LiteFold/InterPro · Datasets at Hugging Face

IPR015308

15,308

Bubble protein

Bubble

Family

113

false

This family includes Penicillium brevicompactum bubble protein (BP) and similar proteins. Bubble protein (BP) is a small cysteine-rich protein that is a member of the growing class of defensins, and may act as a toxin [ ]. Studies show that P. brevicompactum BP inhibits growth of the yeast Saccharomyces cerevisiae in a...

[]

0

[ "PFAM", "CDD" ]

[ "PF09227", "cd22742" ]

[ "Bubble", "BUBL-like" ]

[ 113, 91 ]

2

[]

0

[ "1uoy", "6trm" ]

2

[ "PUB00031842", "PUB00103809" ]

[ "14747700", "21906643" ]

[ "Solving the structure of the bubble protein using the anomalous sulfur signal from single-crystal in-house Cu Kalpha diffraction data only.", "Properties of the bubble protein, a defensin and an abundant component of a fungal exudate." ]

[ 2004, 2011 ]

2

[]

0

null

[ "leotiomyceta" ]

[ 113 ]

1

[]

0

true

Family

Bubble protein

Bubble

5

IPR015310

15,310

Activator of Hsp90 ATPase AHSA1-like, N-terminal

AHSA1-like_N

Domain

6,826

false

This entry includes a group of heat shock protein interacting proteins, including AHSA1/2 from animals and Aha1/Hch1 from budding yeasts, and it represents a domain found at the N-terminal of Aha1 and AHSA1/2, while in Hch1 is the only domain. Aha1 adopts a secondary structure consisting of an N-terminal α-helix leadin...

[ "GO:0001671", "GO:0051087" ]

[ "ATPase activator activity", "protein-folding chaperone binding" ]

[ "molecular_function", "molecular_function" ]

2

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

[ "PF09229", "PTHR13009", "SM01000" ]

[ "Aha1_N", "", "Aha1_N" ]

[ 6796, 6246, 6448 ]

3

[]

0

[ "1usu", "1usv", "3n72", "6xlb", "6xld", "6xle", "6xlf", "6xlg", "6xlh", "7dmd", "7dme" ]

11

[ "PUB00020832", "PUB00020879", "PUB00020903", "PUB00035354", "PUB00090459", "PUB00102524" ]

[ "11554768", "12504007", "12604615", "15039704", "23396352", "33808352" ]

[ "p38: A novel protein that associates with the vesicular stomatitis virus glycoprotein.", "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.", "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecul...

[ 2001, 2002, 2003, 2004, 2013, 2021 ]

6

[]

0

null

[ "Croceibacter atlanticus (strain ATCC BAA-628 / JCM 21780 / CIP 108009 / IAM 15332 / KCTC 12090 / HTCC2559)", "Eukaryota" ]

[ 1, 6825 ]

2

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

[ 8, 1, 3, 1, 5, 6, 1, 7, 7, 2, 1, 13 ]

12

true

Domain

Activator of Hsp90 ATPase AHSA1-like, N-terminal

AHSA1-like_N

9

IPR015311

15,311

DNA fragmentation factor 40, C-terminal

DFF40_C

Domain

1,446

false

Apoptosis, or programmed cell death (PCD), is a common and evolutionarily conserved property of all metazoans [ ]. In many biological processes, apoptosis is required to eliminate supernumerary or dangerous (such as pre-cancerous) cells and to promote normal development. Dysregulation of apoptosis can, therefore, contr...

[ "GO:0016787", "GO:0006309", "GO:0005634", "GO:0005737" ]

[ "hydrolase activity", "apoptotic DNA fragmentation", "nucleus", "cytoplasm" ]

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

4

[ "PFAM" ]

[ "PF09230" ]

[ "DFF40" ]

[ 1446 ]

1

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

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

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

3

[ "1v0d" ]

1

[ "PUB00017281", "PUB00043549", "PUB00043550", "PUB00043551" ]

[ "11341280", "17626049", "15572351", "10318789" ]

[ "Apoptosis. Death of a monopoly?", "Engineered apoptotic nucleases for chromatin research.", "Interaction of DNA fragmentation factor (DFF) with DNA reveals an unprecedented mechanism for nuclease inhibition and suggests that DFF can be activated in a DNA-bound state.", "Activation of the apoptotic endonuclea...

[ 2001, 2007, 2005, 1999 ]

4

[]

0

null

[ "Eumetazoa" ]

[ 1446 ]

1

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

[ 1, 2, 3, 4, 5 ]

5

true

Domain

DNA fragmentation factor 40, C-terminal

DFF40_C

7

IPR015312

15,312

Inner layer core protein VP3, Phytoreovirus

Innr_layr_core_VP3_Phytoreovir

Family

10

false

Members of this family are core structural proteins found in the double-stranded RNA virus Phytoreovirus. They are large proteins without apparent domain division, with a number of all-alpha regions and one all beta domain near the C-terminal end [ ].

[ "GO:0005198" ]

[ "structural molecule activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09231" ]

[ "RDV-p3" ]

[ 10 ]

1

[]

0

[ "1uf2" ]

1

[ "PUB00031754" ]

[ "14527391" ]

[ "The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins." ]

[ 2003 ]

1

[]

0

null

[ "Laodelphax striatellus", "Riboviria" ]

[ 1, 9 ]

2

[]

0

true

Family

Inner layer core protein VP3, Phytoreovirus

Innr_layr_core_VP3_Phytoreovir

5

IPR015313

15,313

Protein Her-1

Her-1

Family

125

false

Her-1 adopts an all-helical structure with two subdomains: residues 19-80 comprise a left-handed three-helix bundle with an overhand connection between the second and third helices, whilst residues 81-164 comprise a left-handed anti-parallel four-helix bundle in which the first helix consists of four consecutive turns ...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09232", "PTHR37979" ]

[ "Caenor_Her-1", "" ]

[ 125, 88 ]

2

[]

0

[ "1szh" ]

1

[ "PUB00035367" ]

[ "15289613" ]

[ "Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A." ]

[ 2004 ]

1

[]

0

null

[ "Chromadorea" ]

[ 125 ]

1

[ "Caenorhabditis elegans" ]

[ 2 ]

1

true

Family

Protein Her-1

Her-1

7

IPR015314

15,314

Restriction endonuclease, type II, EcoRV

Restrct_endonuc_II_EcoRV

Family

232

false

This entry represents EcoRV prokaryotic restriction endonucleases, which recognise the double-stranded sequence 5'-GATATC-3' and cleave after T-3 [ ]. 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 endonucleolyt...

[]

0

[ "PFAM" ]

[ "PF09233" ]

[ "Endonuc-EcoRV" ]

[ 232 ]

1

[]

0

[ "1az0", "1az3", "1az4", "1b94", "1b95", "1b96", "1b97", "1bgb", "1bss", "1bsu", "1bua", "1eo3", "1eo4", "1eon", "1eoo", "1eop", "1rv5", "1rva", "1rvb", "1rvc", "1rve", "1stx", "1suz", "1sx5", "1sx8", "2b0d", "2b0e", "2ge5", "2rve", "4rve", "5f8a", "5hlk"...

32

[ "PUB00031198", "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707" ]

[ "15170321", "15770420", "14576294", "11827971", "11557805", "15121719", "12665693" ]

[ "DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites.", "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 restriction...

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

7

[]

[ "IPR019755" ]

0

1

0

[ "Bacteria", "Halogranum tailed virus 1", "Metazoa", "Stenosarchaea group", "unclassified sequences" ]

[ 209, 1, 2, 6, 14 ]

5

[]

0

true

Family

Restriction endonuclease, type II, EcoRV

Restrct_endonuc_II_EcoRV

8

IPR015315

15,315

Protein of unknown function DUF1963

DUF1963

Family

5,281

false

This entry is a set of hypothetical proteins. Their function has not been described yet.

[]

0

[ "PFAM" ]

[ "PF09234" ]

[ "DUF1963" ]

[ 5281 ]

1

[]

0

[ "1pv5" ]

1

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "Myoviridae sp. ctkfK18", "metagenomes" ]

[ 5066, 192, 2, 21 ]

4

[]

0

true

Family

Protein of unknown function DUF1963

DUF1963

4

IPR015316

15,316

Ste50, sterile alpha motif

SAM_Ste50

Domain

75

false

Ste50-like proteins have a SAM domain at the N terminus and Ras-associated UBQ superfamily domain at the C terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response, and contribute to cell wall integrity in vegetative cells. Ste50 of S.cerevisiae acts as ...

[]

0

[ "PFAM", "CDD" ]

[ "PF09235", "cd09536" ]

[ "SAM_Ste50p", "SAM_Ste50_fungal" ]

[ 75, 27 ]

2

[]

0

[ "1uqv", "1z1v" ]

2

[ "PUB00029616", "PUB00031861", "PUB00038254", "PUB00038710", "PUB00044414", "PUB00079552", "PUB00079553", "PUB00079554", "PUB00079555" ]

[ "15327964", "14573615", "15544813", "16337230", "16543225", "18431466", "16428446", "1494345", "12764668" ]

[ "The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.", "Structure of the sterile alpha motif (SAM) domain of the Saccharomyces cerevisiae mitogen-activated protein kinase pathway-modulating protein STE50 and analysis of its interaction with the STE11 SAM.", "Soluti...

[ 2004, 2004, 2004, 2006, 2006, 2008, 2006, 1992, 2003 ]

9

[]

0

null

[ "Eukaryota" ]

[ 75 ]

1

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

[ 1 ]

1

true

Domain

Ste50, sterile alpha motif

SAM_Ste50

4

IPR015317

15,317

Alpha-haemoglobin stabilising protein

A_Hb_stabilising_prot

Family

189

false

Alpha-haemoglobin stabilising protein (AHSP) acts a molecular chaperone for free alpha-haemoglobin, preventing the harmful aggregation of alpha-haemoglobin during normal erythroid cell development: it specifically protects free alpha-haemoglobin from precipitation. AHSP adopts a helical secondary structure consisting o...

[ "GO:0030492", "GO:0006457", "GO:0030218", "GO:0050821" ]

[ "hemoglobin binding", "protein folding", "erythrocyte differentiation", "protein stabilization" ]

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

4

[ "PFAM", "PANTHER" ]

[ "PF09236", "PTHR15914" ]

[ "AHSP", "" ]

[ 189, 189 ]

2

[]

0

[ "1w09", "1w0a", "1w0b", "1xzy", "1y01", "1z8u", "3ia3", "3ovu" ]

8

[ "PUB00032142" ]

[ "15178680" ]

[ "NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding." ]

[ 2004 ]

1

[]

0

null

[ "Mammalia" ]

[ 189 ]

1

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

[ 3, 2, 2 ]

3

true

Family

Alpha-haemoglobin stabilising protein

A_Hb_stabilising_prot

5

IPR015318

15,318

Zinc finger, GAGA-binding factor

Znf_GAGA-bd_fac

Domain

420

false

Members of this entry bind to a 5'-GAGAG-3' DNA consensus binding site, and contain a Cys2-His2 zinc finger core as well as an N-terminal extension containing two highly basic regions. The zinc finger core binds in the DNA major groove and recognises the first three GAG bases of the consensus in a manner similar to tha...

[]

0

[ "PFAM" ]

[ "PF09237" ]

[ "GAGA" ]

[ 420 ]

1

[]

0

[ "1yui", "1yuj" ]

2

[ "PUB00014077", "PUB00032709", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "12665246", "9033593", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Zinc fingers--folds for many occasions.", "The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA...

[ 2002, 1997, 2007, 2005, 2005, 1999, 2001 ]

7

[]

0

null

[ "Archaea", "Eukaryota", "Lactobacillus johnsonii", "viral metagenome" ]

[ 2, 416, 1, 1 ]

4

[ "Drosophila melanogaster" ]

[ 11 ]

1

true

Domain

Zinc finger, GAGA-binding factor

Znf_GAGA-bd_fac

7

IPR015319

15,319

Interleukin-4 receptor alpha, N-terminal

IL-4_rcpt-alpha_N

Domain

921

false

Interleukin-4 receptor is a type I transmembrane protein that can bind interleukin 4 and interleukin 13 to regulate IgE antibody production in B cells. Among T cells, the encoded protein also can bind interleukin 4 to promote differentiation of Th2 cells. A soluble form of the encoded protein can be produced by an alte...

[ "GO:0004896", "GO:0002532", "GO:0016020" ]

[ "cytokine receptor activity", "production of molecular mediator involved in inflammatory response", "membrane" ]

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

3

[ "PFAM" ]

[ "PF09238" ]

[ "IL4Ra_N" ]

[ 921 ]

1

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

[ "R-HSA-6785807", "R-MMU-6785807", "R-RNO-6785807" ]

[ "REACTOME:R-HSA-6785807", "REACTOME:R-MMU-6785807", "REACTOME:R-RNO-6785807" ]

3

[ "1iar", "3bpl", "3bpn", "3bpo", "5e4e", "6oel", "6wgl", "8k4q", "8z8l" ]

9

[ "PUB00021803" ]

[ "10219247" ]

[ "Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface." ]

[ 1999 ]

1

[]

0

null

[ "Gnathostomata" ]

[ 921 ]

1

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

[ 4, 8, 7, 4 ]

4

true

Domain

Interleukin-4 receptor alpha, N-terminal

IL-4_rcpt-alpha_N

7

IPR015320

15,320

DNA topoisomerase VI, subunit B, transducer

TopoVI_B_transducer

Domain

1,855

false

This entry represents subunit B of topoisomerase VI, an ATP-dependent type IIB enzyme. Members of this family adopt a structure consisting of a four-stranded β-sheet backed by three α-helices, the last of which is over 50 amino acids long and extends from the body of the protein by several turns. This domain has been p...

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

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

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

3

[ "PFAM", "CDD" ]

[ "PF09239", "cd00823" ]

[ "Topo-VIb_trans", "TopoIIB_Trans" ]

[ 1855, 1685 ]

2

[ "EC" ]

[ "5.6.2.2" ]

[ "EC:5.6.2.2" ]

1

[ "1mu5", "1mx0", "1z59", "1z5a", "1z5b", "1z5c", "2hkj", "2q2e", "2zbk" ]

9

[ "PUB00005437", "PUB00014011", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00020795" ]

[ "7770916", "12505993", "11395412", "12596227", "12042765", "7980433" ]

[ "The mechanisms of DNA topoisomerases.", "Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution.", "DNA topoisomerases: structure, function, and mechanism.", "Phylogenomics of type II DNA topoisomerases.", "Cellular roles of DNA topoisomerases: a molecul...

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

6

[]

0

null

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

[ 934, 92, 786, 43 ]

4

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

[ 5, 1, 6 ]

3

true

Domain

DNA topoisomerase VI, subunit B, transducer

TopoVI_B_transducer

1

IPR015321

15,321

Type I cytokine receptor, cytokine-binding domain

TypeI_recpt_CBD

Domain

5,930

false

The alpha chain of the interleukin-6 receptor (IL-6R-alpha) consists of a signal peptide, an extracellular region, a transmembrane domain, and a short cytoplasmic domain. The extracellular region is highly modular, consisting of three domains (D1, D2, and D3). The N-terminal domain D1 is characteristic of the Ig superf...

[]

0

[ "PFAM" ]

[ "PF09240" ]

[ "IL6Ra-bind" ]

[ 5930 ]

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-CFA-6785807", "R-HSA-1059683", "R-HSA-110056", "R-HSA-112411", "R-HSA-512988", "R-HSA-5673001", "R-HSA-5683826", "R-HSA-5688849", "R-HSA-5688890", "R-HSA-6785807", "R-HSA-6788467", "R-HSA-912526", "R-HSA-9616222", "R-HSA-9679191", "R-MMU-1059683", "R-MMU-110056", "R-MMU-112411", ...

[ "REACTOME:R-CFA-6785807", "REACTOME:R-HSA-1059683", "REACTOME:R-HSA-110056", "REACTOME:R-HSA-112411", "REACTOME:R-HSA-512988", "REACTOME:R-HSA-5673001", "REACTOME:R-HSA-5683826", "REACTOME:R-HSA-5688849", "REACTOME:R-HSA-5688890", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6788467", "REACTOME:R...

25

[ "1n26", "1p9m", "3bpn", "3bpo", "3lb6", "3qt2", "3va2", "4jzj", "4nkq", "4rs1", "5dwu", "5e4e", "5fuc", "5uv8", "5uwc", "6h41", "6nmy", "7dc8", "8d82", "8iow", "8j6f", "8qy5", "8qy6", "8tld", "9eza" ]

25

[ "PUB00004714", "PUB00027540" ]

[ "2169613", "12461182" ]

[ "Structural design and molecular evolution of a cytokine receptor superfamily.", "Structure of the extracellular domains of the human interleukin-6 receptor alpha -chain." ]

[ 1990, 2002 ]

2

[]

0

null

[ "Bilateria" ]

[ 5930 ]

1

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

[ 3, 28, 18, 22 ]

4

true

Domain

Type I cytokine receptor, cytokine-binding domain

TypeI_recpt_CBD

5

IPR015322

15,322

Cyclin domain, herpesvirus

Cyclin_dom_herpesvir

Domain

3

false

Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [ ], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essenti...

[]

0

[ "PFAM" ]

[ "PF09241" ]

[ "Herp-Cyclin" ]

[ 3 ]

1

[]

0

[ "1bu2", "1jow", "1xo2", "2euf", "2f2c", "4tth" ]

6

[ "PUB00014101", "PUB00014103", "PUB00023739" ]

[ "11056549", "12910258", "10368294" ]

[ "Cyclin' on the viral path to destruction.", "Cell cycle regulation and neural differentiation.", "Crystal structure of a viral cyclin, a positive regulator of cyclin-dependent kinase 6." ]

[ 2000, 2003, 1999 ]

3

[]

0

null

[ "Rhadinovirus" ]

[ 3 ]

1

[]

0

true

Domain

Cyclin domain, herpesvirus

Cyclin_dom_herpesvir

9

IPR015324

15,324

Ribosomal protein Rsm22-like

Ribosomal_Rsm22-like

Family

6,319

false

Rsm22 is a mitochondrial ribosome (mitoribosome) assembly factor [ , ]. It retains the characteristic folding and ability to bind S-adenosyl-L-methionine, but it probably lost its methyltransferase activity [ ]. In Schizosaccharomyces pombe (Fission yeast), Rsm22 is tandemly fused to Cox11 (a factor required for copper...

[ "GO:0008168", "GO:0006412" ]

[ "methyltransferase activity", "translation" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09243" ]

[ "Rsm22" ]

[ 6319 ]

1

[]

0

[ "6sg9", "6sga", "6sgb", "8csp", "8csq", "8csr", "8css", "8cst", "8csu", "8d8j", "8d8k", "8d8l", "8om2", "9hny" ]

14

[ "PUB00007068", "PUB00007069", "PUB00007070", "PUB00035457", "PUB00150960", "PUB00153722", "PUB00153723" ]

[ "11297922", "11290319", "11114498", "16835444", "36482135", "38199006", "38234605" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Sequential processing of a mitochondrial tandem protein: insights into protein import in Schizosaccharomyces pombe.", "Principles of mitoribosomal small subun...

[ 2001, 2001, 2000, 2006, 2023, 2024, 2023 ]

7

[]

[ "IPR016522" ]

0

1

0

[ "Bacteria", "Eukaryota", "Stenosarchaea group", "ecological metagenomes" ]

[ 1980, 4297, 31, 11 ]

4

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

[ 7, 2, 3, 1, 6, 4, 1, 4, 1, 1, 2, 5 ]

12

true

Family

Ribosomal protein Rsm22-like

Ribosomal_Rsm22-like

6

IPR015325

15,325

Sucrose phosphorylase, C-terminal

Suc_Porlyase_C

Domain

243

false

This domain is C-terminal to the catalytic sucrose phosphorylase β/α barrel domain. It adopts a β-sandwich fold, with Greek-key topology and is functionally uncharacterised [ ].

[]

0

[ "PFAM" ]

[ "PF09244" ]

[ "Suc_Porlyase_C" ]

[ 243 ]

1

[]

0

[ "1r7a", "2gdu", "2gdv", "5c8b", "5m9x", "5man", "5mb2", "6fme" ]

8

[ "PUB00030562" ]

[ "14756551" ]

[ "Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "human gut metagenome" ]

[ 242, 1 ]

2

[]

0

true

Domain

Sucrose phosphorylase, C-terminal

Suc_Porlyase_C

1

IPR015326

15,326

Mycoplasma arthritidis-derived mitogen

M_arthritidis-der_mitogen

Family

5

false

Mycoplasma arthritidis-derived mitogen (MA-Mit) adopts a completely α-helical structure consisting of ten α-helices arranged in two orthogonal bundles. MA-Mit is a superantigen that can activate large fractions of T cells bearing particular TCR V-beta elements. Two MA-Mit molecules form an asymmetric dimer and cross-li...

[]

0

[ "PFAM" ]

[ "PF09245" ]

[ "MA-Mit" ]

[ 5 ]

1

[]

0

[ "1r5i", "2icw", "2oje", "3kph", "8vsj", "9dl1" ]

6

[ "PUB00030533" ]

[ "14962388" ]

[ "Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex." ]

[ 2004 ]

1

[]

0

null

[ "Metamycoplasma arthritidis" ]

[ 5 ]

1

[]

0

true

Family

Mycoplasma arthritidis-derived mitogen

M_arthritidis-der_mitogen

7

IPR015327

15,327

Smaug, PHAT analogous topology

PHAT_dom

Domain

246

false

The PHAT (pseudo-HEAT analogous topology) domain assumes a structure consisting of a layer of three parallel helices packed against a layer of two antiparallel helices, into a cylindrical shaped five-helix bundle. It is found in the RNA-binding protein Smaug, where it is essential for high-affinity RNA binding [ ]. Sma...

[ "GO:0003723", "GO:0006355" ]

[ "RNA binding", "regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09246" ]

[ "PHAT" ]

[ 246 ]

1

[]

0

[ "1oxj" ]

1

[ "PUB00029635", "PUB00075369" ]

[ "12820967", "10606265" ]

[ "RNA recognition via the SAM domain of Smaug.", "Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro." ]

[ 2003, 1999 ]

2

[]

0

null

[ "Bilateria" ]

[ 246 ]

1

[ "Drosophila melanogaster" ]

[ 1 ]

1

true

Domain

Smaug, PHAT analogous topology

PHAT_dom

9

IPR015328

15,328

Domain of unknown function DUF1965

DUF1965

Domain

1,456

false

Members of this family of fungal domains adopt a structure that consists of an α/β motif. Their exact function has not, as yet, been determined [ ].

[]

0

[ "PFAM" ]

[ "PF09248" ]

[ "DUF1965" ]

[ 1456 ]

1

[]

0

[ "1n9e", "1rky", "1w7c", "3pgb" ]

4

[ "PUB00027613" ]

[ "14690425" ]

[ "The crystal structure of Pichia pastoris lysyl oxidase." ]

[ 2003 ]

1

[]

0

null

[ "Eukaryota" ]

[ 1456 ]

1

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

[ 1 ]

1

true

Domain

Domain of unknown function DUF1965

DUF1965

5

IPR015329

15,329

tRNA nucleotidyltransferase, substrate binding

tRNA_NucTransf2

Domain

1,006

false

This domain adopts a structure consisting of a five helical bundle core. It is predominantly found in Archaeal tRNA nucleotidyltransferases, following the catalytic nucleotidyltransferase domain [ ].

[ "GO:0004810" ]

[ "CCA tRNA nucleotidyltransferase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09249" ]

[ "tRNA_NucTransf2" ]

[ 1006 ]

1

[ "EC" ]

[ "2.7.7.72" ]

[ "EC:2.7.7.72" ]

1

[ "1r89", "1r8a", "1r8b", "1r8c", "1sz1", "1tfw", "1tfy", "1uet", "1ueu", "1uev", "2dr5", "2dr7", "2dr8", "2dr9", "2dra", "2drb", "2dvi", "2zh1", "2zh2", "2zh3", "2zh4", "2zh5", "2zh6", "2zh7", "2zh8", "2zh9", "2zha", "2zhb", "3ouy", "3ov7", "3ova", "3ovb"...

42

[ "PUB00015732" ]

[ "14636575" ]

[ "Crystal structures of an archaeal class I CCA-adding enzyme and its nucleotide complexes." ]

[ 2003 ]

1

[]

0

null

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

[ 962, 5, 1, 38 ]

4

[]

0

true

Domain

tRNA nucleotidyltransferase, substrate binding

tRNA_NucTransf2

4

IPR015330

15,330

DNA primase/polymerase, bifunctional, N-terminal

DNA_primase/pol_bifunc_N

Domain

13,520

false

Members of this family adopt a structure consisting of a core of antiparallel β sheets. They are found in various bacterial hypothetical proteins, and have been shown to harbour both primase and polymerase activities [ ].

[]

0

[ "PFAM", "SMART" ]

[ "PF09250", "SM00943" ]

[ "Prim-Pol", "Prim-Pol" ]

[ 13303, 11758 ]

2

[]

0

[ "1rni", "1ro0", "1ro2", "3m1m" ]

4

[ "PUB00030739" ]

[ "14730355" ]

[ "Structure of a bifunctional DNA primase-polymerase." ]

[ 2004 ]

1

[]

0

null

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

[ 139, 12190, 127, 835, 229 ]

5

[]

0

true

Domain

DNA primase/polymerase, bifunctional, N-terminal

DNA_primase/pol_bifunc_N

6

IPR015331

15,331

P22 tailspike C-terminal domain

P22_tailspike_C

Domain

646

false

The tailspike protein of Salmonella bacteriophage P22 is a viral adhesion protein that mediates attachment of the viral protein to host cell-surface lipopolysaccharide. The tailspike protein displays both receptor binding and destroying properties, inactivating the receptor by endoglycosidase activity. P22 tailspike is...

[]

0

[ "PFAM" ]

[ "PF09251" ]

[ "PhageP22-tail" ]

[ 646 ]

1

[]

0

[ "1clw", "1qa1", "1qa2", "1qa3", "1qq1", "1qrb", "1qrc", "1tsp", "1tyu", "1tyv", "1tyw", "1tyx", "2v5i", "2vfm", "2vfn", "2vfo", "2vfp", "2vfq", "2xc1", "3riq", "3th0", "5gai", "8ean", "8tvr", "8u10", "8u11", "8u1o", "9jg6" ]

28

[ "PUB00016276", "PUB00016277", "PUB00016278" ]

[ "14627734", "10600383", "12063249" ]

[ "C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.", "Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 A resolution.", "Biochemical characterization of the chondroitinase B active sit...

[ 2003, 1999, 2002 ]

3

[]

0

null

[ "Pseudomonadati", "Viruses" ]

[ 417, 229 ]

2

[]

0

true

Domain

P22 tailspike C-terminal domain

P22_tailspike_C

5

IPR015332

15,332

Major allergen I polypeptide chain 2-like

CH2-like

Family

293

false

This entry includes major allergen I polypeptide chain 2 (Fel d 1 chain 2) from cat and related proteins, such as SCGB2B from mice. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. ...

[ "GO:0005615" ]

[ "extracellular space" ]

[ "cellular_component" ]

1

[ "PFAM", "PANTHER" ]

[ "PF09252", "PTHR31708" ]

[ "Feld-I_B", "" ]

[ 291, 289 ]

2

[]

0

[ "1puo", "1zkr", "2ejn", "5vyf" ]

4

[ "PUB00035399", "PUB00042589", "PUB00069601" ]

[ "12851385", "17543334", "22155607" ]

[ "The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family.", "Structural characterization of the tetrameric form of the major cat allergen Fel d 1.", "Update of the human secretoglobin (SCGB) gene superfamily and an example of 'evolutionary bloom' of androgen-binding protein...

[ 2003, 2007, 2011 ]

3

[ "IPR016126" ]

[]

1

0

1

[ "Pseudomonas fluorescens", "Theria" ]

[ 1, 292 ]

2

[ "Mus musculus", "Rattus norvegicus" ]

[ 25, 9 ]

2

true

Family

Major allergen I polypeptide chain 2-like

CH2-like

2

IPR015333

15,333

Pollen allergen ole e 6

Pollen_allergen_ole-e-6

Family

413

false

This entry represents pollen allergens, such as ole-e-6, a small acidic protein from Olea europaea (Common olive) which mediates olive allergy. Members of this family have an α-helical hairpin structure cross-linked by three disulphides, followed by a long, unstructured C-terminal tail [ ].

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09253", "PTHR35632" ]

[ "Ole_e_6", "" ]

[ 361, 358 ]

2

[]

0

[ "1ss3" ]

1

[ "PUB00031184" ]

[ "15247256" ]

[ "NMR solution structure of Ole e 6, a major allergen from olive tree pollen." ]

[ 2004 ]

1

[]

0

null

[ "Mesangiospermae" ]

[ 413 ]

1

[]

0

true

Family

Pollen allergen ole e 6

Pollen_allergen_ole-e-6

1

IPR015334

15,334

FokI, cleavage domain

FokI_cleavage_dom

Domain

337

false

Type IIS restriction endonuclease FokI ( ) is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [ , ]. FokI contains amino- an...

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

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

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09254" ]

[ "FokI_cleav_dom" ]

[ 337 ]

1

[]

0

[ "1fok", "2fok" ]

2

[ "PUB00007438", "PUB00010506", "PUB00019577" ]

[ "9214510", "12093751", "9724743" ]

[ "Structure of the multimodular endonuclease FokI bound to DNA.", "Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I.", "Structure of FokI has implications for DNA cleavage." ]

[ 1997, 2002, 1998 ]

3

[]

0

null

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

[ 40, 284, 13 ]

3

[]

0

true

Domain

FokI, cleavage domain

FokI_cleavage_dom

4

IPR015335

15,335

F1 capsule antigen

Caf1

Family

27

false

Members of this family represent the F1 capsule antigen Caf1 synthesised by the Yersinia pestis bacteria. They adopt a structure consisting of a seven strands arranged in two β-sheets, in a Greek-key topology, and mediate targeting of the bacterium to sites of infection [ ].

[]

0

[ "PFAM" ]

[ "PF09255" ]

[ "Antig_Caf1" ]

[ 27 ]

1

[]

0

[ "1p5u", "1p5v", "1z9s", "3dos", "3dpb", "3dsn", "4ayf", "4az8", "4b0m" ]

9

[ "PUB00029732" ]

[ "12787500" ]

[ "Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation." ]

[ 2003 ]

1

[]

0

null

[ "Enterobacterales" ]

[ 27 ]

1

[]

0

true

Family

F1 capsule antigen

Caf1

4

IPR015336

15,336

Tumour necrosis factor receptor 13C, TALL-1 binding domain

TNFR_13C_TALL-1-bd

Domain

287

false

Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a...

[]

0

[ "PFAM" ]

[ "PF09256" ]

[ "BaffR-Tall_bind" ]

[ 287 ]

1

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

[ "R-HSA-5668541", "R-HSA-5676594", "R-MMU-5668541", "R-MMU-5676594" ]

[ "REACTOME:R-HSA-5668541", "REACTOME:R-HSA-5676594", "REACTOME:R-MMU-5668541", "REACTOME:R-MMU-5676594" ]

4

[ "1oqe", "1osx", "2hfg", "4v46", "8zuj", "8zuk" ]

6

[ "PUB00002042", "PUB00004130", "PUB00006091", "PUB00006095", "PUB00006098", "PUB00006101", "PUB00015257", "PUB00029544" ]

[ "8095800", "1377364", "2989794", "3349526", "2777790", "2268312", "15335677", "12721620" ]

[ "A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.", "Emerging cytokine family.", "Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression.", "A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein:...

[ 1993, 1992, 1985, 1988, 1989, 1990, 1993, 2003 ]

8

[]

0

null

[ "Amniota" ]

[ 287 ]

1

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

[ 4, 6, 2 ]

3

true

Domain

Tumour necrosis factor receptor 13C, TALL-1 binding domain

TNFR_13C_TALL-1-bd

3

IPR015337

15,337

BCMA, TALL-1 binding

BCMA_Tall-1-bd

Domain

562

false

Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a...

[]

0

[ "PFAM" ]

[ "PF09257" ]

[ "BCMA-Tall_bind" ]

[ 562 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-5669034", "R-MMU-5669034" ]

[ "REACTOME:R-HSA-5669034", "REACTOME:R-MMU-5669034" ]

2

[ "1oqd", "1xu2", "2kn1", "4zfo", "6j7w", "8hxq", "8hxr", "8qy9", "8qya", "8qyb" ]

10

[ "PUB00002042", "PUB00004130", "PUB00006091", "PUB00006095", "PUB00006098", "PUB00006101", "PUB00015257", "PUB00029544" ]

[ "8095800", "1377364", "2989794", "3349526", "2777790", "2268312", "15335677", "12721620" ]

[ "A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.", "Emerging cytokine family.", "Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression.", "A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein:...

[ 1993, 1992, 1985, 1988, 1989, 1990, 1993, 2003 ]

8

[]

0

null

[ "Vertebrata" ]

[ 562 ]

1

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

[ 1, 4, 1, 3 ]

4

true

Domain

BCMA, TALL-1 binding

BCMA_Tall-1-bd

9

IPR015338

15,338

Glycosyl transferase 64 domain

GT64_dom

Domain

11,256

false

Members of this family catalyse the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. Th...

[ "GO:0016757", "GO:0016020" ]

[ "glycosyltransferase activity", "membrane" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09258" ]

[ "Glyco_transf_64" ]

[ 11256 ]

1

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

[ "2.4.1", "R-BTA-2022928", "R-CEL-2022928", "R-DME-2022928", "R-DRE-2022928", "R-HSA-2022928", "R-HSA-3656237", "R-HSA-3656253", "R-HSA-381038", "R-MMU-2022928" ]

[ "EC:2.4.1", "REACTOME:R-BTA-2022928", "REACTOME:R-CEL-2022928", "REACTOME:R-DME-2022928", "REACTOME:R-DRE-2022928", "REACTOME:R-HSA-2022928", "REACTOME:R-HSA-3656237", "REACTOME:R-HSA-3656253", "REACTOME:R-HSA-381038", "REACTOME:R-MMU-2022928" ]

10

[ "1omx", "1omz", "1on6", "1on8", "7au2", "7aua", "7sch", "7scj", "7sck", "7uqx", "7uqy", "7zay", "8og1", "8og4" ]

14

[ "PUB00029495" ]

[ "12562774" ]

[ "Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis." ]

[ 2003 ]

1

[]

0

null

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

[ 5, 11246, 5 ]

3

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

[ 15, 1, 22, 6, 26, 23, 10, 17, 19 ]

9

true

Domain

Glycosyl transferase 64 domain

GT64_dom

1

IPR015339

15,339

Immunomodulatory protein FIP-Fve, fungal

Immunomodulatory_FIP-Fve_fun

Family

99

false

FIP-Fve (Fungal Immunomodulatory Protein Fve) is a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity [ ]. It stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and oedema, enhances transcription of IL-2, IFN-gamma and TNF-alpha, and haemaggl...

[ "GO:0030246", "GO:0002682" ]

[ "carbohydrate binding", "regulation of immune system process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09259" ]

[ "Fve" ]

[ 99 ]

1

[]

0

[ "1osy", "3f3h", "3kcw", "7wdl", "7wdm", "8go5", "8go6", "8go7" ]

8

[ "PUB00029592", "PUB00066809" ]

[ "12948495", "7705335" ]

[ "A 1.7A structure of Fve, a member of the new fungal immunomodulatory protein family.", "A new fungal immunomodulatory protein, FIP-fve isolated from the edible mushroom, Flammulina velutipes and its complete amino acid sequence." ]

[ 2003, 1995 ]

2

[]

0

null

[ "Bacillota", "Dikarya" ]

[ 22, 77 ]

2

[]

0

true

Family

Immunomodulatory protein FIP-Fve, fungal

Immunomodulatory_FIP-Fve_fun

7

IPR015340

15,340

Alpha-amylase, C domain

A_amylase_C_dom

Domain

2,576

false

This domain is found at the C-terminal of various fungal alpha-amylase proteins. It has been identified as a secondary binding site, which might be part of a starch interaction site [ , ]. It has a β-sandwich fold comprising an antiparallel β-sheet with eight strands. Alpha-amylase is classified as family 13 ( ) of the...

[ "GO:0005509", "GO:0016052" ]

[ "calcium ion binding", "carbohydrate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09260" ]

[ "A_amylase_dom_C" ]

[ 2576 ]

1

[ "EC" ]

[ "3.2.1.1" ]

[ "EC:3.2.1.1" ]

1

[ "2aaa", "2guy", "2gvy", "2taa", "3kwx", "3vm7", "3vx0", "3vx1", "6sao", "6sav", "6taa", "6xsj", "6xsv", "6yq7", "6yq9", "6yqa", "6yqb", "6yqc", "7p4w", "7taa" ]

20

[ "PUB00027666", "PUB00097488", "PUB00097489" ]

[ "11141191", "23536251", "31623309" ]

[ "Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold.", "A novel multifunctional α-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure.", "Structural and Functional Charact...

[ 2001, 2013, 2019 ]

3

[]

0

null

[ "Eukaryota" ]

[ 2576 ]

1

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 2, 4 ]

2

true

Domain

Alpha-amylase, C domain

A_amylase_C_dom

7

IPR015341

15,341

Glycoside hydrolase family 38, central domain

Glyco_hydro_38_cen

Domain

25,984

false

This entry represents a domain found in members of the glycosyl hydrolases families 38. This domain is found in the central region that adopts a structure consisting of three α helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase [ ]. Glycosid...

[ "GO:0004559", "GO:0006013" ]

[ "alpha-mannosidase activity", "mannose metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "SMART" ]

[ "PF09261", "SM00872" ]

[ "Alpha-mann_mid", "Alpha-mann_mid" ]

[ 25473, 25751 ]

2

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

[ "3.2.1.24", "GenProp1299", "GenProp1444", "GenProp1524", "R-BTA-6798695", "R-BTA-8853383", "R-DDI-6798695", "R-DDI-8853383", "R-DME-975578", "R-HSA-6798695", "R-HSA-6811438", "R-HSA-8853383", "R-HSA-9694548", "R-HSA-975578", "R-MMU-6798695", "R-MMU-8853383", "R-MMU-975578", "R-RNO-...

[ "EC:3.2.1.24", "GP:GenProp1299", "GP:GenProp1444", "GP:GenProp1524", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8853383", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-8853383", "REACTOME:R-DME-975578", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6811438", "REACTOME:R-HSA-8853383", "REACTOME:R-HSA-...

21

[ "1hty", "1hww", "1hxk", "1o7d", "1ps3", "1qwn", "1qwu", "1qx1", "1r33", "1r34", "1tqs", "1tqt", "1tqu", "1tqv", "1tqw", "2alw", "2f18", "2f1a", "2f1b", "2f7o", "2f7p", "2f7q", "2f7r", "2fyv", "2ow6", "2ow7", "2wyh", "2wyi", "3blb", "3bub", "3bud", "3bui"...

84

[ "PUB00022319" ]

[ "12634058" ]

[ "The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation." ]

[ 2003 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctaMv1", "unclassified sequences" ]

[ 105, 10071, 15712, 1, 95 ]

5

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

[ 29, 4, 21, 17, 1, 23, 18, 1, 14, 25, 1, 1, 50 ]

13

true

Domain

Glycoside hydrolase family 38, central domain

Glyco_hydro_38_cen

9

IPR015342

15,342

Peroxisomal ATPase PEX1, N-terminal C-lobe

PEX1-N_C-lobe

Domain

4,465

false

The N-terminal domain of PEX1 adopts a double ψ β-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putat...

[ "GO:0005524", "GO:0007031", "GO:0005777" ]

[ "ATP binding", "peroxisome organization", "peroxisome" ]

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

3

[ "PFAM" ]

[ "PF09262" ]

[ "PEX-1N" ]

[ 4465 ]

1

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

[ "3.6.4.-", "PWY-7250", "R-HSA-9033241", "R-MMU-9033241" ]

[ "EC:3.6.4.-", "METACYC:PWY-7250", "REACTOME:R-HSA-9033241", "REACTOME:R-MMU-9033241" ]

4

[ "1wlf", "8u0v" ]

2

[ "PUB00035447" ]

[ "15328346" ]

[ "Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain." ]

[ 2004 ]

1

[]

0

null

[ "Eukaryota" ]

[ 4465 ]

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...

[ 7, 1, 1, 2, 4, 1, 1, 3, 4, 1, 1, 12 ]

12

true

Domain

Peroxisomal ATPase PEX1, N-terminal C-lobe

PEX1-N_C-lobe

3

IPR015343

15,343

Peroxisomal ATPase PEX1, N-terminal N-lobe

PEX1-N-lobe

Domain

1,265

false

The N-terminal domain of PEX1 adopts a Cdc48 domain 2-like fold, with a β-α-β(3) arrangement. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substra...

[]

0

[ "PFAM" ]

[ "PF09263" ]

[ "PEX-2N" ]

[ 1265 ]

1

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

[ "3.6.4.-", "PWY-7250", "R-HSA-9033241", "R-MMU-9033241" ]

[ "EC:3.6.4.-", "METACYC:PWY-7250", "REACTOME:R-HSA-9033241", "REACTOME:R-MMU-9033241" ]

4

[ "1wlf" ]

1

[ "PUB00035447" ]

[ "15328346" ]

[ "Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain." ]

[ 2004 ]

1

[]

0

null

[ "Opisthokonta" ]

[ 1265 ]

1

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

[ 1, 4, 2, 4 ]

4

true

Domain

Peroxisomal ATPase PEX1, N-terminal N-lobe

PEX1-N-lobe

7

IPR015344

15,344

Vibrio cholerae neuraminidase, lectin-like domain

VCNA_lectin-like_dom

Domain

83

false

These lectin-like domains is are found in Vibrio cholerae neuraminidase (VCNA). This enzyme plays a significant role in the pathogenesis of cholera by removing sialic acid from higher order gangliosides to unmask GM1, the receptor for cholera toxin. The domains flank a central β-propeller catalytic domain. They are tho...

[ "GO:0033691" ]

[ "sialic acid binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09264" ]

[ "Sial-lect-inser" ]

[ 83 ]

1

[]

0

[ "1kit", "1w0o", "1w0p", "2w68", "6eks", "6eku" ]

6

[ "PUB00022848" ]

[ "15226294" ]

[ "Sialic acid recognition by Vibrio cholerae neuraminidase." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria" ]

[ 83 ]

1

[]

0

true

Domain

Vibrio cholerae neuraminidase, lectin-like domain

VCNA_lectin-like_dom

6

IPR015345

15,345

Cytokinin dehydrogenase 1, FAD/cytokinin binding domain

Cytokinin_DH_FAD/cytokin-bd

Domain

5,740

false

This domain adopts an α+β sandwich structure with an antiparallel β-sheet, in a ferredoxin-like fold. It is predominantly found in plant cytokinin dehydrogenase 1, where it is capable of binding both FAD and cytokinin substrates. The substrate displays a 'plug-into-socket' binding mode that seals the catalytic site and...

[ "GO:0019139", "GO:0050660", "GO:0009690" ]

[ "cytokinin dehydrogenase activity", "flavin adenine dinucleotide binding", "cytokinin metabolic process" ]

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

3

[ "PFAM" ]

[ "PF09265" ]

[ "Cytokin-bind" ]

[ 5740 ]

1

[ "EC" ]

[ "1.5.99.12" ]

[ "EC:1.5.99.12" ]

1

[ "1w1o", "1w1q", "1w1r", "1w1s", "2exr", "2q4w", "2qkn", "2qpm", "3bw7", "3c0p", "3dq0", "3kjm", "3s1c", "3s1d", "3s1e", "3s1f", "4ml8", "4mla", "4o95", "4oal", "5hhz", "5hmr", "5hqx", "6c80", "6yao", "6yap", "6yaq", "8cj9", "8ck6", "8ckq", "8ckt", "8clw"...

34

[ "PUB00032155" ]

[ "15321719" ]

[ "Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 748, 4992 ]

2

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

[ 37, 22, 52 ]

3

true

Domain

Cytokinin dehydrogenase 1, FAD/cytokinin binding domain

Cytokinin_DH_FAD/cytokin-bd

5

IPR015346

15,346

DNA topoisomerase I, N-terminal, viral

TopoI_N_vir

Domain

135

false

DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi...

[ "GO:0003677", "GO:0003916", "GO:0006265" ]

[ "DNA binding", "DNA topoisomerase activity", "DNA topological change" ]

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

3

[ "PFAM" ]

[ "PF09266" ]

[ "VirDNA-topo-I_N" ]

[ 135 ]

1

[ "EC" ]

[ "5.6.2.1" ]

[ "EC:5.6.2.1" ]

1

[ "1vcc", "2h7f", "2h7g", "3igc" ]

4

[ "PUB00005230", "PUB00005437", "PUB00006312", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00081702", "PUB00081703", "PUB00081704", "PUB00081705" ]

[ "9488644", "7770916", "7994576", "11395412", "12596227", "12042765", "21087076", "20644584", "17722649", "17293019" ]

[ "Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.", "The mechanisms of DNA topoisomerases.", "Crystal structure of the amino-terminal fragment of vaccinia virus DNA topoisomerase I at 1.6 A resolution.", "DNA topoisomerases: structure, function, and mechanism.", "P...

[ 1998, 1995, 1994, 2001, 2003, 2002, 2010, 2010, 2007, 2007 ]

10

[]

0

null

[ "Poxviridae" ]

[ 135 ]

1

[]

0

true

Domain

DNA topoisomerase I, N-terminal, viral

TopoI_N_vir

2

IPR015347

15,347

STAT transcription factor homologue, coiled coil

STAT_TF_homologue_CC

Domain

36

false

This entry represents a domain found in Dictyostelium STAT proteins. This domain adopts a structure consisting of four long α-helices, folded into a coiled coil. It is responsible for nuclear export of the protein [ ]. The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription f...

[]

0

[ "PFAM" ]

[ "PF09267" ]

[ "Dict-STAT-coil" ]

[ 36 ]

1

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

[ "R-DDI-1059683", "R-DDI-1169408", "R-DDI-201556", "R-DDI-3249367", "R-DDI-6783783", "R-DDI-6785807", "R-DDI-877300", "R-DDI-8854691", "R-DDI-8983432", "R-DDI-8984722", "R-DDI-8985947", "R-DDI-9008059", "R-DDI-9020591", "R-DDI-9020933", "R-DDI-9020956", "R-DDI-909733", "R-DDI-9701898"...

[ "REACTOME:R-DDI-1059683", "REACTOME:R-DDI-1169408", "REACTOME:R-DDI-201556", "REACTOME:R-DDI-3249367", "REACTOME:R-DDI-6783783", "REACTOME:R-DDI-6785807", "REACTOME:R-DDI-877300", "REACTOME:R-DDI-8854691", "REACTOME:R-DDI-8983432", "REACTOME:R-DDI-8984722", "REACTOME:R-DDI-8985947", "REACTOME:...

18

[ "1uur", "1uus" ]

2

[ "PUB00007134", "PUB00011807", "PUB00022808", "PUB00032712", "PUB00051157" ]

[ "12039028", "9630226", "15053873", "15780933", "18433722" ]

[ "Signaling through the JAK/STAT pathway, recent advances and future challenges.", "Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.", "Structure of an activated Dictyostelium STAT in its DNA-unbound form.", "Structural bases of unphosphorylated STAT1 association and receptor binding."...

[ 2002, 1998, 2004, 2005, 2008 ]

5

[]

0

null

[ "Amoebozoa", "Subsaximicrobium wynnwilliamsii" ]

[ 35, 1 ]

2

[]

0

true

Domain

STAT transcription factor homologue, coiled coil

STAT_TF_homologue_CC

2

IPR015348

15,348

Clathrin, heavy chain, linker, core motif

Clathrin_H-chain_linker_core

Domain

6,879

false

Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are ...

[ "GO:0005198", "GO:0006886", "GO:0016192", "GO:0030130", "GO:0030132" ]

[ "structural molecule activity", "intracellular protein transport", "vesicle-mediated transport", "clathrin coat of trans-Golgi network vesicle", "clathrin coat of coated pit" ]

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

5

[ "PFAM" ]

[ "PF09268" ]

[ "Clathrin-link" ]

[ 6879 ]

1

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

[ "R-BTA-177504", "R-BTA-190873", "R-BTA-196025", "R-BTA-2132295", "R-BTA-432720", "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-BTA-9013420", "R-BTA-9013424", "R-CEL-190873", "R-CEL-196025", "...

[ "REACTOME:R-BTA-177504", "REACTOME:R-BTA-190873", "REACTOME:R-BTA-196025", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-432720", "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-BT...

114

[ "1bpo", "1c9i", "1c9l", "1utc", "1xi4", "1xi5", "2xzg", "3gc3", "3gd1", "3iyv", "4g55", "5m5r", "5m5s", "5m5t", "5m5u", "5m5v", "5m61", "5ods", "6e4l", "6qnn", "6qnp", "6sct", "6wcj", "6yai", "7bn1", "7bn2", "7zx4", "9c0y", "9c0z", "9ex5", "9exf", "9exg"...

35

[ "PUB00000964", "PUB00035753", "PUB00035765", "PUB00035769", "PUB00035906", "PUB00035907", "PUB00035908", "PUB00035909" ]

[ "9827808", "17449236", "11598180", "15261670", "15752139", "16806884", "16734666", "16699812" ]

[ "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.", "Do different endocytic pathways make different synaptic vesicles?", "Adaptins: the final recount.", "COP and clathrin-coated vesicle budding: different pathways, common approaches.", "New faces of the familiar c...

[ 1998, 2007, 2001, 2004, 2005, 2006, 2006, 2006 ]

8

[]

0

null

[ "Eukaryota" ]

[ 6879 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea ma...

[ 6, 1, 9, 2, 20, 6, 6, 7, 1, 1, 142 ]

11

true

Domain

Clathrin, heavy chain, linker, core motif

Clathrin_H-chain_linker_core

7

IPR015349

15,349

GTP-binding protein OBG, C-terminal

OCT_dom

Domain

11,381

false

Obg subfamily proteins (also known as ObgE, YhbZ and CgtA) are conserved P- loop GTPases, that are involved in a wide range of cellular processes, including sporulation, cellular differentiation, ribosome assembly, DNA replication, chromosome segregation, and stringent response in eubacteria and plant chloroplasts. Obg...

[ "GO:0000166" ]

[ "nucleotide binding" ]

[ "molecular_function" ]

1

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

[ "PF09269", "PS51881", "TIGR03595" ]

[ "DUF1967", "OCT", "Obg_CgtA_exten" ]

[ 11332, 11368, 11252 ]

3

[ "EC" ]

[ "3.6.5.-" ]

[ "EC:3.6.5.-" ]

1

[ "1udx" ]

1

[ "PUB00022779", "PUB00090253", "PUB00094757" ]

[ "15019792", "19636801", "22380942" ]

[ "Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8.", "AtObgC, a plant ortholog of bacterial Obg, is a chloroplast-targeting GTPase essential for early embryogenesis.", "Functional characterization of ObgC in ribosome biogenesis during chloroplast development." ]

[ 2004, 2009, 2012 ]

3

[]

0

null

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

[ 10338, 783, 260 ]

3

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

[ 3, 3, 12 ]

3

true

Domain

GTP-binding protein OBG, C-terminal

OCT_dom

9

IPR015351

15,351

RBP-J/Cbf11/Cbf12, DNA binding

RBP-J/Cbf11/Cbf12_DNA-bd

Domain

5,528

false

This domain is found in RBP-J from human and Cbf11/Cbf12 from fission yeast. These proteins function as transcription factors [ , ]. This domain adopts a β sandwich structure, with nine strands in two β-sheets, in a Greek-key topology, and allow for DNA binding [ ].

[ "GO:0003677", "GO:0003700", "GO:0006355", "GO:0005634" ]

[ "DNA binding", "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "nucleus" ]

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

4

[ "PFAM", "SMART" ]

[ "PF09271", "SM01267" ]

[ "LAG1-DNAbind", "LAG1_DNAbind" ]

[ 5516, 5451 ]

2

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

[ "R-BTA-350054", "R-BTA-8941856", "R-DME-350054", "R-HSA-1912408", "R-HSA-210744", "R-HSA-2122947", "R-HSA-2197563", "R-HSA-2644606", "R-HSA-2894862", "R-HSA-350054", "R-HSA-8941856", "R-HSA-9013508", "R-HSA-9013695", "R-HSA-9793380", "R-HSA-9824272", "R-MMU-2122947", "R-MMU-350054", ...

[ "REACTOME:R-BTA-350054", "REACTOME:R-BTA-8941856", "REACTOME:R-DME-350054", "REACTOME:R-HSA-1912408", "REACTOME:R-HSA-210744", "REACTOME:R-HSA-2122947", "REACTOME:R-HSA-2197563", "REACTOME:R-HSA-2644606", "REACTOME:R-HSA-2894862", "REACTOME:R-HSA-350054", "REACTOME:R-HSA-8941856", "REACTOME:R-...

18

[ "1ttu", "2f8x", "2fo1", "3brd", "3brf", "3brg", "3iag", "3nbn", "3v79", "4j2x", "5e24", "5eg6", "6dks", "6py8", "6wqu", "7rte", "7rti" ]

17

[ "PUB00031569", "PUB00086617", "PUB00086618" ]

[ "15297877", "19101542", "23303788" ]

[ "Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA.", "Cbf11 and Cbf12, the fission yeast CSL proteins, play opposing roles in cell adhesion and coordination of cell and nuclear division.", "Oxygen-dependent expression of cytochrome c oxidase subunit 4-2 gene expression is mediated...

[ 2004, 2009, 2013 ]

3

[]

0

null

[ "Eukaryota" ]

[ 5528 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 2, 2, 29, 8, 14, 2 ]

7

true

Domain

RBP-J/Cbf11/Cbf12, DNA binding

RBP-J/Cbf11/Cbf12_DNA-bd

4

IPR015352

15,352

Hepsin, SRCR domain

Hepsin-SRCR_dom

Domain

708

false

This entry represents the extracellular domain of the serine protease hepsin. The domain is formed primarily by three elements of regular secondary structure: a 12-residue α helix, a twisted five-stranded antiparallel β sheet, and a second, two-stranded, antiparallel sheet. The two β-sheets lie at roughly right angles ...

[ "GO:0004252", "GO:0070008" ]

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

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF09272" ]

[ "Hepsin-SRCR" ]

[ 708 ]

1

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

[ "3.4.21.106", "R-HSA-6806942", "R-HSA-8852405", "R-MMU-6806942", "R-MMU-8852405", "R-RNO-6806942", "R-RNO-8852405" ]

[ "EC:3.4.21.106", "REACTOME:R-HSA-6806942", "REACTOME:R-HSA-8852405", "REACTOME:R-MMU-6806942", "REACTOME:R-MMU-8852405", "REACTOME:R-RNO-6806942", "REACTOME:R-RNO-8852405" ]

7

[ "1o5e", "1o5f", "1p57", "1z8g", "3t2n", "5ce1" ]

6

[ "PUB00029725" ]

[ "12962630" ]

[ "The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain." ]

[ 2003 ]

1

[]

0

null

[ "Gnathostomata" ]

[ 708 ]

1

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

[ 3, 6, 5, 6 ]

4

true

Domain

Hepsin, SRCR domain

Hepsin-SRCR_dom

6

IPR015353

15,353

Rubisco LSMT, substrate-binding domain

Rubisco_LSMT_subst-bd

Domain

11,651

false

This domain adopts a multihelical structure, with an irregular array of long and short α-helices. It allows binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex [ ].

[]

0

[ "PFAM" ]

[ "PF09273" ]

[ "Rubis-subs-bind" ]

[ 11651 ]

1

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

[ "2.1.1", "R-DRE-3214841", "R-HSA-3214841", "R-MMU-3214841", "R-RNO-3214841" ]

[ "EC:2.1.1", "REACTOME:R-DRE-3214841", "REACTOME:R-HSA-3214841", "REACTOME:R-MMU-3214841", "REACTOME:R-RNO-3214841" ]

5

[ "1mlv", "1ozv", "1p0y", "2h21", "2h23", "2h2e", "2h2j", "3qxy", "3rc0", "3smt", "6ict", "6icv", "6jat", "6mbj", "6mbk", "6mbl", "6ox0", "6ox1", "6ox2", "6ox3", "6ox4", "6ox5", "6v62", "6v63", "6wk1", "6wk2", "7lms", "7w28", "7w29", "8qma", "8r5o", "8r6s"...

41

[ "PUB00029671" ]

[ "12819771" ]

[ "Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT." ]

[ 2003 ]

1

[]

0

null

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

[ 26, 11620, 5 ]

3

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

[ 38, 4, 1, 5, 4, 2, 18, 11, 56 ]

9

true

Domain

Rubisco LSMT, substrate-binding domain

Rubisco_LSMT_subst-bd

6

IPR015354

15,354

DNA partition complex, ParG

DNA_partition_ParG

Family

740

false

This entry represents plasmid partition proteins; it adopts a ribbon-helix-helix fold, with a core of four α-helices. The proteins are an essential component of the DNA partition complex of the multi drug resistance plasmid TP228 [ ].

[]

0

[ "PFAM" ]

[ "PF09274" ]

[ "ParG" ]

[ 740 ]

1

[]

0

[ "1p94", "5u1g" ]

2

[ "PUB00029777" ]

[ "14622405" ]

[ "ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure." ]

[ 2003 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Opisthokonta", "metagenomes" ]

[ 15, 711, 2, 12 ]

4

[]

0

true

Family

DNA partition complex, ParG

DNA_partition_ParG

9

IPR015356

15,356

Pertussis toxin, subunit S5

Pertussis_toxin_subS5

Family

13

false

Members of this family of Bordetella pertussis toxins adopt a structure consisting of an OB fold, with a closed or partly opened β-barrel in a Greek-key topology [ ].

[]

0

[ "PFAM" ]

[ "PF09276" ]

[ "Pertus-S5-tox" ]

[ 13 ]

1

[]

0

[ "1bcp", "1prt", "1pto", "6ro0", "9e3h", "9e3j", "9e3k", "9e3l", "9mr7" ]

9

[ "PUB00007592" ]

[ "8075982" ]

[ "The crystal structure of pertussis toxin." ]

[ 1994 ]

1

[]

0

null

[ "Bordetella" ]

[ 13 ]

1

[]

0

true

Family

Pertussis toxin, subunit S5

Pertussis_toxin_subS5

3

IPR015357

15,357

EryA2-like, docking domain

EryA2_docking

Domain

2,554

false

This domain is found at the C-terminal end of Erythronolide synthase EryA2 from Saccharopolyspora erythraea and similar sequences from actinomycetes. EryA2 is involved in the biosynthesis of antibiotic erythromycin via the biosynthesis of its aglycone precursor, 6-deoxyerythronolide B (6-dEB) [ ]. Docking domains are f...

[]

0

[ "PFAM" ]

[ "PF09277" ]

[ "Erythro-docking" ]

[ 2554 ]

1

[]

0

[ "1pzq", "7s6b", "7s6c", "7s6d" ]

4

[ "PUB00030060", "PUB00049083", "PUB00154686", "PUB00158945" ]

[ "12954331", "17719492", "17763486", "20589823" ]

[ "The structure of docking domains in modular polyketide synthases.", "Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase.", "Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective.", "Cloning and ...

[ 2003, 2007, 2007, 2010 ]

4

[]

0

null

[ "Bacteria" ]

[ 2554 ]

1

[]

0

true

Domain

EryA2-like, docking domain

EryA2_docking

7

IPR015358

15,358

Transcription regulator MerR, DNA binding

Tscrpt_reg_MerR_DNA-bd

Domain

20,557

false

This entry represents a DNA-binding domain of the transcriptional regulator MerR and similar sequences predominantly found in bacteria. It adopts a structure consisting of a core of three α-helices, with an architecture that is similar to that of the 'winged helix' fold [ ].

[]

0

[ "PFAM" ]

[ "PF09278" ]

[ "MerR-DNA-bind" ]

[ 20557 ]

1

[]

0

[ "1q08", "1q09", "1q0a", "2zhg", "2zhh", "5crl", "5gpe" ]

7

[ "PUB00015536" ]

[ "12958362" ]

[ "Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR." ]

[ 2003 ]

1

[]

0

null

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

[ 20370, 30, 2, 155 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Transcription regulator MerR, DNA binding

Tscrpt_reg_MerR_DNA-bd

8

IPR015359

15,359

Phosphoinositide-specific phospholipase C, EF-hand-like domain

PLC_EF-hand-like

Domain

16,773

false

This domain is predominantly found in the enzyme phosphoinositol-specific phospholipase C. It adopts a structure consisting of a core of four α-helices, in an EF like fold, and is required for functioning of the enzyme [ ].

[]

0

[ "PFAM" ]

[ "PF09279" ]

[ "EF-hand_like" ]

[ 16773 ]

1

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "R...

[ "3.1.4.11", "GenProp1511", "GenProp1548", "PWY-6351", "PWY-6367", "PWY-7039", "PWY-8052", "R-BTA-1855204", "R-CEL-112043", "R-CEL-1855204", "R-CEL-416476", "R-GGA-1855204", "R-HSA-1855204", "R-MMU-1855204", "R-RNO-1855204", "R-SCE-112043", "R-SCE-114604", "R-SCE-1855204", "R-SCE-...

[ "EC:3.1.4.11", "GP:GenProp1511", "GP:GenProp1548", "METACYC:PWY-6351", "METACYC:PWY-6367", "METACYC:PWY-7039", "METACYC:PWY-8052", "REACTOME:R-BTA-1855204", "REACTOME:R-CEL-112043", "REACTOME:R-CEL-1855204", "REACTOME:R-CEL-416476", "REACTOME:R-GGA-1855204", "REACTOME:R-HSA-1855204", "REAC...

25

[ "1djg", "1djh", "1dji", "1djw", "1djx", "1djy", "1djz", "1qas", "1qat", "2isd", "6pmp", "9bcz" ]

12

[ "PUB00030187" ]

[ "8784353" ]

[ "C2 domain conformational changes in phospholipase C-delta 1." ]

[ 1996 ]

1

[]

[ "IPR028382", "IPR046971", "IPR046972", "IPR046974", "IPR046975" ]

0

5

0

[ "Bacteria", "Eukaryota" ]

[ 3, 16770 ]

2

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]

[ 20, 21, 72, 37, 21, 34, 1, 8 ]

8

true

Domain

Phosphoinositide-specific phospholipase C, EF-hand-like domain

PLC_EF-hand-like

7

IPR015360

15,360

XPC-binding domain

XPC-bd

Domain

7,621

false

This domain adopts a structure consisting of four α-helices, arranged in an array. It binds specifically and directly to the xeroderma pigmentosum group C protein (XPC) to initiate nucleotide excision repair [ ].

[ "GO:0003684", "GO:0006289", "GO:0043161" ]

[ "damaged DNA binding", "nucleotide-excision repair", "proteasome-mediated ubiquitin-dependent protein catabolic process" ]

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

3

[ "PFAM" ]

[ "PF09280" ]

[ "XPC-binding" ]

[ 7621 ]

1

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

[ "R-BTA-532668", "R-BTA-5689877", "R-BTA-5696394", "R-BTA-5696395", "R-DDI-5696394", "R-DDI-5696395", "R-HSA-532668", "R-HSA-5689877", "R-HSA-5696394", "R-HSA-5696395", "R-MMU-532668", "R-MMU-5689877", "R-MMU-5696394", "R-MMU-5696395", "R-RNO-532668", "R-RNO-5689877", "R-RNO-5696394",...

[ "REACTOME:R-BTA-532668", "REACTOME:R-BTA-5689877", "REACTOME:R-BTA-5696394", "REACTOME:R-BTA-5696395", "REACTOME:R-DDI-5696394", "REACTOME:R-DDI-5696395", "REACTOME:R-HSA-532668", "REACTOME:R-HSA-5689877", "REACTOME:R-HSA-5696394", "REACTOME:R-HSA-5696395", "REACTOME:R-MMU-532668", "REACTOME:R...

19

[ "1oqy", "1pve", "1qze", "1tp4", "1x3w", "1x3z", "2f4m", "2f4o", "2qsf", "2qsg", "2qsh", "3esw", "4yir", "6cfi", "6ubf", "6ug1", "6uin", "6xqj", "8ebs", "8ebv", "8ebw", "9vfe", "9vff", "9vfg" ]

24

[ "PUB00035489" ]

[ "15885096" ]

[ "Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B." ]

[ 2005 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "bird metagenome" ]

[ 5, 7615, 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...

[ 20, 1, 6, 4, 10, 10, 1, 10, 10, 1, 1, 40 ]

12

true

Domain

XPC-binding domain

XPC-bd

3

IPR015361

15,361

Taq polymerase, thermostable, exonuclease region

Taq_pol_thermo_exonuc

Domain

140

false

This domain is found in prokaryotic Taq DNA polymerase (thermostable), where it assumes a ribonuclease H-like motif. The domain confers 5'-3' exonuclease activity to the polymerase [ ].

[ "GO:0001882", "GO:0003887", "GO:0006260", "GO:0006281" ]

[ "nucleoside binding", "DNA-directed DNA polymerase activity", "DNA replication", "DNA repair" ]

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

4

[ "PFAM" ]

[ "PF09281" ]

[ "Taq-exonuc" ]

[ 140 ]

1

[ "EC" ]

[ "2.7.7.7" ]

[ "EC:2.7.7.7" ]

1

[ "1bgx", "1jxe", "1ktq", "1qss", "1qsy", "1qtm", "1taq", "1tau", "2ktq", "3ktq", "3lwl", "3lwm", "3m8r", "3m8s", "3ojs", "3oju", "3po4", "3po5", "3py8", "3rr7", "3rr8", "3rrg", "3rrh", "3rtv", "3sv3", "3sv4", "3syz", "3sz2", "3t3f", "4bwj", "4bwm", "4c8k"...

82

[ "PUB00030371" ]

[ "10449720" ]

[ "Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation." ]

[ 1999 ]

1

[]

0

null

[ "Ascaris suum", "Deinococci" ]

[ 1, 139 ]

2

[]

0

true

Domain

Taq polymerase, thermostable, exonuclease region

Taq_pol_thermo_exonuc

3

IPR015362

15,362

WIBG, Mago-binding

WIBG_mago-bd

Domain

3,856

false

Partner of Y14 and mago (PYM, also known as WIBG) is a key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post-transcriptional processes i...

[]

0

[ "PFAM", "SMART" ]

[ "PF09282", "SM01273" ]

[ "Mago-bind", "Mago-bind" ]

[ 3850, 3829 ]

2

[]

0

[ "1rk8" ]

1

[ "PUB00030702", "PUB00052303", "PUB00074898" ]

[ "14968132", "19410547", "18026120" ]

[ "Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex.", "Disassembly of exon junction complexes by PYM.", "PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs." ]

[ 2004, 2009, 2007 ]

3

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 9, 3847 ]

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", "Schizosaccharomyces pombe (stra...

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

11

true

Domain

WIBG, Mago-binding

WIBG_mago-bd

7

IPR015364

15,364

Rhamnogalacturonase B, N-terminal

RhgB_N

Domain

1,994

false

This domain is found in prokaryotic enzyme rhamnogalacturonase B, it adopts a structure consisting of a β-supersandwich, with eighteen strands in two β-sheets. The exact function of the domain is unknown, but a putative role includes carbohydrate-binding [ ].

[ "GO:0016837", "GO:0030246", "GO:0005975" ]

[ "carbon-oxygen lyase activity, acting on polysaccharides", "carbohydrate binding", "carbohydrate metabolic process" ]

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

3

[ "PFAM" ]

[ "PF09284" ]

[ "RhgB_N" ]

[ 1994 ]

1

[ "EC", "METACYC" ]

[ "4.2.2.23", "PWY-6771" ]

[ "EC:4.2.2.23", "METACYC:PWY-6771" ]

2

[ "1nkg", "2xhn", "3njv", "3njx" ]

4

[ "PUB00027701" ]

[ "15135077" ]

[ "Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 510, 1484 ]

2

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

[ 1 ]

1

true

Domain

Rhamnogalacturonase B, N-terminal

RhgB_N

4

IPR015365

15,365

Elongation factor P, C-terminal

Elong-fact-P_C

Domain

29,514

false

Elongation factor P (EF-P) stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S ...

[ "GO:0043043", "GO:0005737" ]

[ "peptide biosynthetic process", "cytoplasm" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "SMART", "CDD" ]

[ "PF09285", "SM00841", "cd05794" ]

[ "Elong-fact-P_C", "Elong-fact-P_C", "S1_EF-P_repeat_2" ]

[ 29502, 29416, 26681 ]

3

[]

0

[ "1ueb", "1yby", "3a5z", "3oyy", "3tre", "4v6a", "5j3b", "6enj", "6enu", "6j7m", "6rji", "6rk3", "6s8z", "8s8u", "8vwq", "8w2n" ]

16

[ "PUB00015919", "PUB00033951", "PUB00033952", "PUB00081045", "PUB00081046" ]

[ "15210970", "12932732", "15922593", "9405429", "16928980" ]

[ "Crystal structure of elongation factor P from Thermus thermophilus HB8.", "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis.", "Characterization of a high-...

[ 2004, 2003, 2005, 1997, 2006 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences", "uncultured crenarchaeote MCG" ]

[ 27372, 1550, 1, 590, 1 ]

5

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

[ 11, 2, 8, 7 ]

4

true

Domain

Elongation factor P, C-terminal

Elong-fact-P_C

7

IPR015366

15,366

Peptidase S53, activation domain

S53_propep

Domain

15,173

false

This domain is found at the N terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an α+β sandwich. Cleavage of the domain results in activation of the peptidase [ ].

[ "GO:0008236" ]

[ "serine-type peptidase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "SMART", "CDD" ]

[ "PF09286", "SM00944", "cd11377" ]

[ "Pro-kuma_activ", "Pro-kuma_activ", "Pro-peptidase_S53" ]

[ 15114, 14755, 14161 ]

3

[ "EC", "REACTOME" ]

[ "3.4.14", "R-HSA-381038" ]

[ "EC:3.4.14", "REACTOME:R-HSA-381038" ]

2

[ "1t1e", "3edy", "3ee6" ]

3

[ "PUB00022723" ]

[ "15242607" ]

[ "1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase." ]

[ 2004 ]

1

[]

0

null

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

[ 253, 4127, 10736, 4, 53 ]

5

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

[ 2, 15, 3, 3, 6 ]

5

true

Domain

Peptidase S53, activation domain

S53_propep

1

IPR015367

15,367

Transcription factor CEP-1, DNA-binding domain

Trans_fact_CEP1_DNA-bd

Domain

15

false

This DNA-binding domain is found in the Caenorhabditis transcription factor CEP-1, which is related to human p53. It adopts a β sandwich structure, with nine strands in two β-sheets, in a Greek-key topology [ ].

[]

0

[ "PFAM" ]

[ "PF09287" ]

[ "CEP1-DNA_bind" ]

[ 15 ]

1

[]

0

[ "1t4w" ]

1

[ "PUB00031334" ]

[ "15242600" ]

[ "Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1." ]

[ 2004 ]

1

[]

0

null

[ "Caenorhabditis" ]

[ 15 ]

1

[ "Caenorhabditis elegans" ]

[ 1 ]

1

true

Domain

Transcription factor CEP-1, DNA-binding domain

Trans_fact_CEP1_DNA-bd

1

IPR015368

15,368

Ubiquitin-conjugating enzyme, C-terminal fungi

UBA_C_fun

Domain

1,359

false

This C-terminal domain is found in ubiquitin binding proteins, it adopts a structure consisting of a three α-helix bundle. This domain is predominantly found in fungi [ ].

[]

0

[ "PFAM" ]

[ "PF09288" ]

[ "UBA_3" ]

[ 1359 ]

1

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

[ "R-SCE-8866652", "R-SCE-983168", "R-SPO-8866652", "R-SPO-983168" ]

[ "REACTOME:R-SCE-8866652", "REACTOME:R-SCE-983168", "REACTOME:R-SPO-8866652", "REACTOME:R-SPO-983168" ]

4

[ "1tte" ]

1

[ "PUB00035476" ]

[ "15328341" ]

[ "Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly." ]

[ 2004 ]

1

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 3, 1356 ]

2

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

[ 1, 1, 1 ]

3

true

Domain

Ubiquitin-conjugating enzyme, C-terminal fungi

UBA_C_fun

5

IPR015369

15,369

Follistatin/Osteonectin EGF domain

Follistatin/Osteonectin_EGF

Domain

5,396

false

This domain is predominantly found in osteonectin and follistatin. They adopt an EGF-like structure [ , ]. Follistatin is involved in diverse activities from embryonic development to cell secretion.

[ "GO:0005515" ]

[ "protein binding" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09289" ]

[ "FOLN" ]

[ 5396 ]

1

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

[ "R-BTA-114608", "R-BTA-201451", "R-BTA-2473224", "R-BTA-3000178", "R-BTA-3000497", "R-BTA-381426", "R-BTA-8957275", "R-CEL-114608", "R-CEL-3000178", "R-CEL-381426", "R-CEL-8957275", "R-DRE-2473224", "R-HSA-114608", "R-HSA-1251985", "R-HSA-201451", "R-HSA-2473224", "R-HSA-3000178", ...

[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-201451", "REACTOME:R-BTA-2473224", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-3000497", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-3000178", "REACTOME:R-CEL-381426", "REACTOME:R-CEL-8957275", "REACTOME:R-D...

38

[ "1bmo", "1lr7", "1lr8", "1lr9", "1nub", "2arp", "2b0u", "2kcx", "2p6a", "2v53", "3b4v", "3hh2", "3sek", "5jhw", "6jza", "7kbu" ]

16

[ "PUB00027110", "PUB00029225" ]

[ "12867435", "9501084" ]

[ "Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding.", "Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin." ]

[ 2003, 1998 ]

2

[ "IPR003645" ]

[]

1

0

1

[ "Bilateria", "Kangiella spongicola" ]

[ 5395, 1 ]

2

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

[ 1, 18, 14, 15, 24 ]

5

true

Domain

Follistatin/Osteonectin EGF domain

Follistatin/Osteonectin_EGF

2

IPR015370

15,370

T-cell receptor alpha chain, constant domain

TCR_alpha_C

Domain

314

false

This entry represents the constant domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. alpha/beta TCRs recognise antigen as pepti...

[]

0

[ "PFAM", "CDD" ]

[ "PF09291", "cd07688" ]

[ "DUF1968", "IgC_TCR_alpha" ]

[ 312, 152 ]

2

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

[ "R-HSA-198933", "R-HSA-202424", "R-HSA-202427", "R-HSA-202430", "R-HSA-202433", "R-HSA-389948", "R-MMU-198933", "R-MMU-202424", "R-MMU-202427", "R-MMU-202430", "R-MMU-202433", "R-MMU-389948" ]

[ "REACTOME:R-HSA-198933", "REACTOME:R-HSA-202424", "REACTOME:R-HSA-202427", "REACTOME:R-HSA-202430", "REACTOME:R-HSA-202433", "REACTOME:R-HSA-389948", "REACTOME:R-MMU-198933", "REACTOME:R-MMU-202424", "REACTOME:R-MMU-202427", "REACTOME:R-MMU-202430", "REACTOME:R-MMU-202433", "REACTOME:R-MMU-389...

12

[ "1ao7", "1bd2", "1fyt", "1g6r", "1j8h", "1kgc", "1lp9", "1mi5", "1mwa", "1nfd", "1oga", "1qrn", "1qse", "1qsf", "1tcr", "1ymm", "1zgl", "2ak4", "2bnq", "2bnr", "2bnu", "2cde", "2cdf", "2cdg", "2ckb", "2esv", "2eyr", "2eys", "2eyt", "2f53", "2f54", "2gj6"...

640

[ "PUB00083150", "PUB00083152", "PUB00083153" ]

[ "18800968", "17011774", "17560120" ]

[ "Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes.", "Specificity on a knife-edge: the alphabeta T cell receptor.", "TCR recognition of peptide/MHC class II complexes and superantigens." ]

[ 2008, 2006, 2007 ]

3

[]

0

null

[ "Actinomycetes", "Tetrapoda" ]

[ 3, 311 ]

2

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

[ 20, 4, 9 ]

3

true

Domain

T-cell receptor alpha chain, constant domain

TCR_alpha_C

6

IPR015374

15,374

Chs5p-Arf1p binding

ChAPs

Family

2,937

false

ChAPs (Chs5p-Arf1p-binding proteins) are required for the export of specialised cargo from the Golgi. They physically interact with Chs3, Chs5 and the small GTPase Arf1, and they also form interactions with each other [ ].

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09295", "PTHR31975" ]

[ "ChAPs", "" ]

[ 2858, 2298 ]

2

[]

0

[ "4in3", "4q66", "4wjw", "4yg8" ]

4

[ "PUB00035369" ]

[ "16498409" ]

[ "Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi." ]

[ 2006 ]

1

[]

0

null

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

[ 476, 2447, 3, 11 ]

4

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

[ 1, 1, 4, 1 ]

4

true

Family

Chs5p-Arf1p binding

ChAPs

7

IPR015375

15,375

NADH pyrophosphatase-like, N-terminal

NADH_PPase-like_N

Domain

12,167

false

This entry represents the N-terminal domain found in NADH pyrophosphatase, which has a rudiment Nudix fold according to SCOP. This domain is also found in Nudix hydrolases, such as NudC, which has been shown to act as a NAD decapping enzyme [ ].

[ "GO:0016787" ]

[ "hydrolase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09296" ]

[ "NUDIX-like" ]

[ 12167 ]

1

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

[ "3.6.1.-", "3.6.1.22", "PWY-5381", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6797", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7761", "PWY-7821", "PWY-8289", "R-BTA-196807", "R-HSA-196807", "R-HSA-499943", "R-MMU-196807", "R-MMU-499943", "R-SPO-196807" ]

[ "EC:3.6.1.-", "EC:3.6.1.22", "METACYC:PWY-5381", "METACYC:PWY-5757", "METACYC:PWY-6147", "METACYC:PWY-6383", "METACYC:PWY-6797", "METACYC:PWY-7206", "METACYC:PWY-7419", "METACYC:PWY-7539", "METACYC:PWY-7719", "METACYC:PWY-7761", "METACYC:PWY-7821", "METACYC:PWY-8289", "REACTOME:R-BTA-196...

20

[ "6o3p", "6scx", "8zb3", "8zb4", "8zb5" ]

5

[ "PUB00095660" ]

[ "27428510" ]

[ "Structure and function of the bacterial decapping enzyme NudC." ]

[ 2016 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriota", "Siphoviridae sp. ct3z32", "metagenomes" ]

[ 7984, 3928, 85, 1, 169 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 3, 8, 4, 9, 1, 3, 4, 1, 3 ]

9

true

Domain

NADH pyrophosphatase-like, N-terminal

NADH_PPase-like_N

9

IPR015376

15,376

Zinc ribbon, NADH pyrophosphatase

Znr_NADH_PPase

Domain

15,209

false

This domain has a zinc ribbon structure and is found in proteins such as NAD-capped RNA hydrolases and NAD(P)H pyrophosphatases. It is often found between two NUDIX domains.

[ "GO:0016787", "GO:0046872" ]

[ "hydrolase activity", "metal ion binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF09297" ]

[ "Zn_ribbon_NUD" ]

[ 15209 ]

1

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

[ "3.6.1.-", "3.6.1.22", "PWY-5381", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6797", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7761", "PWY-7821", "PWY-8289", "R-BTA-196807", "R-HSA-196807", "R-HSA-499943", "R-MMU-196807", "R-MMU-499943", "R-SCE-196807" ]

[ "EC:3.6.1.-", "EC:3.6.1.22", "METACYC:PWY-5381", "METACYC:PWY-5757", "METACYC:PWY-6147", "METACYC:PWY-6383", "METACYC:PWY-6797", "METACYC:PWY-7206", "METACYC:PWY-7419", "METACYC:PWY-7539", "METACYC:PWY-7719", "METACYC:PWY-7761", "METACYC:PWY-7821", "METACYC:PWY-8289", "REACTOME:R-BTA-196...

20

[ "1vk6", "2gb5", "5isy", "5iw4", "5iw5", "6o3p", "6scx", "7e44", "8zb3", "8zb4", "8zb5" ]

11

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctA4D8", "unclassified sequences" ]

[ 117, 11688, 3233, 1, 170 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)...

[ 3, 3, 1, 4, 5, 1, 3, 5, 1, 4 ]

10

true

Domain

Zinc ribbon, NADH pyrophosphatase

Znr_NADH_PPase

9

IPR015377

15,377

Fumarylacetoacetase, N-terminal

Fumarylacetoacetase_N

Domain

12,642

false

Fumarylacetoacetase ( ; also known as fumarylacetoacetate hydrolase or FAH) catalyses the hydrolytic cleavage of a carbon-carbon bond in fumarylacetoacetate to yield fumarate and acetoacetate as the final step in phenylalanine and tyrosine degradation [ ]. This is an essential metabolic function in humans, the lack of ...

[ "GO:0004334", "GO:0009072" ]

[ "fumarylacetoacetase activity", "aromatic amino acid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09298" ]

[ "FAA_hydrolase_N" ]

[ 12642 ]

1

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

[ "3.7.1.2", "R-CEL-8963684", "R-DDI-8963684", "R-HSA-8963684", "R-MMU-8963684", "R-RNO-8963684" ]

[ "EC:3.7.1.2", "REACTOME:R-CEL-8963684", "REACTOME:R-DDI-8963684", "REACTOME:R-HSA-8963684", "REACTOME:R-MMU-8963684", "REACTOME:R-RNO-8963684" ]

6

[ "1hyo", "1qcn", "1qco", "1qqj", "2hzy", "4qku", "5ti1" ]

7

[ "PUB00002007", "PUB00022554", "PUB00025833", "PUB00035625" ]

[ "9101289", "10508789", "11154690", "16602095" ]

[ "Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview.", "Crystal structure and mechanism of a carbon-carbon bond hydrolase.", "Mechanistic inferences from the crystal structure of fumarylacetoacetate hydrolase with a bound phosphorus-based inhibitor.", "The gene...

[ 1997, 1999, 2001, 2006 ]

4

[]

0

null

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

[ 7353, 5241, 12, 36 ]

4

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

[ 5, 1, 3, 1, 6, 2, 1, 1, 3, 15 ]

10

true

Domain

Fumarylacetoacetase, N-terminal

Fumarylacetoacetase_N

5

IPR015379

15,379

Minor capsid protein P30, tectiviridae

VP30

Family

8

false

Members of this family form the minor capsid protein of various Tectiviridae including Minor capsid protein P30 [ ].

[ "GO:0019028" ]

[ "viral capsid" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF09300" ]

[ "Tecti-min-caps" ]

[ 8 ]

1

[]

0

[ "1w8x", "6q5u" ]

2

[ "PUB00032209" ]

[ "15525981" ]

[ "Insights into assembly from structural analysis of bacteriophage PRD1." ]

[ 2004 ]

1

[]

0

null

[ "Alphatectivirus" ]

[ 8 ]

1

[]

0

true

Family

Minor capsid protein P30, tectiviridae

VP30

2

IPR015381

15,381

XLF-like, N-terminal

XLF-like_N

Domain

2,699

false

This entry represents the N-terminal domain of human Non-homologous end-joining factor 1 (NHEJ1 or XLF), Xrcc4-like factor 1 from Schizosaccharomyces pombe (Xlf1) and similar sequences from fungi and animals. XLF (also called Cernunnos) is involved in DNA nonhomologous end joining (NHEJ) required for double-strand brea...

[ "GO:0006302", "GO:0005634" ]

[ "double-strand break repair", "nucleus" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09302" ]

[ "XLF" ]

[ 2699 ]

1

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

[ "R-HSA-5693571", "R-MMU-5693571", "R-RNO-5693571" ]

[ "REACTOME:R-HSA-5693571", "REACTOME:R-MMU-5693571", "REACTOME:R-RNO-5693571" ]

3

[ "2qm4", "2r9a", "3q4f", "3rwr", "3sr2", "3w03", "7lsy", "7lt3", "7nfc", "7nfe", "7zyg", "8bhv", "8bhy", "8bot", "8eza", "8ezb", "9cq3", "9cq6", "9cqc", "9n81", "9n82", "9n83" ]

22

[ "PUB00035487", "PUB00035488", "PUB00074899", "PUB00154352" ]

[ "16439205", "16571728", "23442139", "17151234" ]

[ "XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining.", "Cernunnos interacts with the XRCC4 x DNA-ligase IV complex and is homologous to the yeast nonhomologous end-joining factor Nej1.", "XRCC4 and XLF form long helical protein filaments suitable for DNA end protection a...

[ 2006, 2006, 2013, 2007 ]

4

[]

0

null

[ "Eukaryota" ]

[ 2699 ]

1

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

[ 1, 6, 1, 1, 4, 1 ]

6

true

Domain

XLF-like, N-terminal

XLF-like_N

4

IPR015382

15,382

KCNMB2, ball/chain domain

KCNMB2_ball_chain_dom

Domain

1,040

false

This domain is found in the cytoplasmic N terminus of KCNMB2, the beta-2 subunit of large conductance calcium and voltage-activated potassium channels. It is responsible for the fast inactivation of these channels [ ].

[]

0

[ "PFAM" ]

[ "PF09303" ]

[ "KcnmB2_inactiv" ]

[ 1040 ]

1

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

[ "R-HSA-1296052", "R-HSA-418457", "R-MMU-1296052", "R-RNO-1296052" ]

[ "REACTOME:R-HSA-1296052", "REACTOME:R-HSA-418457", "REACTOME:R-MMU-1296052", "REACTOME:R-RNO-1296052" ]

4

[ "1jo6", "9czh", "9czj", "9czk", "9czm", "9czo", "9czq", "9d18", "9d19" ]

9

[ "PUB00026461" ]

[ "11517232" ]

[ "NMR structure of the \"ball-and-chain\" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels." ]

[ 2001 ]

1

[]

0

null

[ "Euteleostomi" ]

[ 1040 ]

1

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

[ 6, 11, 4, 11 ]

4

true

Domain

KCNMB2, ball/chain domain

KCNMB2_ball_chain_dom

5

IPR015383

15,383

Cortexillin, coiled coil

Cortexillin-I_CC

Domain

14

false

This domain is predominantly found in the actin-bundling protein cortexillin I and II from Dictyostelium discoideum (Slime mold). The domain has a structure consisting of an 18-heptad-repeat α-helical coiled-coil, and is a prerequisite for the assembly of Cortexillin I [ ].

[]

0

[ "PFAM" ]

[ "PF09304" ]

[ "Cortex-I_coil" ]

[ 14 ]

1

[]

0

[ "1d7m" ]

1

[ "PUB00028329" ]

[ "10745004" ]

[ "The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges." ]

[ 2000 ]

1

[]

0

null

[ "Dictyostelia" ]

[ 14 ]

1

[]

0

true

Domain

Cortexillin, coiled coil

Cortexillin-I_CC

7

IPR015384

15,384

TACI, cysteine-rich domain

TACI_Cys-rich-dom

Domain

802

false

Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities [ , , ]. Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a monocyte-derived cytotoxin that has been implicated in tumour regression, septic shock and cachexia [ , ]. The protein is synthesised a...

[]

0

[ "PFAM" ]

[ "PF09305" ]

[ "TACI-CRD2" ]

[ 802 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-5669034", "R-MMU-5669034" ]

[ "REACTOME:R-HSA-5669034", "REACTOME:R-MMU-5669034" ]

2

[ "1xu1", "1xut" ]

2

[ "PUB00002042", "PUB00004130", "PUB00006091", "PUB00006095", "PUB00006098", "PUB00006101", "PUB00015257", "PUB00035472" ]

[ "8095800", "1377364", "2989794", "3349526", "2777790", "2268312", "15335677", "15542592" ]

[ "A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.", "Emerging cytokine family.", "Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression.", "A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein:...

[ 1993, 1992, 1985, 1988, 1989, 1990, 1993, 2005 ]

8

[]

0

null

[ "Actinomycetes", "Vertebrata" ]

[ 2, 800 ]

2

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

[ 2, 6, 4, 2 ]

4

true

Domain

TACI, cysteine-rich domain

TACI_Cys-rich-dom

9

IPR015385

15,385

Bacteriophage P22, Gp8, scaffold

Phage_P22_Gp8_scaffold

Family

442

false

Members of this family of scaffolding proteins are produced by various bacteriophages [ ].

[]

0

[ "PFAM" ]

[ "PF09306" ]

[ "Phage-scaffold" ]

[ 442 ]

1

[]

0

[ "1gp8", "2gp8", "8i1v", "9kyv", "9kyw", "9kyx", "9kyy" ]

7

[ "PUB00028571" ]

[ "10764583" ]

[ "Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus." ]

[ 2000 ]

1

[]

0

null

[ "Pseudomonadota", "Viruses", "marine sediment metagenome" ]

[ 414, 27, 1 ]

3

[]

0

true

Family

Bacteriophage P22, Gp8, scaffold

Phage_P22_Gp8_scaffold

7

IPR015386

15,386

MHC class II-associated invariant chain/CLIP, MHC II-interacting

MHC_II-assoc_invar/CLIP_MHC-bd

Domain

1,369

false

This domain is found in MHC class II-associated invariant chain (Ii), and in class II invariant chain-associated peptide (CLIP), and is required for association with class II major histocompatibility complex (MHC II) in the MHC II processing pathway [ ]. Ii plays a critical role in the assembly of the MHC, as well as i...

[ "GO:0042289", "GO:0006886", "GO:0006955", "GO:0019882", "GO:0016020" ]

[ "MHC class II protein binding", "intracellular protein transport", "immune response", "antigen processing and presentation", "membrane" ]

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

5

[ "PFAM" ]

[ "PF09307" ]

[ "MHC2-interact" ]

[ 1369 ]

1

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

[ "R-HSA-202733", "R-HSA-2132295", "R-HSA-9925563", "R-MMU-202733", "R-MMU-2132295", "R-RNO-202733", "R-RNO-2132295" ]

[ "REACTOME:R-HSA-202733", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-9925563", "REACTOME:R-MMU-202733", "REACTOME:R-MMU-2132295", "REACTOME:R-RNO-202733", "REACTOME:R-RNO-2132295" ]

7

[ "8vrw", "8vsp" ]

2

[ "PUB00011780", "PUB00027464", "PUB00035863", "PUB00035864" ]

[ "9843486", "12589760", "16181341", "16337363" ]

[ "Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii.", "Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif.", "Achieving stability through editing and chaperoning: regulation of MHC class II pept...

[ 1998, 2003, 2005, 2006 ]

4

[]

0

null

[ "Bilateria", "Rhodobacter flavimaris" ]

[ 1368, 1 ]

2

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

[ 2, 6, 3, 6 ]

4

true

Domain

MHC class II-associated invariant chain/CLIP, MHC II-interacting

MHC_II-assoc_invar/CLIP_MHC-bd

5

IPR015387

15,387

LuxQ, periplasmic domain

LuxQ-periplasm_dom

Domain

438

false

LuxQ is a sensor histidine kinase involved in quorum sensing in the marine bacterium Vibrio harveyi. Quorum sensing is a process of bacterial cell-cell communication driven by secreted signaling molecules called autoinducers such as AI-2. The receptor for this autoinducer is LuxPQ, formed as a result of the association...

[ "GO:0004673", "GO:0016791" ]

[ "protein histidine kinase activity", "phosphatase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF09308" ]

[ "LuxQ-periplasm" ]

[ 438 ]

1

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

[ "2.7.13.3", "3.1.3.-", "PWY-4702", "PWY-5491", "PWY-6148", "PWY-6352", "PWY-6365", "PWY-6366", "PWY-6368", "PWY-6456", "PWY-6575", "PWY-6627", "PWY-6664", "PWY-6686", "PWY-6720", "PWY-6724", "PWY-6955", "PWY-6990", "PWY-6991", "PWY-7018", "PWY-7119", "PWY-7321", "PWY-7531...

[ "EC:2.7.13.3", "EC:3.1.3.-", "METACYC:PWY-4702", "METACYC:PWY-5491", "METACYC:PWY-6148", "METACYC:PWY-6352", "METACYC:PWY-6365", "METACYC:PWY-6366", "METACYC:PWY-6368", "METACYC:PWY-6456", "METACYC:PWY-6575", "METACYC:PWY-6627", "METACYC:PWY-6664", "METACYC:PWY-6686", "METACYC:PWY-6720",...

37

[ "1zhh", "2hj9", "2hje", "3c30", "3c38" ]

5

[ "PUB00035414", "PUB00041419" ]

[ "15916958", "16990134" ]

[ "Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2.", "Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing." ]

[ 2005, 2006 ]

2

[]

0

null

[ "Bacteria" ]

[ 438 ]

1

[]

0

true

Domain

LuxQ, periplasmic domain

LuxQ-periplasm_dom

9

IPR015388

15,388

FCP1-like phosphatase, C-terminal

FCP1_C

Domain

1,321

false

The C-terminal domain of FCP-1 is required for interaction with the carboxy terminal domain of RAP74. Interaction relies extensively on van der Waals contacts between hydrophobic residues situated within α-helices in both domains [ ]. Fcp1 catalyses the dephosphorylation of the C-terminal domain of the largest RNA poly...

[]

0

[ "PFAM" ]

[ "PF09309" ]

[ "FCP1_C" ]

[ 1321 ]

1

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

[ "R-HSA-112382", "R-HSA-113418", "R-HSA-167152", "R-HSA-167158", "R-HSA-167200", "R-HSA-167238", "R-HSA-167242", "R-HSA-167243", "R-HSA-167246", "R-HSA-167287", "R-HSA-167290", "R-HSA-674695", "R-HSA-6796648", "R-HSA-75955", "R-MMU-112382", "R-MMU-113418", "R-MMU-674695", "R-MMU-679...

[ "REACTOME:R-HSA-112382", "REACTOME:R-HSA-113418", "REACTOME:R-HSA-167152", "REACTOME:R-HSA-167158", "REACTOME:R-HSA-167200", "REACTOME:R-HSA-167238", "REACTOME:R-HSA-167242", "REACTOME:R-HSA-167243", "REACTOME:R-HSA-167246", "REACTOME:R-HSA-167287", "REACTOME:R-HSA-167290", "REACTOME:R-HSA-674...

19

[ "1j2x", "1onv" ]

2

[ "PUB00029513", "PUB00090490", "PUB00142978" ]

[ "12732728", "12721286", "22692537" ]

[ "NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.", "A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5.", "Fcp1-dependent dephosphorylation is required for M-phase-promoting fact...

[ 2003, 2003, 2012 ]

3

[]

0

null

[ "Bilateria" ]

[ 1321 ]

1

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

[ 2, 5, 4, 5 ]

4

true

Domain

FCP1-like phosphatase, C-terminal

FCP1_C

3

IPR015389

15,389

POU, class 2, associating factor 1

PD-C2-AF1

Family

937

false

Members of this family are transcriptional co-activators that specifically associate with either OCT1 or OCT2, through recognition of their POU domains. They are essential for the response of B-cells to antigens and required for the formation of germinal centres [ ].

[]

0

[ "PFAM" ]

[ "PF09310" ]

[ "PD-C2-AF1" ]

[ 937 ]

1

[]

0

[ "1cqt", "9pfn", "9pfo" ]

3

[ "PUB00024033" ]

[ "10541551" ]

[ "Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface." ]

[ 1999 ]

1

[]

0

null

[ "Gnathostomata" ]

[ 937 ]

1

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

[ 6, 2, 4, 4 ]

4

true

Family

POU, class 2, associating factor 1

PD-C2-AF1

3

IPR015390

15,390

Rabaptin, GTPase-Rab5 binding domain

Rabaptin_Rab5-bd_dom

Domain

3,385

false

This domain is predominantly found in Rabaptin and allows for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes [ ].

[]

0

[ "PFAM" ]

[ "PF09311" ]

[ "Rab5-bind" ]

[ 3385 ]

1

[ "REACTOME" ]

[ "R-HSA-8854214" ]

[ "REACTOME:R-HSA-8854214" ]

1

[ "1tu3", "1x79", "4n3y", "4n3z", "4q9u" ]

5

[ "PUB00022748" ]

[ "15378032" ]

[ "Structural basis of Rab5-Rabaptin5 interaction in endocytosis." ]

[ 2004 ]

1

[]

0

null

[ "Metazoa" ]

[ 3385 ]

1

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

[ 1, 4, 1, 8, 4, 19 ]

6

true

Domain

Rabaptin, GTPase-Rab5 binding domain

Rabaptin_Rab5-bd_dom

3

IPR015391

15,391

SurA N-terminal

SurA_N

Domain

8,920

false

The correct folding of outer membrane proteins (OMPs) in Gram-negative bacteria is facilitated by the survival protein SurA [ , ]. This entry represents the helical domain found at the N-terminal of the chaperone SurA that, together with the C-terminal, forms a core domain which contains OMP binding sites. OMP binding ...

[]

0

[ "PFAM" ]

[ "PF09312" ]

[ "SurA_N" ]

[ 8920 ]

1

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

[ "5.2.1.8", "GenProp0928", "R-HSA-9760173" ]

[ "EC:5.2.1.8", "GP:GenProp0928", "REACTOME:R-HSA-9760173" ]

3

[ "1m5y", "2pv3", "3rgc", "8pz1", "8pz2", "8pzu", "8pzv", "8q0g", "8qp5", "8qpu", "8qpv", "8qpw", "9hg5", "9hg6", "9hg7", "9hg8", "9hg9", "9hga" ]

18

[ "PUB00055597", "PUB00099907" ]

[ "8626309", "32358557" ]

[ "SurA assists the folding of Escherichia coli outer membrane proteins.", "Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients." ]

[ 1996, 2020 ]

2

[]

0

null

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

[ 8770, 11, 139 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

SurA N-terminal

SurA_N

9

IPR015392

15,392

TehB/YeaR-like domain

TehB/YeaR-like_dom

Domain

3,448

false

This domain, previously known as DUF1971, is found at the N-terminal end of the probable S-adenosyl-L-methionine-dependent methyltransferase TehB from Haemophilus influenzae and similar bacterial Tellurite resistance proteins and covering almost the whole length of the sequence in YeaR from Escherichia coli and other u...

[]

0

[ "PFAM" ]

[ "PF09313" ]

[ "TehB-like" ]

[ 3448 ]

1

[]

0

[ "3bb6", "3dl3", "3m70" ]

3

[ "PUB00014885", "PUB00161042" ]

[ "11053398", "20075041" ]

[ "Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance.", "Characterization of the Haemophilus influenzae tehB gene and its role in virulence." ]

[ 2000, 2010 ]

2

[]

0

null

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

[ 3403, 31, 14 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

TehB/YeaR-like domain

TehB/YeaR-like_dom

9

IPR015393

15,393

Domain of unknown function DUF1972

DUF1972

Domain

2,468

false

This domain is functionally uncharacterised and found in bacterial glycosyltransferases and rhamnosyltransferases.

[]

0

[ "PFAM" ]

[ "PF09314" ]

[ "DUF1972" ]

[ 2468 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Alveolata", "Archaea", "Bacteria", "metagenomes" ]

[ 2, 21, 2425, 20 ]

4

[]

0

true

Domain

Domain of unknown function DUF1972

DUF1972

2

IPR015395

15,395

C-myb, C-terminal

C-myb_C

Domain

4,839

false

This entry represents the C-terminal domain of the proto-oncogene c-myb and the viral transforming protein myb. Truncation of the domain results in 'activation' of c-myb and subsequent tumourigenesis [ ].

[]

0

[ "PFAM" ]

[ "PF09316" ]

[ "Cmyb_C" ]

[ 4839 ]

1

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

[ "R-HSA-1362300", "R-HSA-156711", "R-HSA-5601884", "R-HSA-8869496", "R-HSA-8939236", "R-HSA-9018519", "R-HSA-9616222", "R-HSA-983231", "R-HSA-9834899" ]

[ "REACTOME:R-HSA-1362300", "REACTOME:R-HSA-156711", "REACTOME:R-HSA-5601884", "REACTOME:R-HSA-8869496", "REACTOME:R-HSA-8939236", "REACTOME:R-HSA-9018519", "REACTOME:R-HSA-9616222", "REACTOME:R-HSA-983231", "REACTOME:R-HSA-9834899" ]

9

[]

0

[ "PUB00035370" ]

[ "2670562" ]

[ "Activation of c-myb by carboxy-terminal truncation: relationship to transformation of murine haemopoietic cells in vitro." ]

[ 1989 ]

1

[]

0

null

[ "Avian myeloblastosis virus", "Eumetazoa" ]

[ 3, 4836 ]

2

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

[ 12, 2, 21, 15, 14 ]

5

true

Domain

C-myb, C-terminal

C-myb_C

4

IPR015396

15,396

Acyl-CoA dehydrogenase, C-terminal, bacterial-type

FadE_C

Domain

7,458

false

This entry represents a domain found at the C-terminal end of Acyl-coenzyme A dehydrogenase from Escherichia coli (FadE) and similar proteins mainly found in bacteria. FadE catalyses the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation...

[ "GO:0003995", "GO:0033539" ]

[ "acyl-CoA dehydrogenase activity", "fatty acid beta-oxidation using acyl-CoA dehydrogenase" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09317" ]

[ "ACDH_C" ]

[ 7458 ]

1

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

[ "1.3.8.7", "1.3.8.8", "GenProp1562", "GenProp1717", "PWY-7094", "PWY-7654", "PWY-8181", "PWY-8354" ]

[ "EC:1.3.8.7", "EC:1.3.8.8", "GP:GenProp1562", "GP:GenProp1717", "METACYC:PWY-7094", "METACYC:PWY-7654", "METACYC:PWY-8181", "METACYC:PWY-8354" ]

8

[]

0

[ "PUB00101040" ]

[ "12057976" ]

[ "The enigmatic Escherichia coli fadE gene is yafH." ]

[ 2002 ]

1

[]

0

null

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

[ 7203, 147, 3, 105 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Acyl-CoA dehydrogenase, C-terminal, bacterial-type

FadE_C

1

IPR015397

15,397

Glycosyl transferase 1, domain A

Glyco_trans_A_1

Domain

107

false

This entry represents a domain found predominantly at the N terminus of various prokaryotic alpha-glucosyltransferases. According to whether the domain exists as a whole molecule or as a half molecule determines the number of sugar residues that the molecule transfers. Two-domain proteins are processive in that they tr...

[]

0

[ "PFAM" ]

[ "PF09318" ]

[ "Glyco_trans_A_1" ]

[ 107 ]

1

[ "GP" ]

[ "GenProp1398" ]

[ "GP:GenProp1398" ]

1

[]

0

[ "PUB00064844", "PUB00075675" ]

[ "21862581", "7883697" ]

[ "A molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins.", "Multidomain architecture of beta-glycosyl transferases: implications for mechanism of action." ]

[ 2011, 1995 ]

2

[]

0

null

[ "Bacteria" ]

[ 107 ]

1

[]

0

true

Domain

Glycosyl transferase 1, domain A

Glyco_trans_A_1

7

IPR015399

15,399

Domain of unknown function DUF1977, DnaJ-like

DUF1977_DnaJ-like

Domain

7,064

false

This C-terminal domain is functionally uncharacterised and predominantly found in Dnaj-like proteins.

[]

0

[ "PFAM" ]

[ "PF09320" ]

[ "DUF1977" ]

[ 7064 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Eukaryota" ]

[ 7064 ]

1

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

[ 9, 1, 3, 3, 9, 4, 1, 6, 10, 1, 9 ]

11

true

Domain

Domain of unknown function DUF1977, DnaJ-like

DUF1977_DnaJ-like

5

IPR015400

15,400

Domain of unknown function DUF1978, IncA

DUF1978_IncA

Domain

84

false

This domain is found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified. This entry includes the IncA proteins

[]

0

[ "PFAM" ]

[ "PF09321" ]

[ "DUF1978" ]

[ 84 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Chaenocephalus aceratus", "Chlamydia" ]

[ 1, 83 ]

2

[]

0

true

Domain

Domain of unknown function DUF1978, IncA

DUF1978_IncA

1

IPR015401

15,401

Transposase, MuDR, N-terminal

Transposase_MuDR_N

Domain

369

false

This N-terminal domain is functionally uncharacterised and found in various Oryza sativa (Rice) mutator-like transposases.

[]

0

[ "PFAM" ]

[ "PF09322" ]

[ "DUF1979" ]

[ 369 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Poaceae", "Robertmurraya kyonggiensis" ]

[ 368, 1 ]

2

[ "Oryza sativa subsp. japonica" ]

[ 188 ]

1

true

Domain

Transposase, MuDR, N-terminal

Transposase_MuDR_N

3

IPR015402

15,402

Protein of unknown function DUF1980

DUF1980

Family

5,035

false

Members of this occur in gene pairs with members of . The N-terminal region contains several predicted transmembrane helix regions while the few invariant residues (G, CxxD, and W) occur in the C-terminal region [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR03943" ]

[ "" ]

[ 5035 ]

1

[]

0

[]

0

[ "PUB00159624" ]

[ "24142257" ]

[ "SMU.746-SMU.747, a putative membrane permease complex, is involved in aciduricity, acidogenesis, and biofilm formation in Streptococcus mutans." ]

[ 2014 ]

1

[]

0

null

[ "Bacteria", "Trichuris trichiura", "metagenomes" ]

[ 5014, 1, 20 ]

3

[]

0

true

Family

Protein of unknown function DUF1980

DUF1980

7

IPR015403

15,403

Mon2/Sec7/BIG1-like, HDS

Mon2/Sec7/BIG1-like_HDS

Domain

14,693

false

This entry represents a HDS (homology downstream of Sec7) domain found towards the C-terminal of guanine nucleotide exchange factors involved Golgi transport, such as budding yeast protein Sec7, protein Mon2 and BIG1-like proteins [ , ]. Sec7 is involved in the secretory pathway as a protein binding scaffold for the CO...

[]

0

[ "PFAM" ]

[ "PF09324" ]

[ "Sec7-like_HDS" ]

[ 14693 ]

1

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

[ "R-HSA-390471", "R-SCE-6811438", "R-SPO-6811438" ]

[ "REACTOME:R-HSA-390471", "REACTOME:R-SCE-6811438", "REACTOME:R-SPO-6811438" ]

3

[ "8ucq" ]

1

[ "PUB00076747", "PUB00101184", "PUB00101185" ]

[ "11208097", "26765562", "27373159" ]

[ "Sec7p directs the transitions required for yeast Golgi biogenesis.", "The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.", "Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi." ]

[ 2000, 2016, 2016 ]

3

[]

0

null

[ "Eukaryota" ]

[ 14693 ]

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...

[ 24, 2, 9, 4, 18, 7, 1, 12, 16, 1, 2, 196 ]

12

true

Domain

Mon2/Sec7/BIG1-like, HDS

Mon2/Sec7/BIG1-like_HDS

3

IPR015404

15,404

Sorting nexin/Vps5-like, C-terminal

Vps5_C

Domain

14,639

false

Vps5 is a sorting nexin that functions in membrane trafficking. This is the C-terminal dimerisation domain [ ].

[]

0

[ "PFAM" ]

[ "PF09325" ]

[ "Vps5" ]

[ 14639 ]

1

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

[ "R-BTA-432722", "R-HSA-432722", "R-MMU-432722", "R-RNO-432722" ]

[ "REACTOME:R-BTA-432722", "REACTOME:R-HSA-432722", "REACTOME:R-MMU-432722", "REACTOME:R-RNO-432722" ]

4

[ "4fzs", "6h7w", "7d6d", "7d6e", "8a1g", "8abq", "8afz" ]

7

[ "PUB00035482" ]

[ "12181349" ]

[ "Identification of the functional domains of yeast sorting nexins Vps5p and Vps17p." ]

[ 2002 ]

1

[]

[ "IPR028654", "IPR028657", "IPR028660", "IPR035803" ]

0

4

0

[ "Candidatus Cryptobacteroides excrementipullorum", "Eukaryota" ]

[ 1, 14638 ]

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...

[ 11, 4, 10, 5, 22, 16, 3, 10, 22, 2, 1, 36 ]

12

true

Domain

Sorting nexin/Vps5-like, C-terminal

Vps5_C

7

IPR015405

15,405

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial-like

NDUFS1-like_C

Domain

7,357

false

This entry represents a domain found at the C-terminal end of various NADH dehydrogenases from bacteria and eukaryotes, including NADH-quinone oxidoreductase subunit G from Rickettsia typhi (NuoG) and NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial from humans (NDUFS1, also known as Complex I-75kD, CI-75kD...

[ "GO:0016651", "GO:0051536" ]

[ "oxidoreductase activity, acting on NAD(P)H", "iron-sulfur cluster binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF09326" ]

[ "NADH_dhqG_C" ]

[ 7357 ]

1

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

[ "7.1.1.2", "PWY-3781", "PWY-4302", "PWY-5083", "PWY-6692", "R-BTA-611105", "R-BTA-6799198", "R-BTA-9837999", "R-DME-611105", "R-DME-6799198", "R-DME-9837999", "R-HSA-611105", "R-HSA-6799198", "R-HSA-9837999", "R-MMU-611105", "R-MMU-6799198", "R-MMU-9837999", "R-RNO-611105", "R-RN...

[ "EC:7.1.1.2", "METACYC:PWY-3781", "METACYC:PWY-4302", "METACYC:PWY-5083", "METACYC:PWY-6692", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-6799198", "REACTOME:R-BTA-9837999", "REACTOME:R-DME-611105", "REACTOME:R-DME-6799198", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-679...

20

[ "5gpn", "5gup", "5lnk", "5o31", "5xtb", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6gcs", "6q9d", "6qa9", "6qbx", "6qc2", "6qc3", "6qc4", "6qc5", "6qc6", "6qc7", "6qc8", "6qc9", "6qca", "6qcf", "6rfq", "6rfr", "6rfs", "6x89", "6y79", "6yj4", "6zk9", "6zkc"...

262

[ "PUB00103528", "PUB00103529", "PUB00103530" ]

[ "31557978", "30879903", "21203893" ]

[ "Mutations in NDUFS1 Cause Metabolic Reprogramming and Disruption of the Electron Transfer.", "MDM2 Integrates Cellular Respiration and Apoptotic Signaling through NDUFS1 and the Mitochondrial Network.", "Progressive cavitating leukoencephalopathy associated with respiratory chain complex I deficiency and a nov...

[ 2019, 2019, 2011 ]

3

[]

0

null

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

[ 2913, 4415, 29 ]

3

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

[ 9, 1, 1, 3, 5, 4, 1, 4, 4, 8 ]

10

true

Domain

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial-like

NDUFS1-like_C

5

IPR015406

15,406

Tip attachment protein J, central straight fiber domain

GpJ_CSF

Domain

5,419

false

This entry represents the central straight fiber (CSF) domain of Tip attachment protein J from Escherichia phage lambda (GpJ) and similar bacterial and viral proteins. This longitudinally oriented domain, folds into a mixed β-sheet prism and undergoes a range of structural rearrangements [ ]. It is often found in assoc...

[]

0

[ "PFAM" ]

[ "PF09327" ]

[ "Phage_Tail_Tip" ]

[ 5419 ]

1

[]

0

[ "7z4b", "8iyk", "8iyl", "8jvm", "8k35", "8xcg", "8xci", "8xcj", "8xck", "9l9p" ]

10

[ "PUB00075602", "PUB00075672", "PUB00155963", "PUB00155964" ]

[ "6228546", "23542343", "38760367", "18294652" ]

[ "Proteinase sensitivity of bacteriophage lambda tail proteins gpJ and pH in complexes with the lambda receptor.", "Tail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster.", "Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor.", "Genomic and ...

[ 1984, 2013, 2024, 2008 ]

4

[]

0

null

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

[ 4774, 7, 625, 13 ]

4

[]

0

true

Domain

Tip attachment protein J, central straight fiber domain

GpJ_CSF

8

IPR015407

15,407

Phytochelatin synthase, C-terminal

Phytochelatin_synthase_C

Domain

1,323

false

This entry represents the C-terminal region of plant phytochelatin synthases (also known as glutathione gamma-glutamylcysteinyltransferase; ), which is involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. This enzyme is required for detoxification of...

[ "GO:0016756", "GO:0046872", "GO:0010038", "GO:0046938" ]

[ "glutathione gamma-glutamylcysteinyltransferase activity", "metal ion binding", "response to metal ion", "phytochelatin biosynthetic process" ]

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

4

[ "PFAM" ]

[ "PF09328" ]

[ "Phytochelatin_C" ]

[ 1323 ]

1

[ "EC", "METACYC" ]

[ "2.3.2.15", "PWY-6745" ]

[ "EC:2.3.2.15", "METACYC:PWY-6745" ]

2

[]

0

[ "PUB00044775" ]

[ "18270423" ]

[ "Chelation of cadmium ions by phytochelatin synthase: role of the cysteine-rich C-terminal." ]

[ 2008 ]

1

[]

0

null

[ "Nannocystis", "Streptophyta" ]

[ 2, 1321 ]

2

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

[ 9, 10, 3 ]

3

true

Domain

Phytochelatin synthase, C-terminal

Phytochelatin_synthase_C

2

IPR015408

15,408

Zinc finger, Mcm10/DnaG-type

Znf_Mcm10/DnaG

Domain

3,781

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:0006260", "GO:0005634" ]

[ "DNA replication", "nucleus" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09329" ]

[ "zf-primase" ]

[ 3781 ]

1

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

[ "R-DME-176187", "R-DME-68962", "R-HSA-176187", "R-HSA-68962", "R-MMU-176187", "R-MMU-68962", "R-SCE-176187", "R-SCE-68962", "R-SPO-176187", "R-SPO-68962", "R-XTR-68962" ]

[ "REACTOME:R-DME-176187", "REACTOME:R-DME-68962", "REACTOME:R-HSA-176187", "REACTOME:R-HSA-68962", "REACTOME:R-MMU-176187", "REACTOME:R-MMU-68962", "REACTOME:R-SCE-176187", "REACTOME:R-SCE-68962", "REACTOME:R-SPO-176187", "REACTOME:R-SPO-68962", "REACTOME:R-XTR-68962" ]

11

[ "3ebe", "3h15", "7y01" ]

3

[ "PUB00014077", "PUB00035481", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "12665246", "16704411", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Zinc fingers--folds for many occasions.", "The beta domain is required for Vps4p oligomerization into a functionally active ATPase.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA.", ...

[ 2002, 2006, 2007, 2005, 2005, 1999, 2001 ]

7

[]

0

null

[ "Eukaryota" ]

[ 3781 ]

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...

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

12

true

Domain

Zinc finger, Mcm10/DnaG-type

Znf_Mcm10/DnaG

3

IPR015409

15,409

D-lactate dehydrogenase, membrane binding, C-terminal

Lactate_DH_C

Domain

3,495

false

Members of this entry are predominantly found in prokaryotic D-lactate dehydrogenase, forming the cap-membrane-binding domain, which consists of a large seven-stranded antiparallel β-sheet flanked on both sides by α-helices. They allow for membrane association [ ].

[ "GO:0050660", "GO:0055085" ]

[ "flavin adenine dinucleotide binding", "transmembrane transport" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09330" ]

[ "Lact-deh-memb" ]

[ 3495 ]

1

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

[ "1.1.5.12", "GenProp1367", "GenProp1578", "PWY-5386", "PWY-7425" ]

[ "EC:1.1.5.12", "GP:GenProp1367", "GP:GenProp1578", "METACYC:PWY-5386", "METACYC:PWY-7425" ]

5

[ "1f0x" ]

1

[ "PUB00024738" ]

[ "10944213" ]

[ "The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme." ]

[ 2000 ]

1

[]

0

null

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

[ 3402, 78, 15 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

D-lactate dehydrogenase, membrane binding, C-terminal

Lactate_DH_C

1

IPR015410

15,410

Domain of unknown function DUF1985

DUF1985

Domain

9,185

false

This domain is functionally uncharacterised; it is predominantly found in proteins from Magnoliopsida (flowering plants).

[]

0

[ "PFAM" ]

[ "PF09331" ]

[ "DUF1985" ]

[ 9185 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Eukaryota" ]

[ 9185 ]

1

[ "Arabidopsis thaliana" ]

[ 220 ]

1

true

Domain

Domain of unknown function DUF1985

DUF1985

3

IPR015411

15,411

Replication factor Mcm10, C-terminal

Rep_factor_Mcm10_C

Domain

1,569

false

This entry represents a domain found in the C-terminal region of the Mcm10 protein, which is a eukaryotic DNA replication factor that regulates the stability and chromatin association of DNA polymerase alpha [ ].

[]

0

[ "SMART" ]

[ "SM01280" ]

[ "Mcm10" ]

[ 1569 ]

1

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

[ "R-DME-176187", "R-DME-68962", "R-HSA-176187", "R-HSA-68962", "R-MMU-176187", "R-MMU-68962", "R-XTR-68962" ]

[ "REACTOME:R-DME-176187", "REACTOME:R-DME-68962", "REACTOME:R-HSA-176187", "REACTOME:R-HSA-68962", "REACTOME:R-MMU-176187", "REACTOME:R-MMU-68962", "REACTOME:R-XTR-68962" ]

7

[ "2kwq" ]

1

[ "PUB00035418" ]

[ "15494305" ]

[ "Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha." ]

[ 2004 ]

1

[]

0

null

[ "Eukaryota" ]

[ 1569 ]

1

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

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

6

true

Domain

Replication factor Mcm10, C-terminal

Rep_factor_Mcm10_C

9

IPR015413

15,413

Methionyl/Leucyl tRNA synthetase

Methionyl/Leucyl_tRNA_Synth

Domain

70,679

false

This entry represents the methionyl and leucyl tRNA synthetases, which are class I aminoacyl-tRNA synthetases. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes...

[ "GO:0000166", "GO:0004812", "GO:0005524", "GO:0006418" ]

[ "nucleotide binding", "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation" ]

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

4

[ "PFAM" ]

[ "PF09334" ]

[ "tRNA-synt_1g" ]

[ 70679 ]

1

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

[ "6.1.1", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-9856649", "R-MMU-9856649" ]

[ "EC:6.1.1", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

7

[ "1a8h", "1f4l", "1h3n", "1mea", "1med", "1obc", "1obh", "1p7p", "1pfu", "1pfv", "1pfw", "1pfy", "1pg0", "1pg2", "1qqt", "1rqg", "1woy", "2bte", "2byt", "2csx", "2ct8", "2d54", "2d5b", "2v0c", "2v0g", "2x1l", "2x1m", "3h97", "3h99", "3h9b", "3h9c", "3kfl"...

157

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[]

[ "IPR033911" ]

0

1

0

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

[ 1372, 53643, 14459, 41, 1164 ]

5

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

[ 16, 6, 5, 6, 2, 10, 6, 3, 16, 6, 2, 3, 47 ]

13

true

Domain

Methionyl/Leucyl tRNA synthetase

Methionyl/Leucyl_tRNA_Synth

8

IPR015415

15,415

Spastin/Vps4, C-terminal

Spast_Vps4_C

Domain

21,339

false

This domain is found at the C-terminal of a group of eukaryotic and archaeal proteins that belong to the AAA ATPase family, including human Spastin [ , ] and Vacuolar protein sorting-associated protein 4 (Vps4) from Saccharomyces cerevisiae [ ]. It forms an α-helix structure and is required for oligomerisation [ ].

[]

0

[ "PFAM" ]

[ "PF09336" ]

[ "Vps4_C" ]

[ 21339 ]

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-917729", "R-BTA-9668328", "R-CEL-110320", "R-CEL-3371511", "R-CEL-382556", "R-CEL-532668", "R-CEL-5358346", "R-CEL-5689877", "R-CEL-6798695", "R-CEL-8876725", "R-CEL-8951664", "R-CEL-9013407", "R-CEL-9755511", "R-DDI-917729", "R-DDI-9668328", "R-DME-110320", "R-DME-3371511", ...

[ "REACTOME:R-BTA-917729", "REACTOME:R-BTA-9668328", "REACTOME:R-CEL-110320", "REACTOME:R-CEL-3371511", "REACTOME:R-CEL-382556", "REACTOME:R-CEL-532668", "REACTOME:R-CEL-5358346", "REACTOME:R-CEL-5689877", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8876725", "REACTOME:R-CEL-8951664", "REACTOME:R-...

56

[ "1xwi", "2qp9", "2qpa", "2rko", "2zam", "2zan", "2zao", "3b9p", "3cf0", "3d8b", "3eie", "3eih", "3mhv", "3vfd", "4l15", "4l16", "5c19", "5c1a", "5uie", "5xmi", "5xmk", "5z6q", "5z6r", "5zql", "5zqm", "6ap1", "6b5c", "6bmf", "6chs", "6g2v", "6g2w", "6g2x"...

51

[ "PUB00035481", "PUB00063869", "PUB00103859", "PUB00103860" ]

[ "16704411", "11809724", "11329380", "22637577" ]

[ "The beta domain is required for Vps4p oligomerization into a functionally active ATPase.", "Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics.", "End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces ce...

[ 2006, 2002, 2001, 2012 ]

4

[]

0

null

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

[ 276, 4, 21045, 14 ]

4

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

[ 7, 6, 30, 20, 33, 16, 2, 16, 29, 3, 4, 30 ]

12

true

Domain

Spastin/Vps4, C-terminal

Spast_Vps4_C

5

IPR015416

15,416

Zinc finger, H2C2-type, histone UAS binding

Znf_H2C2_histone_UAS-bd

Domain

1,573

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...

[]

0

[ "PFAM" ]

[ "PF09337" ]

[ "zf-H2C2" ]

[ 1573 ]

1

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

[ "2.7.7.-", "2.7.7.49", "2.7.7.7", "3.1.26.4", "3.4.23.-", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179" ]

[ "EC:2.7.7.-", "EC:2.7.7.49", "EC:2.7.7.7", "EC:3.1.26.4", "EC:3.4.23.-", "METACYC:PWY-6322", "METACYC:PWY-6626", "METACYC:PWY-6749", "METACYC:PWY-6955", "METACYC:PWY-6998", "METACYC:PWY-7127", "METACYC:PWY-7419", "METACYC:PWY-7529", "METACYC:PWY-7706", "METACYC:PWY-7719", "METACYC:PWY-...

22

[]

0

[ "PUB00014077", "PUB00035495", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]

[ "12665246", "16415340", "17210253", "15963892", "15718139", "10529348", "11179890" ]

[ "Zinc fingers--folds for many occasions.", "The DNA-binding domain of the yeast Spt10p activator includes a zinc finger that is homologous to foamy virus integrase.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger pro...

[ 2002, 2006, 2007, 2005, 2005, 1999, 2001 ]

7

[]

0

null

[ "Eukaryota", "Viruses" ]

[ 1475, 98 ]

2

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

[ 1, 1 ]

2

true

Domain

Zinc finger, H2C2-type, histone UAS binding

Znf_H2C2_histone_UAS-bd

9

IPR015417

15,417

Glycine/sarcosine/betaine reductase complex, protein B, subunit alpha/ beta

Gly_reductase_pB_sua/b

Family

1,980

false

This is a family of glycine reductase, sarcosine reductase and betaine reductases. These enzymes catalyse the following reactions: sarcosine reductase: Acetyl phosphate + methylamine + thioredoxin disulphide = N-methylglycine + phosphate + thioredoxin. glycine reductase: Acetyl phosphate + NH3 + thioredoxin disulphide ...

[ "GO:0050485" ]

[ "oxidoreductase activity, acting on X-H and Y-H to form an X-Y bond, with a disulfide as acceptor" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF09338" ]

[ "Gly_reductase" ]

[ 1980 ]

1

[]

0

[]

0

[]

0

[]

[ "IPR016585", "IPR031000", "IPR031002" ]

0

3

0

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

[ 1934, 7, 39 ]

3

[]

0

true

Family

Glycine/sarcosine/betaine reductase complex, protein B, subunit alpha/ beta

Gly_reductase_pB_sua/b

7

IPR015418

15,418

Chromatin modification-related protein Eaf6

Eaf6

Family

5,149

false

Eaf6 is a component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 histone acetyltransferase complex is conserved from yeast to humans [ ]. Budding yeast Eaf6 is also a component of th...

[ "GO:0000123" ]

[ "histone acetyltransferase complex" ]

[ "cellular_component" ]

1

[ "PFAM", "PANTHER" ]

[ "PF09340", "PTHR13476" ]

[ "NuA4", "" ]

[ 4882, 4889 ]

2

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

[ "R-DME-6804758", "R-DRE-6804758", "R-GGA-6804758", "R-HSA-3214847", "R-HSA-6804758", "R-MMU-3214847", "R-MMU-6804758", "R-SPO-3214847", "R-SPO-6804758", "R-XTR-6804758" ]

[ "REACTOME:R-DME-6804758", "REACTOME:R-DRE-6804758", "REACTOME:R-GGA-6804758", "REACTOME:R-HSA-3214847", "REACTOME:R-HSA-6804758", "REACTOME:R-MMU-3214847", "REACTOME:R-MMU-6804758", "REACTOME:R-SPO-3214847", "REACTOME:R-SPO-6804758", "REACTOME:R-XTR-6804758" ]

10

[ "5j9q", "5j9t", "5j9u", "5j9w", "7vvu", "7vvz", "8x2x", "8x2y", "8x2z", "8x30", "8x31", "8x32" ]

12

[ "PUB00035439", "PUB00041945", "PUB00075219" ]

[ "14966270", "17157260", "18794358" ]

[ "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans.", "Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs.", "Molecular architecture of quartet MOZ/MORF histone acetyltra...

[ 2004, 2006, 2008 ]

3

[]

0

null

[ "Eukaryota" ]

[ 5149 ]

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...

[ 7, 1, 2, 1, 2, 4, 1, 4, 11, 1, 1, 4 ]

12

true

Family

Chromatin modification-related protein Eaf6

Eaf6

1

IPR015419

15,419

CTAG/Pcc1 family

CTAG/Pcc1

Family

4,836

false

This entry represents the CTAG/Pcc1 family. Its members include yeast EKC/KEOPS complex subunit Pcc1, mammalian EKC/KEOPS complex subunit Lage3 and human cancer/testis antigen (CTAG) 1/2. In Saccharomyces cerevisiae, Pcc1 is a component of the EKC/KEOPS protein complex that is required for the formation of a threonylca...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09341", "PTHR31283" ]

[ "Pcc1", "" ]

[ 4834, 3244 ]

2

[ "REACTOME" ]

[ "R-HSA-6782315" ]

[ "REACTOME:R-HSA-6782315" ]

1

[ "3enc", "3eno", "4wx8", "4wxa", "5jmv", "6gwj", "7a66", "7a67", "8k20", "8unk", "8up5", "9d85" ]

12

[ "PUB00035445", "PUB00072933", "PUB00072934", "PUB00084171" ]

[ "16874308", "22912744", "24970819", "27903914" ]

[ "Yeast homolog of a cancer-testis antigen defines a new transcription complex.", "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by the human tumour antigen PRAME.", "NY-ESO-1 as a potential immunotherapeutic target in renal cell carcinoma.", "Proteomic analysis of the human KEOPS compl...

[ 2006, 2012, 2014, 2017 ]

4

[]

0

null

[ "Archaea", "Eukaryota", "Nitrosococcus oceani C-27", "ecological metagenomes" ]

[ 1044, 3760, 1, 31 ]

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...

[ 3, 1, 1, 1, 5, 8, 1, 6, 7, 1, 1, 6 ]

12

true

Family

CTAG/Pcc1 family

CTAG/Pcc1

7

IPR015420

15,420

Peptidase S1A, nudel

Peptidase_S1A_nudel

Domain

399

false

This domain is found in serine endopeptidases belonging to MEROPS peptidase family S1A (clan PA). It is found in unusual mosaic proteins, which are encoded by the Drosophila nudel gene (see ). Nudel is involved in defining embryonic dorsoventral polarity. Three proteases; ndl, gd and snk process easter to create active...

[]

0

[ "PFAM" ]

[ "PF09342" ]

[ "DUF1986" ]

[ 399 ]

1

[]

0

[]

0

[ "PUB00000522", "PUB00003576", "PUB00054161" ]

[ "8439290", "7845208", "7671306" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "An unusual mosaic protein with a protease domain, encoded by the nudel gene, is involved in defining embryonic dorsoventral polarity in Drosophila." ]

[ 1993, 1994, 1995 ]

3

[ "IPR001254" ]

[]

1

0

1

[ "Bilateria" ]

[ 399 ]

1

[ "Drosophila melanogaster", "Rattus norvegicus" ]

[ 1, 1 ]

2

true

Domain

Peptidase S1A, nudel

Peptidase_S1A_nudel

3

IPR015421

15,421

Pyridoxal phosphate-dependent transferase, major domain

PyrdxlP-dep_Trfase_major

Homologous_superfamily

1,206,305

false

The monomer of PLP-dependent transferases consists of two domains, a large domain and a small domain. This entry represents the large domain, which has a 3-layer α/β/α sandwich topology [ ]. This domain can be found in the following PLP-dependent transferase families: Aspartate aminotransferase (AAT)-like enzymes, such...

[]

0

[ "CATHGENE3D" ]

[ "G3DSA:3.40.640.10" ]

[ "" ]

[ 1206305 ]

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-1483213", "R-BTA-1614558", "R-BTA-1660661", "R-BTA-189451", "R-BTA-196757", "R-BTA-2408508", "R-BTA-389661", "R-BTA-70921", "R-BTA-888568", "R-BTA-888590", "R-BTA-8963684", "R-BTA-8963693", "R-BTA-8964539", "R-BTA-9013408", "R-BTA-947581", "R-BTA-9837999", "R-BTA-9856872", "...

[ "REACTOME:R-BTA-1483213", "REACTOME:R-BTA-1614558", "REACTOME:R-BTA-1660661", "REACTOME:R-BTA-189451", "REACTOME:R-BTA-196757", "REACTOME:R-BTA-2408508", "REACTOME:R-BTA-389661", "REACTOME:R-BTA-70921", "REACTOME:R-BTA-888568", "REACTOME:R-BTA-888590", "REACTOME:R-BTA-8963684", "REACTOME:R-BTA...

240

[ "1aam", "1aat", "1aaw", "1ahe", "1ahf", "1ahg", "1ahx", "1ahy", "1aia", "1aib", "1aic", "1ajr", "1ajs", "1aka", "1akb", "1akc", "1ama", "1amq", "1amr", "1ams", "1arg", "1arh", "1ari", "1ars", "1art", "1asa", "1asb", "1asc", "1asd", "1ase", "1asf", "1asg"...

1,791

[ "PUB00006322", "PUB00014087", "PUB00035504", "PUB00035505", "PUB00035506", "PUB00035507", "PUB00035508", "PUB00035511", "PUB00035512", "PUB00035513", "PUB00035514", "PUB00035515", "PUB00043268", "PUB00153780", "PUB00153781" ]

[ "7748903", "10666573", "15581583", "8690703", "15189147", "17109392", "16763894", "17300176", "16790938", "15690345", "17014820", "15848278", "17583737", "20142041", "36320885" ]

[ "Pyridoxal phosphate-dependent enzymes.", "Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.", "Reaction specificity in pyridoxal phosphate enzymes.", "Pyridoxal enzymes: mechanistic diversity and uniformity.", "Pyridoxal phosphate enzymes: mechanis...

[ 1995, 1999, 2005, 1995, 2004, 2006, 2006, 2007, 2006, 2005, 2006, 2005, 2007, 2010, 2022 ]

15

[]

0

null

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

[ 20097, 900269, 266905, 289, 18745 ]

5

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

[ 412, 59, 130, 78, 41, 268, 147, 47, 318, 215, 34, 31, 711 ]

13

true

Homologous_superfamily

Pyridoxal phosphate-dependent transferase, major domain

PyrdxlP-dep_Trfase_major

4