LiteFold/InterPro · Datasets at Hugging Face

IPR015079

15,079

Protein of unknown function DUF1889

DUF1889

Family

701

false

This family consist of hypothetical bacterial proteins.

[]

0

[ "PFAM" ]

[ "PF08986" ]

[ "DUF1889" ]

[ 701 ]

1

[]

0

[ "2es9", "2jn8" ]

2

[]

0

[]

0

null

[ "Bacteria", "Halobacteriales", "Peduovirinae sp. ctySy20", "metagenomes" ]

[ 689, 7, 1, 4 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Protein of unknown function DUF1889

DUF1889

5

IPR015080

15,080

Protein of unknown function DUF1892

DUF1892

Family

142

false

Proteins in this entry, which are synthesised by Saccharomycetes, adopt a structure consisting of a four-stranded β-sheet, with strand order beta2-beta1-beta4-beta3, and two α-helices, with an overall topology of β-β-α-β-β-α. They have no known function [ ].

[]

0

[ "PFAM" ]

[ "PF08987" ]

[ "DUF1892" ]

[ 142 ]

1

[]

0

[ "1n6z" ]

1

[ "PUB00029007" ]

[ "12717036" ]

[ "A novel member of the split betaalphabeta fold: Solution structure of the hypothetical protein YML108W from Saccharomyces cerevisiae." ]

[ 2003 ]

1

[]

0

null

[ "Dikarya" ]

[ 142 ]

1

[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1 ]

1

true

Family

Protein of unknown function DUF1892

DUF1892

1

IPR015082

15,082

Protein of unknown function DUF1896

DUF1896

Family

1,431

false

This domain is found in a set of hypothetical bacterial proteins.

[]

0

[ "PFAM" ]

[ "PF08989" ]

[ "DUF1896" ]

[ 1431 ]

1

[]

0

[ "2apl" ]

1

[]

0

[]

0

null

[ "Bacteria", "unclassified sequences" ]

[ 1390, 41 ]

2

[]

0

true

Family

Protein of unknown function DUF1896

DUF1896

9

IPR015083

15,083

Polyketide synthase NorB/C/GfsB-E-like, docking domain

NorB/c/GfsB-D-like_docking

Domain

8,367

false

This entry represents the N-terminal docking domain found in modular polyketide synthases, such as Spectinabilin polyketide synthase system protein NorB/C [ ] and polyketide synthase GfsB-D [ ] and related sequences from actinomycetes, which assumes an α-helical structure, wherein two α-helices are connected by a short...

[ "GO:0016740" ]

[ "transferase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF08990" ]

[ "Docking" ]

[ 8367 ]

1

[ "EC" ]

[ "2.3.1" ]

[ "EC:2.3.1" ]

1

[ "1pzr", "2hg4", "3f5h", "6c9u", "7m7e", "7m7f", "7m7g", "7m7h", "7m7i", "7m7j", "7s6b", "7s6c", "7s6d", "7wvz", "8ee0", "8ee1", "8i4y", "8i4z", "8tjn", "8tjo", "8tjp", "8tko", "8tpw", "8tpx", "9pat", "9pav", "9pc6" ]

27

[ "PUB00030060", "PUB00154686", "PUB00158945" ]

[ "12954331", "17763486", "20589823" ]

[ "The structure of docking domains in modular polyketide synthases.", "Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective.", "Cloning and characterization of the biosynthetic gene cluster of 16-membered macrolide antibiotic FD-891: involvement of a dual f...

[ 2003, 2007, 2010 ]

3

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 8363, 4 ]

2

[]

0

true

Domain

Polyketide synthase NorB/C/GfsB-E-like, docking domain

NorB/c/GfsB-D-like_docking

1

IPR015084

15,084

Quinohemoprotein amine dehydrogenase, gamma subunit, structural domain

QH-AmDH_gsu_dom

Domain

472

false

Quinohemoprotein amine dehydrogenases (QHNDH) ) are enzymes produced in the periplasmic space of certain Gram-negative bacteria, such as Paracoccus denitrificans and Pseudomonas putida, in response to primary amines, including n-butylamine and benzylamine. QHNDH catalyses the oxidative deamination of a wide range of al...

[ "GO:0016638" ]

[ "oxidoreductase activity, acting on the CH-NH2 group of donors" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF08992" ]

[ "QH-AmDH_gamma" ]

[ 472 ]

1

[ "GP" ]

[ "GenProp0902" ]

[ "GP:GenProp0902" ]

1

[ "1jju", "1jmx", "1jmz", "1pby" ]

4

[ "PUB00013277", "PUB00022422", "PUB00035735", "PUB00035736", "PUB00035737" ]

[ "11704672", "12925784", "15234267", "12974623", "12427036" ]

[ "Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges.", "Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution.", ...

[ 2002, 2003, 2004, 2003, 2002 ]

5

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 461, 11 ]

2

[]

0

true

Domain

Quinohemoprotein amine dehydrogenase, gamma subunit, structural domain

QH-AmDH_gsu_dom

4

IPR015085

15,085

Bacteriophage T4, Gp59, helicase assembly protein, N-terminal

Phage_T4_Gp59_N

Domain

468

false

The structure of Gp59 helicase assembly protein reveals a novel α-helical bundle fold with two domains of similar size. Surface residues are predominantly basic (pI 9.37) with clusters of acidic residues but exposed hydrophobic residues suggest sites for potential contact with DNA and with other protein molecules [ ]. ...

[]

0

[ "PFAM" ]

[ "PF08993" ]

[ "T4_Gp59_N" ]

[ 468 ]

1

[]

0

[ "1c1k" ]

1

[ "PUB00010626", "PUB00097909" ]

[ "10669611", "22427673" ]

[ "Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical two-domain fold.", "Mutational analysis of the T4 gp59 helicase loader reveals its sites for interaction with helicase, single-stranded binding protein, and DNA." ]

[ 2000, 2012 ]

2

[]

0

null

[ "Flagellimonas marina", "Viruses", "metagenomes" ]

[ 1, 445, 22 ]

3

[]

0

true

Domain

Bacteriophage T4, Gp59, helicase assembly protein, N-terminal

Phage_T4_Gp59_N

7

IPR015086

15,086

Bacteriophage T4, Gp59, helicase assembly protein, C-terminal

Phage_T4_Gp59_C

Domain

411

false

The Bacteriophage T4 gene 59 helicase assembly protein (Gp59) is required for recombination-dependent DNA replication and repair, which is the predominant mode of DNA replication in the late stage of T4 infection. Gp59 accelerates the loading of the T4 gene 41 helicase during DNA synthesis by the T4 replication system ...

[]

0

[ "PFAM" ]

[ "PF08994" ]

[ "T4_Gp59_C" ]

[ 411 ]

1

[]

0

[ "1c1k" ]

1

[ "PUB00010626", "PUB00097909" ]

[ "10669611", "22427673" ]

[ "Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical two-domain fold.", "Mutational analysis of the T4 gp59 helicase loader reveals its sites for interaction with helicase, single-stranded binding protein, and DNA." ]

[ 2000, 2012 ]

2

[]

0

null

[ "Flagellimonas marina", "Viruses", "metagenomes" ]

[ 1, 393, 17 ]

3

[]

0

true

Domain

Bacteriophage T4, Gp59, helicase assembly protein, C-terminal

Phage_T4_Gp59_C

6

IPR015087

15,087

Necrosis inducing protein-1

NIP1

Family

38

false

Necrosis inducing protein-1 (NIP1) is a small phytotoxic protein secreted by the barley pathogen Rhynchosporium secalisconsists. It is a fungal avirulence protein on host plants of the Rrs1 resistance genotype [ ]. NIP1 consists of two parts containing β-sheets of two and three anti-parallel strands, respectively. Five...

[]

0

[ "PFAM" ]

[ "PF08995" ]

[ "NIP_1" ]

[ 38 ]

1

[]

0

[ "1kg1" ]

1

[ "PUB00028828", "PUB00069139" ]

[ "12944393", "7556057" ]

[ "Solution structure of the plant disease resistance-triggering protein NIP1 from the fungus Rhynchosporium secalis shows a novel beta-sheet fold.", "The race-specific elicitor, NIP1, from the barley pathogen, Rhynchosporium secalis, determines avirulence on host plants of the Rrs1 resistance genotype." ]

[ 2003, 1995 ]

2

[]

0

null

[ "Rhynchosporium" ]

[ 38 ]

1

[]

0

true

Family

Necrosis inducing protein-1

NIP1

3

IPR015088

15,088

Zinc finger, DNA-directed DNA polymerase, family B, alpha

Znf_DNA-dir_DNA_pol_B_alpha

Domain

4,697

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:0003887", "GO:0006260" ]

[ "DNA-directed DNA polymerase activity", "DNA replication" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF08996" ]

[ "zf-DNA_Pol" ]

[ 4697 ]

1

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

[ "2.7.7.7", "R-DDI-113501", "R-DDI-68952", "R-DDI-68962", "R-DDI-69091", "R-DDI-69166", "R-DDI-69183", "R-DME-113501", "R-DME-68952", "R-DME-68962", "R-DME-69091", "R-DME-69166", "R-DME-69183", "R-HSA-113501", "R-HSA-174411", "R-HSA-174430", "R-HSA-68952", "R-HSA-68962", "R-HSA-69...

[ "EC:2.7.7.7", "REACTOME:R-DDI-113501", "REACTOME:R-DDI-68952", "REACTOME:R-DDI-68962", "REACTOME:R-DDI-69091", "REACTOME:R-DDI-69166", "REACTOME:R-DDI-69183", "REACTOME:R-DME-113501", "REACTOME:R-DME-68952", "REACTOME:R-DME-68962", "REACTOME:R-DME-69091", "REACTOME:R-DME-69166", "REACTOME:R-...

51

[ "1n5g", "3flo", "4y97", "5exr", "7opl", "7u5c", "8b9a", "8b9b", "8b9c", "8b9d", "8d0b", "8d0k", "8d96", "8d9d", "8foc", "8fod", "8foe", "8foh", "8foj", "8fok", "8g99", "8g9f", "8g9l", "8g9n", "8g9o", "8qj7", "8ucu", "8ucv", "8ucw", "8v5m", "8v5n", "8v5o"...

38

[ "PUB00014077", "PUB00028785", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812", "PUB00052915", "PUB00097438" ]

[ "12665246", "14499601", "17210253", "15963892", "15718139", "10529348", "11179890", "19494830", "28747437" ]

[ "Zinc fingers--folds for many occasions.", "Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on R...

[ 2002, 2003, 2007, 2005, 2005, 1999, 2001, 2009, 2017 ]

9

[]

0

null

[ "Candidatus Nitrosopumilus koreensis AR1", "Eukaryota", "Pectobacterium polaris" ]

[ 1, 4695, 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...

[ 4, 2, 1, 1, 2, 1, 1, 3, 7, 1, 1, 9 ]

12

true

Domain

Zinc finger, DNA-directed DNA polymerase, family B, alpha

Znf_DNA-dir_DNA_pol_B_alpha

5

IPR015089

15,089

Cytochrome b-c1 complex subunit 10

UQCR

Family

1,057

false

The ubiquinol-cytochrome C reductase complex (cytochrome bc1 complex) is an essential component of the mitochondrial cellular respiratory chain. This family represents the 6.4kDa protein, which may be closely linked to the iron-sulphur protein in the complex and function as an iron-sulphur protein-binding factor [ ].

[ "GO:0006122" ]

[ "mitochondrial electron transport, ubiquinol to cytochrome c" ]

[ "biological_process" ]

1

[ "PFAM", "PANTHER" ]

[ "PF08997", "PTHR15420" ]

[ "UCR_6-4kD", "" ]

[ 1051, 922 ]

2

[ "REACTOME", "REACTOME" ]

[ "R-HSA-611105", "R-HSA-9865881" ]

[ "REACTOME:R-HSA-611105", "REACTOME:R-HSA-9865881" ]

2

[ "1be3", "1bgy", "1l0l", "1l0n", "1ntk", "1ntm", "1ntz", "1nu1", "1qcr", "1sqb", "1sqp", "1sqq", "1sqv", "1sqx", "2fyu", "2ybb", "5gpn", "5gup", "5j4z", "5j7y", "5j8k", "5klv", "5luf", "5nmi", "5xte", "5xth", "5xti", "6nhg", "7dgq", "7dgr", "7dgs", "7dkf"...

75

[ "PUB00031170" ]

[ "15312779" ]

[ "Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex." ]

[ 2004 ]

1

[]

0

null

[ "Eukaryota" ]

[ 1057 ]

1

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

[ 1, 1, 2, 1, 2, 4 ]

6

true

Family

Cytochrome b-c1 complex subunit 10

UQCR

2

IPR015090

15,090

Antitoxin epsilon/PezA domain

Epsilon_PezA_dom

Domain

522

false

The epsilon antitoxin, produced by various prokaryotes, forms part of a post-segregational killing system, which is involved in the initiation of programmed cell death of plasmid-free cells. The protein is folded into a three-helix bundle directly interacting with the zeta toxin, inactivating it [ ]. PezA is the cognat...

[ "GO:0015643", "GO:0009636", "GO:0031342" ]

[ "toxic substance binding", "response to toxic substance", "negative regulation of cell killing" ]

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

3

[ "PFAM" ]

[ "PF08998" ]

[ "Epsilon_antitox" ]

[ 522 ]

1

[]

0

[ "1gvn", "2p5t", "3q8x" ]

3

[ "PUB00012377", "PUB00048622" ]

[ "12571357", "17488720" ]

[ "Crystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formation.", "Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae." ]

[ 2003, 2007 ]

2

[]

0

null

[ "Bacteria", "bioreactor metagenome", "plasmids" ]

[ 519, 1, 2 ]

3

[]

0

true

Domain

Antitoxin epsilon/PezA domain

Epsilon_PezA_dom

8

IPR015091

15,091

Surfactant protein C, N-terminal propeptide

Surfactant_protein_propep

Domain

807

false

The N-terminal propeptide of surfactant protein C adopts an α-helical structure, with turn and extended regions. Its main function is the stabilisation of metastable surfactant protein C (SP-C), since the latter can irreversibly transform from its native α-helical structure to β-sheet aggregates and form amyloid-like f...

[]

0

[ "PFAM" ]

[ "PF08999" ]

[ "SP_C-Propep" ]

[ 807 ]

1

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

[ "R-HSA-5683826", "R-HSA-5688354", "R-HSA-5688849", "R-HSA-5688890", "R-MMU-5683826", "R-RNO-5683826" ]

[ "REACTOME:R-HSA-5683826", "REACTOME:R-HSA-5688354", "REACTOME:R-HSA-5688849", "REACTOME:R-HSA-5688890", "REACTOME:R-MMU-5683826", "REACTOME:R-RNO-5683826" ]

6

[ "1spf", "2esy", "2yad" ]

3

[ "PUB00035469" ]

[ "16478467" ]

[ "Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C." ]

[ 2006 ]

1

[]

0

null

[ "Bilateria", "Blautia hansenii", "bird metagenome" ]

[ 805, 1, 1 ]

3

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

[ 8, 2, 4 ]

3

true

Domain

Surfactant protein C, N-terminal propeptide

Surfactant_protein_propep

2

IPR015093

15,093

Card1, endonuclease domain

Card1_endonucl_dom

Domain

929

false

This entry represents the endonuclease domain found in a set of proteins mainly found in bacteria, including Card1 (cyclic-oligoadenylate-activated single-stranded ribonuclease and single-stranded deoxyribonuclease 1) from Treponema succinifaciens ( ), a protein that is part of type III CRISPR-Cas immune response syste...

[]

0

[ "PFAM" ]

[ "PF09002" ]

[ "Card1_endonuc" ]

[ 929 ]

1

[]

0

[ "1xmx", "6wxw", "6wxx", "6wxy", "6xl1", "7bdv" ]

6

[ "PUB00153094" ]

[ "33461211" ]

[ "The Card1 nuclease provides defence during type III CRISPR immunity." ]

[ 2021 ]

1

[]

0

null

[ "Bacteria", "Methanobacteriota", "unclassified sequences" ]

[ 907, 3, 19 ]

3

[]

0

true

Domain

Card1, endonuclease domain

Card1_endonucl_dom

8

IPR015094

15,094

Integrase, lambda-type, N-terminal DNA-binding

Integrase_lambda-typ_DNA-bd_N

Domain

2,146

false

The amino terminal domain of bacteriophage lambda integrase folds into a three-stranded, antiparallel β-sheet that packs against a C-terminal α-helix, adopting a fold that is structurally related to the three-stranded β-sheet family of DNA-binding domains (which includes the GCC-box DNA-binding domain and the N-termina...

[ "GO:0003677", "GO:0008907", "GO:0015074" ]

[ "DNA binding", "integrase activity", "DNA integration" ]

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

3

[ "PFAM" ]

[ "PF09003" ]

[ "Arm-DNA-bind_1" ]

[ 2146 ]

1

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

[ "2.7.7.-", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179" ]

[ "EC:2.7.7.-", "METACYC:PWY-6322", "METACYC:PWY-6626", "METACYC:PWY-6749", "METACYC:PWY-6955", "METACYC:PWY-6998", "METACYC:PWY-7127", "METACYC:PWY-7419", "METACYC:PWY-7529", "METACYC:PWY-7706", "METACYC:PWY-7719", "METACYC:PWY-7735", "METACYC:PWY-7737", "METACYC:PWY-7769", "METACYC:PWY-7...

18

[ "1kjk", "1z1b", "1z1g", "2wcc", "5j0n" ]

5

[ "PUB00028838" ]

[ "11904406" ]

[ "Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "Caudoviricetes", "Eukaryota", "hydrothermal vent metagenome" ]

[ 2107, 31, 4, 4 ]

4

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

[ 1, 1 ]

2

true

Domain

Integrase, lambda-type, N-terminal DNA-binding

Integrase_lambda-typ_DNA-bd_N

7

IPR015095

15,095

Alkylated DNA repair protein AlkB, homologue 8, N-terminal

AlkB_hom8_N

Domain

8,285

false

This domain is found at the extreme N terminus of eukaryotic alkylated DNA repair protein homologues.

[ "GO:0008168", "GO:0016706" ]

[ "methyltransferase activity", "2-oxoglutarate-dependent dioxygenase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF09004" ]

[ "ALKBH8_N" ]

[ 8285 ]

1

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

[ "2.1.1.229", "PWY-6829", "PWY-7888", "R-HSA-6782315" ]

[ "EC:2.1.1.229", "METACYC:PWY-6829", "METACYC:PWY-7888", "REACTOME:R-HSA-6782315" ]

4

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eumetazoa" ]

[ 5, 8280 ]

2

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

[ 3, 2, 5, 4 ]

4

true

Domain

Alkylated DNA repair protein AlkB, homologue 8, N-terminal

AlkB_hom8_N

9

IPR015096

15,096

Far upstream element-binding protein, C-terminal

FUBP_C

Domain

5,064

false

This entry represents the transactivation domain found in the C-terminal of Far upstream element-binding protein 1/2 (FUBP1/2) [ , ]. FUBP1 regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter [ , ]. FUBP2, also known as KSRP (K homology-type splicing regulat...

[ "GO:0003676", "GO:0006355" ]

[ "nucleic acid binding", "regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09005" ]

[ "FUBP_C" ]

[ 5064 ]

1

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

[ "R-HSA-380994", "R-HSA-450604", "R-MMU-450604", "R-RNO-450604" ]

[ "REACTOME:R-HSA-380994", "REACTOME:R-HSA-450604", "REACTOME:R-MMU-450604", "REACTOME:R-RNO-450604" ]

4

[ "2bn5", "2bn6" ]

2

[ "PUB00084321", "PUB00084322", "PUB00084323", "PUB00084324", "PUB00153366" ]

[ "8940189", "8125259", "28076379", "24845017", "32778776" ]

[ "The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators.", "A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif.", "Upregulation of Far Upstream Element-Binding Protein 1 (FU...

[ 1996, 1994, 2017, 2014, 2020 ]

5

[]

0

null

[ "Eukaryota", "Lachnospiraceae", "Siphoviridae sp. ctUGR26" ]

[ 5060, 3, 1 ]

3

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

[ 7, 13, 15, 17, 13, 20 ]

6

true

Domain

Far upstream element-binding protein, C-terminal

FUBP_C

1

IPR015097

15,097

Lung surfactant protein D coiled-coil trimerisation

Surfac_D-trimer

Domain

477

false

This domain is found in the SFTPD family, which includes lung surfactant protein D (SFTPD), conglutinin, collectin-43 and collectin-46. It forms a triple-helical parallel coiled coil, and mediates trimerisation of the protein [ ].

[]

0

[ "PFAM" ]

[ "PF09006" ]

[ "Surfac_D-trimer" ]

[ 477 ]

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-166016", "R-BTA-198933", "R-BTA-391160", "R-BTA-5683826", "R-BTA-5686938", "R-HSA-166016", "R-HSA-168179", "R-HSA-198933", "R-HSA-391160", "R-HSA-5683826", "R-HSA-5686938", "R-HSA-5688849", "R-HSA-5688890", "R-HSA-9692916", "R-HSA-9705671", "R-MMU-166016", "R-MMU-198933", "R...

[ "REACTOME:R-BTA-166016", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-391160", "REACTOME:R-BTA-5683826", "REACTOME:R-BTA-5686938", "REACTOME:R-HSA-166016", "REACTOME:R-HSA-168179", "REACTOME:R-HSA-198933", "REACTOME:R-HSA-391160", "REACTOME:R-HSA-5683826", "REACTOME:R-HSA-5686938", "REACTOME:R-HSA...

30

[ "1b08", "1m7l", "1pw9", "1pwb", "2ggu", "2ggx", "2orj", "2ork", "2os9", "2ria", "2rib", "2ric", "2rid", "2rie", "3dbz", "3g81", "3g83", "3g84", "3ikn", "3ikp", "3ikq", "3ikr", "4dn8", "4e52", "4m17", "4m18", "5oxr", "5oxs", "6bbd", "6bbe", "6ryg", "6ryj"...

34

[ "PUB00028933" ]

[ "12495025" ]

[ "Solution structure of the coiled-coil trimerization domain from lung surfactant protein D." ]

[ 2002 ]

1

[]

0

null

[ "Tetrapoda" ]

[ 477 ]

1

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

[ 1, 1, 6 ]

3

true

Domain

Lung surfactant protein D coiled-coil trimerisation

Surfac_D-trimer

5

IPR015098

15,098

EBP50, C-terminal

EBP50_C

Domain

2,467

false

This entry represents the C-terminal domain of EBP50 and similar proteins from vertebrates. This region comprises a mostly disordered region and the EBD. Association of Ezrin allows interaction of EBP50 with FERM (four-point one ERM) domains, resulting in the activation of Ezrin-radixin-moesin (ERM), with subsequent cy...

[]

0

[ "PFAM" ]

[ "PF09007" ]

[ "EBP50_C" ]

[ 2467 ]

1

[]

0

[ "1sgh", "2d10", "2d11", "2kjd", "2krg", "2m0v", "6rqr" ]

7

[ "PUB00031051", "PUB00075053", "PUB00103873" ]

[ "15020681", "23200831", "23583913" ]

[ "The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain.", "Modulatory roles of NHERF1 and NHERF2 in cell surface expression of the glutamate transporter GLAST.", "Ligand-induced dynamic changes in extended PDZ domains from NHERF1." ]

[ 2004, 2013, 2013 ]

3

[]

0

null

[ "Chordata" ]

[ 2467 ]

1

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

[ 6, 9, 8, 9 ]

4

true

Domain

EBP50, C-terminal

EBP50_C

6

IPR015099

15,099

Exotoxin A catalytic domain

Exotox-A_cataly_dom

Domain

141

false

Prokaryotic exotoxin A catalyses the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis [ ].

[ "GO:0047286" ]

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

[ "molecular_function" ]

1

[ "PFAM", "CDD" ]

[ "PF09009", "cd01436" ]

[ "Exotox-A_cataly", "Dipth_tox_like" ]

[ 140, 119 ]

2

[]

0

[ "1aer", "1dma", "1ikp", "1ikq", "1xk9", "1zm2", "1zm3", "1zm4", "1zm9", "2q5t", "2q6m", "2zit", "3b78", "3b82", "3b8h", "3ess", "3ki0", "3ki1", "3ki2", "3ki3", "3ki4", "3ki5", "3ki6", "3ki7", "3ny6", "3q9o", "6edg", "6z5h", "9g7m", "9g7n", "9g7o", "9g7p"...

32

[ "PUB00035394" ]

[ "8692916" ]

[ "Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation." ]

[ 1996 ]

1

[]

0

null

[ "Bacteria", "Opisthokonta" ]

[ 125, 16 ]

2

[]

0

true

Domain

Exotoxin A catalytic domain

Exotox-A_cataly_dom

9

IPR015100

15,100

Anti-Sigma Factor A

AsiA

Family

282

false

Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. It is an all-helical protein, composed of six helical segments and intervening loops and turns, as well as a helix-turn-helix DNA binding motif, altho...

[ "GO:0006355" ]

[ "regulation of DNA-templated transcription" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF09010" ]

[ "AsiA" ]

[ 282 ]

1

[]

0

[ "1jr5", "1tkv", "1tl6", "1tlh", "6k4y" ]

5

[ "PUB00028758" ]

[ "11830637" ]

[ "Solution structure and stability of the anti-sigma factor AsiA: implications for novel functions." ]

[ 2002 ]

1

[]

0

null

[ "Viruses" ]

[ 282 ]

1

[]

0

true

Family

Anti-Sigma Factor A

AsiA

9

IPR015103

15,103

Protein-tyrosine phosphatase, YopH, N-terminal

ProtTyrPase_YopH_N

Domain

49

false

This entry represents the N-terminal domain of YopH protein tyrosine phosphatase (PTP). This domain has a compact structure composed of four α-helices and two β-hairpins. Helices alpha-1 and alpha-3 are parallel to each other and antiparallel to helices alpha-2 and alpha-4. This domain targets YopH for secretion from t...

[ "GO:0004725", "GO:0006470" ]

[ "protein tyrosine phosphatase activity", "protein dephosphorylation" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09013" ]

[ "YopH_N" ]

[ 49 ]

1

[]

0

[ "1huf", "1k46", "1m0v", "1ttw", "4gf3" ]

5

[ "PUB00020581", "PUB00028634", "PUB00035656" ]

[ "1860816", "11375498", "17352459" ]

[ "Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica.", "Structure of the N-terminal domain of Yersinia pestis YopH at 2.0 A resolution.", "Loop dynamics and ligand binding kinetics in the reaction catalyzed by the Yersinia protein tyrosine phosphatase." ]

[ 1991, 2001, 2007 ]

3

[]

0

null

[ "Gammaproteobacteria" ]

[ 49 ]

1

[]

0

true

Domain

Protein-tyrosine phosphatase, YopH, N-terminal

ProtTyrPase_YopH_N

5

IPR015104

15,104

Beta-2-glycoprotein-1 fifth domain

Sushi_2

Domain

1,310

false

The fifth domain of beta-2-glycoprotein-1 (b2GP-1) is composed of four well-defined anti-parallel β-strands and two short α-helices, as well as a long highly flexible loop. It plays an important role in the binding of b2GP-1 to negatively charged compounds and subsequent capture for binding of anti-b2GP-1 antibodies [ ...

[]

0

[ "PFAM" ]

[ "PF09014" ]

[ "Sushi_2" ]

[ 1310 ]

1

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

[ "R-CFA-114608", "R-HSA-114608", "R-MMU-114608", "R-RNO-114608" ]

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

4

[ "1c1z", "1g4f", "1g4g", "1qub", "2kri", "3op8", "4jhs", "6v06", "6v08", "6v09", "6xsd", "6xst", "7jik", "7kg4" ]

14

[ "PUB00021645" ]

[ "11124037" ]

[ "Identification of the phospholipid-binding site of human beta(2)-glycoprotein I domain V by heteronuclear magnetic resonance." ]

[ 2000 ]

1

[]

0

null

[ "Bilateria" ]

[ 1310 ]

1

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

[ 1, 4, 3, 4 ]

4

true

Domain

Beta-2-glycoprotein-1 fifth domain

Sushi_2

8

IPR015105

15,105

Type-2 restriction enzyme NgoMIV

NgoMIV

Family

328

false

There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi...

[ "GO:0009036", "GO:0009307" ]

[ "type II site-specific deoxyribonuclease activity", "DNA restriction-modification system" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09015" ]

[ "NgoMIV_restric" ]

[ 328 ]

1

[]

0

[ "1fiu", "4abt" ]

2

[ "PUB00035426", "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707" ]

[ "10966652", "15770420", "14576294", "11827971", "11557805", "15121719", "12665693" ]

[ "Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA.", "Type II restriction endonucleases: structure and mechanism.", "Diversity of type II restriction endonucleases that require two DNA recognition sites.", "Evolutionary relationship between different subgroups of restric...

[ 2000, 2005, 2003, 2002, 2001, 2004, 2003 ]

7

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 323, 5 ]

2

[]

0

true

Family

Type-2 restriction enzyme NgoMIV

NgoMIV

1

IPR015106

15,106

Pas factor saposin domain

Pas_Saposin

Domain

150

false

Members of this entry adopt a compact structure comprising five α helices. Charged and polar residues are exposed mostly on the surface, while most of the hydrophobic residues are buried inside the hydrophobic core of the helical bundle. The precise function of this domain is unknown, but it is has been shown to induce...

[]

0

[ "PFAM" ]

[ "PF09016" ]

[ "Pas_Saposin" ]

[ 150 ]

1

[]

0

[ "2b8i" ]

1

[ "PUB00035444" ]

[ "16318855" ]

[ "Crystal structure and functional studies reveal that PAS factor from Vibrio vulnificus is a novel member of the saposin-fold family." ]

[ 2006 ]

1

[]

0

null

[ "Bacteria" ]

[ 150 ]

1

[]

0

true

Domain

Pas factor saposin domain

Pas_Saposin

8

IPR015107

15,107

Protein-glutamine gamma-glutamyltransferase

Transglut_prok

Family

96

false

Protein-glutamine gamma-glutamyltransferase (also known as microbial transglutaminase, MTG) catalyses an acyl transfer reaction by means of a Cys-Asp diad mechanism, in which the gamma-carboxyamide groups of peptide-bound glutamine residues act as the acyl donors. The MTG molecule forms a single, compact domain belongi...

[ "GO:0003810" ]

[ "protein-glutamine gamma-glutamyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PIRSF" ]

[ "PF09017", "PIRSF037210" ]

[ "Transglut_prok", "Transglut_prok" ]

[ 96, 69 ]

2

[]

0

[ "1iu4", "3iu0", "5m6q", "6gmg", "9ihs" ]

5

[ "PUB00028702" ]

[ "12221081" ]

[ "Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria" ]

[ 96 ]

1

[]

0

true

Family

Protein-glutamine gamma-glutamyltransferase

Transglut_prok

7

IPR015108

15,108

P3, N-terminal domain

P3_N

Domain

14

false

This entry represents the N-terminal in P3 major capside protein from Bacteriophage PRD1. P3 adopts a double-barrel structure comprising two eight-stranded viral β-barrels or jelly rolls, each of which contains a 12-residue α-helix. This protein then trimerises through a 'trimerisation loop' sequence, and is incorporat...

[]

0

[ "PFAM" ]

[ "PF09018" ]

[ "Phage_Capsid_P3_N" ]

[ 14 ]

1

[]

0

[ "1cjd", "1gw7", "1gw8", "1hb5", "1hb7", "1hb9", "1hqn", "1hx6", "1w8x", "6q5u", "7ook" ]

11

[ "PUB00028629" ]

[ "11752778" ]

[ "The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution." ]

[ 2002 ]

1

[]

0

null

[ "Actinomycetes", "Tectiviridae" ]

[ 5, 9 ]

2

[]

0

true

Domain

P3, N-terminal domain

P3_N

5

IPR015109

15,109

Restriction endonuclease, type II, EcoRII, C-terminal

Restrct_endonuc_II_EcoRII_C

Domain

1,108

false

There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi...

[ "GO:0003677", "GO:0009036", "GO:0009307" ]

[ "DNA binding", "type II site-specific deoxyribonuclease activity", "DNA restriction-modification system" ]

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

3

[ "PFAM" ]

[ "PF09019" ]

[ "EcoRII-C" ]

[ 1108 ]

1

[]

0

[ "1na6", "2fqz", "2gb7", "3bm3", "3hqg" ]

5

[ "PUB00029018", "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707" ]

[ "14659759", "15770420", "14576294", "11827971", "11557805", "15121719", "12665693" ]

[ "Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold.", "Type II restriction endonucleases: structure and mechanism.", "Diversity of type II restriction endonucleases that require two DNA recognition sites.", "Evolutionary relation...

[ 2004, 2005, 2003, 2002, 2001, 2004, 2003 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Burkholderia phage KL3", "Protostomia", "unclassified sequences" ]

[ 8, 1084, 1, 3, 12 ]

5

[]

0

true

Domain

Restriction endonuclease, type II, EcoRII, C-terminal

Restrct_endonuc_II_EcoRII_C

3

IPR015110

15,110

YopE, N-terminal domain

YopE_N_dom

Domain

18

false

The N-terminal YopE domain targets YopE for secretion from the bacterium and translocation into eukaryotic cells [ ].

[ "GO:0050765" ]

[ "negative regulation of phagocytosis" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF09020" ]

[ "YopE_N" ]

[ 18 ]

1

[]

0

[ "1hy5", "1l2w" ]

2

[ "PUB00026901" ]

[ "12049734" ]

[ "Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens." ]

[ 2002 ]

1

[]

0

null

[ "Yersinia" ]

[ 18 ]

1

[]

0

true

Domain

YopE, N-terminal domain

YopE_N_dom

7

IPR015111

15,111

Hut operon regulatory protein HutP

Regulatory_HutP

Family

1,208

false

The HutP protein regulates the expression of Bacillus 'hut' structural genes by an anti-termination complex, which recognises three UAG triplet units, separated by four non-conserved nucleotides on the RNA terminator region. L-Histidine and Mg2+ ions are also required. These proteins exhibit the structural elements of ...

[]

0

[ "PFAM" ]

[ "PF09021" ]

[ "HutP" ]

[ 1208 ]

1

[]

0

[ "1vea", "1wmq", "1wps", "1wpt", "1wpu", "1wpv", "1wrn", "1wro", "1wrq", "3boy", "4h4l", "4ok9", "4okq" ]

13

[ "PUB00032271" ]

[ "15758992" ]

[ "Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand." ]

[ 2005 ]

1

[]

[ "IPR023552" ]

0

1

0

[ "Bacteria", "ecological metagenomes" ]

[ 1191, 17 ]

2

[]

0

true

Family

Hut operon regulatory protein HutP

Regulatory_HutP

4

IPR015112

15,112

Staphostatin A

Staphostatin_A

Domain

37

false

The staphostatin A polypeptide chain folds into a slightly deformed, eight-stranded β-barrel, with strands β4 through β8 forming an antiparallel sheet while the N terminus forms a ψ-loop motif. Members of this family constitute a class of cysteine protease inhibitors distinct in the fold and the mechanism of action fro...

[]

0

[ "PFAM" ]

[ "PF09022" ]

[ "Staphostatin_A" ]

[ 37 ]

1

[]

0

[ "1oh1" ]

1

[ "PUB00029436" ]

[ "14621990" ]

[ "A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus." ]

[ 2003 ]

1

[]

0

null

[ "Staphylococcus" ]

[ 37 ]

1

[]

0

true

Domain

Staphostatin A

Staphostatin_A

8

IPR015113

15,113

Staphostatin B

Staphostatin_B

Domain

30

false

Staphostatin B inhibits the cysteine protease Staphopain B, produced by Staphylococcus aureus, by blocking the active site of the enzyme. This domain adopts an eight-stranded mixed β-barrel structure, with a deviation from the up-down topology of canonical β-barrels in the amino-terminal part of the molecule [ ].

[]

0

[ "PFAM" ]

[ "PF09023" ]

[ "Staphostatin_B" ]

[ 30 ]

1

[]

0

[ "1nyc", "1pxv", "1qwx", "1y4h" ]

4

[ "PUB00032579" ]

[ "15644332" ]

[ "A comparison of staphostatin B with standard mechanism serine protease inhibitors." ]

[ 2005 ]

1

[]

0

null

[ "Bacteria" ]

[ 30 ]

1

[]

0

true

Domain

Staphostatin B

Staphostatin_B

8

IPR015116

15,116

Cdc42 binding domain-like

Cdc42-bd-like

Domain

3,693

false

This entry represents the Cdc42 (a GTPase) binding domain. The domain is largely unstructured in the absence of Cdc42 [ ]. Proteins containing this domain include the tyrosine-protein kinase sid-3 [ ], the ERBB receptor feedback inhibitor 1, the activated CDC42 kinase 1 and the probable tyrosine-protein kinase kin-25.

[]

0

[ "PFAM" ]

[ "PF09027" ]

[ "GTPase_binding" ]

[ 3693 ]

1

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

[ "2.7.10.2", "R-HSA-9842663", "R-MMU-9842663", "R-RNO-9842663" ]

[ "EC:2.7.10.2", "REACTOME:R-HSA-9842663", "REACTOME:R-MMU-9842663", "REACTOME:R-RNO-9842663" ]

4

[ "1cf4" ]

1

[ "PUB00018132", "PUB00094394" ]

[ "10360579", "22912399" ]

[ "Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK.", "Conserved tyrosine kinase promotes the import of silencing RNA into Caenorhabditis elegans cells." ]

[ 1999, 2012 ]

2

[]

0

null

[ "Bilateria" ]

[ 3693 ]

1

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

[ 1, 22, 15, 12, 13 ]

5

true

Domain

Cdc42 binding domain-like

Cdc42-bd-like

3

IPR015117

15,117

Ig protease IdeS

IdeS

Domain

295

false

IdeS from Streptococcus pyogenes, also known as Mac-1, is an endopeptidase with specificity for IgG [ ]. The bacterial protein Mac-1 adopts an α/β fold, with 14 β strands and 9 α helices . The N-terminal domain is made up predominantly of α helices, whereas the C-terminal domain consists predominantly of β sheets. Mac ...

[ "GO:0008233" ]

[ "peptidase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09028" ]

[ "Mac-1" ]

[ 295 ]

1

[]

0

[ "1y08", "2au1", "2avw", "8a47", "9arc", "9hb1", "9hb2", "9mdk", "9mdm", "9mdo" ]

10

[ "PUB00038397", "PUB00074606", "PUB00074607" ]

[ "15574492", "19659725", "23243300" ]

[ "Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.", "Two novel IgG endopeptidases of Streptococcus equi.", "Identification of a novel host-specific IgM protease in Streptococcus suis." ]

[ 2004, 2009, 2013 ]

3

[]

0

null

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

[ 290, 3, 2 ]

3

[]

0

true

Domain

Ig protease IdeS

IdeS

8

IPR015118

15,118

5-aminolevulinate synthase presequence

5aminolev_synth_preseq

Domain

2,074

false

The N-terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the...

[ "GO:0003870", "GO:0030170", "GO:0006778", "GO:0005759" ]

[ "5-aminolevulinate synthase activity", "pyridoxal phosphate binding", "porphyrin-containing compound metabolic process", "mitochondrial matrix" ]

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

4

[ "PFAM" ]

[ "PF09029" ]

[ "Preseq_ALAS" ]

[ 2074 ]

1

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

[ "2.3.1.37", "GenProp1525", "PWY-5189", "PWY-7536", "R-BTA-189451", "R-DRE-189451", "R-GGA-421984", "R-HSA-189451", "R-HSA-1989781", "R-HSA-2151201", "R-HSA-9837999", "R-MMU-189451", "R-MMU-9837999", "R-RNO-189451", "R-RNO-9837999" ]

[ "EC:2.3.1.37", "GP:GenProp1525", "METACYC:PWY-5189", "METACYC:PWY-7536", "REACTOME:R-BTA-189451", "REACTOME:R-DRE-189451", "REACTOME:R-GGA-421984", "REACTOME:R-HSA-189451", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-189451", "REACTOME:R-MMU-...

15

[]

0

[ "PUB00028606" ]

[ "11566198" ]

[ "The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase." ]

[ 2001 ]

1

[]

0

null

[ "Eukaryota", "Microbacterium marinum" ]

[ 2073, 1 ]

2

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

[ 2, 8, 10, 14 ]

4

true

Domain

5-aminolevulinate synthase presequence

5aminolev_synth_preseq

4

IPR015120

15,120

Siah interacting protein, N-terminal

Siah-Interact_N

Domain

2,097

false

The N-terminal domain of Siah interacting protein (SIP) adopts a helical hairpin structure with a hydrophobic core stabilised by a classic knobs-and-holes arrangement of side chains contributed by the two amphipathic helices. Little is known about this domain's function, except that it is crucial for interactions with ...

[]

0

[ "PFAM" ]

[ "PF09032" ]

[ "Siah-Interact_N" ]

[ 2097 ]

1

[]

0

[ "1ysm", "2a26" ]

2

[ "PUB00035462" ]

[ "15996101" ]

[ "The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies." ]

[ 2005 ]

1

[]

0

null

[ "Eukaryota" ]

[ 2097 ]

1

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

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

8

true

Domain

Siah interacting protein, N-terminal

Siah-Interact_N

7

IPR015121

15,121

DNA fragmentation factor 45kDa, middle domain

DNA_fragmentation_mid_dom

Domain

1,082

false

One of the hallmarks of the terminal stages of apoptosis is internucleosomal DNA breakdown. DNA fragmentation factor (DFF) and endonuclease G (Endo G) are responsible for this process. DFF exists in the nucleus as a heterodimer composed of a 45kDa chaperone and inhibitor subunit (DFF45, also called ICAD-L) and a 40kDa ...

[]

0

[ "PFAM" ]

[ "PF09033" ]

[ "DFF-C" ]

[ 1082 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-140342", "R-MMU-140342" ]

[ "REACTOME:R-HSA-140342", "REACTOME:R-MMU-140342" ]

2

[ "1iyr", "1koy" ]

2

[ "PUB00090023" ]

[ "15723341" ]

[ "Discovery, regulation, and action of the major apoptotic nucleases DFF40/CAD and endonuclease G." ]

[ 2005 ]

1

[]

0

null

[ "Opisthokonta" ]

[ 1082 ]

1

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

[ 1, 3, 3, 5 ]

4

true

Domain

DNA fragmentation factor 45kDa, middle domain

DNA_fragmentation_mid_dom

6

IPR015122

15,122

Excisionase from transposon Tn916

Tn916-Xis

Family

1,495

false

The phage-encoded excisionase protein Tn916-Xis adopts a winged-helix structure that consists of a three-stranded anti-parallel β-sheet that packs against a helix-turn-helix (HTH) motif and a third C-terminal α-helix. It is encoded for by Tn916, which also codes for the integrase Tn916-Int. The protein interacts with D...

[]

0

[ "PFAM", "PIRSF" ]

[ "PF09035", "PIRSF004323" ]

[ "Tn916-Xis", "Tn916-Xis" ]

[ 1495, 655 ]

2

[]

0

[ "1y6u" ]

1

[ "PUB00032591" ]

[ "15733914" ]

[ "The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases." ]

[ 2005 ]

1

[]

0

null

[ "Bacteria", "Methanosarcina mazei", "Viruses", "metagenomes" ]

[ 1468, 1, 16, 10 ]

4

[]

0

true

Family

Excisionase from transposon Tn916

Tn916-Xis

1

IPR015123

15,123

Bcr-Abl oncoprotein oligomerisation

Bcr-Abl_oncoprot_oligo

Domain

1,980

false

This entry represents the oligomerisation domain of the breakpoint cluster region oncoprotein Bcr, and the Bcr/Abl (Abelson-leukemia-virus) fusion protein created by a reciprocal (9;22) fusion [ ]. Brc displays serine/threonine protein kinase activity ( ), acting as a GTPase-activating protein for RAC1 and CDC42. Brc p...

[ "GO:0004674", "GO:0005096", "GO:0006468", "GO:0007165" ]

[ "protein serine/threonine kinase activity", "GTPase activator activity", "protein phosphorylation", "signal transduction" ]

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

4

[ "PFAM" ]

[ "PF09036" ]

[ "Bcr-Abl_Oligo" ]

[ 1980 ]

1

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

[ "2.7.11.1", "R-HSA-1839117", "R-HSA-5655302", "R-HSA-8980692", "R-HSA-9013026", "R-HSA-9013106", "R-HSA-9013148", "R-HSA-9013149", "R-HSA-9013404", "R-HSA-9013423", "R-MMU-8980692", "R-MMU-9013026", "R-MMU-9013106", "R-MMU-9013148", "R-MMU-9013149", "R-MMU-9013404", "R-MMU-9013423", ...

[ "EC:2.7.11.1", "REACTOME:R-HSA-1839117", "REACTOME:R-HSA-5655302", "REACTOME:R-HSA-8980692", "REACTOME:R-HSA-9013026", "REACTOME:R-HSA-9013106", "REACTOME:R-HSA-9013148", "REACTOME:R-HSA-9013149", "REACTOME:R-HSA-9013404", "REACTOME:R-HSA-9013423", "REACTOME:R-MMU-8980692", "REACTOME:R-MMU-901...

22

[ "1k1f" ]

1

[ "PUB00028791", "PUB00042932", "PUB00042933" ]

[ "11780146", "17090304", "15302586" ]

[ "Structure of the Bcr-Abl oncoprotein oligomerization domain.", "BCR and its mutants, the reciprocal t(9;22)-associated ABL/BCR fusion proteins, differentially regulate the cytoskeleton and cell motility.", "The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite ...

[ 2002, 2006, 2004 ]

3

[]

0

null

[ "Bilateria" ]

[ 1980 ]

1

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

[ 7, 19, 3, 4 ]

4

true

Domain

Bcr-Abl oncoprotein oligomerisation

Bcr-Abl_oncoprot_oligo

3

IPR015124

15,124

Trehalose 2-sulfotransferase

Stf0

Family

819

false

The trehalose 2-sulfotransferase catalyses the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall glycolipid in pathogenic mycobacteria [ ...

[ "GO:0016740" ]

[ "transferase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM", "PIRSF" ]

[ "NF047724", "PIRSF021497" ]

[ "TrhSuTaseStf0", "Sulphotransferase_Stf0" ]

[ 367, 818 ]

2

[ "EC", "METACYC" ]

[ "2.8.2.37", "PWY-7746" ]

[ "EC:2.8.2.37", "METACYC:PWY-7746" ]

2

[ "1tex" ]

1

[ "PUB00031430", "PUB00159421", "PUB00159422" ]

[ "15258569", "22360425", "15866533" ]

[ "Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis.", "Sulfolipid-1 biosynthesis restricts Mycobacterium tuberculosis growth in human macrophages.", "Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrome...

[ 2004, 2012, 2005 ]

3

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 809, 10 ]

2

[]

0

true

Family

Trehalose 2-sulfotransferase

Stf0

8

IPR015125

15,125

Tumour suppressor p53-binding protein-1, Tudor domain

53-BP1_Tudor

Domain

1,553

false

This domain consist of two tandem tudor folds with a deep pocket at their interface. The domain is essential for the recruitment of proteins to double stranded breaks in DNA, which is mediated by interaction with methylated Lys 79 of histone H3 [ ].

[]

0

[ "PFAM" ]

[ "PF09038" ]

[ "53-BP1_Tudor" ]

[ 1553 ]

1

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

[ "R-HSA-3232118", "R-HSA-5693565", "R-HSA-5693571", "R-HSA-5693607", "R-HSA-69473", "R-MMU-3232118", "R-MMU-5693565", "R-MMU-5693571", "R-MMU-5693607", "R-MMU-69473" ]

[ "REACTOME:R-HSA-3232118", "REACTOME:R-HSA-5693565", "REACTOME:R-HSA-5693571", "REACTOME:R-HSA-5693607", "REACTOME:R-HSA-69473", "REACTOME:R-MMU-3232118", "REACTOME:R-MMU-5693565", "REACTOME:R-MMU-5693571", "REACTOME:R-MMU-5693607", "REACTOME:R-MMU-69473" ]

10

[ "1ssf", "1xni", "2g3r", "2ig0", "2lvm", "2mwo", "2mwp", "3lgf", "3lgl", "3lh0", "4cri", "4rg2", "4x34", "5j26", "5z78", "5zcj", "6co1", "6co2", "6mxx", "6mxy", "6mxz", "6my0", "6upt", "6va5", "6vip", "7yqk", "8eom", "8f0w", "8svg", "8svh", "8svi", "8svj"...

36

[ "PUB00032470" ]

[ "15525939" ]

[ "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks." ]

[ 2004 ]

1

[]

0

null

[ "Eukaryota" ]

[ 1553 ]

1

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

[ 20, 5, 6, 7 ]

4

true

Domain

Tumour suppressor p53-binding protein-1, Tudor domain

53-BP1_Tudor

2

IPR015126

15,126

Mu DNA binding, I gamma subdomain

Mu_I-gamma

Domain

1,149

false

This domain is responsible for binding the DNA attachment sites at each end of the Mu genome. They adopt a secondary structure comprising a four helix bundle tightly packed around a hydrophobic core consisting of aliphatic and aromatic amino acid residues. Helices 1 and 2 are oriented antiparallel to each other. Helix ...

[]

0

[ "PFAM" ]

[ "PF09039" ]

[ "HTH_Tnp_Mu_2" ]

[ 1149 ]

1

[]

0

[ "2ezh", "2ezi", "4fcy" ]

3

[ "PUB00023051" ]

[ "9367742" ]

[ "Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase." ]

[ 1997 ]

1

[]

0

null

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

[ 1129, 2, 11, 7 ]

4

[]

0

true

Domain

Mu DNA binding, I gamma subdomain

Mu_I-gamma

7

IPR015127

15,127

Gastric H+/K+-transporter P-type ATPase, N-terminal

ATPase_P-typ_H/K-transp_N

Domain

266

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:0000287", "GO:0005524", "GO:0008900", "GO:1902600", "GO:0016020" ]

[ "magnesium ion binding", "ATP binding", "P-type potassium:proton transporter activity", "proton transmembrane transport", "membrane" ]

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

5

[ "PFAM" ]

[ "PF09040" ]

[ "H-K_ATPase_N" ]

[ 266 ]

1

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

[ "7.2.2.19", "R-HSA-936837", "R-MMU-936837", "R-RNO-936837" ]

[ "EC:7.2.2.19", "REACTOME:R-HSA-936837", "REACTOME:R-MMU-936837", "REACTOME:R-RNO-936837" ]

4

[ "1iwc", "1iwf", "2xzb", "2yn9", "3ixz", "4ux1", "4ux2", "5y0b", "5ylu", "5ylv", "7w47", "7w48", "7w49", "7w4a", "8ijv", "8ijw", "8ijx", "8jmn", "8wa5" ]

19

[ "PUB00009616", "PUB00020603", "PUB00020604", "PUB00020661", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]

[ "9419228", "15473999", "15078220", "12480547", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]

[ "Evolution of substrate specificities in the P-type ATPase superfamily.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "Structure determination and conformational chang...

[ 1998, 2004, 2004, 2003, 2010, 2008, 1992, 1998, 2023, 2023 ]

10

[]

0

null

[ "Tetrapoda" ]

[ 266 ]

1

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

[ 3, 2, 6 ]

3

true

Domain

Gastric H+/K+-transporter P-type ATPase, N-terminal

ATPase_P-typ_H/K-transp_N

9

IPR015128

15,128

Aurora-A binding

Aurora-A-bd

Domain

867

false

The Aurora-A binding domain in TPX2 (targeting protein for Xklp2) binds to two distinct sites on the Aurora kinase: the upstream residues bind at the N-terminal lobe, whilst the downstream residues bind in an α-helical conformation between the N- and C-terminal lobes. The two Aurora-A binding motifs are connected by a ...

[]

0

[ "PFAM" ]

[ "PF09041" ]

[ "Aurora-A_bind" ]

[ 867 ]

1

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

[ "R-HSA-6804756", "R-HSA-8854518", "R-MMU-6804756", "R-MMU-8854518", "R-XTR-6804756", "R-XTR-8854518" ]

[ "REACTOME:R-HSA-6804756", "REACTOME:R-HSA-8854518", "REACTOME:R-MMU-6804756", "REACTOME:R-MMU-8854518", "REACTOME:R-XTR-6804756", "REACTOME:R-XTR-8854518" ]

6

[ "1ol5", "3e5a", "3ha6", "4c3p", "5lxm", "6bjc", "6vpg", "6vph", "6vpi", "6vpj", "6vpl", "6vpm", "6xka" ]

13

[ "PUB00022351" ]

[ "14580337" ]

[ "Structural basis of Aurora-A activation by TPX2 at the mitotic spindle." ]

[ 2003 ]

1

[]

0

null

[ "Bilateria" ]

[ 867 ]

1

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

[ 2, 2, 4 ]

3

true

Domain

Aurora-A binding

Aurora-A-bd

4

IPR015129

15,129

Titin, Z repeat

Titin_Z_rpt

Repeat

1,375

false

This entry represents the Z-repeat (approximately 45 amino acid sequences) found in the N terminus of titin [ ]. The Z-repeat recognises and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34). It adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs...

[]

0

[ "PFAM" ]

[ "PF09042" ]

[ "Titin_Z" ]

[ 1375 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-114608", "R-HSA-390522" ]

[ "REACTOME:R-HSA-114608", "REACTOME:R-HSA-390522" ]

2

[ "1h8b" ]

1

[ "PUB00025570", "PUB00046420" ]

[ "11573089", "10819994" ]

[ "Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex.", "Binding of alpha-actinin to titin: implications for Z-disk assembly." ]

[ 2001, 2000 ]

2

[]

0

null

[ "Vertebrata" ]

[ 1375 ]

1

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

[ 30, 9, 7, 4 ]

4

true

Repeat

Titin, Z repeat

Titin_Z_rpt

6

IPR015130

15,130

D-Lysine 5,6-aminomutase alpha subunit

Lys-AminoMut_A

Domain

1,915

false

This domain is found in proteins involved in the 1,2 rearrangement of the terminal amino group of DL-lysine and of L-beta-lysine, using adenosylcobalamin (AdoCbl) and pyridoxal-5'-phosphate as cofactors. The structure is predominantly a PLP-binding TIM barrel domain, with several additional α-helices and β-strands at t...

[]

0

[ "PFAM", "PFAM" ]

[ "PF09043", "PF16552" ]

[ "Lys-AminoMut_A", "OAM_alpha" ]

[ 1581, 335 ]

2

[]

0

[ "1xrs", "3kow", "3kox", "3koy", "3koz", "3kp0", "3kp1", "8t0v", "9q1a" ]

9

[]

0

[]

0

null

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

[ 1857, 4, 2, 52 ]

4

[]

0

true

Domain

D-Lysine 5,6-aminomutase alpha subunit

Lys-AminoMut_A

9

IPR015131

15,131

Killer toxin, Kp4

Killer_tox_Kp4

Domain

935

false

Killer toxins are polypeptides secreted by some fungal species that kill sensitive cells of the same or related species, often functioning by creating pores in target cell membranes. The fungal killer toxin KP4 from the corn smut fungus, Ustilago maydis (Smut fungus), is encoded by a resident symbiotic double-stranded ...

[ "GO:0005576" ]

[ "extracellular region" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF09044" ]

[ "Kp4" ]

[ 935 ]

1

[]

0

[ "1kpt" ]

1

[ "PUB00028852", "PUB00035673" ]

[ "7582897", "8145639" ]

[ "Structure and function of a virally encoded fungal toxin from Ustilago maydis: a fungal and mammalian Ca2+ channel inhibitor.", "Structure and heterologous expression of the Ustilago maydis viral toxin KP4." ]

[ 1995, 1994 ]

2

[]

0

null

[ "Eukaryota", "Ustilago maydis P4 virus" ]

[ 934, 1 ]

2

[]

0

true

Domain

Killer toxin, Kp4

Killer_tox_Kp4

2

IPR015133

15,133

Effector protein HopAB, E3 ubiquitin ligase domain

E3_ubiquit_lig_AvrPtoB

Domain

100

false

HopAB family members are type III effector proteins that are secreted by the plant pathogen Pseudomonas syringae into the host plant to inhibit its immune system and facilitate the spread of the pathogen [ ]. AvrPtoB, also called HopAB3, is the best studied member of the family. It suppresses host basal defenses by int...

[]

0

[ "PFAM" ]

[ "PF09046" ]

[ "AvrPtoB-E3_ubiq" ]

[ 100 ]

1

[]

0

[ "2fd4" ]

1

[ "PUB00035360", "PUB00057523", "PUB00076029", "PUB00080432", "PUB00080434", "PUB00080437" ]

[ "16373536", "22191472", "22169508", "21112235", "15808932", "19062288" ]

[ "A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase.", "Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of Pseudomonas syringae type III effectors.", "Structural analysis of Pseudomonas syringae AvrPtoB bound to host B...

[ 2006, 2012, 2011, 2011, 2005, 2008 ]

6

[]

0

null

[ "Pseudomonadota" ]

[ 100 ]

1

[]

0

true

Domain

Effector protein HopAB, E3 ubiquitin ligase domain

E3_ubiquit_lig_AvrPtoB

4

IPR015134

15,134

Calcineurin-binding protein cabin-1, MEF2-binding domain

MEF2-bd

Domain

1,239

false

The myocyte enhancer factor-2 (MEF2) binding domain, predominantly found in the calcineurin-binding protein CABIN 1, adopts an amphipathic α-helical structure, which allows it to bind a hydrophobic groove on the MEF2S domain, forming a triple-helical interaction. Interaction of this domain with MEF2 causes repression o...

[]

0

[ "PFAM", "CDD" ]

[ "PF09047", "cd13839" ]

[ "MEF2_binding", "MEF2_binding" ]

[ 1239, 1215 ]

2

[ "REACTOME", "REACTOME" ]

[ "R-HSA-2559584", "R-RNO-2559584" ]

[ "REACTOME:R-HSA-2559584", "REACTOME:R-RNO-2559584" ]

2

[ "1n6j" ]

1

[ "PUB00027575" ]

[ "12700764" ]

[ "Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2." ]

[ 2003 ]

1

[]

0

null

[ "Chordata" ]

[ 1239 ]

1

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

[ 8, 5, 6, 6 ]

4

true

Domain

Calcineurin-binding protein cabin-1, MEF2-binding domain

MEF2-bd

6

IPR015135

15,135

Stannin transmembrane

SNN_transmemb

Domain

650

false

This region consists of a single highly hydrophobic transmembrane helix that transverses the lipid bilayer at a 20 degree angle with respect to the membrane normal. It contains a conserved cysteine residue (Cys32) that, together with Cys34 found in the stannin unstructured linker domain, constitutes the putative trimet...

[]

0

[ "PFAM" ]

[ "PF09049" ]

[ "SNN_transmemb" ]

[ 650 ]

1

[]

0

[ "1zza" ]

1

[ "PUB00035467" ]

[ "16246365" ]

[ "Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride." ]

[ 2005 ]

1

[]

0

null

[ "Vertebrata" ]

[ 650 ]

1

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

[ 1, 1, 2, 3 ]

4

true

Domain

Stannin transmembrane

SNN_transmemb

9

IPR015136

15,136

Stannin unstructured linker

SNN_linker

Domain

650

false

This entry represents an unstructured protein region which connects two adjacent stannin helical domains. It contains a conserved CXC metal-binding motif and a putative 14-3-3-zeta binding domain. Upon coordinating dimethytin, considerable structural or dynamic changes in the flexible loop region of SNN may take place,...

[]

0

[ "PFAM" ]

[ "PF09050" ]

[ "SNN_linker" ]

[ 650 ]

1

[]

0

[ "1zza" ]

1

[ "PUB00035467" ]

[ "16246365" ]

[ "Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride." ]

[ 2005 ]

1

[]

0

null

[ "Vertebrata" ]

[ 650 ]

1

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

[ 1, 1, 2, 3 ]

4

true

Domain

Stannin unstructured linker

SNN_linker

9

IPR015137

15,137

Stannin cytoplasmic

SNN_cytoplasm

Domain

643

false

This domain forms a distorted cytoplasmic helix that is partially absorbed into the plane of the lipid bilayer with a tilt angle of approximately 80 degrees from the membrane normal. It interacts with the surface of the lipid bilayer, and contributes to the initiation of the apoptotic cascade on binding of the unstruct...

[]

0

[ "PFAM" ]

[ "PF09051" ]

[ "SNN_cytoplasm" ]

[ 643 ]

1

[]

0

[ "1zza" ]

1

[ "PUB00035467" ]

[ "16246365" ]

[ "Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride." ]

[ 2005 ]

1

[]

0

null

[ "Gnathostomata" ]

[ 643 ]

1

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

[ 1, 1, 2, 3 ]

4

true

Domain

Stannin cytoplasmic

SNN_cytoplasm

8

IPR015138

15,138

Salmonella invasion protein A, N-terminal

SipA_N

Domain

781

false

Salmonella invasion protein A (SipA) is a virulence factor that is translocated into host cells by a type III secretion system. In the host cell it binds to actin, stimulates actin polymerisation and counteracts F-actin destabilising proteins. This contributes towards cytoskeletal rearrangements that allow the entry of...

[]

0

[ "PFAM" ]

[ "PF09052" ]

[ "SipA" ]

[ 781 ]

1

[]

0

[ "2fm8", "2fm9", "8vfm" ]

3

[ "PUB00054077", "PUB00163366" ]

[ "11331579", "25486861" ]

[ "Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin.", "PERP, a host tetraspanning membrane protein, is required for Salmonella-induced inflammation." ]

[ 2001, 2015 ]

2

[]

0

null

[ "Pseudomonadota" ]

[ 781 ]

1

[]

0

true

Domain

Salmonella invasion protein A, N-terminal

SipA_N

2

IPR015139

15,139

Cag pathogenicity island protein, CagZ

CagPAI_CagZ

Family

134

false

Helicobacter pylori (Campylobacter pylori) clinical isolates can be classified into two types according to their degree of pathogenicity. Type I strains are associated with a severe disease pathology, express functional VacA (vacuolating cytotoxin A) and contain an insertion of 40 kb of foreign DNA: the cag (cytotoxin-...

[]

0

[ "PFAM" ]

[ "PF09053" ]

[ "CagZ" ]

[ 134 ]

1

[]

0

[ "1s2x", "6jho" ]

2

[ "PUB00030883", "PUB00035538", "PUB00035539" ]

[ "15223328", "17172510", "16933206" ]

[ "Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system.", "Helicobacter pylori cag pathogenicity island genes: clinical relevance for peptic ulcer disease development in Brazil.", "CagA protein secreted by the intact type IV secretion ...

[ 2004, 2007, 2006 ]

3

[]

0

null

[ "Helicobacter pylori" ]

[ 134 ]

1

[]

0

true

Family

Cag pathogenicity island protein, CagZ

CagPAI_CagZ

9

IPR015141

15,141

Phospholipase A2, prokaryotic/fungal

PLipase_A2_prok/fun

Family

2,495

false

This entry represents bacterial and fungal phospholipase A2 proteins, as well as various hypothetical and putative proteins. They enable the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The phospholipase domain adopts an α-helical secondary structu...

[]

0

[ "PFAM" ]

[ "PF09056" ]

[ "Phospholip_A2_3" ]

[ 2495 ]

1

[]

0

[ "1faz", "1it4", "1it5", "1kp4", "1lwb", "4aup", "7ygk", "8k1w" ]

8

[ "PUB00028486" ]

[ "11897785" ]

[ "The crystal structure of prokaryotic phospholipase A2." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "freshwater metagenome" ]

[ 1589, 878, 28 ]

3

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]

[ 2 ]

1

true

Family

Phospholipase A2, prokaryotic/fungal

PLipase_A2_prok/fun

9

IPR015143

15,143

L27-1

L27_1

Domain

5,559

false

The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three ...

[]

0

[ "PFAM" ]

[ "PF09058" ]

[ "L27_1" ]

[ 5559 ]

1

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

[ "R-CEL-438066", "R-CEL-451308", "R-CEL-6794361", "R-CEL-8849932", "R-CFA-399719", "R-CFA-438066", "R-CFA-451308", "R-CFA-5673001", "R-CFA-8849932", "R-DME-438066", "R-DME-451308", "R-DME-5625900", "R-DME-6794361", "R-DME-8849932", "R-DRE-438066", "R-DRE-8849932", "R-HSA-399719", "R...

[ "REACTOME:R-CEL-438066", "REACTOME:R-CEL-451308", "REACTOME:R-CEL-6794361", "REACTOME:R-CEL-8849932", "REACTOME:R-CFA-399719", "REACTOME:R-CFA-438066", "REACTOME:R-CFA-451308", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-8849932", "REACTOME:R-DME-438066", "REACTOME:R-DME-451308", "REACTOME:R-DME...

38

[ "1rso", "3lra", "4rp3", "4rp4", "4rp5" ]

5

[ "PUB00018474" ]

[ "15048107" ]

[ "The tetrameric L27 domain complex as an organization platform for supramolecular assemblies." ]

[ 2004 ]

1

[ "IPR004172" ]

[]

1

0

1

[ "Eukaryota" ]

[ 5559 ]

1

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

[ 1, 81, 4, 32, 9, 12 ]

6

true

Domain

L27-1

L27_1

5

IPR015144

15,144

Type III secretion system effector delivery regulator TyeA

T3SS_TyeA

Domain

541

false

This domain is composed of two pairs of parallel α-helices, and interacts with the bacterial protein YopN via hydrophobic residues located on the helices. Association of TyeA with the C terminus of YopN is accompanied by conformational changes in both polypeptides that create order out of disorder: the resulting struct...

[]

0

[ "PFAM" ]

[ "PF09059" ]

[ "TyeA" ]

[ 541 ]

1

[]

0

[ "1xl3", "7yyg" ]

2

[ "PUB00020751" ]

[ "15701523" ]

[ "Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis." ]

[ 2005 ]

1

[ "IPR013351" ]

[]

1

0

1

[ "Bacteria", "metagenomes" ]

[ 539, 2 ]

2

[]

0

true

Domain

Type III secretion system effector delivery regulator TyeA

T3SS_TyeA

7

IPR015145

15,145

L27-N

L27_N

Domain

1,377

false

The L27_N domain plays a role in the biogenesis of tight junctions and in the establishment of cell polarity in epithelial cells. Each L27_N domain consists of three α-helices, the first two of which form an antiparallel coiled-coil. Two L27 domains come together to form a four-helical bundle with the antiparallel coil...

[]

0

[ "PFAM" ]

[ "PF09060" ]

[ "L27_N" ]

[ 1377 ]

1

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

[ "R-HSA-420029", "R-HSA-9692912", "R-HSA-9705677" ]

[ "REACTOME:R-HSA-420029", "REACTOME:R-HSA-9692912", "REACTOME:R-HSA-9705677" ]

3

[ "1vf6", "1y76", "3uit" ]

3

[ "PUB00018475", "PUB00074897" ]

[ "15241471", "15677456" ]

[ "Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes.", "PALS1 specifies the localization of ezrin to the apical membrane of gastric parietal cells." ]

[ 2004, 2005 ]

2

[]

0

null

[ "Bilateria" ]

[ 1377 ]

1

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

[ 6, 4, 3, 1 ]

4

true

Domain

L27-N

L27_N

9

IPR015146

15,146

Ribonucleotide reductase, stirrup

RNR_stirrup

Domain

9

false

The Stirrup domain, found in the prokaryotic protein ribonucleotide reductase, has a molecular mass of 9kDa and is folded into an α/β structure. It allows for binding of the reductase to DNA via electrostatic interactions, since it has a predominance of positive charges distributed on its surface [ ].

[ "GO:0016788" ]

[ "hydrolase activity, acting on ester bonds" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09061" ]

[ "Stirrup" ]

[ 9 ]

1

[]

0

[ "1dq3" ]

1

[ "PUB00024294" ]

[ "10891276" ]

[ "Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI." ]

[ 2000 ]

1

[]

0

null

[ "Thermococcaceae" ]

[ 9 ]

1

[]

0

true

Domain

Ribonucleotide reductase, stirrup

RNR_stirrup

4

IPR015147

15,147

PI-PfuI intein endonuclease, subdomain

PI-PfuI_intein_endonucl_subdom

Domain

8

false

Ribonucleotide reductase from Pyrococcus species has been shown to contain two inteins, PI-PfuI and PI-PfuII. The endonuclease domain from the PI-PfuI intein (also known as Vitamin B12-dependent ribonucleoside-diphosphate reductase) is composed of two subdomains, each of which assumes an α-β-β-α-β-β-α-α topology. The f...

[]

0

[ "PFAM" ]

[ "PF09062" ]

[ "Endonuc_subdom" ]

[ 8 ]

1

[]

0

[ "1dq3" ]

1

[ "PUB00024294" ]

[ "10891276" ]

[ "Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI." ]

[ 2000 ]

1

[ "IPR004042" ]

[]

1

0

1

[ "Thermococcaceae" ]

[ 8 ]

1

[]

0

true

Domain

PI-PfuI intein endonuclease, subdomain

PI-PfuI_intein_endonucl_subdom

6

IPR015148

15,148

Bacteriophage PP7 capsid

Phage_PP7_CP

Family

7

false

This entry represents the capsid protein (CP) of Pseudomonas phage PP7. CP adopts a secondary structure consisting of a six stranded β sheet and an α helix [ ].

[]

0

[ "PFAM" ]

[ "PF09063" ]

[ "Phage_coat" ]

[ 7 ]

1

[]

0

[ "1dwn", "2qud", "2qux", "6n4v", "8tux" ]

5

[ "PUB00028377" ]

[ "10739912" ]

[ "Structure determination of bacteriophage PP7 from Pseudomonas aeruginosa: from poor data to a good map." ]

[ 2000 ]

1

[]

0

null

[ "Fiersviridae" ]

[ 7 ]

1

[]

0

true

Family

Bacteriophage PP7 capsid

Phage_PP7_CP

9

IPR015149

15,149

Thrombomodulin-like, EGF-like

Tme5_EGF-like

Domain

757

false

This domain adopts a fold similar to other EGF domains, with a flat major and a twisted minor β sheet. Disulphide pairing, however, is not of the usual 1-3, 2-4, 5-6 type; rather 1-2, 3-4, 5-6 pairing is found. Its extended major sheet (strands beta-2 and beta-3 and the connecting loop) projects into thrombin's active ...

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

[ "transmembrane signaling receptor activity", "membrane" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09064" ]

[ "EGF_Tme5" ]

[ 757 ]

1

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

[ "R-HSA-140875", "R-HSA-202733", "R-MMU-140875", "R-MMU-202733" ]

[ "REACTOME:R-HSA-140875", "REACTOME:R-HSA-202733", "REACTOME:R-MMU-140875", "REACTOME:R-MMU-202733" ]

4

[ "1adx", "1dqb", "1dx5", "1egt", "2adx", "3gis", "5to3", "7t4r" ]

8

[ "PUB00024342" ]

[ "10761923" ]

[ "Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex." ]

[ 2000 ]

1

[]

0

null

[ "Bilateria", "Brenneria rubrifaciens" ]

[ 756, 1 ]

2

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

[ 1, 2, 3, 3 ]

4

true

Domain

Thrombomodulin-like, EGF-like

Tme5_EGF-like

4

IPR015150

15,150

Haemadin

Family

2

false

Members of this family adopt a secondary structure consisting of five short β-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This β-sandwich is stabilised by six enclosed cysteines arranged in a [1-2, 3-5, 4-6] disulp...

[]

0

[ "PFAM" ]

[ "PF09065" ]

[ "Haemadin" ]

[ 2 ]

1

[]

0

[ "1e0f" ]

1

[ "PUB00024384" ]

[ "11060016" ]

[ "Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor." ]

[ 2000 ]

1

[]

0

null

[ "Haemadipsa sylvestris" ]

[ 2 ]

1

[]

0

true

Family

Haemadin

9

IPR015151

15,151

Beta-adaptin appendage, C-terminal subdomain

B-adaptin_app_sub_C

Domain

9,164

false

This entry represents a subdomain of the appendage (ear) domain of beta-adaptin. This domain has a three-layer arrangement, α-β-α, with a bifurcated antiparallel β-sheet [ ]. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also b...

[ "GO:0006886", "GO:0016192", "GO:0030131" ]

[ "intracellular protein transport", "vesicle-mediated transport", "clathrin adaptor complex" ]

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

3

[ "PFAM", "SMART" ]

[ "PF09066", "SM01020" ]

[ "B2-adapt-app_C", "B2-adapt-app_C" ]

[ 8219, 8571 ]

2

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

[ "R-BTA-177504", "R-BTA-2132295", "R-BTA-416993", "R-BTA-432722", "R-BTA-437239", "R-BTA-5099900", "R-BTA-5140745", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8866427", "R-BTA-8964038", "R-DDI-432720", "R-DDI-437239", "R-DDI-8856825", "R-DDI-8856828", "R-DDI-8866427", "R-DDI-8964038", ...

[ "REACTOME:R-BTA-177504", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-416993", "REACTOME:R-BTA-432722", "REACTOME:R-BTA-437239", "REACTOME:R-BTA-5099900", "REACTOME:R-BTA-5140745", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8866427", "REACTOME:R-BTA-8964038", "REACTOME:R-...

59

[ "1e42", "2g30", "2iv8", "2iv9", "2mj7", "3h1z", "3hs9", "6yaf", "6yah", "6yai", "7om8", "7ux3", "8d4c", "8d4d", "8d4e", "8d4f", "8d4g", "8d9r", "8d9s", "8d9t", "8d9u", "8d9v", "8d9w" ]

23

[ "PUB00011753", "PUB00011791" ]

[ "10944104", "10430869" ]

[ "The structure and function of the beta 2-adaptin appendage domain.", "Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly." ]

[ 2000, 1999 ]

2

[]

0

null

[ "Ciceribacter ferrooxidans", "Eukaryota" ]

[ 1, 9163 ]

2

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

[ 14, 1, 23, 2, 27, 22, 10, 23, 45 ]

9

true

Domain

Beta-adaptin appendage, C-terminal subdomain

B-adaptin_app_sub_C

2

IPR015152

15,152

Growth hormone/erythropoietin receptor, ligand binding

Growth/epo_recpt_lig-bind

Domain

5,956

false

Members of this entry include the growth hormone and erythropoietin receptors. The latter interacts with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through inducti...

[]

0

[ "PFAM" ]

[ "PF09067" ]

[ "EpoR_lig-bind" ]

[ 5956 ]

1

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

[ "R-HSA-1170546", "R-HSA-6788467", "R-HSA-76009", "R-HSA-9006335", "R-HSA-9020956", "R-HSA-9027276", "R-HSA-9027277", "R-HSA-9027283", "R-HSA-9027284", "R-HSA-982772", "R-MMU-1170546", "R-MMU-512988", "R-MMU-5673001", "R-MMU-6788467", "R-MMU-9006335", "R-MMU-9020956", "R-MMU-9027276",...

[ "REACTOME:R-HSA-1170546", "REACTOME:R-HSA-6788467", "REACTOME:R-HSA-76009", "REACTOME:R-HSA-9006335", "REACTOME:R-HSA-9020956", "REACTOME:R-HSA-9027276", "REACTOME:R-HSA-9027277", "REACTOME:R-HSA-9027283", "REACTOME:R-HSA-9027284", "REACTOME:R-HSA-982772", "REACTOME:R-MMU-1170546", "REACTOME:R...

30

[ "1a22", "1axi", "1bp3", "1cn4", "1eba", "1ebp", "1eer", "1ern", "1f6f", "1hwg", "1hwh", "1kf9", "2aew", "2jix", "3d48", "3ew3", "3hhr", "3mzg", "3n06", "3n0p", "3ncb", "3ncc", "3nce", "3ncf", "3npz", "4i18", "4qqv", "4y5v", "4y5x", "4y5y", "6moe", "6mof"...

44

[ "PUB00023995" ]

[ "9774108" ]

[ "Efficiency of signalling through cytokine receptors depends critically on receptor orientation." ]

[ 1998 ]

1

[]

0

null

[ "Deuterostomia" ]

[ 5956 ]

1

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

[ 25, 21, 41, 32 ]

4

true

Domain

Growth hormone/erythropoietin receptor, ligand binding

Growth/epo_recpt_lig-bind

4

IPR015153

15,153

EF-hand domain, type 1

EF-hand_dom_typ1

Domain

14,447

false

Like other EF hand domains, this domain forms a helix-loop-helix motif, though since it does not contain the canonical pattern of calcium binding residues found in many EF hand domains, it does not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, thou...

[]

0

[ "PFAM" ]

[ "PF09068" ]

[ "EF-hand_2" ]

[ 14447 ]

1

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

[ "R-CEL-9913351", "R-DME-114608", "R-DME-446388", "R-DME-9013405", "R-DME-9013418", "R-DME-9035034", "R-HSA-3000171", "R-HSA-390522", "R-HSA-9619665", "R-HSA-9913351", "R-MMU-390522", "R-MMU-9913351", "R-RNO-390522", "R-RNO-9913351" ]

[ "REACTOME:R-CEL-9913351", "REACTOME:R-DME-114608", "REACTOME:R-DME-446388", "REACTOME:R-DME-9013405", "REACTOME:R-DME-9013418", "REACTOME:R-DME-9035034", "REACTOME:R-HSA-3000171", "REACTOME:R-HSA-390522", "REACTOME:R-HSA-9619665", "REACTOME:R-HSA-9913351", "REACTOME:R-MMU-390522", "REACTOME:R-...

14

[ "1eg3", "1eg4", "8yt8", "9c3c" ]

4

[ "PUB00024537" ]

[ "10932245" ]

[ "Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan." ]

[ 2000 ]

1

[]

0

null

[ "Eukaryota" ]

[ 14447 ]

1

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

[ 8, 72, 28, 63, 49, 45 ]

6

true

Domain

EF-hand domain, type 1

EF-hand_dom_typ1

3

IPR015154

15,154

EF-hand domain, type 2

EF-hand_dom_typ2

Domain

15,032

false

Like other EF hand domains, this domain forms a helix-loop-helix motif, though since it does not contain the canonical pattern of calcium binding residues found in many EF hand domains, it does not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, thou...

[]

0

[ "PFAM" ]

[ "PF09069" ]

[ "EF-hand_3" ]

[ 15032 ]

1

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

[ "R-CEL-9913351", "R-DME-114608", "R-DME-446388", "R-DME-9013405", "R-DME-9013418", "R-DME-9035034", "R-HSA-3000171", "R-HSA-390522", "R-HSA-9619665", "R-HSA-9913351", "R-MMU-390522", "R-MMU-9913351", "R-RNO-390522", "R-RNO-9913351" ]

[ "REACTOME:R-CEL-9913351", "REACTOME:R-DME-114608", "REACTOME:R-DME-446388", "REACTOME:R-DME-9013405", "REACTOME:R-DME-9013418", "REACTOME:R-DME-9035034", "REACTOME:R-HSA-3000171", "REACTOME:R-HSA-390522", "REACTOME:R-HSA-9619665", "REACTOME:R-HSA-9913351", "REACTOME:R-MMU-390522", "REACTOME:R-...

14

[ "1eg3", "1eg4", "8yt8", "9c3c" ]

4

[ "PUB00024537" ]

[ "10932245" ]

[ "Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan." ]

[ 2000 ]

1

[]

0

null

[ "Eukaryota" ]

[ 15032 ]

1

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

[ 8, 72, 18, 57, 44, 45 ]

6

true

Domain

EF-hand domain, type 2

EF-hand_dom_typ2

6

IPR015155

15,155

PLAA family ubiquitin binding domain

PFU

Domain

5,070

false

null

[]

0

[ "PFAM", "PROFILE" ]

[ "PF09070", "PS51394" ]

[ "PFU", "PFU" ]

[ 4946, 4985 ]

2

[]

0

[ "2k89", "2k8a", "2k8b", "2k8c", "3l3f", "3psp", "3pst" ]

7

[ "PUB00035448", "PUB00043395" ]

[ "16428438", "18508771" ]

[ "Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.", "DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodies." ]

[ 2006, 2008 ]

2

[]

0

null

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

[ 37, 5027, 2, 4 ]

4

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

[ 6, 1, 1, 2, 5, 2, 1, 3, 5, 1, 1, 14 ]

12

true

Domain

PLAA family ubiquitin binding domain

PFU

7

IPR015156

15,156

Malto-oligosyltrehalose trehalohydrolase, archaeal, C-terminal

Maltooligo_trehalose_arc_C

Domain

38

false

This C-terminal domain is found in the prokaryotic protein glycosyltrehalose trehalohydrolase; it assumes a gamma-crystallin-type fold with a five-stranded anti-parallel β-sheet that packs against the C-terminal side of a β-α barrel. The domain is common to family 13 glycosidases and typically contains a five to ten st...

[]

0

[ "PFAM" ]

[ "PF09071" ]

[ "Alpha-amyl_C" ]

[ 38 ]

1

[]

0

[ "1eh9", "1eha", "3vgb", "3vgd", "3vge", "3vgf", "3vgg", "3vgh" ]

8

[ "PUB00017782" ]

[ "10926520" ]

[ "Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus." ]

[ 2000 ]

1

[]

0

null

[ "Thermoprotei" ]

[ 38 ]

1

[]

0

true

Domain

Malto-oligosyltrehalose trehalohydrolase, archaeal, C-terminal

Maltooligo_trehalose_arc_C

4

IPR015158

15,158

Bud22 domain

Bud22_dom

Domain

2,708

false

This entry represents a domain found in the fungal Bud22 protein and the animal SRFB1 (serum response factor-binding protein 1) protein. Budding yeast Bud22 is required for rRNA maturation and ribosomal subunit biogenesis [ , ]. SRFB1 may be involved in regulating transcriptional activation of cardiac genes during the ...

[]

0

[ "PFAM" ]

[ "PF09073" ]

[ "BUD22" ]

[ 2708 ]

1

[]

0

[]

0

[ "PUB00056759", "PUB00078855", "PUB00078856", "PUB00078857" ]

[ "19806183", "20498295", "15492011", "16647043" ]

[ "Rational extension of the ribosome biogenesis pathway using network-guided genetics.", "BUD22 affects Ty1 retrotransposition and ribosome biogenesis in Saccharomyces cerevisiae.", "Identification of a novel serum response factor cofactor in cardiac gene regulation.", "Identification and characterization of p...

[ 2009, 2010, 2004, 2006 ]

4

[]

0

null

[ "Eukaryota" ]

[ 2708 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

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

8

true

Domain

Bud22 domain

Bud22_dom

1

IPR015159

15,159

Recombination protein 107

Rec107

Family

78

false

Rec107 forms part of a complex (Rec107-Mei4-Rec114) that is required for meiotic double strand DNA break formation. Rec107 increases in abundance and is phosphorylated during the prophase phase of cell division [ ]. Rec107 is not required for mitosis and mitotic DNA repair mechanisms [ ].

[ "GO:0007131", "GO:0000794" ]

[ "reciprocal meiotic recombination", "condensed nuclear chromosome" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09074" ]

[ "Mer2" ]

[ 78 ]

1

[]

0

[]

0

[ "PUB00035420" ]

[ "16783010" ]

[ "Saccharomyces cerevisiae Mer2, Mei4 and Rec114 form a complex required for meiotic double-strand break formation." ]

[ 2006 ]

1

[]

0

null

[ "Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)", "Saccharomycotina" ]

[ 1, 77 ]

2

[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1 ]

1

true

Family

Recombination protein 107

Rec107

6

IPR015160

15,160

Heat-stable enterotoxin B, secretory

STb_secrete

Family

11

false

Members of this family assume a helical secondary structure, with two α helices forming a disulphide cross-linked α-helical hairpin. The disulphide bonds are crucial for the toxic activity of the protein, and are required for maintenance of the tertiary structure, and subsequent interaction with the particulate form of...

[]

0

[ "PFAM" ]

[ "PF09075" ]

[ "STb_secrete" ]

[ 11 ]

1

[]

0

[ "1ehs" ]

1

[ "PUB00035471" ]

[ "8528070" ]

[ "The structure of Escherichia coli heat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism." ]

[ 1995 ]

1

[]

0

null

[ "Enterobacterales" ]

[ 11 ]

1

[]

0

true

Family

Heat-stable enterotoxin B, secretory

STb_secrete

5

IPR015161

15,161

Streptomyces killer toxin-like, beta/gamma crystallin

Sklp_toxin_b/g_crystallin

Domain

366

false

This domain consists of a beta-gamma-crystallin fold [ , ], wherein nine β-strands are connected by loop, and are separated into two sheets, each sheet forming the Greek key motif. The two Greek key motifs face each other in the global topology. The three-dimensional structure of the molecule is a 'sandwich'-shaped β-b...

[]

0

[ "PFAM" ]

[ "PF09076" ]

[ "Crystall_2" ]

[ 366 ]

1

[]

0

[ "1f53", "1g6e", "1gh5" ]

3

[ "PUB00025140", "PUB00035465", "PUB00066679" ]

[ "11350173", "11114251", "10601197" ]

[ "Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901.", "NMR structure of Streptomyces killer toxin-like protein, SKLP: further evidence for the wide distribution of single-domain betagamma-crystallin superfamily proteins.", "Characterization of a n...

[ 2001, 2001, 1999 ]

3

[]

0

null

[ "Bacillati", "Metarhizium" ]

[ 361, 5 ]

2

[]

0

true

Domain

Streptomyces killer toxin-like, beta/gamma crystallin

Sklp_toxin_b/g_crystallin

1

IPR015162

15,162

CheY binding

CheY-binding

Domain

2,474

false

The CheY binding domain is found in the response regulator histidine kinase CheA. It adopts a secondary structure consisting of an open-face β/α sandwich, with four antiparallel β-strands and two α-helices. It binds to a corresponding domain on CheY, with subsequent phosphorylation of the CheY Asp57 residue, and activa...

[]

0

[ "PFAM" ]

[ "PF09078" ]

[ "CheY-binding" ]

[ 2474 ]

1

[ "EC" ]

[ "2.7.13.3" ]

[ "EC:2.7.13.3" ]

1

[ "1a0o", "1eay", "1ffg", "1ffs", "1ffw", "1fwp", "2lp4", "6s1k" ]

8

[ "PUB00021590" ]

[ "11134926" ]

[ "Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex." ]

[ 2001 ]

1

[]

0

null

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

[ 2454, 4, 16 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

CheY binding

CheY-binding

4

IPR015167

15,167

Domain of unknown function DUF1923

DUF1923

Domain

7

false

This domain is found in maltosyltransferases, adopting a secondary structure that consists of eight antiparallel β-strands forming an open-sided 'jelly roll' Greek key β-barrel. Their exact function is, as yet, unknown [ ].

[]

0

[ "PFAM" ]

[ "PF09083" ]

[ "DUF1923" ]

[ 7 ]

1

[]

0

[ "1gju", "1gjw" ]

2

[ "PUB00025274" ]

[ "11545590" ]

[ "The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity." ]

[ 2001 ]

1

[]

0

null

[ "Thermotoga" ]

[ 7 ]

1

[]

0

true

Domain

Domain of unknown function DUF1923

DUF1923

1

IPR015168

15,168

SsuA/THI5-like

SsuA/THI5

Domain

67,376

false

This domain is found in NMT1/THI5 family proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine [ , , ]. This domain is also found in aliphatic sulfonates-binding protein SsuA, which is part of a transport system for aliphatic sulfonates [ ].

[]

0

[ "PFAM" ]

[ "PF09084" ]

[ "NMT1" ]

[ 67376 ]

1

[]

0

[ "2x26", "3e4r", "3ix1", "3ksj", "3ksx", "3uif", "4esw", "4esx", "4h65", "4h67", "4h6d", "4nmy", "9b1u", "9b1v", "9jp7", "9ooz" ]

16

[ "PUB00013474", "PUB00035428", "PUB00035429", "PUB00035430" ]

[ "10506196", "12271461", "2358444", "12777485" ]

[ "The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl.", "Functional analysis of yeast gene families involved in metabolism of vitamins B1 and B6.", "nmt1 of fission yeast. A highly transcribed gene c...

[ 1999, 2002, 1990, 2003 ]

4

[]

0

null

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

[ 435, 64431, 4, 1928, 578 ]

5

[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 1, 1, 4, 1, 1 ]

5

true

Domain

SsuA/THI5-like

SsuA/THI5

3

IPR015169

15,169

Adhesion molecule, immunoglobulin-like

Adhes-Ig-like

Domain

391

false

This domain is found in mucosal vascular addressin cell adhesion molecule 1 proteins (MAdCAM-1). These are cell adhesion molecules expressed on the endothelium in mucosa that guide the specific homing of lymphocytes into mucosal tissues. MAdCAM-1 belongs to a subclass of the immunoglobulin superfamily (IgSF), the membe...

[ "GO:0007155", "GO:0016020" ]

[ "cell adhesion", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09085" ]

[ "Adhes-Ig_like" ]

[ 391 ]

1

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

[ "R-HSA-198933", "R-HSA-216083", "R-MMU-198933", "R-MMU-216083", "R-RNO-198933", "R-RNO-216083" ]

[ "REACTOME:R-HSA-198933", "REACTOME:R-HSA-216083", "REACTOME:R-MMU-198933", "REACTOME:R-MMU-216083", "REACTOME:R-RNO-198933", "REACTOME:R-RNO-216083" ]

6

[ "1bqs", "1gsm", "4hbq", "4hc1", "4hcr", "4hd9", "9p95" ]

7

[ "PUB00034614", "PUB00035353" ]

[ "11807247", "9655832" ]

[ "A reassessment of the MAdCAM-1 structure and its role in integrin recognition.", "The structure of immunoglobulin superfamily domains 1 and 2 of MAdCAM-1 reveals novel features important for integrin recognition." ]

[ 2002, 1998 ]

2

[]

0

null

[ "Euteleostomi" ]

[ 391 ]

1

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

[ 4, 4, 4 ]

3

true

Domain

Adhesion molecule, immunoglobulin-like

Adhes-Ig-like

6

IPR015170

15,170

Protein of unknown function DUF1924, Cytochrome c-type protein SHP-like

DUF1924_SHP

Family

689

false

This family of proteins includes Cytochrome c-type proteins from proteobacteria, such as Cytochrome c-type protein SHP from Rhodobacter sphaeroides ( ), a high-spin cytochrome able to transiently bind oxygen during autoxidation. It is organized into a series of four α-helices and extended loop configuration, showing st...

[]

0

[ "PFAM" ]

[ "PF09086" ]

[ "DUF1924" ]

[ 689 ]

1

[]

0

[ "1dw0", "1dw1", "1dw2", "1dw3", "1e8e", "1gu2", "1oae" ]

7

[ "PUB00024334" ]

[ "10821858" ]

[ "Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides." ]

[ 2000 ]

1

[]

0

null

[ "Potamilus streckersoni", "Pseudomonadati", "metagenomes" ]

[ 1, 664, 24 ]

3

[]

0

true

Family

Protein of unknown function DUF1924, Cytochrome c-type protein SHP-like

DUF1924_SHP

3

IPR015171

15,171

Cyclomaltodextrinase, N-terminal

Cyc-maltodext_N

Domain

2,514

false

This domain is found at the N terminus of cyclomaltodextrinase. The domain assumes a β-sandwich structure composed of the eight antiparallel β-strands. A ten residue linker is also present at the C-terminal end, which connects the N-terminal domain to a distal domain in the protein. This domain participates in oligomer...

[]

0

[ "PFAM" ]

[ "PF09087" ]

[ "Cyc-maltodext_N" ]

[ 2514 ]

1

[]

0

[ "1h3g", "3edd", "3ede", "3edf", "3edj", "3edk", "9fyz" ]

7

[ "PUB00025492", "PUB00074896" ]

[ "12752453", "8955399" ]

[ "Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92.", "Contribution of a neopullulanase, a pullulanase, and an alpha-glucosidase to growth of Bacteroides thetaiotaomicron on starch." ]

[ 2003, 1996 ]

2

[]

0

null

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

[ 2474, 9, 31 ]

3

[]

0

true

Domain

Cyclomaltodextrinase, N-terminal

Cyc-maltodext_N

9

IPR015172

15,172

MIF4G-like, type 1

MIF4G-like_typ-1

Domain

4,706

false

This entry represents an MIF4G-like domain. MIF4G domains share a common structure but can differ in sequence. This entry is designated "type 1", and is found in nuclear cap-binding proteins and eIF4G. The MIF4G domain is a structural motif with an ARM (Armadillo) repeat-type fold, consisting of a 2-layer α/α right-han...

[ "GO:0016070" ]

[ "RNA metabolic process" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF09088" ]

[ "MIF4G_like" ]

[ 4706 ]

1

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

[ "R-CEL-111367", "R-CEL-113418", "R-CEL-159236", "R-CEL-674695", "R-CEL-6803529", "R-CEL-6807505", "R-CEL-72086", "R-CEL-72163", "R-CEL-72165", "R-CEL-72187", "R-CEL-72203", "R-CEL-73856", "R-CEL-77588", "R-CEL-77595", "R-CEL-975956", "R-CEL-975957", "R-CEL-9930044", "R-DDI-111367",...

[ "REACTOME:R-CEL-111367", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-159236", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6803529", "REACTOME:R-CEL-6807505", "REACTOME:R-CEL-72086", "REACTOME:R-CEL-72163", "REACTOME:R-CEL-72165", "REACTOME:R-CEL-72187", "REACTOME:R-CEL-72203", "REACTOME:R-CEL-73856"...

172

[ "1h2t", "1h2u", "1h2v", "1h6k", "1n52", "1n54", "3fex", "3fey", "5oo6", "5oob", "6d0y", "6n7p", "7abg", "8by6", "8pmp", "8pnt", "8srr", "8suy", "9hfl" ]

19

[ "PUB00025544", "PUB00035800", "PUB00035801", "PUB00035802" ]

[ "11545740", "10958635", "16043498", "16156639" ]

[ "Crystal structure of the human nuclear cap binding complex.", "Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.", "Specificity of recognition of mRNA 5' cap by human nuclear cap-binding complex.", "eIF4G and CBP80 s...

[ 2001, 2000, 2005, 2005 ]

4

[]

0

null

[ "Eukaryota" ]

[ 4706 ]

1

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

[ 6, 1, 2, 3, 1, 2, 1, 2, 3, 1, 1, 18 ]

12

true

Domain

MIF4G-like, type 1

MIF4G-like_typ-1

3

IPR015173

15,173

Bacteriophage T4, Gp12

Phage_T4_Gp12

Domain

189

false

This domain adopts a right-handed triple-stranded β-helix fold, and is found in the central region of the phage short tail fibre protein Gp12 [ ].

[ "GO:0098024" ]

[ "virus tail, fiber" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF09089" ]

[ "gp12-short_mid" ]

[ 189 ]

1

[]

0

[ "1pdi", "5iv5", "5lye" ]

3

[ "PUB00025550" ]

[ "11743729" ]

[ "Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre." ]

[ 2001 ]

1

[]

0

null

[ "Viruses" ]

[ 189 ]

1

[]

0

true

Domain

Bacteriophage T4, Gp12

Phage_T4_Gp12

2

IPR015174

15,174

MIF4G-like, type 2

MIF4G-like_typ-2

Domain

4,792

false

This entry represents an MIF4G-like domain. MIF4G domains share a common structure but can differ in sequence. This entry is designated "type 2", and is found in nuclear cap-binding proteins and eIF4G. The MIF4G domain is a structural motif with an ARM (Armadillo) repeat-type fold, consisting of a 2-layer α/α right-han...

[ "GO:0016070" ]

[ "RNA metabolic process" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF09090" ]

[ "MIF4G_like_2" ]

[ 4792 ]

1

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

[ "R-CEL-111367", "R-CEL-113418", "R-CEL-159236", "R-CEL-674695", "R-CEL-6803529", "R-CEL-6807505", "R-CEL-72086", "R-CEL-72163", "R-CEL-72165", "R-CEL-72187", "R-CEL-72203", "R-CEL-73856", "R-CEL-77588", "R-CEL-77595", "R-CEL-975956", "R-CEL-975957", "R-CEL-9930044", "R-DDI-111367",...

[ "REACTOME:R-CEL-111367", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-159236", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6803529", "REACTOME:R-CEL-6807505", "REACTOME:R-CEL-72086", "REACTOME:R-CEL-72163", "REACTOME:R-CEL-72165", "REACTOME:R-CEL-72187", "REACTOME:R-CEL-72203", "REACTOME:R-CEL-73856"...

172

[ "1h2t", "1h2u", "1h2v", "1h6k", "1n52", "1n54", "3fex", "3fey", "5oo6", "5oob", "6d0y", "6n7p", "7abg", "8by6", "8pmp", "8pnt", "8srr", "8suy", "9hfl" ]

19

[ "PUB00025544", "PUB00035800", "PUB00035801", "PUB00035802" ]

[ "11545740", "10958635", "16043498", "16156639" ]

[ "Crystal structure of the human nuclear cap binding complex.", "Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.", "Specificity of recognition of mRNA 5' cap by human nuclear cap-binding complex.", "eIF4G and CBP80 s...

[ 2001, 2000, 2005, 2005 ]

4

[]

0

null

[ "Aerococcus viridans", "Eukaryota" ]

[ 1, 4791 ]

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...

[ 6, 1, 2, 3, 2, 1, 1, 3, 4, 1, 1, 19 ]

12

true

Domain

MIF4G-like, type 2

MIF4G-like_typ-2

8

IPR015176

15,176

Lyase, N-terminal

Lyase_N

Domain

1,042

false

This entry represents a domain predominantly found in chondroitin ABC lyase I, adopting a jelly-roll fold topology consisting of a two-layered bent β-sheet sandwich with one short α-helix. The convex β sheet is composed of five antiparallel strands, whilst the concave β-sheet contains five antiparallel β-strands with a...

[]

0

[ "PFAM" ]

[ "PF09092" ]

[ "Lyase_N" ]

[ 1042 ]

1

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

[ "4.2.2.21", "PWY-6572", "PWY-7646" ]

[ "EC:4.2.2.21", "METACYC:PWY-6572", "METACYC:PWY-7646" ]

3

[ "1hn0", "2q1f", "7eip", "7eiq", "7eir", "7eis", "7yke" ]

7

[ "PUB00014313" ]

[ "12706721" ]

[ "Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution." ]

[ 2003 ]

1

[]

0

null

[ "Bacteria", "Eumetazoa", "metagenomes" ]

[ 936, 96, 10 ]

3

[]

0

true

Domain

Lyase, N-terminal

Lyase_N

9

IPR015177

15,177

Lyase, catalytic

Lyase_catalyt

Domain

1,149

false

This domain is predominantly found in chondroitin ABC lyase I, adopting a helical structure, with fifteen α-helices which are at least two turns long and several short helical turns. The bulk of the domain is formed by ten α-helices forming five hairpin-like pairs and arranged into an incomplete toroid, the (α/α)5 fold...

[]

0

[ "PFAM" ]

[ "PF09093" ]

[ "Lyase_catalyt" ]

[ 1149 ]

1

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

[ "4.2.2.21", "PWY-6572", "PWY-7646" ]

[ "EC:4.2.2.21", "METACYC:PWY-6572", "METACYC:PWY-7646" ]

3

[ "1hn0", "2q1f", "7eip", "7eiq", "7eir", "7eis", "7yke" ]

7

[ "PUB00014313" ]

[ "12706721" ]

[ "Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution." ]

[ 2003 ]

1

[]

0

null

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

[ 1035, 101, 13 ]

3

[]

0

true

Domain

Lyase, catalytic

Lyase_catalyt

6

IPR015178

15,178

Alpha-amylase/4-alpha-glucanotransferase, central domain

A-amylase/a-glucTrfase_central

Domain

575

false

This entry represents a domain found in prokaryotic alpha-amylase ( ) and 4-alpha-glucanotransferase ( ). It is adjacent to the C-terminal domain (see ). This domain adopts an immunoglobulin/albumin-binding domain-like fold, with a bundle of three α-helices [ ]. The exact function of this domain is, as yet, unknown. Al...

[]

0

[ "PFAM" ]

[ "PF09094" ]

[ "AmyA-A_glucT_m" ]

[ 575 ]

1

[ "EC" ]

[ "3.2.1.1" ]

[ "EC:3.2.1.1" ]

1

[ "1k1w", "1k1x", "1k1y" ]

3

[ "PUB00014074", "PUB00027666" ]

[ "12618437", "11141191" ]

[ "Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor.", "Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold." ]

[ 2003, 2001 ]

2

[]

0

null

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

[ 66, 468, 41 ]

3

[]

0

true

Domain

Alpha-amylase/4-alpha-glucanotransferase, central domain

A-amylase/a-glucTrfase_central

8

IPR015179

15,179

Alpha-amylase/4-alpha-glucanotransferase, C-terminal

A-amylase/a-glucTrfase_C

Domain

630

false

This entry represents a domain found in prokaryotic alpha-amylase ( ) and 4-alpha-glucanotransferase ( ). This domain adopts a β-sandwich fold, in which two layers of anti-parallel β-sheets are arranged in a nearly parallel fashion. The exact function of this domain is, as yet, unknown, however it has been proposed tha...

[ "GO:0003824", "GO:0030246", "GO:0005975" ]

[ "catalytic activity", "carbohydrate binding", "carbohydrate metabolic process" ]

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

3

[ "PFAM" ]

[ "PF09095" ]

[ "AmyA-gluTrfs_C" ]

[ 630 ]

1

[ "EC" ]

[ "3.2.1.1" ]

[ "EC:3.2.1.1" ]

1

[ "1k1w", "1k1x", "1k1y" ]

3

[ "PUB00014074", "PUB00027666" ]

[ "12618437", "11141191" ]

[ "Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor.", "Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold." ]

[ 2003, 2001 ]

2

[]

0

null

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

[ 68, 519, 43 ]

3

[]

0

true

Domain

Alpha-amylase/4-alpha-glucanotransferase, C-terminal

A-amylase/a-glucTrfase_C

5

IPR015180

15,180

Bacteriophage T4, Gp27, baseplate hub, C-terminal

Phage_T4_Gp27_C

Domain

275

false

This domain adopts a β barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. It is found at the C terminus of the Gp27 protein; a structural component of the viral baseplate [ ].

[ "GO:0098025" ]

[ "virus tail, baseplate" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF09096" ]

[ "Phage-tail_2" ]

[ 275 ]

1

[]

0

[ "1k28", "1pdj", "1wth", "2z6b", "5iv5", "9f4a", "9f4b" ]

7

[ "PUB00012803" ]

[ "11823865" ]

[ "Structure of the cell-puncturing device of bacteriophage T4." ]

[ 2002 ]

1

[]

0

null

[ "Viruses" ]

[ 275 ]

1

[]

0

true

Domain

Bacteriophage T4, Gp27, baseplate hub, C-terminal

Phage_T4_Gp27_C

5

IPR015181

15,181

Bacteriophage T4, Gp27, baseplate hub, N-terminal

Phage_T4_Gp27_N

Domain

307

false

This domain adopts a β barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. It is found at the N terminus of the Gp27 protein; a structural component of the viral baseplate [ ].

[]

0

[ "PFAM" ]

[ "PF09097" ]

[ "Phage-tail_1" ]

[ 307 ]

1

[]

0

[ "1k28", "1pdj", "1wth", "2z6b", "5iv5", "9f4a", "9f4b" ]

7

[ "PUB00012803" ]

[ "11823865" ]

[ "Structure of the cell-puncturing device of bacteriophage T4." ]

[ 2002 ]

1

[]

0

null

[ "Pseudomonadati", "Viruses" ]

[ 2, 305 ]

2

[]

0

true

Domain

Bacteriophage T4, Gp27, baseplate hub, N-terminal

Phage_T4_Gp27_N

3

IPR015183

15,183

Quinohemoprotein amine dehydrogenase, alpha subunit domain III

QH-AmDH_asu_dom_III

Domain

570

false

Members of this family, which are predominantly found in the prokaryotic protein quinohemoprotein amine dehydrogenase, adopt an immunoglobulin-like β-sandwich fold, with seven strands arranged into two β sheets; the fold is possibly related to the immunoglobulin and/or fibronectin type III superfamilies. The precise fu...

[]

0

[ "PFAM" ]

[ "PF09099" ]

[ "Qn_am_d_aIII" ]

[ 570 ]

1

[]

0

[ "1jju", "1jmx", "1jmz", "1pby" ]

4

[ "PUB00013277", "PUB00022422" ]

[ "11704672", "12925784" ]

[ "Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges.", "Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution." ]

[ 2002, 2003 ]

2

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 555, 15 ]

2

[]

0

true

Domain

Quinohemoprotein amine dehydrogenase, alpha subunit domain III

QH-AmDH_asu_dom_III

4

IPR015184

15,184

Quinohemoprotein amine dehydrogenase, alpha subunit domain IV

QH-AmDH_asu_dom_IV

Domain

554

false

Members of this entry, which are predominantly found in the prokaryotic protein quinohemoprotein amine dehydrogenase, adopt an immunoglobulin-like β-sandwich fold, with seven strands arranged into two β sheets; the fold is possibly related to the immunoglobulin and/or fibronectin type III superfamilies. The precise fun...

[]

0

[ "PFAM" ]

[ "PF09100" ]

[ "Qn_am_d_aIV" ]

[ 554 ]

1

[]

0

[ "1jju", "1jmx", "1jmz", "1pby" ]

4

[ "PUB00013277", "PUB00022422" ]

[ "11704672", "12925784" ]

[ "Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges.", "Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution." ]

[ 2002, 2003 ]

2

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 541, 13 ]

2

[]

0

true

Domain

Quinohemoprotein amine dehydrogenase, alpha subunit domain IV

QH-AmDH_asu_dom_IV

3

IPR015185

15,185

Exotoxin A, binding

Exotox-A_bind

Domain

203

false

This domain is found in Pseudomonas aeruginosa exotoxin A, and is responsible for binding of the toxin to the alpha-2-macroglobulin receptor, with subsequent internalisation into endosomes. It adopts a thirteen-strand antiparallel β jelly roll topology, which belongs to the concanavalin A-like lectins/glucanases fold s...

[]

0

[ "PFAM" ]

[ "PF09101" ]

[ "Exotox-A_bind" ]

[ 203 ]

1

[]

0

[ "1ikp", "1ikq", "2q5t", "3q9o", "6z5h", "9g7m", "9g7n", "9g7o", "9g7p" ]

9

[ "PUB00010690" ]

[ "11734000" ]

[ "Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria" ]

[ 203 ]

1

[]

0

true

Domain

Exotoxin A, binding

Exotox-A_bind

2

IPR015186

15,186

Exotoxin A, middle domain

Exotox-A_middle_dom

Domain

111

false

This domain, found in Pseudomonas aeruginosa exotoxin A, is responsible for transmembrane targeting of the toxin, as well as transmembrane translocation of the catalytic domain into the cytoplasmic compartment. A furin cleavage site is present within the domain: cleavage generates a 37kDa carboxy-terminal fragment, whi...

[]

0

[ "PFAM" ]

[ "PF09102" ]

[ "Exotox-A_target" ]

[ 111 ]

1

[]

0

[ "1ikp", "1ikq", "2q5t", "3q9o", "6z5h", "9g7m", "9g7n", "9g7o", "9g7p" ]

9

[ "PUB00010690", "PUB00048870" ]

[ "11734000", "18276581" ]

[ "Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity.", "Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae." ]

[ 2001, 2008 ]

2

[]

0

null

[ "Bacteria" ]

[ 111 ]

1

[]

0

true

Domain

Exotoxin A, middle domain

Exotox-A_middle_dom

1

IPR015187

15,187

BRCA2, OB1

BRCA2_OB_1

Domain

3,124

false

BRCA2 participates in homologous recombination-mediated repair of double-strand DNA breaks [ , ]. It stimulates the displacement of Replication protein A (RPA), the most abundant eukaryotic ssDNA binding protein [ ]. Mutations that map throughout the BRCA2 protein are associated with breast cancer susceptibility [ ]. B...

[ "GO:0000724" ]

[ "double-strand break repair via homologous recombination" ]

[ "biological_process" ]

1

[ "PFAM", "CDD" ]

[ "PF09103", "cd04493" ]

[ "BRCA-2_OB1", "BRCA2DBD_OB1" ]

[ 3123, 2227 ]

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-HSA-5685939", "R-HSA-5685942", "R-HSA-5693554", "R-HSA-5693568", "R-HSA-5693579", "R-HSA-5693616", "R-HSA-912446", "R-HSA-9701192", "R-HSA-9704331", "R-HSA-9704646", "R-HSA-9709275", "R-HSA-9709570", "R-HSA-9709603", "R-HSA-9763198", "R-MMU-5685939", "R-MMU-5685942", "R-MMU-569356...

[ "REACTOME:R-HSA-5685939", "REACTOME:R-HSA-5685942", "REACTOME:R-HSA-5693554", "REACTOME:R-HSA-5693568", "REACTOME:R-HSA-5693579", "REACTOME:R-HSA-5693616", "REACTOME:R-HSA-912446", "REACTOME:R-HSA-9701192", "REACTOME:R-HSA-9704331", "REACTOME:R-HSA-9704646", "REACTOME:R-HSA-9709275", "REACTOME...

24

[ "1iyj", "1miu", "1mje" ]

3

[ "PUB00016304", "PUB00021040", "PUB00027524", "PUB00066909", "PUB00086003" ]

[ "15102447", "12228710", "12442171", "20513136", "12727514" ]

[ "From RPA to BRCA2: lessons from single-stranded DNA binding by the OB-fold.", "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure.", "Insights into DNA recombination from the structure of a RAD51-BRCA2 complex.", "Detection of splicing aberrations caused by BRCA1 and BRCA2 sequ...

[ 2004, 2002, 2002, 2010, 2003 ]

5

[]

0

null

[ "Eukaryota" ]

[ 3124 ]

1

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

[ 14, 3, 24, 4, 3, 6, 25 ]

7

true

Domain

BRCA2, OB1

BRCA2_OB_1

8

IPR015188

15,188

BRCA2, OB3

BRCA2_OB_3

Domain

1,397

false

BRCA2 participates in homologous recombination-mediated repair of double-strand DNA breaks [ , ]. It stimulates the displacement of Replication protein A (RPA), the most abundant eukaryotic ssDNA binding protein [ ]. Mutations that map throughout the BRCA2 protein are associated with breast cancer susceptibility [ ]. B...

[]

0

[ "PFAM", "CDD" ]

[ "PF09104", "cd04495" ]

[ "BRCA-2_OB3", "BRCA2DBD_OB3" ]

[ 1397, 513 ]

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-HSA-5685939", "R-HSA-5685942", "R-HSA-5693554", "R-HSA-5693568", "R-HSA-5693579", "R-HSA-5693616", "R-HSA-912446", "R-HSA-9701192", "R-HSA-9704331", "R-HSA-9704646", "R-HSA-9709275", "R-HSA-9709570", "R-HSA-9709603", "R-HSA-9763198", "R-MMU-5685939", "R-MMU-5685942", "R-MMU-569356...

[ "REACTOME:R-HSA-5685939", "REACTOME:R-HSA-5685942", "REACTOME:R-HSA-5693554", "REACTOME:R-HSA-5693568", "REACTOME:R-HSA-5693579", "REACTOME:R-HSA-5693616", "REACTOME:R-HSA-912446", "REACTOME:R-HSA-9701192", "REACTOME:R-HSA-9704331", "REACTOME:R-HSA-9704646", "REACTOME:R-HSA-9709275", "REACTOME...

24

[ "1iyj", "1miu", "1mje" ]

3

[ "PUB00016304", "PUB00021040", "PUB00027524", "PUB00066909", "PUB00086003" ]

[ "15102447", "12228710", "12442171", "20513136", "12727514" ]

[ "From RPA to BRCA2: lessons from single-stranded DNA binding by the OB-fold.", "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure.", "Insights into DNA recombination from the structure of a RAD51-BRCA2 complex.", "Detection of splicing aberrations caused by BRCA1 and BRCA2 sequ...

[ 2004, 2002, 2002, 2010, 2003 ]

5

[]

0

null

[ "Eukaryota" ]

[ 1397 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus" ]

[ 3, 14, 3, 2, 6 ]

5

true

Domain

BRCA2, OB3

BRCA2_OB_3

9

IPR015189

15,189

Translation elongation factor SelB, winged helix, type 1

Elong_fac_SelB-wing-hlx_typ-1

Domain

11

false

This entry represents a domain with a winged helix-type fold, which consists of a closed 3-helical bundle with a right-handed twist, and a small β-sheet wing [ ]. Different winged helix domains share a common structure, but can differ in sequence. This entry is designated "type 1".

[]

0

[ "PFAM" ]

[ "PF09105" ]

[ "WHD_1st_SelB" ]

[ 11 ]

1

[]

0

[ "1lva", "2ply", "2uwm", "2v9v" ]

4

[ "PUB00022119", "PUB00033963" ]

[ "12145214", "15665870" ]

[ "Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.", "Structural basis for mRNA recognition by elongation factor SelB." ]

[ 2002, 2005 ]

2

[]

0

null

[ "Neomoorellaceae" ]

[ 11 ]

1

[]

0

true

Domain

Translation elongation factor SelB, winged helix, type 1

Elong_fac_SelB-wing-hlx_typ-1

3

IPR015190

15,190

Translation elongation factor SelB, winged helix, type 2

Elong_fac_SelB-wing-hlx_typ-2

Domain

4,837

false

This entry represents a domain with a winged helix-type fold, which consists of a closed 3-helical bundle with a right-handed twist, and a small β-sheet wing [ ]. Different winged helix domains share a common structure, but can differ in sequence. This entry is designated "type 2".

[ "GO:0003723", "GO:0003746", "GO:0005525", "GO:0001514", "GO:0005737" ]

[ "RNA binding", "translation elongation factor activity", "GTP binding", "selenocysteine incorporation", "cytoplasm" ]

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

5

[ "PFAM" ]

[ "PF09106" ]

[ "WHD_2nd_SelB" ]

[ 4837 ]

1

[]

0

[ "1lva", "2ply", "2uwm", "2v9v", "5lzb", "5lzc", "5lzd" ]

7

[ "PUB00022119", "PUB00033963" ]

[ "12145214", "15665870" ]

[ "Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.", "Structural basis for mRNA recognition by elongation factor SelB." ]

[ 2002, 2005 ]

2

[]

0

null

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

[ 4758, 14, 65 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Translation elongation factor SelB, winged helix, type 2

Elong_fac_SelB-wing-hlx_typ-2

9

IPR015191

15,191

Elongation factor SelB, fourth winged-helix domain

SelB_WHD4

Domain

7,239

false

This domain is found in Elongation factor SelB from Moorella thermoacetica ( ) and similar bacterial proteins. SelB is a selenocysteine(Sec)-specific elongation factor that brings the selenocysteinyl-tRNA(Sec) to the ribosome. It consists of three EF-Tu-like domains followed by four winged-helix domains (WHD1-4). This ...

[ "GO:0003723", "GO:0003746", "GO:0005525", "GO:0001514", "GO:0005737" ]

[ "RNA binding", "translation elongation factor activity", "GTP binding", "selenocysteine incorporation", "cytoplasm" ]

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

5

[ "PFAM" ]

[ "PF09107" ]

[ "WHD_3rd_SelB" ]

[ 7239 ]

1

[]

0

[ "1lva", "1wsu", "2pjp", "2ply", "2uwm", "4zu9", "5lzb", "5lzc", "5lzd" ]

9

[ "PUB00022119", "PUB00033963" ]

[ "12145214", "15665870" ]

[ "Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.", "Structural basis for mRNA recognition by elongation factor SelB." ]

[ 2002, 2005 ]

2

[]

0

null

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

[ 7067, 17, 155 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Elongation factor SelB, fourth winged-helix domain

SelB_WHD4

9

IPR015192

15,192

Switch protein XOL-1, N-terminal

Xol-1_N

Domain

31

false

This domain, found in sex-determining protein Xol-1, adopts a secondary structure consisting of five α helices and six antiparallel β sheets, in a β-α-β-β-β-α-β-α-α-α-β arrangement. The fold of this family is similar to that found in ribosomal protein S5 domain 2-like [ ]. The active site of the enzyme is found at the ...

[]

0

[ "PFAM" ]

[ "PF09108" ]

[ "Xol-1_N" ]

[ 31 ]

1

[]

0

[ "1mg7" ]

1

[ "PUB00016021" ]

[ "12672694" ]

[ "XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators." ]

[ 2003 ]

1

[]

0

null

[ "Caenorhabditis" ]

[ 31 ]

1

[ "Caenorhabditis elegans" ]

[ 1 ]

1

true

Domain

Switch protein XOL-1, N-terminal

Xol-1_N

7

IPR015193

15,193

Switch protein XOL-1, GHMP-like

Xol-1_GHMP-like

Domain

21

false

This domain, found in sex-determining protein Xol-1, adopts a secondary structure consisting of five α helices and seven antiparallel β sheets, in a β-α-β-α-α-α-β-β-α-β-β-β arrangement. The fold of this family is structurally similar to that found in the C-terminal domain of GHMP Kinase [ ]. The active site of the enzy...

[]

0

[ "PFAM" ]

[ "PF09109" ]

[ "Xol-1_GHMP-like" ]

[ 21 ]

1

[]

0

[ "1mg7" ]

1

[ "PUB00016021" ]

[ "12672694" ]

[ "XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators." ]

[ 2003 ]

1

[]

0

null

[ "Caenorhabditis" ]

[ 21 ]

1

[ "Caenorhabditis elegans" ]

[ 1 ]

1

true

Domain

Switch protein XOL-1, GHMP-like

Xol-1_GHMP-like

6

IPR015194

15,194

ISWI, HAND domain

ISWI_HAND-dom

Domain

6,623

false

Nucleosome remodelling is an energy-dependent process that alters histone-DNA interactions within nucleosomes, thereby rendering nucleosomal DNA accessible to regulatory factors. The ATPases involved belong to the SWI2/SNF2 subfamily of DEAD/H-helicases, which contain a conserved ATPase domain characterised by seven mo...

[ "GO:0003677", "GO:0031491", "GO:0006338" ]

[ "DNA binding", "nucleosome binding", "chromatin remodeling" ]

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

3

[ "PFAM" ]

[ "PF09110" ]

[ "HAND" ]

[ 6623 ]

1

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

[ "3.6.4.-", "PWY-7250", "R-CEL-5250924", "R-HSA-427413", "R-HSA-5250924", "R-HSA-5693565", "R-HSA-606279", "R-MMU-5250924", "R-MMU-5693565", "R-MMU-606279" ]

[ "EC:3.6.4.-", "METACYC:PWY-7250", "REACTOME:R-CEL-5250924", "REACTOME:R-HSA-427413", "REACTOME:R-HSA-5250924", "REACTOME:R-HSA-5693565", "REACTOME:R-HSA-606279", "REACTOME:R-MMU-5250924", "REACTOME:R-MMU-5693565", "REACTOME:R-MMU-606279" ]

10

[ "1ofc", "2nog", "2y9y", "2y9z", "5jxr", "6iro", "6jyl", "6k1p", "7x3t", "7x3w", "7x3x", "8v4y", "8v6v", "8v7l", "9e1l", "9e1m", "9e1n", "9e1o", "9e1p", "9e1q", "9e1r", "9e1u", "9e1v", "9e1w", "9e1x", "9jnp", "9jnt", "9jnu", "9jnv", "9jnw", "9jnx", "9jnz"...

36

[ "PUB00029414", "PUB00097421" ]

[ "14536084", "24414837" ]

[ "Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.", "Regulation of ISWI chromatin remodelling activity." ]

[ 2003, 2014 ]

2

[]

0

null

[ "Eukaryota" ]

[ 6623 ]

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...

[ 11, 1, 5, 2, 7, 4, 1, 3, 9, 2, 40 ]

11

true

Domain

ISWI, HAND domain

ISWI_HAND-dom

3

IPR015195

15,195

SLIDE domain

SLIDE

Domain

7,108

false

The SLIDE domain adopts a secondary structure comprising a main core of three α-helices. It has a role in DNA binding, contacting DNA target sites similar to c-Myb repeats or homeodomains [ , ].

[ "GO:0003677", "GO:0006338", "GO:0005634" ]

[ "DNA binding", "chromatin remodeling", "nucleus" ]

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

3

[ "PFAM" ]

[ "PF09111" ]

[ "SLIDE" ]

[ 7108 ]

1

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

[ "3.6.4.-", "PWY-7250", "R-CEL-5250924", "R-HSA-427413", "R-HSA-5250924", "R-HSA-5693565", "R-HSA-606279", "R-MMU-5250924", "R-MMU-5693565", "R-MMU-606279" ]

[ "EC:3.6.4.-", "METACYC:PWY-7250", "REACTOME:R-CEL-5250924", "REACTOME:R-HSA-427413", "REACTOME:R-HSA-5250924", "REACTOME:R-HSA-5693565", "REACTOME:R-HSA-606279", "REACTOME:R-MMU-5250924", "REACTOME:R-MMU-5693565", "REACTOME:R-MMU-606279" ]

10

[ "1ofc", "2y9y", "2y9z", "6iro", "6jyl", "6k1p", "7x3t", "7x3w", "7x3x", "8v4y", "8v6v", "8v7l", "9e1l", "9e1m", "9e1n", "9e1o", "9e1p", "9e1q", "9e1r", "9e1u", "9e1v", "9e1w", "9e1x", "9jnp", "9jnt", "9jnu", "9jnv", "9jnw", "9jnx", "9jnz", "9jo2", "9jo5"...

34

[ "PUB00029414", "PUB00097421" ]

[ "14536084", "24414837" ]

[ "Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.", "Regulation of ISWI chromatin remodelling activity." ]

[ 2003, 2014 ]

2

[]

0

null

[ "Eukaryota" ]

[ 7108 ]

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...

[ 11, 1, 5, 2, 7, 4, 1, 3, 10, 2, 37 ]

11

true

Domain

SLIDE domain

SLIDE

5