, 816, 797 ]

4

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-381426", "R-BTA-8957275", "R-HSA-381426", "R-HSA-8957275", "R-MMU-381426", "R-MMU-8957275", "R-RNO-381426", "R-RNO-8957275", "R-SSC-381426", "R-SSC-8957275" ]

[ "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-8957275", "REACTOME:R-MMU-381426", "REACTOME:R-MMU-8957275", "REACTOME:R-RNO-381426", "REACTOME:R-RNO-8957275", "REACTOME:R-SSC-381426", "REACTOME:R-SSC-8957275" ]

10

[]

0

[ "PUB00007367", "PUB00011224", "PUB00011225", "PUB00011226", "PUB00011227" ]

[ "11223334", "8118759", "8454575", "2598664", "7782077" ]

[ "Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta.", "Production of a monoclonal antibody against human amelogenin.", "Molecular conformation of porcine amelogenin in solution: three folding units at the N-terminal, central, and C-terminal regions.", "Secondary structure and lim...

[ 2001, 1994, 1993, 1989, 1995 ]

5

[]

0

null

[ "Bacilli", "Dipnotetrapodomorpha" ]

[ 2, 927 ]

2

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 4, 12 ]

3

true

Family

Amelogenin

1

IPR004117

4,117

Olfactory receptor, insect

7tm6_olfct_rcpt

Family

30,939

false

This entry represents Odorant receptors and Odorant receptor coreceptors that are found mainly insects. The odorant receptor repertoire encodes a large collection of odour stimuli that vary widely in identity, intensity, and duration [ , ]. The atypical heteromeric and topological design of the odorant receptors appear...

[ "GO:0004984", "GO:0005549", "GO:0007608", "GO:0016020" ]

[ "olfactory receptor activity", "odorant binding", "sensory perception of smell", "membrane" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "PFAM", "PANTHER" ]

[ "PF02949", "PTHR21137" ]

[ "7tm_6", "" ]

[ 30451, 28852 ]

2

[]

0

[ "6c70", "7lic", "7lid", "7lig", "8v00", "8v02", "8v3c", "8v3d", "8z9a", "8z9z" ]

10

[ "PUB00153752", "PUB00153753", "PUB00153754", "PUB00153755" ]

[ "16615896", "21613503", "22174894", "22272331" ]

[ "Coding of odors by a receptor repertoire.", "Similar odorants elicit different behavioral and physiological responses, some supersustained.", "Heteromeric Anopheline odorant receptors exhibit distinct channel properties.", "Allosteric antagonism of insect odorant receptor ion channels." ]

[ 2006, 2011, 2011, 2012 ]

4

[]

0

null

[ "Eukaryota" ]

[ 30939 ]

1

[ "Drosophila melanogaster" ]

[ 462 ]

1

true

Family

Olfactory receptor, insect

7tm6_olfct_rcpt

1

IPR004118

4,118

Hepatitis TT virus, Orf2/Gyrovirus Vp2, N-terminal domain

HEV_TT_vir_Orf2/Gyrovir_Vp2_N

Domain

1,600

false

This entry represents a domain found in ORF2 from Torque teno virus (TTV) and related viruses. This domain contains a set of conserved cysteine and histidine residues suggesting a zinc binding domain and has been implicated in kinases regulation [ ]. TTV, isolated initially from a Japanese patient with hepatitis of unk...

[]

0

[ "PFAM" ]

[ "PF02957" ]

[ "TT_ORF2-like" ]

[ 1600 ]

1

[ "REACTOME" ]

[ "R-HSA-9610379" ]

[ "REACTOME:R-HSA-9610379" ]

1

[]

0

[ "PUB00007368", "PUB00154305", "PUB00154306" ]

[ "10388667", "17686849", "17146841" ]

[ "The entire nucleotide sequence of a TT virus isolate from the United States (TUS01): comparison with reported isolates and phylogenetic analysis.", "Torque teno virus (SANBAN isolate) ORF2 protein suppresses NF-kappaB pathways via interaction with IkappaB kinases.", "Torque teno virus (TTV): current status." ]

[ 1999, 2007, 2007 ]

3

[]

0

null

[ "Bdelloidea", "Viruses" ]

[ 19, 1581 ]

2

[]

0

true

Domain

Hepatitis TT virus, Orf2/Gyrovirus Vp2, N-terminal domain

HEV_TT_vir_Orf2/Gyrovir_Vp2_N

6

IPR004119

4,119

Ecdysteroid kinase-like

EcKL

Family

14,855

false

This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates [ ]. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 2...

[]

0

[ "PFAM" ]

[ "PF02958" ]

[ "EcKL" ]

[ 14855 ]

1

[]

0

[]

0

[ "PUB00086873", "PUB00091343", "PUB00094481" ]

[ "28763571", "16899460", "32540344" ]

[ "Enzymatic Synthesis of Psilocybin.", "Purification, kinetic characterization, and molecular cloning of a novel enzyme, ecdysteroid 22-kinase.", "Genomic and transcriptomic analyses in Drosophila suggest that the ecdysteroid kinase-like (EcKL) gene family encodes the 'detoxification-by-phosphorylation' enzymes ...

[ 2017, 2006, 2020 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes", "unclassified Klosneuvirinae" ]

[ 1697, 13029, 127, 2 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster" ]

[ 1, 1, 129 ]

3

true

Family

Ecdysteroid kinase-like

EcKL

5

IPR004120

4,120

HTLV Tax

Tax

Family

1,291

false

Human T-lymphotropic virus 1 is the etiological agent for adult T-cell leukemia (ATL), as well as for tropical spastic paraparesis (TSP) and HTLV-I associate myelopathy (HAM). A biological understanding of the involvement of HTLV-I and in ATL has focused significantly on the workings of the virally-encoded 40kDa phosph...

[ "GO:0045893" ]

[ "positive regulation of DNA-templated transcription" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF02959" ]

[ "Tax" ]

[ 1291 ]

1

[]

0

[]

0

[ "PUB00007369" ]

[ "11325603" ]

[ "Functional activities of the human T-cell leukemia virus type I Tax oncoprotein: cellular signaling through NF-kappa B." ]

[ 2001 ]

1

[]

0

null

[ "Retroviridae" ]

[ 1291 ]

1

[]

0

true

Family

HTLV Tax

Tax

8

IPR004121

4,121

Human herpesvirus K1 glycoprotein, C-terminal

K1_C

Domain

1,281

false

Current genotyping systems for Human herpesvirus 8 (HHV-8) are based on the highly variable gene encoding the K1 glycoprotein [ ]. This entry represents the C-terminal region of the K1 glycoprotein.

[]

0

[ "PFAM" ]

[ "PF02960" ]

[ "K1" ]

[ 1281 ]

1

[]

0

[]

0

[ "PUB00014489" ]

[ "11172090" ]

[ "Molecular characterization of strains of Human herpesvirus 8 from Japan, Argentina and Kuwait." ]

[ 2001 ]

1

[]

0

null

[ "Human herpesvirus 8" ]

[ 1281 ]

1

[]

0

true

Domain

Human herpesvirus K1 glycoprotein, C-terminal

K1_C

1

IPR004122

4,122

Barrier- to-autointegration factor, BAF

BAF_prot

Family

2,216

false

Barrier-to-autointegration factor (BAF) is an essential protein that is highly conserved in metazoan evolution, and which may act as a DNA-bridging protein [ ]. BAF binds directly to double-stranded DNA, to transcription activators, and to inner nuclear membrane proteins, including lamin A filament proteins that anchor...

[ "GO:0003677" ]

[ "DNA binding" ]

[ "molecular_function" ]

1

[ "PFAM", "SMART" ]

[ "PF02961", "SM01023" ]

[ "SAM_BAF", "BAF" ]

[ 2216, 2076 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-2980766", "R-BTA-2995383", "R-CEL-2995383", "R-DME-2995383", "R-DRE-2995383", "R-HSA-162592", "R-HSA-164843", "R-HSA-175567", "R-HSA-177539", "R-HSA-180689", "R-HSA-180910", "R-HSA-2980766", "R-HSA-2995383", "R-MMU-2980766", "R-MMU-2995383", "R-RNO-2980766", "R-RNO-2995383" ]

[ "REACTOME:R-BTA-2980766", "REACTOME:R-BTA-2995383", "REACTOME:R-CEL-2995383", "REACTOME:R-DME-2995383", "REACTOME:R-DRE-2995383", "REACTOME:R-HSA-162592", "REACTOME:R-HSA-164843", "REACTOME:R-HSA-175567", "REACTOME:R-HSA-177539", "REACTOME:R-HSA-180689", "REACTOME:R-HSA-180910", "REACTOME:R-HS...

17

[ "1ci4", "1qck", "2bzf", "2ezx", "2ezy", "2ezz", "2odg", "6ghd", "6rpr", "6unt", "6ure", "6urj", "6urk", "6url", "6urn", "6urr", "6urz", "6us0", "6us1", "6us7", "6usb", "6usd", "6usi", "7abm", "7ndy", "7z21", "9j8m", "9j8n", "9j8o" ]

29

[ "PUB00015060", "PUB00015061", "PUB00015062" ]

[ "15130582", "14645565", "12902403" ]

[ "BAF: roles in chromatin, nuclear structure and retrovirus integration.", "Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions.", "Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organiz...

[ 2004, 2003, 2003 ]

3

[]

0

null

[ "Eukaryota", "Sylvanvirus sp.", "organismal metagenomes" ]

[ 2213, 1, 2 ]

3

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 3, 2, 6, 2, 3 ]

6

true

Family

Barrier- to-autointegration factor, BAF

BAF_prot

8

IPR004123

4,123

Dim1 family

Dim1

Family

6,710

false

This entry represents fission yeast Dim1 and its homologues, including Dib1 from budding yeasts, YLS8 from plants and TXNL4 from animals. Dim1 was originally identified as a mitosis protein [ ]. Later, it was found to interact with spliceosome component Prp6, which is involved in pre-mRNA splicing [ ]. Dim1 may act at ...

[ "GO:0000398", "GO:0046540" ]

[ "mRNA splicing, via spliceosome", "U4/U6 x U5 tri-snRNP complex" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PIRSF", "PANTHER", "SMART", "CDD" ]

[ "PF02966", "PIRSF017199", "PTHR12052", "SM01410", "cd02954" ]

[ "DIM1", "mRNA_splic_U5", "", "DIM1", "DIM1" ]

[ 6709, 5233, 6560, 6478, 4194 ]

5

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-72163", "R-HSA-72165", "R-MMU-72163", "R-MMU-72165" ]

[ "REACTOME:R-HSA-72163", "REACTOME:R-HSA-72165", "REACTOME:R-MMU-72163", "REACTOME:R-MMU-72165" ]

4

[ "1pqn", "1qgv", "1syx", "1xbs", "2av4", "3gix", "3jcm", "3jcr", "4bwq", "4bws", "4cdo", "4in0", "5gan", "5gap", "5nrl", "5o9z", "5zwm", "5zwo", "6ah0", "6ahd", "6qw6", "6qx9", "8h6e", "8h6j", "8h6k", "8h6l", "8q7n", "8qo9", "8qoz", "8qp8", "8qp9", "8qpa"...

43

[ "PUB00075149", "PUB00075151", "PUB00075152", "PUB00075153" ]

[ "9182666", "11054566", "15755920", "17558560" ]

[ "Fission yeast dim1(+) encodes a functionally conserved polypeptide essential for mitosis.", "Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1.", "Dim1p is required for efficient splicing and expo...

[ 1997, 2000, 2005, 2007 ]

4

[]

0

null

[ "Dictyobacter", "Eukaryota", "bird metagenome" ]

[ 5, 6704, 1 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 8, 1, 2, 1, 12, 4, 1, 4, 7, 1, 1, 12 ]

12

true

Family

Dim1 family

Dim1

2

IPR004124

4,124

Glycoside hydrolase, family 33, N-terminal

Glyco_hydro_33_N

Domain

635

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:0004308", "GO:0005975" ]

[ "exo-alpha-sialidase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF02973" ]

[ "Sialidase" ]

[ 635 ]

1

[ "CAZY", "EC" ]

[ "GH33", "3.2.1.18" ]

[ "CAZY:GH33", "EC:3.2.1.18" ]

2

[ "1sli", "1sll", "2jkb", "2sli", "2v73", "2vw0", "2vw1", "2vw2", "3sli", "4c1w", "4c1x", "4foq", "4fov", "4fow", "4foy", "4fp2", "4fp3", "4fpc", "4fpe", "4fpf", "4fpg", "4fph", "4fpj", "4fpk", "4fpl", "4fpo", "4fpy", "4fq4", "4sli", "4xe9", "4xhb", "4xhx"...

62

[ "PUB00004870", "PUB00005266", "PUB00007372", "PUB00009756" ]

[ "7624375", "8535779", "9562562", "2034213" ]

[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity.", "The sialidase gene from Clostridium sept...

[ 1995, 1995, 1998, 1991 ]

4

[]

0

null

[ "Bacteria", "Macrobdella decora" ]

[ 634, 1 ]

2

[]

0

true

Domain

Glycoside hydrolase, family 33, N-terminal

Glyco_hydro_33_N

1

IPR004125

4,125

Signal recognition particle, SRP54 subunit, M-domain

Signal_recog_particle_SRP54_M

Domain

32,197

false

The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [ , , ]. SRP recognises the signal sequence of the nascent po...

[ "GO:0008312", "GO:0006614", "GO:0048500" ]

[ "7S RNA binding", "SRP-dependent cotranslational protein targeting to membrane", "signal recognition particle" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PFAM" ]

[ "PF02978" ]

[ "SRP_SPB" ]

[ 32197 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.6.5.4", "R-BTA-1799339", "R-CFA-1799339", "R-DDI-1799339", "R-DRE-1799339", "R-HSA-1799339", "R-MMU-1799339", "R-RNO-1799339", "R-SCE-1799339", "R-SPO-1799339" ]

[ "EC:3.6.5.4", "REACTOME:R-BTA-1799339", "REACTOME:R-CFA-1799339", "REACTOME:R-DDI-1799339", "REACTOME:R-DRE-1799339", "REACTOME:R-HSA-1799339", "REACTOME:R-MMU-1799339", "REACTOME:R-RNO-1799339", "REACTOME:R-SCE-1799339", "REACTOME:R-SPO-1799339" ]

10

[ "1dul", "1hq1", "1mfq", "1qb2", "1qzw", "1qzx", "1ry1", "2ffh", "2go5", "2iy3", "2j28", "2j37", "2jqe", "2pxb", "2pxd", "2pxe", "2pxf", "2pxk", "2pxl", "2pxp", "2pxq", "2pxt", "2pxu", "2pxv", "2v3c", "2xkv", "2xxa", "3dm5", "3kl4", "3lqx", "3ndb", "3zn8"...

51

[ "PUB00028143", "PUB00035998", "PUB00035999", "PUB00053948", "PUB00063486", "PUB00100261", "PUB00103724", "PUB00103725" ]

[ "16469117", "17622352", "17507650", "12364595", "12605305", "34020957", "9922234", "7511896" ]

[ "Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.", "X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.", "The signal recognition particle (SRP) RNA links conformational changes in the SRP to pro...

[ 2006, 2007, 2007, 2002, 2003, 2021, 1999, 1994 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Escherichia phage vB_EcoM-613R3", "Eukaryota", "unclassified sequences" ]

[ 928, 23842, 1, 6853, 573 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 20, 1, 1, 2, 1, 6, 4, 1, 11, 2, 1, 1, 24 ]

13

true

Domain

Signal recognition particle, SRP54 subunit, M-domain

Signal_recog_particle_SRP54_M

8

IPR004126

4,126

Phospholipase A2 inhibitor, N-terminal domain

PLipase_A2_inh_N

Domain

914

false

This entry represents a domain located at the N-terminal end of a group of proteins predominantly found in vertebrates that inhibit basic phospholipase A2 isozymes in snake's venom [ , ].

[ "GO:0004859", "GO:0005576" ]

[ "phospholipase inhibitor activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM" ]

[ "PF02988" ]

[ "PLA2_inh" ]

[ 914 ]

1

[]

0

[]

0

[ "PUB00009757", "PUB00020135" ]

[ "9395334", "8195214" ]

[ "Characterization and evolution of a gene encoding a Trimeresurus flavoviridis serum protein that inhibits basic phospholipase A2 isozymes in the snake's venom.", "A phospholipase A2 inhibitor from the plasma of the South American rattlesnake (Crotalus durissus terrificus). Protein structure, genomic structure, a...

[ 1997, 1994 ]

2

[]

0

null

[ "Eumetazoa" ]

[ 914 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 2, 2 ]

3

true

Domain

Phospholipase A2 inhibitor, N-terminal domain

PLipase_A2_inh_N

2

IPR004127

4,127

Prefoldin alpha-like

Prefoldin_subunit_alpha

Family

14,869

false

This entry represents prefoldin subunit alpha-like proteins. Prefoldin (PFD) is a chaperone that interacts exclusively with type II chaperonins, hetero-oligomers lacking an obligate co-chaperonin that are found only in eukaryotes (chaperonin-containing T-complex polypeptide-1 (CCT)) and archaea. Eukaryotic PFD is a mul...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF02996", "TIGR00293" ]

[ "Prefoldin", "" ]

[ 14868, 6092 ]

2

[ "REACTOME", "REACTOME" ]

[ "R-HSA-389957", "R-HSA-8953750" ]

[ "REACTOME:R-HSA-389957", "REACTOME:R-HSA-8953750" ]

2

[ "1fxk", "2zdi", "6nr8", "6nr9", "6nrb", "6nrc", "6nrd", "6vy1", "7wu7" ]

9

[ "PUB00013187", "PUB00013306" ]

[ "12456645", "11106732" ]

[ "Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.", "Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins." ]

[ 2002, 2000 ]

2

[]

[ "IPR003994", "IPR011599", "IPR016655" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 939, 14, 13872, 44 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 15, 4, 6, 6, 11, 16, 2, 12, 18, 3, 2, 34 ]

12

true

Family

Prefoldin alpha-like

Prefoldin_subunit_alpha

4

IPR004130

4,130

GPN-loop GTPase

Gpn

Family

30,984

false

Proteins in this entry belong to the GPN-loop GTPase family [ ], including Npa3 (also known as Gpn1) and Gpn2/3 from budding yeasts. In humans, Npa3 homologue is known as XAB1; Gpn2 is known as GPN2/ATPBD1B; Gpn3 is known as Parcs.

[]

0

[ "PFAM", "PANTHER" ]

[ "PF03029", "PTHR21231" ]

[ "ATP_bind_1", "" ]

[ 30973, 14687 ]

2

[ "EC" ]

[ "3.6.5.-" ]

[ "EC:3.6.5.-" ]

1

[ "1yr6", "1yr7", "1yr8", "1yr9", "1yra", "1yrb", "2oxr", "5hci", "5hcn", "7zhf", "7zhk" ]

11

[ "PUB00042299", "PUB00072003", "PUB00072006", "PUB00072007", "PUB00072018" ]

[ "17468740", "23324351", "23267056", "21844196", "21532343" ]

[ "Structural insights into a new homodimeric self-activated GTPase family.", "Eukaryotic GPN-loop GTPases paralogs use a dimeric assembly reminiscent of archeal GPN.", "Biogenesis of RNA polymerases II and III requires the conserved GPN small GTPases in Saccharomyces cerevisiae.", "GTP-dependent binding and nu...

[ 2007, 2013, 2013, 2011, 2011 ]

5

[]

[ "IPR030228", "IPR030231" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 392, 15954, 14571, 67 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 14, 3, 4, 4, 10, 10, 3, 12, 13, 3, 3, 24 ]

12

true

Family

GPN-loop GTPase

Gpn

2

IPR004132

4,132

Kinetoplastid membrane protein 11

KMP11

Family

94

false

Kinetoplastid membrane protein 11 is a major cell surface glycoprotein of the parasite Leishmania donovani. It stimulates T-cell proliferation and may play a role in the immunlogy of the dieases Leishmaniasis.

[ "GO:0006952", "GO:0008284" ]

[ "defense response", "positive regulation of cell population proliferation" ]

[ "biological_process", "biological_process" ]

2

[ "PFAM" ]

[ "PF03037" ]

[ "KMP11" ]

[ 94 ]

1

[]

0

[ "5y70", "7f0k" ]

2

[]

0

[]

0

null

[ "Eukaryota", "Xenorhabdus bovienii str. Intermedium" ]

[ 93, 1 ]

2

[]

0

true

Family

Kinetoplastid membrane protein 11

KMP11

2

IPR004134

4,134

Peptidase C1B, bleomycin hydrolase

Peptidase_C1B

Family

9,911

false

This group of proteins belong to MEROPS peptidase family C1, subfamily C1B. This family contains prokaryotic and eukaryotic aminopeptidases and includes bleomycin hydrolases. Bleomycins are antitumour glycopeptide antibiotics originally isolated from the actinomycete Streptomyces verticillus, and are inactivated by ble...

[ "GO:0070005", "GO:0006508" ]

[ "cysteine-type aminopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PIRSF", "PANTHER", "CDD" ]

[ "PF03051", "PIRSF005700", "PTHR10363", "cd00585" ]

[ "Peptidase_C1_2", "PepC", "", "Peptidase_C1B" ]

[ 9896, 8856, 9395, 7119 ]

4

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.4.22.40", "R-GGA-983168", "R-HSA-983168", "R-MMU-983168", "R-RNO-983168", "R-SCE-983168" ]

[ "EC:3.4.22.40", "REACTOME:R-GGA-983168", "REACTOME:R-HSA-983168", "REACTOME:R-MMU-983168", "REACTOME:R-RNO-983168", "REACTOME:R-SCE-983168" ]

6

[ "1a6r", "1cb5", "1gcb", "2cb5", "2dzy", "2dzz", "2e00", "2e01", "2e02", "2e03", "3gcb", "3pw3", "4k7c", "5wdk", "5wdl", "6w4n", "7v5l", "7v5s", "7v5t", "7xf9" ]

20

[ "PUB00011704", "PUB00020025", "PUB00020029", "PUB00030423", "PUB00036768", "PUB00076953", "PUB00077104", "PUB00077105", "PUB00077107", "PUB00077108" ]

[ "11517925", "9891971", "9546396", "14725770", "7638617", "7044372", "4122312", "16472072", "8639621", "2477059" ]

[ "Evolutionary lines of cysteine peptidases.", "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.", "The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.", "T...

[ 2001, 1998, 1998, 2004, 1995, 1982, 1972, 2006, 1996, 1989 ]

10

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "metagenomes" ]

[ 6089, 3658, 18, 11, 135 ]

5

[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 3, 7, 8, 6, 1, 7, 1 ]

7

true

Family

Peptidase C1B, bleomycin hydrolase

Peptidase_C1B

8

IPR004136

4,136

Nitronate monooxygenase

NMO

Domain

48,175

false

Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) ( ), is an FMN-dependent enzyme that uses molecular oxygen to oxidise (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Prev...

[ "GO:0018580" ]

[ "nitronate monooxygenase activity" ]

[ "molecular_function" ]

1

[ "CDD" ]

[ "cd04730" ]

[ "NPD_like" ]

[ 48175 ]

1

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "1.13.12.-", "GenProp1746", "PWY-5305", "PWY-5469", "PWY-6806", "PWY-7352", "PWY-7354", "PWY-7513", "PWY-7898", "PWY-8012", "PWY-8166", "PWY-8437", "PWY-8447" ]

[ "EC:1.13.12.-", "GP:GenProp1746", "METACYC:PWY-5305", "METACYC:PWY-5469", "METACYC:PWY-6806", "METACYC:PWY-7352", "METACYC:PWY-7354", "METACYC:PWY-7513", "METACYC:PWY-7898", "METACYC:PWY-8012", "METACYC:PWY-8166", "METACYC:PWY-8437", "METACYC:PWY-8447" ]

13

[ "2gjl", "2gjn", "2z6i", "2z6j", "3bo9", "3bw2", "3bw3", "3bw4", "4iql", "4q4k", "4qis", "4qit", "4qiu", "5gvh", "5gvj", "5lsm", "6bka", "6e2a", "7e1q", "7e1r", "7e1s", "7l00", "9jsy", "9k7h" ]

24

[ "PUB00016932", "PUB00019937", "PUB00041080", "PUB00075572" ]

[ "15582992", "9501443", "16682407", "19577534" ]

[ "Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase.", "Purification, characterization, and mechanism of a flavin mononucleotide-dependent 2-nitropropane dioxygenase from Neurospora crassa.", "Crystal structure of 2-nitropropane dioxygenase compl...

[ 2005, 1998, 2006, 2010 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Yasminevirus sp. GU-2018", "unclassified sequences" ]

[ 102, 38896, 8552, 1, 1, 623 ]

6

[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]

[ 6, 4, 5, 1, 4 ]

5

true

Domain

Nitronate monooxygenase

NMO

5

IPR004137

4,137

Hydroxylamine reductase/Ni-containing CO dehydrogenase

HCP/CODH

Family

9,700

false

This entry represent the hydroxylamine reductases (Hcp, also known as Prismane) and the Ni-containing CO dehydrogenases (CODH) ( ). Hydroxylamine reductases have been identified in bacteria, archaea and eukaryotic protozoa. They contain two Fe/S centres - a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster. The...

[ "GO:0016491" ]

[ "oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PANTHER" ]

[ "PF03063", "PTHR30109" ]

[ "Prismane", "" ]

[ 9697, 9630 ]

2

[ "EC" ]

[ "1.7.99.1" ]

[ "EC:1.7.99.1" ]

1

[ "1e1d", "1e2u", "1e9v", "1gn9", "1gnl", "1gnt", "1jqk", "1mjg", "1oa0", "1oa1", "1oao", "1su6", "1su7", "1su8", "1suf", "1upx", "1w9m", "2yiv", "2z8y", "3b51", "3b52", "3b53", "3cf4", "3i01", "3i04", "3i39", "4udx", "4udy", "5fle", "6b6v", "6b6w", "6b6x"...

132

[ "PUB00007375", "PUB00020178", "PUB00063808", "PUB00063809" ]

[ "10651802", "12374823", "12374822", "8561463" ]

[ "The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S].", "Hydroxylamine reductase activity of the hybrid c...

[ 2000, 2002, 2002, 1995 ]

4

[]

[ "IPR004460", "IPR010047", "IPR010048" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 777, 8223, 274, 426 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Hydroxylamine reductase/Ni-containing CO dehydrogenase

HCP/CODH

7

IPR004139

4,139

Glycosyl transferase, family 13

Glyco_trans_13

Family

5,759

false

The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas...

[ "GO:0008375", "GO:0009101" ]

[ "acetylglucosaminyltransferase activity", "glycoprotein biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF03071" ]

[ "GNT-I" ]

[ 5759 ]

1

[ "CAZY", "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "GH13", "2.4.1", "GenProp1444", "GenProp1524", "R-CEL-964739", "R-HSA-5083628", "R-HSA-8932504", "R-HSA-8932506", "R-HSA-964739", "R-HSA-9683686", "R-HSA-9694548", "R-HSA-9939291", "R-MMU-8932504", "R-MMU-8932506", "R-MMU-964739", "R-MMU-9939291", "R-RNO-8932504", "R-RNO-8932506", ...

[ "CAZY:GH13", "EC:2.4.1", "GP:GenProp1444", "GP:GenProp1524", "REACTOME:R-CEL-964739", "REACTOME:R-HSA-5083628", "REACTOME:R-HSA-8932504", "REACTOME:R-HSA-8932506", "REACTOME:R-HSA-964739", "REACTOME:R-HSA-9683686", "REACTOME:R-HSA-9694548", "REACTOME:R-HSA-9939291", "REACTOME:R-MMU-8932504",...

20

[ "1fo8", "1fo9", "1foa", "2am3", "2am4", "2am5", "2apc", "5ggf", "5ggg", "5ggi" ]

10

[ "PUB00007376", "PUB00009409", "PUB00089708", "PUB00090058", "PUB00092645" ]

[ "10406843", "9334165", "11709191", "27493216", "28512129" ]

[ "Molecular cloning and characterization of cDNA coding for beta1, 2N-acetylglucosaminyltransferase I (GlcNAc-TI) from Nicotiana tabacum.", "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.", "Muscular dystrophy and neuronal migration disorder caused ...

[ 1999, 1997, 2001, 2016, 2017 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP)", "metagenomes" ]

[ 86, 5669, 1, 3 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 7, 3, 22, 2, 22, 5, 3, 12, 10 ]

9

true

Family

Glycosyl transferase, family 13

Glyco_trans_13

1

IPR004140

4,140

Exocyst complex component Exo70

Exo70

Family

17,933

false

The Exo70 protein forms one subunit of the exocyst complex (consist of Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70, and Exo84 in budding yeast). First discovered in Saccharomyces cerevisiae [ ], it is evolutionarily conserved in eukaryotes. It mediates the tethering of post-Golgi secretory vesicles to the plasma membra...

[ "GO:0006887", "GO:0000145" ]

[ "exocytosis", "exocyst" ]

[ "biological_process", "cellular_component" ]

2

[ "PANTHER" ]

[ "PTHR12542" ]

[ "" ]

[ 17933 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DDI-264876", "R-DME-264876", "R-DME-5620916", "R-HSA-1445148", "R-HSA-264876", "R-HSA-5620916", "R-MMU-264876", "R-MMU-5620916", "R-RNO-264876", "R-RNO-5620916" ]

[ "REACTOME:R-DDI-264876", "REACTOME:R-DME-264876", "REACTOME:R-DME-5620916", "REACTOME:R-HSA-1445148", "REACTOME:R-HSA-264876", "REACTOME:R-HSA-5620916", "REACTOME:R-MMU-264876", "REACTOME:R-MMU-5620916", "REACTOME:R-RNO-264876", "REACTOME:R-RNO-5620916" ]

10

[ "2b1e", "2b7m", "2pft", "2pfv", "4rl5", "5yfp", "6vkl", "7pp2" ]

8

[ "PUB00007377", "PUB00007378", "PUB00007379", "PUB00007380", "PUB00033660", "PUB00100047", "PUB00100048", "PUB00100078" ]

[ "8978675", "10207081", "10588647", "9405631", "16359701", "34061181", "29335562", "17717527" ]

[ "The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae.", "Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70.", "The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from it...

[ 1996, 1999, 1999, 1997, 2006, 2021, 2018, 2007 ]

8

[]

0

null

[ "Eukaryota" ]

[ 17933 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 106, 1, 15, 3, 7, 8, 1, 140, 8, 1, 1, 109 ]

12

true

Family

Exocyst complex component Exo70

Exo70

7

IPR004142

4,142

NDRG

Family

13,367

false

This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted [ ]. The precise molecular and cellular function of members of this family is still unknown, yet they are known to be involved in cellular differentiation events. The Ndr1 group was the fi...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF03096", "PTHR11034" ]

[ "Ndr", "" ]

[ 13366, 13031 ]

2

[ "REACTOME" ]

[ "R-HSA-6803205" ]

[ "REACTOME:R-HSA-6803205" ]

1

[ "2qmq", "2xmq", "2xmr", "2xms", "6l4b", "6l4g", "6l4h", "6zmm", "9kcl", "9kcm", "9kcr" ]

11

[ "PUB00007381" ]

[ "10581191" ]

[ "Identification of new genes ndr2 and ndr3 which are related to Ndr1/RTP/Drg1 but show distinct tissue specificity and response to N-myc." ]

[ 1999 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobrevibacter thaueri", "marine metagenome" ]

[ 44, 13321, 1, 1 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 11, 2, 41, 23, 102, 26, 12, 39, 67 ]

9

true

Family

NDRG

2

IPR004143

4,143

Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain

BPL_LPL_catalytic

Domain

81,026

false

This entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [ , , , , ]. These proteins catalyse the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of l...

[ "GO:0036211" ]

[ "protein modification process" ]

[ "biological_process" ]

1

[ "PFAM", "PFAM", "PFAM", "PROFILE" ]

[ "PF03099", "PF16917", "PF21948", "PS51733" ]

[ "BPL_LplA_LipB", "BPL_LplA_LipB_2", "LplA-B_cat", "BPL_LPL_CATALYTIC" ]

[ 31536, 703, 48422, 77956 ]

4

[ "EC", "EC", "GP", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.3.1", "2.3.1.181", "GenProp1625", "PWY-6987", "PWY-7382", "R-BTA-9857492", "R-DME-9857492", "R-DRE-9857492", "R-HSA-196780", "R-HSA-3371599", "R-HSA-9857492", "R-MMU-196780", "R-MMU-9857492", "R-PFA-9857492", "R-SCE-196780", "R-SCE-9857492", "R-SPO-196780", "R-SPO-9857492", "R...

[ "EC:2.3.1", "EC:2.3.1.181", "GP:GenProp1625", "METACYC:PWY-6987", "METACYC:PWY-7382", "REACTOME:R-BTA-9857492", "REACTOME:R-DME-9857492", "REACTOME:R-DRE-9857492", "REACTOME:R-HSA-196780", "REACTOME:R-HSA-3371599", "REACTOME:R-HSA-9857492", "REACTOME:R-MMU-196780", "REACTOME:R-MMU-9857492", ...

19

[ "1bia", "1bib", "1hxd", "1vqz", "1w66", "1wnl", "1wpy", "1wq7", "1wqw", "1x01", "1x2g", "1x2h", "2ars", "2art", "2aru", "2c7i", "2c8m", "2cgh", "2deq", "2djz", "2dkg", "2dth", "2dti", "2dto", "2dve", "2dxt", "2dxu", "2dz9", "2dzc", "2e10", "2e1h", "2e41"...

110

[ "PUB00019228", "PUB00038032", "PUB00038115", "PUB00038224", "PUB00039383", "PUB00039916", "PUB00047340" ]

[ "11106165", "16735476", "16169557", "16043486", "16141198", "16384580", "17570395" ]

[ "Lipoylating and biotinylating enzymes contain a homologous catalytic module.", "The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase.", "Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation....

[ 2000, 2006, 2005, 2005, 2005, 2006, 2007 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1993, 62197, 15397, 5, 1434 ]

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",...

[ 39, 5, 6, 7, 3, 9, 11, 3, 12, 11, 3, 3, 13 ]

13

true

Domain

Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain

BPL_LPL_catalytic

1

IPR004145

4,145

Domain of unknown function DUF243

DUF243

Domain

2,413

false

This domain is only found in arthropod proteins. It is found associated with YLP motifs ( ) in some proteins.

[]

0

[ "PFAM", "SMART" ]

[ "PF03103", "SM00690" ]

[ "DUF243", "DM5" ]

[ 2409, 2369 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Eukaryota" ]

[ 2413 ]

1

[ "Drosophila melanogaster" ]

[ 39 ]

1

true

Domain

Domain of unknown function DUF243

DUF243

4

IPR004146

4,146

DC1

Domain

15,137

false

This entry represents a domain found predominantly in plant proteins, including Probable nucleoredoxin 1 (NRX1) and Protein VACUOLELESS GAMETOPHYTES (VLG) from Arabidopsis thaliana. This region is found at the C- terminal end of NRX1, which is likely to be a thiol-disulfide oxidoreductase required for pollen tube growt...

[]

0

[ "PFAM" ]

[ "PF03107" ]

[ "C1_2" ]

[ 15137 ]

1

[ "EC" ]

[ "1.8.1.8" ]

[ "EC:1.8.1.8" ]

1

[ "1v5n" ]

1

[ "PUB00099167", "PUB00103727", "PUB00103728" ]

[ "24253198", "28107777", "19714218" ]

[ "NTR/NRX define a new thioredoxin system in the nucleus of Arabidopsis thaliana cells.", "The DC1-domain protein VACUOLELESS GAMETOPHYTES is essential for development of female and male gametophytes in Arabidopsis.", "Penetration of the stigma and style elicits a novel transcriptome in pollen tubes, pointing to...

[ 2014, 2017, 2009 ]

3

[]

0

null

[ "Eukaryota" ]

[ 15137 ]

1

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 688, 50, 27 ]

3

true

Domain

DC1

3

IPR004147

4,147

ABC1 atypical kinase-like domain

ABC1_dom

Domain

63,172

false

This entry represents a domain found in Escherichia coli UbiB, known in Providencia stuartii as Aarf, which is required for ubiquinone (CoQ) biosynthesis [ , , ]. Some proteins with this domain are described as aarF domain-containing protein kinases (ADCKs). This domain is also found in yeast ABC1 proteins ( ) required...

[]

0

[ "PFAM" ]

[ "PF03109" ]

[ "ABC1" ]

[ 63172 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-2142789", "R-CEL-2142789", "R-DDI-2142789", "R-DRE-2142789", "R-HSA-2142789", "R-MMU-2142789", "R-RNO-2142789", "R-SCE-2142789", "R-SPO-2142789" ]

[ "REACTOME:R-BTA-2142789", "REACTOME:R-CEL-2142789", "REACTOME:R-DDI-2142789", "REACTOME:R-DRE-2142789", "REACTOME:R-HSA-2142789", "REACTOME:R-MMU-2142789", "REACTOME:R-RNO-2142789", "REACTOME:R-SCE-2142789", "REACTOME:R-SPO-2142789" ]

9

[ "4ped", "5i35", "5yjz", "5yk0", "5yk1", "5yk2", "7cy2", "7cyr", "7cz2", "7udp", "7udq", "9ugq" ]

12

[ "PUB00007384", "PUB00007385", "PUB00013772", "PUB00058159", "PUB00068672" ]

[ "1648478", "9422602", "10960098", "9799791", "23709220" ]

[ "ABC1, a novel yeast nuclear gene has a dual function in mitochondria: it suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex.", "Identification and characterization of aarF, a locus required for production of ubiquinone in Providencia stuartii and Esch...

[ 1991, 1998, 2000, 1998, 2013 ]

5

[]

[ "IPR034646", "IPR044095", "IPR045307", "IPR045308" ]

0

4

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 873, 29171, 32518, 85, 525 ]

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",...

[ 96, 4, 18, 4, 1, 25, 14, 4, 61, 19, 3, 4, 153 ]

13

true

Domain

ABC1 atypical kinase-like domain

ABC1_dom

7

IPR004148

4,148

BAR domain

BAR_dom

Domain

67,035

false

Endocytosis and intracellular transport involve several mechanistic steps: For the internalisation of cargo molecules, the membrane needs to bend to form a vesicular structure, which requires membrane curvature and a rearrangement of the cytoskeleton; Following its formation, the vesicle has to be pinched off the membr...

[ "GO:0005515", "GO:0005737" ]

[ "protein binding", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM", "PFAM", "PROFILE", "SMART" ]

[ "PF03114", "PF16746", "PS51021", "SM00721" ]

[ "BAR", "BAR_3", "BAR", "BAR" ]

[ 36511, 29059, 33669, 34719 ]

4

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC51021", "R-BTA-182971", "R-BTA-6807004", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8980692", "R-BTA-9013148", "R-BTA-9013149", "R-CEL-182971", "R-CEL-432720", "R-CEL-432722", "R-CEL-437239", "R-CEL-6807004", "R-CEL-8856825", "R-CEL-8856828", "R-DDI-9013148", "R-DDI-9013149", "R...

[ "PROSITEDOC:PDOC51021", "REACTOME:R-BTA-182971", "REACTOME:R-BTA-6807004", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8980692", "REACTOME:R-BTA-9013148", "REACTOME:R-BTA-9013149", "REACTOME:R-CEL-182971", "REACTOME:R-CEL-432720", "REACTOME:R-CEL-432722", "REACTOME:R-CE...

150

[ "1uru", "1x03", "1x04", "1zww", "2c08", "2d4c", "2elb", "2fic", "2q12", "2q13", "2z0n", "2z0o", "2z0v", "3sog", "4atm", "4avm", "4ckg", "4ckh", "4h8s", "4i1q", "4nsw", "5c5b", "5h3d", "6up6", "6upn", "9bqx", "9g2r", "9g2u", "9g2w" ]

29

[ "PUB00014978" ]

[ "14993925" ]

[ "The BAR-domain family of proteins: a case of bending and binding?" ]

[ 2004 ]

1

[]

[ "IPR032469", "IPR035670", "IPR035695", "IPR037428", "IPR037429", "IPR046984", "IPR047239", "IPR047267" ]

0

8

0

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 2, 67029, 4 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 23, 10, 280, 19, 124, 120, 10, 11, 161, 3, 7, 40 ]

12

true

Domain

BAR domain

BAR_dom

4

IPR004149

4,149

Zinc-finger, NAD-dependent DNA ligase C4-type

Znf_DNAligase_C4

Domain

23,116

false

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b...

[ "GO:0003911", "GO:0006260", "GO:0006281" ]

[ "DNA ligase (NAD+) activity", "DNA replication", "DNA repair" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "PFAM" ]

[ "PF03119" ]

[ "DNA_ligase_ZBD" ]

[ 23116 ]

1

[ "EC" ]

[ "6.5.1.2" ]

[ "EC:6.5.1.2" ]

1

[ "1v9p", "2owo", "3sgi", "4glx", "5tt5", "8ak4" ]

6

[ "PUB00007386", "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "10698952", "12665246", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications.", "Zinc fingers--folds for many occasions.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip...

[ 2000, 2002, 2007, 2005, 2005, 1999, 2001 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 24, 22573, 58, 8, 453 ]

5

[ "Escherichia coli (strain K12)", "Homo sapiens" ]

[ 1, 1 ]

2

true

Domain

Zinc-finger, NAD-dependent DNA ligase C4-type

Znf_DNAligase_C4

5

IPR004150

4,150

NAD-dependent DNA ligase, OB-fold

NAD_DNA_ligase_OB

Domain

32,445

false

DNA ligases catalyse the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor [ ]. This family is a small domain found after the adenylation domain DNA_ligase_N in NAD+-dependent ligases ( ). OB-fold domains generally are involve...

[ "GO:0003911", "GO:0006260", "GO:0006281" ]

[ "DNA ligase (NAD+) activity", "DNA replication", "DNA repair" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "PFAM" ]

[ "PF03120" ]

[ "OB_DNA_ligase" ]

[ 32445 ]

1

[ "EC" ]

[ "6.5.1.2" ]

[ "EC:6.5.1.2" ]

1

[ "1dgs", "1v9p", "2owo", "3sgi", "4glx", "5tt5", "8ak4" ]

7

[ "PUB00007386" ]

[ "10698952" ]

[ "Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications." ]

[ 2000 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 351, 30710, 266, 353, 765 ]

5

[ "Escherichia coli (strain K12)", "Homo sapiens" ]

[ 2, 1 ]

2

true

Domain

NAD-dependent DNA ligase, OB-fold

NAD_DNA_ligase_OB

1

IPR004151

4,151

7TM GPCR, serpentine receptor class e (Sre)

7TM_GPCR_serpentine_rcpt_Sre

Family

2,502

false

This entry represents serpentine receptor class e (Sre) from the Sra superfamily [ ]. The nematode Caenorhabditis elegans has only 14 types of chemosensory neuron, yet is able to sense and respond to several hundred different chemicals because each neuron detects several stimuli [ ]. Chemoperception is one of the centr...

[ "GO:0007606", "GO:0016020" ]

[ "sensory perception of chemical stimulus", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF03125" ]

[ "Sre" ]

[ 2502 ]

1

[]

0

[]

0

[ "PUB00000924", "PUB00004961", "PUB00007387", "PUB00044128", "PUB00044129", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]

[ "7585938", "8170923", "10580986", "18050473", "15618405", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]

[ "Divergent seven transmembrane receptors are candidate chemosensory receptors in C. elegans.", "Fingerprinting G-protein-coupled receptors.", "Chemosensory signaling in C. elegans.", "The putative chemoreceptor families of C. elegans.", "Identification of a nematode chemosensory gene family.", "The G prot...

[ 1995, 1994, 1999, 2006, 2005, 2003, 1994, 2005, 2009, 2006, 2013 ]

11

[]

0

null

[ "Protostomia" ]

[ 2502 ]

1

[ "Caenorhabditis elegans" ]

[ 67 ]

1

true

Family

7TM GPCR, serpentine receptor class e (Sre)

7TM_GPCR_serpentine_rcpt_Sre

2

IPR004152

4,152

GAT domain

GAT_dom

Domain

21,888

false

The GAT domain is a region of homology of ~130 residues, which is found in eukaryotic GGAs (for Golgi-localized, gamma ear-containing ADP ribosylation factor (ARF)-binding proteins) and vertebrate TOMs (for target of myb). The GAT domain is found in its entirety only in GGAs, although, at the C terminus it shares parti...

[ "GO:0035091", "GO:0043130" ]

[ "phosphatidylinositol binding", "ubiquitin binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM", "PROFILE" ]

[ "PF03127", "PS50909" ]

[ "GAT", "GAT" ]

[ 21133, 20111 ]

2

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "PDOC50909", "R-GGA-6798695", "R-HSA-6798695", "R-HSA-8854214", "R-HSA-8875656", "R-HSA-977225", "R-MMU-6798695", "R-MMU-8875656", "R-RNO-8875656", "R-SPO-5689901", "R-SPO-9013420" ]

[ "PROSITEDOC:PDOC50909", "REACTOME:R-GGA-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-8854214", "REACTOME:R-HSA-8875656", "REACTOME:R-HSA-977225", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-8875656", "REACTOME:R-RNO-8875656", "REACTOME:R-SPO-5689901", "REACTOME:R-SPO-9013420" ]

11

[ "1j2j", "1naf", "1nwm", "1o3x", "1oxz", "1wr6", "1wrd", "1x79", "1yd8", "2n2n", "2n9d" ]

11

[ "PUB00007389", "PUB00018380", "PUB00018381", "PUB00018382" ]

[ "11301005", "12636914", "12679809", "15457209" ]

[ "The GGAs promote ARF-dependent recruitment of clathrin to the TGN.", "The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs.", "Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport.", "Crystal structure of human G...

[ 2001, 2003, 2003, 2004 ]

4

[]

[ "IPR027428", "IPR044111" ]

0

2

0

[ "Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18)", "Bacteria", "Eukaryota" ]

[ 1, 19, 21868 ]

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...

[ 41, 4, 19, 5, 31, 19, 5, 24, 35, 2, 3, 79 ]

12

true

Domain

GAT domain

GAT_dom

1

IPR004153

4,153

CXCXC repeat

CXCXC_repeat

Repeat

1,947

false

This repeat contains the conserved pattern CXCXC where X can be any amino acid. The repeat is found in up to five copies in Vascular endothelial growth factor C and D [ , ]. In the salivary glands of the dipteran Chironomus tentans, a specific messenger ribonucleoprotein (mRNP) particle, the Balbiani ring (BR) granule,...

[]

0

[ "PFAM" ]

[ "PF03128" ]

[ "CXCXC" ]

[ 1947 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-114608", "R-HSA-194313", "R-HSA-195399", "R-MMU-114608", "R-MMU-194313", "R-MMU-195399", "R-RNO-114608", "R-RNO-194313", "R-RNO-195399" ]

[ "REACTOME:R-HSA-114608", "REACTOME:R-HSA-194313", "REACTOME:R-HSA-195399", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-194313", "REACTOME:R-MMU-195399", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-194313", "REACTOME:R-RNO-195399" ]

9

[]

0

[ "PUB00007390", "PUB00007391", "PUB00094368" ]

[ "8612600", "9089085", "20145116" ]

[ "A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases.", "Extraordinary conservation of cysteines among homologous Chironomus silk proteins sp185 and sp220.", "Structural determinants of growth factor binding and specificity by VEGF r...

[ 1996, 1997, 2010 ]

3

[]

0

null

[ "Bacteria", "Betabaculovirus", "Eukaryota" ]

[ 37, 6, 1904 ]

3

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 6, 4, 2, 9 ]

4

true

Repeat

CXCXC repeat

CXCXC_repeat

7

IPR004154

4,154

Anticodon-binding

Anticodon-bd

Domain

133,957

false

tRNA synthetases, or tRNA ligases are involved in protein synthesis. This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases [ ]. It is probably the anticodon binding domain [ ].

[]

0

[ "PFAM" ]

[ "PF03129" ]

[ "HGTP_anticodon" ]

[ 133957 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1", "R-BTA-9913635", "R-DME-9856649", "R-DME-9913635", "R-HSA-2151201", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-6782315", "R-HSA-9856649", "R-HSA-9913635", "R-MMU-9856649", "R-MMU-9913635" ]

[ "EC:6.1.1", "REACTOME:R-BTA-9913635", "REACTOME:R-DME-9856649", "REACTOME:R-DME-9913635", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-9856649", "REACTOME:R-HSA-9913635", "REACTOME:R-MMU-9856649"...

13

[ "1adj", "1ady", "1ati", "1b76", "1evk", "1evl", "1fyf", "1g5h", "1g5i", "1ggm", "1h4q", "1h4s", "1h4t", "1h4v", "1hc7", "1htt", "1kmm", "1kmn", "1kog", "1nj1", "1nj2", "1nj5", "1nj6", "1nj8", "1nyq", "1nyr", "1qe0", "1qf6", "1v95", "1wu7", "2el9", "2g4c"...

259

[ "PUB00007363", "PUB00007392" ]

[ "10447505", "9115984" ]

[ "Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.", "Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase." ]

[ 1999, 1997 ]

2

[]

[ "IPR033656", "IPR042064", "IPR044140", "IPR047246" ]

0

4

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 3852, 93492, 34269, 60, 2284 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 53, 10, 21, 14, 3, 46, 25, 6, 29, 45, 6, 6, 77 ]

13

true

Domain

Anticodon-binding

Anticodon-bd

9

IPR004155

4,155

PBS lyase HEAT-like repeat

PBS_lyase_HEAT

Repeat

31,142

false

This short bi-helical repeat is related to HEAT repeats and is present in phycocyanobilin lyases and other proteins. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the ph...

[]

0

[ "PFAM", "SMART" ]

[ "PF03130", "SM00567" ]

[ "HEAT_PBS", "EZ_HEAT" ]

[ 5566, 30685 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-204626", "R-CEL-204626", "R-DDI-204626", "R-DME-204626", "R-DRE-204626", "R-GGA-204626", "R-HSA-204626", "R-MMU-204626", "R-RNO-204626", "R-SCE-204626", "R-SPO-204626" ]

[ "REACTOME:R-BTA-204626", "REACTOME:R-CEL-204626", "REACTOME:R-DDI-204626", "REACTOME:R-DME-204626", "REACTOME:R-DRE-204626", "REACTOME:R-GGA-204626", "REACTOME:R-HSA-204626", "REACTOME:R-MMU-204626", "REACTOME:R-RNO-204626", "REACTOME:R-SCE-204626", "REACTOME:R-SPO-204626" ]

11

[ "1te4", "3ltj", "3ltm", "4d4z", "4d50", "4hxt", "4jw2", "4jw3", "4plq", "4plr", "4pls", "4rv1", "4rzp", "4v3o", "4v3r", "4xl5", "4xvp", "4zv6", "5d08", "5d0a", "5d0b", "5dcq", "5mfd", "5mfl", "5mfm", "5n3u", "5t8y", "6bzx", "6fsq", "6ft5", "6g4j", "6gwc"...

62

[ "PUB00007393", "PUB00007394", "PUB00007395", "PUB00007396", "PUB00058199", "PUB00058202", "PUB00058203", "PUB00058205" ]

[ "8132596", "9023176", "10708746", "9882677", "19291314", "21502530", "882677", "9546244" ]

[ "Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase.", "A role for cpeYZ in cyanobacterial phycoerythrin biosynthesis.", "Novel activity of a phycobiliprotein lyase: both the attachment of phycocyanobilin and the isomerization to phycoviolobil...

[ 1994, 1997, 2000, 1999, 2009, 2011, 1977, 1998 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1915, 20667, 7991, 569 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 10, 1, 3, 1, 2, 5, 1, 6, 4, 1, 1, 10 ]

12

true

Repeat

PBS lyase HEAT-like repeat

PBS_lyase_HEAT

1

IPR004156

4,156

Organic anion transporter polypeptide

OATP

Family

19,080

false

This family consists of several eukaryotic Organic-Anion-Transporting Polypeptides (OATPs). Several have been identified mostly in human and rat. Different OATPs vary in tissue distribution and substrate specificity. Since the numbering of different OATPs in particular species was based originally on the order of disco...

[ "GO:0055085", "GO:0016020" ]

[ "transmembrane transport", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF03137", "PTHR11388", "TIGR00805" ]

[ "OATP", "", "oat" ]

[ 19024, 18689, 13638 ]

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-879518", "R-DME-6798695", "R-DME-879518", "R-HSA-159418", "R-HSA-189483", "R-HSA-5619058", "R-HSA-5619095", "R-HSA-5619110", "R-HSA-6798695", "R-HSA-879518", "R-HSA-9749641", "R-HSA-9754706", "R-HSA-9793528", "R-MMU-159418", "R-MMU-189483", "R-MMU-6798695", "R-MMU-879518", "...

[ "REACTOME:R-BTA-879518", "REACTOME:R-DME-6798695", "REACTOME:R-DME-879518", "REACTOME:R-HSA-159418", "REACTOME:R-HSA-189483", "REACTOME:R-HSA-5619058", "REACTOME:R-HSA-5619095", "REACTOME:R-HSA-5619110", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-879518", "REACTOME:R-HSA-9749641", "REACTOME:R-H...

27

[ "7eeb", "8hnb", "8hnc", "8hnd", "8hnh", "8k6l", "8kgi", "8kgv", "8kgw", "8pg0", "8phw", "9cy1", "9cy3", "9cy4", "9dxo", "9dxp", "9juq", "9jv1", "9mgk", "9mr5" ]

20

[ "PUB00007397", "PUB00087218" ]

[ "10873595", "23506880" ]

[ "Molecular identification and characterization of novel members of the human organic anion transporter (OATP) family.", "The SLCO (former SLC21) superfamily of transporters." ]

[ 2000, 2013 ]

2

[]

[ "IPR046329" ]

0

1

0

[ "Bacteria", "Eukaryota" ]

[ 10, 19070 ]

2

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Zea mays" ]

[ 1, 9, 80, 16, 64, 57, 91, 1 ]

8

true

Family

Organic anion transporter polypeptide

OATP

7

IPR004158

4,158

Protein of unknown function DUF247, plant

DUF247_pln

Family

23,720

false

The function of the plant proteins constituting this family is unknown.

[]

0

[ "PFAM", "PANTHER" ]

[ "PF03140", "PTHR31170" ]

[ "DUF247", "" ]

[ 23712, 18418 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Alkalihalophilus pseudofirmus", "Eukaryota" ]

[ 1, 23719 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 141, 230, 70 ]

3

true

Family

Protein of unknown function DUF247, plant

DUF247_pln

7

IPR004159

4,159

Putative S-adenosyl-L-methionine-dependent methyltransferase

Put_SAM_MeTrfase

Family

19,810

false

This is a family of putative S-adenosyl-L-methionine (SAM)-dependent methyltransferases [ , , ].

[ "GO:0008168" ]

[ "methyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PANTHER" ]

[ "PF03141", "PTHR10108" ]

[ "Methyltransf_29", "" ]

[ 19808, 17476 ]

2

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...

[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...

[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...

146

[]

0

[ "PUB00057439", "PUB00057440", "PUB00066764" ]

[ "17461780", "18167546", "17425712" ]

[ "The TUMOROUS SHOOT DEVELOPMENT2 gene of Arabidopsis encoding a putative methyltransferase is required for cell adhesion and co-ordinated plant development.", "The OSU1/QUA2/TSD2-encoded putative methyltransferase is a critical modulator of carbon and nitrogen nutrient balance response in Arabidopsis.", "Homoga...

[ 2007, 2008, 2007 ]

3

[]

0

null

[ "Eukaryota" ]

[ 19810 ]

1

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 149, 96, 263 ]

3

true

Family

Putative S-adenosyl-L-methionine-dependent methyltransferase

Put_SAM_MeTrfase

8

IPR004160

4,160

Translation elongation factor EFTu/EF1A, C-terminal

Transl_elong_EFTu/EF1A_C

Domain

46,646

false

Elongation factor EF1A (also known as EF-1alpha or EF-Tu) promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. EF1A consists of three structural domains. Release factor eRF3, which governs translation termination, has a similar overall structure. RF3 has an N-term...

[]

0

[ "PFAM" ]

[ "PF03143" ]

[ "GTP_EFTU_D3" ]

[ 46646 ]

1

[ "EC", "REACTOME", "REACTOME" ]

[ "3.6.5.3", "R-HSA-5389840", "R-HSA-9754560" ]

[ "EC:3.6.5.3", "REACTOME:R-HSA-5389840", "REACTOME:R-HSA-9754560" ]

3

[ "1aip", "1b23", "1d2e", "1d8t", "1dg1", "1efc", "1efm", "1eft", "1efu", "1etu", "1exm", "1ha3", "1ls2", "1mj1", "1ob2", "1ob5", "1qzd", "1ttt", "1tui", "1xb2", "1zc8", "2bvn", "2c77", "2c78", "2fx3", "2hcj", "2hdn", "3agp", "3agq", "3avt", "3avu", "3avv"...

135

[ "PUB00007399", "PUB00007747", "PUB00070083" ]

[ "9253415", "10676813", "20974926" ]

[ "Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.", "The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.", "Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination,...

[ 1997, 2000, 2010 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 469, 32539, 13095, 3, 540 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 11, 3, 1, 3, 2, 3, 2, 3, 10, 5, 1, 1, 28 ]

13

true

Domain

Translation elongation factor EFTu/EF1A, C-terminal

Transl_elong_EFTu/EF1A_C

4

IPR004161

4,161

Translation elongation factor EFTu-like, domain 2

EFTu-like_2

Domain

231,553

false

This entry represents a domain found in a number of translation factors that is homologous to domain 2 of EF2-Tu (also known as EF1A and EF-1alpha). EF2-Tu (EF1A) consists of three structural domains. This entry represents domain 2, which adopts a β-barrel structure, and is involved in binding to both charged tRNA [ ]....

[ "GO:0005525" ]

[ "GTP binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF03144" ]

[ "GTP_EFTU_D2" ]

[ 231553 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-156827", "R-BTA-156842", "R-BTA-156902", "R-BTA-3371511", "R-BTA-381042", "R-BTA-382556", "R-BTA-5358493", "R-BTA-6798695", "R-BTA-72649", "R-BTA-72695", "R-BTA-72702", "R-BTA-72731", "R-BTA-8876725", "R-BTA-9840373", "R-CEL-156902", "R-CEL-3371511", "R-CEL-5358493", "R-CEL-...

[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-156842", "REACTOME:R-BTA-156902", "REACTOME:R-BTA-3371511", "REACTOME:R-BTA-381042", "REACTOME:R-BTA-382556", "REACTOME:R-BTA-5358493", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-727...

167

[ "1aip", "1b23", "1d1n", "1d2e", "1d8t", "1dar", "1dg1", "1efc", "1efg", "1efm", "1eft", "1efu", "1elo", "1etu", "1exm", "1f60", "1fnm", "1g7c", "1g7r", "1g7s", "1g7t", "1ha3", "1ije", "1ijf", "1jny", "1jqm", "1kjz", "1kk0", "1kk1", "1kk2", "1kk3", "1ktv"...

570

[ "PUB00007398", "PUB00033951", "PUB00033952", "PUB00033953", "PUB00033960", "PUB00033961" ]

[ "7491491", "12932732", "15922593", "12762045", "15680978", "12102560" ]

[ "Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.", "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors.", "Recognition and selection of tRNA in translation.", "Mechanisms of EF-Tu, a pi...

[ 1995, 2003, 2005, 2001, 2005, 2002 ]

6

[]

[ "IPR033720", "IPR044127", "IPR047042" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 3661, 114630, 111280, 15, 1967 ]

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",...

[ 97, 13, 69, 32, 7, 94, 59, 11, 54, 48, 9, 9, 166 ]

13

true

Domain

Translation elongation factor EFTu-like, domain 2

EFTu-like_2

4

IPR004162

4,162

E3 ubiquitin-protein ligase SINA-like, animal

SINA-like_animal

Family

7,543

false

Proteins in this entry are E3 ubiquitin-protein ligases that mediate ubiquitination and subsequent proteasomal degradation of target proteins. Proteins in this entry include Sina and Sinah (Sina homologue) from flies and SIAH1/2 from humans. The seven in absentia (sina) gene was first identified in Drosophila. The Dros...

[ "GO:0006511", "GO:0007275" ]

[ "ubiquitin-dependent protein catabolic process", "multicellular organism development" ]

[ "biological_process", "biological_process" ]

2

[ "PANTHER" ]

[ "PTHR45877" ]

[ "" ]

[ 7543 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.3.2.27", "PWY-7511", "R-CEL-373752", "R-CEL-983168", "R-DME-373752", "R-DME-5689880", "R-DME-983168", "R-DRE-373752", "R-DRE-5689880", "R-DRE-983168", "R-HSA-373752", "R-HSA-5689880", "R-HSA-977225", "R-HSA-983168", "R-MMU-5689880", "R-MMU-983168", "R-RNO-5689880", "R-RNO-983168...

[ "EC:2.3.2.27", "METACYC:PWY-7511", "REACTOME:R-CEL-373752", "REACTOME:R-CEL-983168", "REACTOME:R-DME-373752", "REACTOME:R-DME-5689880", "REACTOME:R-DME-983168", "REACTOME:R-DRE-373752", "REACTOME:R-DRE-5689880", "REACTOME:R-DRE-983168", "REACTOME:R-HSA-373752", "REACTOME:R-HSA-5689880", "REA...

18

[ "1k2f", "2a25", "2an6", "4c9z", "4ca1", "4i7b", "4i7c", "4i7d", "4x3g", "5h9m", "5wzz", "8heo", "9g0l" ]

13

[ "PUB00007400", "PUB00007401", "PUB00007402" ]

[ "9403064", "9267026", "11389839" ]

[ "Characterization of human homologs of the Drosophila seven in absentia (sina) gene.", "PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism.", "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses...

[ 1997, 1997, 2001 ]

3

[]

0

null

[ "Eukaryota", "Marseillevirus LCMAC103", "organismal metagenomes" ]

[ 7539, 2, 2 ]

3

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 6, 15, 9, 8, 6 ]

6

true

Family

E3 ubiquitin-protein ligase SINA-like, animal

SINA-like_animal

5

IPR004163

4,163

Coenzyme A transferase binding site

CoA_transf_BS

Binding_site

15,418

false

Coenzyme A (CoA) transferases belong to an evolutionary conserved [ , ] family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd ...

[ "GO:0008410" ]

[ "CoA-transferase activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01273" ]

[ "COA_TRANSF_1" ]

[ 15418 ]

1

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.8.3.5", "PDOC00980", "R-CEL-77108", "R-CEL-9837999", "R-DDI-77108", "R-DDI-9837999", "R-DME-77108", "R-DME-9837999", "R-HSA-77108", "R-HSA-9837999", "R-MMU-77108", "R-MMU-9837999", "R-RNO-77108", "R-RNO-9837999", "R-SSC-77108", "R-SSC-9837999" ]

[ "EC:2.8.3.5", "PROSITEDOC:PDOC00980", "REACTOME:R-CEL-77108", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-77108", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-77108", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-77108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-77108", "REACTOME:R-MMU-9837999", "REA...

16

[ "1k6d", "1m3e", "1o9l", "1ooy", "1ooz", "1ope", "2nrb", "2nrc", "3cdk", "3dlx", "3k6m", "3oxo", "3rrl", "4kgb", "5dbn", "6lp1", "8i3y", "8i40" ]

18

[ "PUB00002192", "PUB00002998" ]

[ "1624453", "9325289" ]

[ "Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida.", "Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family." ]

[ 1992, 1997 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 2, 13377, 1972, 67 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 2, 3, 1, 6, 8, 10 ]

7

true

Binding_site

Coenzyme A transferase binding site

CoA_transf_BS

1

IPR004164

4,164

Coenzyme A transferase active site

CoA_transf_AS

Active_site

16,061

false

Coenzyme A (CoA) transferases belong to an evolutionary conserved [ , ] family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimers of two subunits (A and B) of about 25 Kd...

[ "GO:0008410" ]

[ "CoA-transferase activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01274" ]

[ "COA_TRANSF_2" ]

[ 16061 ]

1

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.8.3.5", "PDOC00980", "R-CEL-77108", "R-CEL-9837999", "R-DDI-77108", "R-DDI-9837999", "R-DME-77108", "R-DME-9837999", "R-HSA-77108", "R-HSA-9837999", "R-MMU-77108", "R-MMU-9837999", "R-RNO-77108", "R-RNO-9837999", "R-SSC-77108", "R-SSC-9837999" ]

[ "EC:2.8.3.5", "PROSITEDOC:PDOC00980", "REACTOME:R-CEL-77108", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-77108", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-77108", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-77108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-77108", "REACTOME:R-MMU-9837999", "REA...

16

[ "1m3e", "1o9l", "1ooy", "1ooz", "1ope", "2nrb", "2nrc", "3cdk", "3dlx", "3k6m", "3oxo", "3rrl", "4kgb", "5dbn", "6lp1", "8i3y", "8i40", "9csc" ]

18

[ "PUB00002192", "PUB00002998" ]

[ "1624453", "9325289" ]

[ "Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida.", "Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family." ]

[ 1992, 1997 ]

2

[]

0

null

[ "Bacteria", "Candidatus Lokiarchaeum ossiferum", "Eukaryota", "metagenomes" ]

[ 11610, 1, 4393, 57 ]

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" ]

[ 1, 2, 3, 1, 8, 7, 1, 10 ]

8

true

Active_site

Coenzyme A transferase active site

CoA_transf_AS

2

IPR004165

4,165

Coenzyme A transferase family I

CoA_trans_fam_I

Family

60,598

false

This family consists of 3-oxoacid CoA-transferases and related CoA-transferases from family I. Coenzyme A (CoA) transferases belong to an evolutionary conserved [ , ] family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mam...

[ "GO:0008410" ]

[ "CoA-transferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PANTHER", "SMART" ]

[ "PF01144", "PTHR13707", "SM00882" ]

[ "CoA_trans", "", "CoA_trans" ]

[ 59827, 45893, 59468 ]

3

[ "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.8.3", "GenProp1240", "GenProp1441", "R-CEL-77108", "R-CEL-9837999", "R-DDI-77108", "R-DDI-9837999", "R-DME-77108", "R-DME-9837999", "R-HSA-77108", "R-HSA-9837999", "R-MMU-77108", "R-MMU-9837999", "R-RNO-77108", "R-RNO-9837999", "R-SSC-77108", "R-SSC-9837999" ]

[ "EC:2.8.3", "GP:GenProp1240", "GP:GenProp1441", "REACTOME:R-CEL-77108", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-77108", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-77108", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-77108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-77108", "REACTOME:R-MMU-9837...

17

[ "1k6d", "1m3e", "1o9l", "1ooy", "1ooz", "1ope", "1poi", "2ahu", "2ahv", "2ahw", "2nrb", "2nrc", "3cdk", "3dlx", "3k6m", "3oxo", "3rrl", "4kgb", "5dbn", "5mzw", "5mzx", "5mzy", "5mzz", "5n00", "5n01", "5n02", "5n03", "6co6", "6co9", "6coj", "6con", "6lp1"...

39

[ "PUB00002192", "PUB00002998", "PUB00019325", "PUB00031320", "PUB00032440", "PUB00035619", "PUB00035620", "PUB00093662" ]

[ "1624453", "9325289", "11749953", "15213226", "15823031", "11418570", "10849007", "28932214" ]

[ "Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida.", "Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family.", "A new family of CoA-transferases.", "K...

[ 1992, 1997, 2001, 2004, 2005, 2001, 2000, 2017 ]

8

[]

[ "IPR014388" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 391, 53246, 6371, 590 ]

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" ]

[ 1, 4, 4, 3, 10, 10, 2, 10 ]

8

true

Family

Coenzyme A transferase family I

CoA_trans_fam_I

8

IPR004166

4,166

Alpha-type protein kinase, alpha-kinase domain

a-kinase_dom

Domain

13,329

false

This entry represents a protein kinase catalytic domain with no detectable similarity to conventional kinases that is found in eukaryotic alpha-kinases [ ]. This domain is shared by EF-2 kinase and the myosin heavy chain kinase A (MHCK A) [ , ]. As in classical kinase, this domain consists of two lobes that bind nucleo...

[ "GO:0004674", "GO:0005524", "GO:0006468" ]

[ "protein serine/threonine kinase activity", "ATP binding", "protein phosphorylation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "PFAM", "PROFILE", "SMART" ]

[ "PF02816", "PS51158", "SM00811" ]

[ "Alpha_kinase", "ALPHA_KINASE", "Alpha_kinase" ]

[ 13163, 12715, 11212 ]

3

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.11", "PDOC51158", "R-CEL-166208", "R-DDI-166208", "R-HSA-166208", "R-HSA-3295583", "R-HSA-445989", "R-HSA-9645460", "R-MMU-166208", "R-MMU-3295583", "R-MMU-445989", "R-MMU-9645460", "R-RNO-166208", "R-RNO-3295583" ]

[ "EC:2.7.11", "PROSITEDOC:PDOC51158", "REACTOME:R-CEL-166208", "REACTOME:R-DDI-166208", "REACTOME:R-HSA-166208", "REACTOME:R-HSA-3295583", "REACTOME:R-HSA-445989", "REACTOME:R-HSA-9645460", "REACTOME:R-MMU-166208", "REACTOME:R-MMU-3295583", "REACTOME:R-MMU-445989", "REACTOME:R-MMU-9645460", "...

14

[ "1ia9", "1iah", "1iaj", "3lkm", "3lla", "3lmh", "3lmi", "3pdt", "4kuj", "4nl0", "4zme", "4zmf", "4zs4", "5dyj", "5e4h", "5e9e", "7shq", "8fny", "8fo6", "8gm4", "8gm5", "8zd3", "9j4p" ]

23

[ "PUB00007403", "PUB00007404", "PUB00007405", "PUB00033799" ]

[ "7822274", "9054368", "11161216", "15050379" ]

[ "Structural analysis of myosin heavy chain kinase A from Dictyostelium. Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the beta-subunit of heterotrimeric G proteins.", "Mapping of the novel protein kinase catalytic domain of Dictyostelium my...

[ 1995, 1997, 2001, 2004 ]

4

[]

[ "IPR029597", "IPR029601", "IPR047588" ]

0

3

0

[ "Bacteria", "Eukaryota", "Fadolivirus FV1/VV64", "Natrialbaceae" ]

[ 16, 13310, 1, 2 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]

[ 1, 48, 12, 16, 2, 28 ]

6

true

Domain

Alpha-type protein kinase, alpha-kinase domain

a-kinase_dom

8

IPR004167

4,167

Peripheral subunit-binding domain

PSBD

Domain

71,600

false

The ubiquitous 2-oxoacid dehydrogenases are a family of very large multienzyme complexes consisting of multiple copies of at least three enzymes which catalyze the oxidative decarboxylation of several different 2-oxoacids, resulting in acyl-CoA products. Members of this family include pyruvate dehydrogenase (PDH), 2-ox...

[ "GO:0016746" ]

[ "acyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE" ]

[ "PF02817", "PS51826" ]

[ "E3_binding", "PSBD" ]

[ 70654, 71003 ]

2

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "2.3.1", "GenProp1408", "R-BTA-204174", "R-BTA-5362517", "R-BTA-70895", "R-BTA-9013407", "R-BTA-9837999", "R-BTA-9857492", "R-BTA-9859138", "R-BTA-9861559", "R-CEL-204174", "R-CEL-5362517", "R-CEL-9013407", "R-CEL-9837999", "R-CEL-9857492", "R-CEL-9859138", "R-CEL-9861559", "R-DDI-...

[ "EC:2.3.1", "GP:GenProp1408", "REACTOME:R-BTA-204174", "REACTOME:R-BTA-5362517", "REACTOME:R-BTA-70895", "REACTOME:R-BTA-9013407", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9857492", "REACTOME:R-BTA-9859138", "REACTOME:R-BTA-9861559", "REACTOME:R-CEL-204174", "REACTOME:R-CEL-5362517", "REACT...

51

[ "1bal", "1bbl", "1ebd", "1w3d", "1w4e", "1w4f", "1w4g", "1w4h", "1w4i", "1w4j", "1w4k", "1w85", "1w88", "1zwv", "1zy8", "2btg", "2bth", "2coo", "2cyu", "2eq7", "2eq8", "2eq9", "2f5z", "2f60", "2pdd", "2pde", "2wxc", "3duf", "3dv0", "3dva", "3rnm", "4qoy"...

51

[ "PUB00019486", "PUB00021197", "PUB00040550", "PUB00043601", "PUB00087116" ]

[ "8805537", "1554728", "16442803", "10966480", "24077172" ]

[ "Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.", "Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxog...

[ 1996, 1992, 2006, 2000, 2013 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 574, 55515, 14675, 836 ]

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",...

[ 26, 2, 7, 1, 2, 25, 7, 3, 23, 12, 2, 2, 49 ]

13

true

Domain

Peripheral subunit-binding domain

PSBD

8

IPR004168

4,168

PPAK motif

PPAK_motif

Repeat

709

false

PPAK is a repeated protein motif found in the PEVK (Pro-Glu-Val-Lys) domain of the titin protein and in a number of other proteins. Titin ( ) is a giant elastic protein found in striated muscle that is a key component in the assembly and functioning of sarcomeres [ ]. PPAK motifs (PPAK refers to the four amino acids fo...

[]

0

[ "PFAM" ]

[ "PF02818" ]

[ "PPAK" ]

[ 709 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-114608", "R-HSA-390522" ]

[ "REACTOME:R-HSA-114608", "REACTOME:R-HSA-390522" ]

2

[]

0

[ "PUB00020167", "PUB00044085" ]

[ "11276084", "15507486" ]

[ "Identification of new repeating motifs in titin.", "Differential actin binding along the PEVK domain of skeletal muscle titin." ]

[ 2001, 2004 ]

2

[]

0

null

[ "Eukaryota" ]

[ 709 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 13, 14, 4 ]

3

true

Repeat

PPAK motif

PPAK_motif

6

IPR004169

4,169

Spider toxin

Spidertoxin

Family

561

false

This family contains spider toxins that include the omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta [ , ], as well as purotoxin-1 (PT1), a spider peptide venom of the Central Asian spider Geolycosa sp., which specifically exerts inhibitory action on P2X3 purino...

[ "GO:0008200", "GO:0005576" ]

[ "ion channel inhibitor activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM", "CDD" ]

[ "PF02819", "cd12960" ]

[ "Toxin_9", "Spider_toxin" ]

[ 408, 500 ]

2

[]

0

[ "1agg", "1iva", "1oav", "1oaw", "1oma", "1omb", "2kgu", "2ndb" ]

8

[ "PUB00021127", "PUB00037327", "PUB00057528", "PUB00082080" ]

[ "7703698", "8241166", "20437566", "8232218" ]

[ "The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta.", "Sequential assignment and structure determination of spider toxin omega-Aga-IVB.", "Novel peptide from spider venom inhibits P2X3 receptors and inflammatory pain.", "Struct...

[ 1995, 1993, 2010, 1993 ]

4

[]

0

null

[ "Eukaryota" ]

[ 561 ]

1

[]

0

true

Family

Spider toxin

Spidertoxin

6

IPR004170

4,170

WWE domain

WWE_dom

Domain

26,254

false

The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein-protein interactions in ubiquitin and ADP ribose conjugation systems. This domain is found as a tandem repeat at the N-terminal of Deltex, a cytosolic effector of Notch signalling thought to bind the N-terminal of...

[]

0

[ "PFAM", "PROFILE" ]

[ "PF02825", "PS50918" ]

[ "WWE", "WWE" ]

[ 22398, 25146 ]

2

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "2.3.2", "PDOC50918", "R-BTA-201681", "R-BTA-4641257", "R-BTA-5689880", "R-BTA-8948751", "R-BTA-983168", "R-DME-2122948", "R-DRE-8948751", "R-DRE-983168", "R-HSA-1483166", "R-HSA-1606341", "R-HSA-196807", "R-HSA-201681", "R-HSA-204005", "R-HSA-2122948", "R-HSA-3134975", "R-HSA-3270...

[ "EC:2.3.2", "PROSITEDOC:PDOC50918", "REACTOME:R-BTA-201681", "REACTOME:R-BTA-4641257", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-8948751", "REACTOME:R-BTA-983168", "REACTOME:R-DME-2122948", "REACTOME:R-DRE-8948751", "REACTOME:R-DRE-983168", "REACTOME:R-HSA-1483166", "REACTOME:R-HSA-1606341", ...

43

[ "1ujr", "1x4r", "2a90", "2dk6", "2rsf", "3v3l", "4qpl", "6miw", "6pfl", "7jq9", "7kzh", "7mop", "7mwd", "7mwe", "7mwf", "7sz2", "7sz3", "7tgq", "8r5n", "8r6a", "8r6b", "8r7o", "8rd0", "8rd1", "8rd7", "9bkr", "9bks", "9bnh", "9gkm", "9gkn", "9ken" ]

31

[ "PUB00018391", "PUB00039194" ]

[ "11343911", "16271883" ]

[ "The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation.", "Structure and Notch receptor binding of the tandem WWE domain of Deltex." ]

[ 2001, 2005 ]

2

[]

[ "IPR018123" ]

0

1

0

[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 63, 26152, 30, 9 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Zea mays" ]

[ 24, 4, 108, 28, 62, 33, 47, 1 ]

8

true

Domain

WWE domain

WWE_dom

9

IPR004171

4,171

cAMP-dependent protein kinase inhibitor

cAMP_dep_PKI

Family

3,445

false

Members of this family are extremely potent competitive inhibitors of cAMP-dependent protein kinase activity. These proteins interact with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.

[ "GO:0004862", "GO:0006469" ]

[ "cAMP-dependent protein kinase inhibitor activity", "negative regulation of protein kinase activity" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PIRSF", "PANTHER" ]

[ "PF02827", "PIRSF001667", "PTHR15416" ]

[ "PKI", "PKI", "" ]

[ 3443, 982, 3275 ]

3

[]

0

[ "1apm", "1atp", "1cdk", "1cmk", "1ctp", "1fmo", "1jbp", "1jlu", "1l3r", "1q24", "1q61", "1q62", "1q8t", "1q8u", "1q8w", "1rdq", "1smh", "1stc", "1sve", "1svg", "1svh", "1veb", "1xh4", "1xh5", "1xh6", "1xh7", "1xh8", "1xh9", "1xha", "1ydr", "1yds", "1ydt"...

264

[]

0

[]

0

null

[ "Eumetazoa" ]

[ 3445 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 7, 8, 12, 14 ]

5

true

Family

cAMP-dependent protein kinase inhibitor

cAMP_dep_PKI

9

IPR004172

4,172

L27 domain

L27_dom

Domain

27,584

false

The L27 domain is a ~50-amino acid module, initially identified in the Lin-2 and Lin-7 proteins, that exists in a large family of animal scaffold proteins [ ]. The L27 domain is a specific protein-protein interaction module capable of forming heteromeric complexes that can integrate multiple scaffold proteins into supr...

[ "GO:0005515" ]

[ "protein binding" ]

[ "molecular_function" ]

1

[ "PROFILE", "SMART" ]

[ "PS51022", "SM00569" ]

[ "L27", "L27" ]

[ 27450, 23456 ]

2

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC51022", "R-BTA-212676", "R-BTA-5666185", "R-BTA-9013149", "R-BTA-9013404", "R-BTA-9013406", "R-BTA-9013408", "R-BTA-9013423", "R-CEL-212676", "R-CEL-438066", "R-CEL-451308", "R-CEL-6794361", "R-CEL-8849932", "R-CFA-399719", "R-CFA-438066", "R-CFA-451308", "R-CFA-5673001", "R-C...

[ "PROSITEDOC:PDOC51022", "REACTOME:R-BTA-212676", "REACTOME:R-BTA-5666185", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013404", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013408", "REACTOME:R-BTA-9013423", "REACTOME:R-CEL-212676", "REACTOME:R-CEL-438066", "REACTOME:R-CEL-451308", "REACTOME:R-CE...

89

[ "1rso", "1vf6", "1y74", "1y76", "1zl8", "2r2v", "3lra", "3uit", "4rp3", "4rp4", "4rp5" ]

11

[ "PUB00018473", "PUB00018474", "PUB00018475" ]

[ "10871881", "15048107", "15241471" ]

[ "L27, a novel heterodimerization domain in receptor targeting proteins Lin-2 and Lin-7.", "The tetrameric L27 domain complex as an organization platform for supramolecular assemblies.", "Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes." ]

[ 2000, 2004, 2004 ]

3

[]

[ "IPR015132", "IPR015143" ]

0

2

0

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "ecological metagenomes" ]

[ 2, 90, 11, 27478, 3 ]

5

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Zea mays" ]

[ 5, 266, 41, 101, 53, 74, 7 ]

7

true

Domain

L27 domain

L27_dom

2

IPR004173

4,173

3H domain

3H_domain

Domain

3,359

false

The 3H domain is named after its three highly conserved histidine residues. The 3H domain appears to be a small molecule-binding domain, based on its occurrence with other domains [ ]. Several proteins carrying this domain are transcriptional regulators from the biotin repressor family. The transcription regulator TM16...

[ "GO:0036094" ]

[ "small molecule binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF02829" ]

[ "3H" ]

[ 3359 ]

1

[]

0

[ "1j5y", "7cv0", "7cv2", "9ebr" ]

4

[ "PUB00007364", "PUB00035679" ]

[ "11292341", "17256761" ]

[ "Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains.", "Crystal structure of a transcription regulator (TM1602) from Thermotoga maritima at 2.3 A resolution." ]

[ 2001, 2007 ]

2

[]

0

null

[ "Bacteria", "Methanomada group", "Trichuris trichiura", "unclassified Caudoviricetes", "unclassified sequences" ]

[ 3236, 92, 1, 2, 28 ]

5

[]

0

true

Domain

3H domain

3H_domain

5

IPR004174

4,174

Head-to-tail joining protein W

GpW

Family

1,035

false

GpW is a 68 residue protein known to be present in phage particles. Extracts of phage-infected cells lacking GpW contain DNA-filled heads, and active tails, but no infectious virions. GpW is required for the addition of GpFII to the head, which is, in turn, required for the attachment of tails. Since GpFII and tails ar...

[ "GO:0019058" ]

[ "viral life cycle" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF02831" ]

[ "gpW" ]

[ 1035 ]

1

[]

0

[ "1hyw", "2l6q", "2l6r", "8k38", "8vhx", "8xow", "8xpm", "8xqb" ]

8

[ "PUB00007406" ]

[ "11302702" ]

[ "The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria", "Caudoviricetes", "Durusdinium trenchii", "uncultured microorganism" ]

[ 939, 87, 5, 4 ]

4

[]

0

true

Family

Head-to-tail joining protein W

GpW

3

IPR004175

4,175

RNA 2',3'-cyclic phosphodiesterase

RNA_CPDase

Family

14,318

false

Members of this entry are bacterial and archaeal RNA cyclic phosphodiesterases (CPDases). They hydrolyse RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester [ ]. In vitro, they are able to ligate half-tRNA molecules [ ], though the RNA ligase activity appears to be weak in archaea [ ].

[ "GO:0004113", "GO:0008664" ]

[ "2',3'-cyclic-nucleotide 3'-phosphodiesterase activity", "RNA 2',3'-cyclic 3'-phosphodiesterase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_01940", "PTHR35561", "TIGR02258" ]

[ "RNA_CPDase", "", "2_5_ligase" ]

[ 13036, 14231, 13275 ]

3

[ "EC" ]

[ "3.1.4.58" ]

[ "EC:3.1.4.58" ]

1

[ "1iuh", "1vdx", "1vgj", "2fyh", "4qak", "5h7e", "5h7f", "5ldi", "5ldj", "5ldk", "5ldm", "5ldo", "5ldp", "5ldq" ]

14

[ "PUB00007407", "PUB00013642", "PUB00016758", "PUB00017746", "PUB00059633", "PUB00075358" ]

[ "11080166", "12466548", "8940112", "12798681", "19155324", "25239919" ]

[ "Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction.", "Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily.", "The 2'-5' RNA ligase of Escherichia coli. Purification, cl...

[ 2000, 2002, 1996, 2003, 2009, 2014 ]

6

[]

0

null

[ "Archaea", "Bacillus phage G", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 937, 1, 13086, 45, 249 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

RNA 2',3'-cyclic phosphodiesterase

RNA_CPDase

9

IPR004176

4,176

Clp, repeat (R) N-terminal domain

Clp_R_N

Domain

79,063

false

Molecular chaperones recognise unfolded or misfolded proteins by binding to hydrophobic surface patches not normally exposed in the native proteins. Members of the Clp/Hsp100 family of chaperones are present in eubacteria and within organelles of all eukaryotes, promoting disaggregation and disassembly of protein compl...

[]

0

[ "PFAM", "PROFILE" ]

[ "PF02861", "PS51903" ]

[ "Clp_N", "CLP_R" ]

[ 75539, 74550 ]

2

[]

0

[ "1k6k", "1khy", "1ksf", "1lzw", "1mbu", "1mbv", "1mbx", "1mg9", "1qvr", "1r6b", "1r6c", "1r6o", "1r6q", "2k77", "2y1q", "2y1r", "3fes", "3fh2", "3j3r", "3j3s", "3j3t", "3j3u", "3pxg", "3pxi", "3wdb", "3wdc", "3wdd", "3wde", "3zri", "3zrj", "4d2q", "4d2u"...

133

[ "PUB00028807", "PUB00030547", "PUB00048252", "PUB00094775", "PUB00094776", "PUB00094777", "PUB00094778", "PUB00106739" ]

[ "12205096", "15037248", "19361434", "25921872", "11344323", "28375147", "27317673", "19131969" ]

[ "Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.", "Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.", "Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.", "Structures, Fun...

[ 2002, 2004, 2009, 2015, 2001, 2017, 2016, 2009 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 49, 65252, 16, 12867, 879 ]

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" ]

[ 85, 2, 1, 37, 1, 1, 96 ]

7

true

Domain

Clp, repeat (R) N-terminal domain

Clp_R_N

3

IPR004177

4,177

DDHD domain

DDHD_dom

Domain

15,654

false

The Nir/rdgB (N-terminal domain-interacting receptor/Drosophila retinal degeneration B proteins) family has been identified in a variety of eukaryotic organisms, ranging from worms to mammals. Members of this family are implicated in regulation of lipid trafficking, metabolism, and signaling. The Nir/rdgB proteins cont...

[ "GO:0046872" ]

[ "metal ion binding" ]

[ "molecular_function" ]

1

[ "PFAM", "PROFILE", "SMART" ]

[ "PF02862", "PS51043", "SM01127" ]

[ "DDHD", "DDHD", "DDHD" ]

[ 15561, 15546, 15346 ]

3

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "PDOC51043", "R-DME-1483226", "R-HSA-1483166", "R-HSA-1483226", "R-HSA-204005", "R-MMU-1483166", "R-MMU-1483226", "R-MMU-204005", "R-RNO-1483226", "R-SCE-1483166", "R-SCE-1483226", "R-SCE-204005", "R-SPO-1483166", "R-SPO-1483226", "R-SPO-204005" ]

[ "PROSITEDOC:PDOC51043", "REACTOME:R-DME-1483226", "REACTOME:R-HSA-1483166", "REACTOME:R-HSA-1483226", "REACTOME:R-HSA-204005", "REACTOME:R-MMU-1483166", "REACTOME:R-MMU-1483226", "REACTOME:R-MMU-204005", "REACTOME:R-RNO-1483226", "REACTOME:R-SCE-1483166", "REACTOME:R-SCE-1483226", "REACTOME:R-...

15

[ "9c38", "9jyx" ]

2

[ "PUB00018498" ]

[ "15194420" ]

[ "The role of the Nir/rdgB protein family in membrane trafficking and cytoskeleton remodeling." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 3, 15651 ]

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...

[ 4, 2, 31, 12, 24, 26, 2, 2, 25, 1, 2, 27 ]

12

true

Domain

DDHD domain

DDHD_dom

3

IPR004178

4,178

Calmodulin-binding domain

CaM-bd_dom

Domain

6,214

false

Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM) [ ]. CaM binds to the SK channel through this the CaM-bi...

[ "GO:0005516", "GO:0015269", "GO:0006813", "GO:0016020" ]

[ "calmodulin binding", "calcium-activated potassium channel activity", "potassium ion transport", "membrane" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "PFAM", "SMART" ]

[ "PF02888", "SM01053" ]

[ "CaMBD", "CaMBD" ]

[ 6206, 6001 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-CEL-1296052", "R-DME-1296052", "R-HSA-1296052", "R-HSA-9667769", "R-MMU-1296052", "R-RNO-1296052", "R-SSC-1296052" ]

[ "REACTOME:R-CEL-1296052", "REACTOME:R-DME-1296052", "REACTOME:R-HSA-1296052", "REACTOME:R-HSA-9667769", "REACTOME:R-MMU-1296052", "REACTOME:R-RNO-1296052", "REACTOME:R-SSC-1296052" ]

7

[ "1g4y", "1kkd", "1qx7", "3sjq", "4g27", "4g28", "4j9y", "4j9z", "4qnh", "5v02", "5v03", "5wbx", "5wc5", "6ale", "6cnm", "6cnn", "6cno", "6czq", "8v2g", "8v2h", "8v3g", "9ed1", "9eio", "9o48", "9o51", "9o52", "9o53", "9o5o", "9o7s", "9o85", "9o93", "9oa8"...

34

[ "PUB00007409" ]

[ "11323678" ]

[ "Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin." ]

[ 2001 ]

1

[]

0

null

[ "Eukaryota" ]

[ 6214 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 20, 25, 9, 23, 13, 32 ]

6

true

Domain

Calmodulin-binding domain

CaM-bd_dom

4

IPR004179

4,179

Sec63 domain

Sec63-dom

Domain

20,712

false

This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons [ , ]. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative ...

[]

0

[ "PFAM", "SMART" ]

[ "PF02889", "SM00973" ]

[ "Sec63", "Sec63" ]

[ 20340, 19230 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-CEL-72163", "R-CEL-72165", "R-DDI-72163", "R-DME-72163", "R-DME-72165", "R-HSA-112126", "R-HSA-72163", "R-HSA-72165", "R-MMU-72163", "R-MMU-72165", "R-RNO-72163", "R-RNO-72165", "R-SPO-72163" ]

[ "REACTOME:R-CEL-72163", "REACTOME:R-CEL-72165", "REACTOME:R-DDI-72163", "REACTOME:R-DME-72163", "REACTOME:R-DME-72165", "REACTOME:R-HSA-112126", "REACTOME:R-HSA-72163", "REACTOME:R-HSA-72165", "REACTOME:R-MMU-72163", "REACTOME:R-MMU-72165", "REACTOME:R-RNO-72163", "REACTOME:R-RNO-72165", "RE...

13

[ "2q0z", "3hib", "3im1", "3im2", "3jcm", "3jcr", "4bgd", "4f91", "4f92", "4f93", "4kit", "5dca", "5gan", "5gao", "5gap", "5gm6", "5lj5", "5lqw", "5m52", "5m59", "5m5p", "5nrl", "5o9z", "5urj", "5urk", "5urm", "5xjc", "5yzg", "5z56", "5z57", "5z58", "5zwm"...

124

[ "PUB00018577", "PUB00044780" ]

[ "11023840", "16368690" ]

[ "Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction.", "The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons." ]

[ 2000, 2006 ]

2

[]

0

null

[ "Eukaryota", "Stenosarchaea group", "marine sediment metagenome" ]

[ 20372, 339, 1 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 35, 6, 29, 4, 26, 8, 4, 20, 16, 4, 3, 60 ]

12

true

Domain

Sec63 domain

Sec63-dom

4

IPR004180

4,180

Protein of unknown function DUF226, Borrelia species

DUF226_BOR_spp

Family

633

false

This family of proteins are found in Borrelia burgdorferi and Borrelia garinii. The proteins are about 190 amino acids long and have no known function.

[]

0

[ "PFAM" ]

[ "PF02890" ]

[ "DUF226" ]

[ 633 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Borreliaceae" ]

[ 633 ]

1

[]

0

true

Family

Protein of unknown function DUF226, Borrelia species

DUF226_BOR_spp

3

IPR004181

4,181

Zinc finger, MIZ-type

Znf_MIZ

Domain

22,157

false

This entry represents MIZ-type zinc finger domains. Miz1 (Msx-interacting-zinc finger) is a zinc finger-containing protein with homology to the yeast protein, Nfi-1. Miz1 is a sequence specific DNA binding protein that can function as a positive-acting transcription factor. Miz1 binds to the homeobox protein Msx2, enha...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "PFAM", "PFAM", "PROFILE", "CDD" ]

[ "PF02891", "PF11789", "PS51044", "cd16651" ]

[ "zf-MIZ", "zf-Nse", "ZF_SP_RING", "SPL-RING_NSE2" ]

[ 17239, 4281, 21142, 3923 ]

4

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "2.3.2.-", "PWY-6289", "PWY-6462", "PWY-6463", "PWY-6682", "PWY-6841", "PWY-7815", "PWY-7816", "PWY-7817", "PWY-7818", "PWY-7887", "PDOC51044", "R-CEL-3108214", "R-CEL-3232118", "R-CEL-3232142", "R-CEL-3899300", "R-CEL-4085377", "R-CEL-4090294", "R-CEL-4551638", "R-CEL-5696395"...

[ "EC:2.3.2.-", "METACYC:PWY-6289", "METACYC:PWY-6462", "METACYC:PWY-6463", "METACYC:PWY-6682", "METACYC:PWY-6841", "METACYC:PWY-7815", "METACYC:PWY-7816", "METACYC:PWY-7817", "METACYC:PWY-7818", "METACYC:PWY-7887", "PROSITEDOC:PDOC51044", "REACTOME:R-CEL-3108214", "REACTOME:R-CEL-3232118", ...

81

[ "2yu4", "3htk", "3i2d", "4fo9", "4mvt", "5jne", "6u75", "7p47", "7qcd", "7ylm", "7yqh", "8i13", "8i21", "8i4u", "8i4v", "8i4x", "8wjl", "8wjo" ]

18

[ "PUB00007410", "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "9256341", "12665246", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA.", "Zinc fingers--folds for many occasions.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting...

[ 1997, 2002, 2007, 2005, 2005, 1999, 2001 ]

7

[]

[ "IPR031141" ]

0

1

0

[ "Eukaryota", "Mimiviridae", "Pseudomonadati", "metagenomes" ]

[ 22143, 3, 5, 6 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 21, 2, 48, 49, 26, 17, 3, 7, 48, 3, 2, 78 ]

12

true

Domain

Zinc finger, MIZ-type

Znf_MIZ

7

IPR004182

4,182

GRAM domain

GRAM

Domain

47,947

false

The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. It is normally about 70 amino acids in length. It is thought to be an intracellular protein-binding or lipid-binding signalling domain, which has an important function in membrane-associated processes. The s...

[]

0

[ "PFAM", "SMART" ]

[ "PF02893", "SM00568" ]

[ "GRAM", "GRAM" ]

[ 47187, 42338 ]

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-1483248", "R-BTA-1660499", "R-BTA-1660516", "R-BTA-1660517", "R-CEL-1483248", "R-CEL-1660499", "R-CEL-1660516", "R-CEL-1660517", "R-CEL-8876198", "R-CEL-9035034", "R-DRE-1660516", "R-DRE-1660517", "R-GGA-1483248", "R-GGA-1660516", "R-GGA-1660517", "R-HSA-1483248", "R-HSA-16604...

[ "REACTOME:R-BTA-1483248", "REACTOME:R-BTA-1660499", "REACTOME:R-BTA-1660516", "REACTOME:R-BTA-1660517", "REACTOME:R-CEL-1483248", "REACTOME:R-CEL-1660499", "REACTOME:R-CEL-1660516", "REACTOME:R-CEL-1660517", "REACTOME:R-CEL-8876198", "REACTOME:R-CEL-9035034", "REACTOME:R-DRE-1660516", "REACTOM...

37

[ "1lw3", "1m7r", "1zsq", "1zvr", "4tyz", "5c16", "5gnh", "5yqr", "8ujw" ]

9

[ "PUB00019649", "PUB00022130" ]

[ "11050430", "14690594" ]

[ "GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins.", "Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome." ]

[ 2000, 2003 ]

2

[]

[ "IPR036009", "IPR036012", "IPR036014", "IPR036015", "IPR036016", "IPR036017", "IPR037823", "IPR037845", "IPR037857", "IPR048065", "IPR048066" ]

0

11

0

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 4, 234, 47700, 9 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 61, 13, 190, 18, 117, 60, 3, 53, 100, 6, 2, 129 ]

12

true

Domain

GRAM domain

GRAM

8