LiteFold/InterPro · Datasets at Hugging Face

IPR018938

18,938

Glycophorin, conserved site

Glycophorin_CS

Conserved_site

161

false

Proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins [Reid M.E., Lomas-Francis C. The Blood Group Antigen FactsBook Academic...

[ "GO:0016020" ]

[ "membrane" ]

[ "cellular_component" ]

1

[ "PROSITE" ]

[ "PS00312" ]

[ "GLYCOPHORIN_A" ]

[ 161 ]

1

[ "REACTOME" ]

[ "R-HSA-202733" ]

[ "REACTOME:R-HSA-202733" ]

1

[ "1afo", "2kpe", "2kpf", "2xq2", "7uz3", "7v07", "7v0k", "7v19", "8crq", "8crr", "8crt", "8cs9", "8csl", "8ct3", "8cte" ]

15

[ "PUB00000593" ]

[ "2605264" ]

[ "Amino acid sequence of monkey erythrocyte glycophorin MK. Its amino acid sequence has a striking homology with that of human glycophorin A." ]

[ 1989 ]

1

[]

0

null

[ "Bacteria", "Opisthokonta" ]

[ 6, 155 ]

2

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

[ 54, 4, 2 ]

3

true

Conserved_site

Glycophorin, conserved site

Glycophorin_CS

2

IPR018939

18,939

Autophagy-related protein 27

Autophagy-rel_prot_27

Family

3,569

false

Autophagy is a degradative transport pathway that delivers cytosolic proteins to the lysosome (vacuole) [ ] and is induced by starvation [ ]. Cytosolic proteins appear inside the vacuole enclosed in autophagic vesicles. Autophagy significantly differs from other transport pathways by using double membrane layered trans...

[]

0

[ "PFAM" ]

[ "PF09451" ]

[ "ATG27" ]

[ 3569 ]

1

[ "REACTOME" ]

[ "R-SCE-8856825" ]

[ "REACTOME:R-SCE-8856825" ]

1

[]

0

[ "PUB00043581", "PUB00043582", "PUB00043583", "PUB00043584", "PUB00044915" ]

[ "11058089", "9190802", "11675007", "18472412", "17297289" ]

[ "The breakdown of autophagic vesicles inside the vacuole depends on Aut4p.", "AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae.", "A genomic screen identifies AUT8 as a novel gene essential for autophagy in the yeast Saccharomyces cerevisiae.", "Toward unrave...

[ 2000, 1997, 2001, 2008, 2007 ]

5

[]

0

null

[ "Eukaryota", "Marseillevirus LCMAC103" ]

[ 3568, 1 ]

2

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

[ 9, 1, 2, 1, 4 ]

5

true

Family

Autophagy-related protein 27

Autophagy-rel_prot_27

4

IPR018940

18,940

Elongation factor 1 beta central acidic region, eukaryote

EF-1_beta_acid_region_euk

Domain

7,335

false

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept...

[]

0

[ "PFAM", "SMART" ]

[ "PF10587", "SM01182" ]

[ "EF-1_beta_acid", "EF-1_beta_acid" ]

[ 6924, 6766 ]

2

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

[ "R-BTA-156842", "R-DDI-156842", "R-DME-156842", "R-HSA-156842", "R-MMU-156842", "R-RNO-156842", "R-SCE-156842", "R-SPO-156842" ]

[ "REACTOME:R-BTA-156842", "REACTOME:R-DDI-156842", "REACTOME:R-DME-156842", "REACTOME:R-HSA-156842", "REACTOME:R-MMU-156842", "REACTOME:R-RNO-156842", "REACTOME:R-SCE-156842", "REACTOME:R-SPO-156842" ]

8

[ "2mvm", "2mvn", "2n51" ]

3

[ "PUB00033951", "PUB00033952", "PUB00033953" ]

[ "12932732", "15922593", "12762045" ]

[ "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors." ]

[ 2003, 2005, 2001 ]

3

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 15, 7320 ]

2

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

[ 2, 19, 3, 16, 12, 1, 17, 1, 1 ]

9

true

Domain

Elongation factor 1 beta central acidic region, eukaryote

EF-1_beta_acid_region_euk

8

IPR018941

18,941

Tyrosine-protein kinase, receptor Tie-2, Ig-like domain 1, N-terminal

Tyr_kin_Tie2_Ig-like_dom-1_N

Domain

960

false

This entry represents the N-terminal domain of human Angiopoietin-1 receptor, also known as Tyrosine-protein kinase receptor TIE-2, and similar sequences from vertebrates. Angiogenesis is a physiological process whereby new blood vessels are formed from existing ones. It is essential for tissue repair and regeneration ...

[ "GO:0004714", "GO:0005524", "GO:0006468", "GO:0007169", "GO:0005886" ]

[ "transmembrane receptor protein tyrosine kinase activity", "ATP binding", "protein phosphorylation", "cell surface receptor protein tyrosine kinase signaling pathway", "plasma membrane" ]

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

5

[ "PFAM" ]

[ "PF10430" ]

[ "Ig_Tie2_1" ]

[ 960 ]

1

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

[ "2.7.10.1", "R-BTA-210993", "R-BTA-5673001", "R-DRE-210993", "R-DRE-5673001", "R-HSA-210993", "R-HSA-5673001", "R-MMU-210993", "R-MMU-5673001" ]

[ "EC:2.7.10.1", "REACTOME:R-BTA-210993", "REACTOME:R-BTA-5673001", "REACTOME:R-DRE-210993", "REACTOME:R-DRE-5673001", "REACTOME:R-HSA-210993", "REACTOME:R-HSA-5673001", "REACTOME:R-MMU-210993", "REACTOME:R-MMU-5673001" ]

9

[ "2gy5", "2gy7", "4k0v" ]

3

[ "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00041214", "PUB00045000", "PUB00052410", "PUB00052411", "PUB00052412" ]

[ "3291115", "12368087", "12471243", "15078142", "15320712", "16732286", "16849318", "19275641", "16700535", "15845350" ]

[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "High-throughput structural biology in drug discovery: protein kinases.", "Creating chemical dive...

[ 1988, 2002, 2002, 2004, 2004, 2006, 2006, 2009, 2006, 2005 ]

10

[]

0

null

[ "Deuterostomia" ]

[ 960 ]

1

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

[ 4, 5, 3, 6 ]

4

true

Domain

Tyrosine-protein kinase, receptor Tie-2, Ig-like domain 1, N-terminal

Tyr_kin_Tie2_Ig-like_dom-1_N

2

IPR018942

18,942

Seminal vesicle protein repeat

Seminal_vesicle_protein_repeat

Repeat

25

false

The rat seminal vesicle contains six major androgen-dependent secretory proteins referred to as SVS I-VI. The SVS I-III proteins appear to be components of the rat copulatory plug, with the SVS II protein being the major component [ ]. This entry represents a repeat that is found in seminal vesical proteins.

[]

0

[ "PFAM" ]

[ "PF10578" ]

[ "SVS_QK" ]

[ 25 ]

1

[]

0

[]

0

[ "PUB00002629" ]

[ "2351680" ]

[ "Structural characterization of the rat seminal vesicle secretion II protein and gene." ]

[ 1990 ]

1

[]

0

null

[ "Corallincola spongiicola", "Eumetazoa" ]

[ 1, 24 ]

2

[ "Mus musculus", "Rattus norvegicus" ]

[ 6, 4 ]

2

true

Repeat

Seminal vesicle protein repeat

Seminal_vesicle_protein_repeat

3

IPR018943

18,943

Oligosaccaryltransferase

Family

1,885

false

Ost4 is a very short, approximately 30 residues, enzyme found from fungi to vertebrates. It is a member of the ER oligosaccaryltansferase complex, , that catalyses the asparagine-linked glycosylation of proteins. It appears to be an integral membrane protein that mediates the en bloc transfer of a pre-assembled high-ma...

[]

0

[ "PFAM" ]

[ "PF10215" ]

[ "Ost4" ]

[ 1885 ]

1

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

[ "R-HSA-446203", "R-HSA-9694548", "R-HSA-9768727", "R-MMU-9768727", "R-RNO-9768727" ]

[ "REACTOME:R-HSA-446203", "REACTOME:R-HSA-9694548", "REACTOME:R-HSA-9768727", "REACTOME:R-MMU-9768727", "REACTOME:R-RNO-9768727" ]

5

[ "1rkl", "2lat", "6c26", "6ezn", "6ftg", "6fti", "6ftj", "6s7o", "6s7t", "6xcr", "6xcu", "7oci", "8agb", "8agc", "8age", "8b6l", "8pn9" ]

17

[]

0

[]

[ "IPR044165" ]

0

1

0

[ "Eukaryota" ]

[ 1885 ]

1

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

[ 8, 1, 1, 2, 1, 1, 1, 4, 1, 1, 1, 2 ]

12

true

Family

Oligosaccaryltransferase

7

IPR018944

18,944

DNA polymerase lambda, fingers domain

DNA_pol_lambd_fingers_domain

Domain

8,448

false

DNA polymerases catalyse the addition of dNMPs onto the 3-prime ends of DNA chains. There is a general polymerase fold consisting of three subdomains that have been likened to the fingers, palm, and thumb of a right hand. This entry represents the central three-helical region of DNA polymerase lambda referred to as the...

[ "GO:0003677", "GO:0034061" ]

[ "DNA binding", "DNA polymerase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF10391" ]

[ "DNA_pol_lambd_f" ]

[ 8448 ]

1

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

[ "2.7.7.7", "R-BTA-110362", "R-BTA-110373", "R-BTA-110381", "R-BTA-5649702", "R-BTA-5651801", "R-BTA-5689880", "R-BTA-73930", "R-DRE-110362", "R-DRE-110373", "R-DRE-5649702", "R-DRE-73930", "R-HSA-110362", "R-HSA-110373", "R-HSA-110381", "R-HSA-5649702", "R-HSA-5651801", "R-HSA-5689...

[ "EC:2.7.7.7", "REACTOME:R-BTA-110362", "REACTOME:R-BTA-110373", "REACTOME:R-BTA-110381", "REACTOME:R-BTA-5649702", "REACTOME:R-BTA-5651801", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-73930", "REACTOME:R-DRE-110362", "REACTOME:R-DRE-110373", "REACTOME:R-DRE-5649702", "REACTOME:R-DRE-73930", "...

36

[ "1bpb", "1bpd", "1bpe", "1bpx", "1bpy", "1bpz", "1huo", "1huz", "1jms", "1jn3", "1kdh", "1kej", "1mq2", "1mq3", "1nom", "1rpl", "1rzt", "1tv9", "1tva", "1xsl", "1xsn", "1xsp", "1zjm", "1zjn", "1zqa", "1zqb", "1zqc", "1zqd", "1zqe", "1zqf", "1zqg", "1zqh"...

706

[ "PUB00030862" ]

[ "14992725" ]

[ "A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology." ]

[ 2004 ]

1

[]

0

null

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

[ 6, 8263, 45, 134 ]

4

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

[ 5, 12, 22, 8, 2, 2, 14, 1, 8 ]

9

true

Domain

DNA polymerase lambda, fingers domain

DNA_pol_lambd_fingers_domain

9

IPR018946

18,946

PhoD-like phosphatase, metallophosphatase domain

PhoD-like_MPP

Domain

27,834

false

Alkaline phosphatase D (PhoD) [ ] catalyses the reaction: phosphate monoester + H(2)O = an alcohol + phosphate. PhoD is similar to Ca(2+)-dependent phospholipase D [ ], which catalyses the hydrolysis of the ester bond between the phosphatidic acid and alcohol moieties of phospholipids [ , ]. PhoD (also known as alkalin...

[]

0

[ "PFAM", "CDD" ]

[ "PF09423", "cd07389" ]

[ "PhoD", "MPP_PhoD" ]

[ 22602, 24839 ]

2

[]

0

[ "2yeq" ]

1

[ "PUB00071261", "PUB00071262", "PUB00071264", "PUB00071265", "PUB00088140", "PUB00094642", "PUB00094643", "PUB00094644", "PUB00094645" ]

[ "8760916", "15588701", "12519726", "17906150", "25217636", "19180538", "16517638", "11719524", "18039941" ]

[ "A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD.", "Expression and characterization of a heterodimer of Streptomyces chromofuscus phospholipase D.", "An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases.", "Phosphat...

[ 1996, 2004, 2003, 2007, 2014, 2009, 2006, 2002, 2008 ]

9

[]

[ "IPR043904" ]

0

1

0

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

[ 19109, 8407, 138, 19, 161 ]

5

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

[ 7, 9, 3, 1, 11 ]

5

true

Domain

PhoD-like phosphatase, metallophosphatase domain

PhoD-like_MPP

6

IPR018947

18,947

Neuromodulin, N-terminal

Neuromodulin_N

Domain

975

false

This entry represents the neuromodulin N-terminal domain. Neuromodulin (also known as growth-associated protein 43 or GAP-43) is a component of the motile growth cones. It is membrane protein whose expression is widely correlated with successful axon elongation [ ]. It is a crucial component of an effective regeneratio...

[]

0

[ "PFAM" ]

[ "PF10580" ]

[ "Neuromodulin_N" ]

[ 975 ]

1

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

[ "R-BTA-373760", "R-HSA-373760", "R-MMU-373760", "R-RNO-373760" ]

[ "REACTOME:R-BTA-373760", "REACTOME:R-HSA-373760", "REACTOME:R-MMU-373760", "REACTOME:R-RNO-373760" ]

4

[]

0

[ "PUB00004299", "PUB00004303" ]

[ "3272162", "2641999" ]

[ "Human GAP-43: its deduced amino acid sequence and chromosomal localization in mouse and human.", "Selective conservation of GAP-43 structure in vertebrate evolution." ]

[ 1988, 1989 ]

2

[]

0

null

[ "Gnathostomata" ]

[ 975 ]

1

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

[ 2, 2, 1, 2 ]

4

true

Domain

Neuromodulin, N-terminal

Neuromodulin_N

4

IPR018951

18,951

Fumarase C, C-terminal

Fumarase_C_C

Domain

37,332

false

Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Krebs cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 α-helices from the fiv...

[ "GO:0016829", "GO:0006099" ]

[ "lyase activity", "tricarboxylic acid cycle" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF10415" ]

[ "FumaraseC_C" ]

[ 37332 ]

1

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

[ "4.2.1.2", "PWY-5392", "PWY-561", "PWY-5690", "PWY-5913", "PWY-6728", "PWY-6969", "PWY-7254", "PWY-7384", "PWY-8086", "R-CEL-71403", "R-CEL-9837999", "R-DDI-71403", "R-DDI-9837999", "R-DRE-71403", "R-HSA-71403", "R-HSA-9837999", "R-MMU-71403", "R-MMU-9837999", "R-RNO-71403", ...

[ "EC:4.2.1.2", "METACYC:PWY-5392", "METACYC:PWY-561", "METACYC:PWY-5690", "METACYC:PWY-5913", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7254", "METACYC:PWY-7384", "METACYC:PWY-8086", "REACTOME:R-CEL-71403", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-71403", "REACTOME:R-DDI-9837999...

27

[ "1fuo", "1fup", "1fuq", "1fur", "1j3u", "1jsw", "1kq7", "1vdk", "1yfe", "1yfm", "2fus", "3e04", "3gtd", "3no9", "3oce", "3ocf", "3qbp", "3r6q", "3r6v", "3rd8", "3rrp", "3tv2", "4adl", "4adm", "4apa", "4apb", "4hgv", "5d6b", "5f91", "5f92", "5upp", "6ebt"...

60

[ "PUB00025036" ]

[ "8909293" ]

[ "Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli." ]

[ 1996 ]

1

[]

0

null

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

[ 548, 31426, 5042, 316 ]

4

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

[ 10, 1, 1, 6, 2, 5, 2, 1, 2, 1, 1, 1, 7 ]

13

true

Domain

Fumarase C, C-terminal

Fumarase_C_C

5

IPR018952

18,952

2'-5'-oligoadenylate synthetase 1, domain 2/C-terminal

2-5-oligoAdlate_synth_1_dom2/C

Domain

2,681

false

This is the largely α-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between residues 320 and 344 at the extreme C-terminal end [ ]. Oligoadenylate synthetases are antiviral e...

[]

0

[ "PFAM" ]

[ "PF10421" ]

[ "OAS1_C" ]

[ 2681 ]

1

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

[ "2.7.7.84", "R-HSA-877300", "R-HSA-8983711", "R-HSA-909733", "R-HSA-9833110", "R-MMU-8983711", "R-RNO-8983711" ]

[ "EC:2.7.7.84", "REACTOME:R-HSA-877300", "REACTOME:R-HSA-8983711", "REACTOME:R-HSA-909733", "REACTOME:R-HSA-9833110", "REACTOME:R-MMU-8983711", "REACTOME:R-RNO-8983711" ]

7

[ "1px5", "4ig8", "4rwn", "4rwo", "4rwp", "4rwq", "4s3n", "4xq7", "9h1z" ]

9

[ "PUB00030016", "PUB00044412" ]

[ "14636576", "1651324" ]

[ "Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase.", "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships." ]

[ 2003, 1991 ]

2

[]

0

null

[ "Actinomycetes", "Eukaryota", "Squirrelpox virus" ]

[ 19, 2661, 1 ]

3

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

[ 49, 37, 34 ]

3

true

Domain

2'-5'-oligoadenylate synthetase 1, domain 2/C-terminal

2-5-oligoAdlate_synth_1_dom2/C

8

IPR018953

18,953

AMP nucleoside phosphorylase, N-terminal

AMP_nucleoside_Pase_N

Domain

5,665

false

This is the N-terminal domain of bacterial AMP nucleoside phosphorylase (AMNp). The N- and C-termini form distinct domains which intertwine with each other to form a stable monomer which associates with five other monomers to yield the active hexamer. The N terminus consists of a long helix and a four-stranded sheet wi...

[]

0

[ "PFAM" ]

[ "PF10423" ]

[ "AMNp_N" ]

[ 5665 ]

1

[]

0

[ "1t8r", "1t8s", "1t8w", "1t8y", "2guw", "7uwq" ]

6

[ "PUB00031378" ]

[ "15296732" ]

[ "Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases." ]

[ 2004 ]

1

[]

0

null

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

[ 5632, 8, 25 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

AMP nucleoside phosphorylase, N-terminal

AMP_nucleoside_Pase_N

1

IPR018954

18,954

Beta-galactosidase, domain 2

Betagal_dom2

Domain

4,492

false

This entry represents the second domain of the five-domain beta-galactosidase enzyme that altogether catalyses the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel β-str...

[]

0

[ "PFAM", "SMART" ]

[ "PF10435", "SM01029" ]

[ "BetaGal_dom2", "BetaGal_dom2" ]

[ 4375, 4355 ]

2

[ "EC", "METACYC" ]

[ "3.2.1.23", "PWY-6807" ]

[ "EC:3.2.1.23", "METACYC:PWY-6807" ]

2

[ "1tg7", "1xc6", "3og2", "3ogr", "3ogs", "3ogv", "4iug", "5ifp", "5ift", "5ihr", "5juv", "5mgc", "5mgd", "8qqh", "8uid" ]

15

[]

0

[]

0

null

[ "Bacteria", "Desulfurococcaceae", "Eukaryota", "marine sediment metagenome" ]

[ 899, 13, 3579, 1 ]

4

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

[ 2 ]

1

true

Domain

Beta-galactosidase, domain 2

Betagal_dom2

7

IPR018955

18,955

Branched-chain alpha-ketoacid dehydrogenase kinase/Pyruvate dehydrogenase kinase, N-terminal

BCDHK/PDK_N

Domain

15,109

false

Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. Regulating the activity of the branched-chain alpha-ketoacid dehydrogenase (BCDH) complex is the primary ...

[]

0

[ "PFAM" ]

[ "PF10436" ]

[ "BCDHK_Adom3" ]

[ 15109 ]

1

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

[ "2.7.11", "2.7.11.2", "R-BTA-70895", "R-CEL-204174", "R-CEL-5362517", "R-CEL-9837999", "R-DME-204174", "R-DME-5362517", "R-DME-9837999", "R-HSA-204174", "R-HSA-5362517", "R-HSA-70895", "R-HSA-9837999", "R-HSA-9841922", "R-HSA-9912481", "R-MMU-204174", "R-MMU-5362517", "R-MMU-70895"...

[ "EC:2.7.11", "EC:2.7.11.2", "REACTOME:R-BTA-70895", "REACTOME:R-CEL-204174", "REACTOME:R-CEL-5362517", "REACTOME:R-CEL-9837999", "REACTOME:R-DME-204174", "REACTOME:R-DME-5362517", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-204174", "REACTOME:R-HSA-5362517", "REACTOME:R-HSA-70895", "REACTOME:R...

26

[ "1gjv", "1gkx", "1gkz", "1jm6", "1y8n", "1y8o", "1y8p", "2btz", "2bu2", "2bu5", "2bu6", "2bu7", "2bu8", "2e0a", "2pnr", "2q8f", "2q8g", "2q8h", "2q8i", "2zdx", "2zdy", "2zkj", "3crk", "3crl", "3d2r", "3tz0", "3tz2", "3tz4", "3tz5", "3vad", "4dzy", "4e00"...

84

[]

0

[]

0

null

[ "Eukaryota", "metagenomes" ]

[ 15102, 7 ]

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...

[ 3, 1, 9, 4, 25, 18, 3, 7, 27, 2, 1, 36 ]

12

true

Domain

Branched-chain alpha-ketoacid dehydrogenase kinase/Pyruvate dehydrogenase kinase, N-terminal

BCDHK/PDK_N

7

IPR018959

18,959

Domain of unknown function DUF1989

DUF1989

Domain

12,963

false

This domain can be found in TMAO demethylase (Tdm) from M. silvestris and R. pomeroyi. Tdm catalyzes the first step in TMAO degradation [ ]. Proteins containing this domain are mostly uncharacterised.

[]

0

[ "PFAM" ]

[ "PF09347" ]

[ "DUF1989" ]

[ 12963 ]

1

[]

0

[ "3di4", "3oru", "3siy" ]

3

[ "PUB00093079" ]

[ "24550299" ]

[ "Trimethylamine N-oxide metabolism by abundant marine heterotrophic bacteria." ]

[ 2014 ]

1

[]

0

null

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

[ 26, 10685, 2107, 145 ]

4

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

[ 1, 1, 1, 1 ]

4

true

Domain

Domain of unknown function DUF1989

DUF1989

7

IPR018961

18,961

DnaJ homologue, subfamily C, member 28, conserved domain

DnaJ_homolog_subfam-C_membr-28

Domain

9,487

false

This entry represents a domain found in a group of sequences that may have a role in protein folding or as a chaperone. DnaJ is a member of the J-protein family, which are defined by the presence of a J domain that can regulate the activity of 70kDa heat-shock proteins [ ]. Some of the proteins in this entry contain a ...

[]

0

[ "PFAM" ]

[ "PF09350" ]

[ "DJC28_CD" ]

[ 9487 ]

1

[]

0

[]

0

[ "PUB00020790" ]

[ "15170475" ]

[ "The J-protein family: modulating protein assembly, disassembly and translocation." ]

[ 2004 ]

1

[]

0

null

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

[ 6109, 3353, 25 ]

3

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

[ 7, 1, 3, 1, 1, 3, 1, 3, 2, 2 ]

10

true

Domain

DnaJ homologue, subfamily C, member 28, conserved domain

DnaJ_homolog_subfam-C_membr-28

1

IPR018962

18,962

Domain of unknown function DUF1995

DUF1995

Domain

4,514

false

This entry includes proteins from bacteria and plants. This domain can be found in a chloroplastic protein, LOW PSII ACCUMULATION 3 (LPA3, At1g73060), from Arabidopsis. LPA3 is involved in assisting chlorophyll a binding protein psbC assembly within photosystem II (PSII) [ ]. This domain can also be found in some putat...

[]

0

[ "PFAM" ]

[ "PF09353" ]

[ "DUF1995" ]

[ 4514 ]

1

[]

0

[]

0

[ "PUB00071572", "PUB00096841" ]

[ "18162585", "26909098" ]

[ "Functions of chloroplastic adenylate kinases in Arabidopsis.", "Identification and Roles of Photosystem II Assembly, Stability, and Repair Factors in Arabidopsis." ]

[ 2008, 2016 ]

2

[]

0

null

[ "Cyanobacteriota", "Eukaryota" ]

[ 364, 4150 ]

2

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

[ 22, 12, 31 ]

3

true

Domain

Domain of unknown function DUF1995

DUF1995

5

IPR018963

18,963

Mycobacteriophage D29, Gp19

Mycophage_D29_Gp19

Family

842

false

This entry is represented by Mycobacteriophage D29, Gp19 [ ]. The characteristics of the protein distribution suggest prophage matches in addition to the phage matches.

[]

0

[ "PFAM" ]

[ "PF09355" ]

[ "Phage_Gp19" ]

[ 842 ]

1

[]

0

[ "9d94" ]

1

[ "PUB00045072" ]

[ "9636706" ]

[ "Genome structure of mycobacteriophage D29: implications for phage evolution." ]

[ 1998 ]

1

[]

0

null

[ "Bacteria", "Suillus", "Viruses", "bioreactor metagenome" ]

[ 469, 2, 369, 2 ]

4

[]

0

true

Family

Mycobacteriophage D29, Gp19

Mycophage_D29_Gp19

5

IPR018964

18,964

Bacteriophage phiJL001, Gp84, C-terminal

Phage_phiJL001_Gp84_C

Domain

3,012

false

This entry describes the C-terminal region of a family of proteins found almost exclusively in phage or in prophage regions of bacterial genomes, including the phage-like Rhodobacter capsulatus (Rhodopseudomonas capsulata) gene transfer agent, which packages DNA. An apparent exception is Wolbachia pipientis wMel, a bac...

[]

0

[ "PFAM" ]

[ "PF09356" ]

[ "Phage_BR0599" ]

[ 3012 ]

1

[]

0

[ "6tba", "6teh", "8gtc", "8rk3", "8rk6", "8rk7", "8vjh" ]

7

[]

0

[]

0

null

[ "Bacteria", "Ecdysozoa", "Viruses", "metagenomes" ]

[ 2728, 5, 245, 34 ]

4

[]

0

true

Domain

Bacteriophage phiJL001, Gp84, C-terminal

Phage_phiJL001_Gp84_C

9

IPR018965

18,965

Ubiquitin-activating enzyme E1, C-terminal

Ub-activating_enz_E1_C

Domain

8,533

false

This domain is found at the C terminus of Ubiquitin-activating enzyme E1 proteins. It binds to E2 enzymes [ ].

[]

0

[ "PFAM", "SMART" ]

[ "PF09358", "SM00985" ]

[ "E1_UFD", "UBA_e1_C" ]

[ 8238, 8453 ]

2

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

[ "6.2.1.45", "PWY-7511", "R-BTA-8866652", "R-BTA-983168", "R-DDI-1169408", "R-DDI-8866652", "R-DDI-936440", "R-DDI-983168", "R-DDI-9909505", "R-HSA-1169408", "R-HSA-168928", "R-HSA-5656169", "R-HSA-8866652", "R-HSA-936440", "R-HSA-983168", "R-HSA-9909505", "R-MMU-1169408", "R-MMU-56...

[ "EC:6.2.1.45", "METACYC:PWY-7511", "REACTOME:R-BTA-8866652", "REACTOME:R-BTA-983168", "REACTOME:R-DDI-1169408", "REACTOME:R-DDI-8866652", "REACTOME:R-DDI-936440", "REACTOME:R-DDI-983168", "REACTOME:R-DDI-9909505", "REACTOME:R-HSA-1169408", "REACTOME:R-HSA-168928", "REACTOME:R-HSA-5656169", "...

27

[ "3cmm", "4ii2", "4ii3", "4nnj", "5knl", "5l6h", "5l6i", "5l6j", "5tr4", "5um6", "6dc6", "6nya", "6o82", "6o83", "6zhs", "6zht", "6zhu", "6zqh", "7k5j", "7pvn", "7pyv", "7sol", "7zh9", "8oif", "8se9", "8sea", "8seb", "8sv8", "8wwx", "9b5c", "9b5d", "9b5e"...

66

[ "PUB00075384" ]

[ "18662542" ]

[ "Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes." ]

[ 2008 ]

1

[]

0

null

[ "Eukaryota", "Mimiviridae", "metagenomes" ]

[ 8515, 10, 8 ]

3

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

[ 8, 3, 5, 3, 10, 10, 1, 14, 17, 1, 1, 36 ]

12

true

Domain

Ubiquitin-activating enzyme E1, C-terminal

Ub-activating_enz_E1_C

8

IPR018967

18,967

Iron-binding zinc finger, CDGSH type

FeS-contain_CDGSH-typ

Domain

12,941

false

This entry represents iron-sulphur domain containing proteins that have a CDGSH sequence motif (although the Ser residue can also be an Ala or Thr), and is found in proteins from a wide range of organisms with the exception of fungi. The CDGSH-type domain binds a redox-active pH-labile 2Fe-2S cluster. The conserved seq...

[ "GO:0051537", "GO:0043231" ]

[ "2 iron, 2 sulfur cluster binding", "intracellular membrane-bounded organelle" ]

[ "molecular_function", "cellular_component" ]

2

[ "PFAM", "SMART" ]

[ "PF09360", "SM00704" ]

[ "zf-CDGSH", "ZnF_CDGSH" ]

[ 12650, 12732 ]

2

[]

0

[ "2qd0", "2qh7", "2r13", "3ew0", "3fnv", "3lpq", "3ree", "3s2q", "3s2r", "3tbm", "3tbn", "3tbo", "4ezf", "4f1e", "4f28", "4f2c", "4oo7", "4ooa", "6avj", "6de9", "6z1p", "7p0o", "7p0p", "7w5z", "7yvz", "8b6h", "8bqs", "8gym", "8gzu" ]

29

[ "PUB00035840", "PUB00042908", "PUB00044559" ]

[ "17376863", "17766440", "17584744" ]

[ "MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity.", "MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone.", "The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster." ]

[ 2007, 2007, 2007 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "uncultured Caudovirales phage" ]

[ 445, 6882, 5339, 274, 1 ]

5

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

[ 2, 5, 4, 2, 4, 6, 2, 14, 2 ]

9

true

Domain

Iron-binding zinc finger, CDGSH type

FeS-contain_CDGSH-typ

5

IPR018968

18,968

Phasin

Domain

10,926

false

Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granul...

[]

0

[ "PFAM" ]

[ "PF09361" ]

[ "Phasin_2" ]

[ 10926 ]

1

[]

0

[ "5ip0" ]

1

[ "PUB00045301", "PUB00045302", "PUB00045303" ]

[ "17965215", "18223073", "15256572" ]

[ "Effects of granule-associated protein PhaP on glycerol-dependent growth and polymer production in poly(3-hydroxybutyrate)-producing Escherichia coli.", "Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules.", "The complex structure of polyhydroxybutyrate (PHB) gra...

[ 2007, 2008, 2004 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "Riboviria sp.", "unclassified sequences" ]

[ 10833, 22, 1, 70 ]

4

[]

0

true

Domain

Phasin

1

IPR018969

18,969

Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal

Xul5P/Fru6P_PKetolase_C

Domain

9,833

false

Phosphoketolases (PK) are key enzymes of the pentose phosphate pathway of heterofermentative and facultative homofermentative lactic acid bacteria and of the D-fructose 6-phosphate shunt of bifidobacteria. PK activity has been sporadically reported in other microorganisms including eukaryotic yeasts. Xylulose-5-phospha...

[ "GO:0016832", "GO:0005975" ]

[ "aldehyde-lyase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09363" ]

[ "XFP_C" ]

[ 9833 ]

1

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

[ "4.1.2.-", "PWY-7085", "PWY-7089" ]

[ "EC:4.1.2.-", "METACYC:PWY-7085", "METACYC:PWY-7089" ]

3

[ "3ahc", "3ahd", "3ahe", "3ahf", "3ahg", "3ahh", "3ahi", "3ahj", "3ai7", "6gua", "6lxv", "7c8h", "7c8i", "8io6", "8io7", "8io8", "8io9", "8ioa", "8ioe", "9cd3", "9cd4" ]

21

[ "PUB00008466", "PUB00045300" ]

[ "11292814", "15899413" ]

[ "Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis.", "The gene encoding xylulose-5-phosphate/fructose-6-phosphate phosphoketolase (xfp) is conserved among Bifidobacterium species within a more variable region of the genome and both are us...

[ 2001, 2005 ]

2

[]

0

null

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

[ 7837, 1937, 59 ]

3

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

[ 2, 1 ]

2

true

Domain

Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal

Xul5P/Fru6P_PKetolase_C

6

IPR018970

18,970

Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal

Xul5P/Fru6P_PKetolase_N

Domain

10,834

false

Phosphoketolases (PK) are key enzymes of the pentose phosphate pathway of heterofermentative and facultative homofermentative lactic acid bacteria and of the D-fructose 6-phosphate shunt of bifidobacteria. PK activity has been sporadically reported in other microorganisms including eukaryotic yeasts. Xylulose-5-phospha...

[]

0

[ "PFAM" ]

[ "PF09364" ]

[ "XFP_N" ]

[ 10834 ]

1

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

[ "4.1.2.-", "PWY-7085", "PWY-7089" ]

[ "EC:4.1.2.-", "METACYC:PWY-7085", "METACYC:PWY-7089" ]

3

[ "3ahc", "3ahd", "3ahe", "3ahf", "3ahg", "3ahh", "3ahi", "3ahj", "3ai7", "6gua", "6lxv", "7c8h", "7c8i", "8io6", "8io7", "8io8", "8io9", "8ioa", "8ioe", "9cd3", "9cd4" ]

21

[ "PUB00008466", "PUB00045300" ]

[ "11292814", "15899413" ]

[ "Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis.", "The gene encoding xylulose-5-phosphate/fructose-6-phosphate phosphoketolase (xfp) is conserved among Bifidobacterium species within a more variable region of the genome and both are us...

[ 2001, 2005 ]

2

[]

0

null

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

[ 8818, 1952, 64 ]

3

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

[ 2, 1 ]

2

true

Domain

Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal

Xul5P/Fru6P_PKetolase_N

2

IPR018971

18,971

Protein of unknown function DUF1997

DUF1997

Family

3,240

false

This family of proteins are functionally uncharacterised.

[]

0

[ "PFAM" ]

[ "PF09366" ]

[ "DUF1997" ]

[ 3240 ]

1

[]

0

[]

0

[]

0

[]

0

null

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

[ 745, 2494, 1 ]

3

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

[ 24, 14, 24 ]

3

true

Family

Protein of unknown function DUF1997

DUF1997

6

IPR018973

18,973

MrfA-like Zn-binding domain

MZB

Domain

14,217

false

This is the C-terminal MrfA (Mitomycin repair factor A, also known as YprA in Bacillus subtilis) Zn+2-binding domain (MZB, also referred to as DUF1998) which contains a conserved four-cysteine signature motif. These four Cys reside in a short coil between two α-helices and form a metal ion-binding site [ ]. This domain...

[]

0

[ "PFAM" ]

[ "PF09369" ]

[ "MZB" ]

[ 14217 ]

1

[]

0

[ "6znp", "6znq", "6zns", "7s9v", "7s9w" ]

5

[ "PUB00054163", "PUB00098193" ]

[ "18701350", "33300032" ]

[ "In silico analyses of a new group of fungal and plant RecQ4-homologous proteins.", "A skipping rope translocation mechanism in a widespread family of DNA repair helicases." ]

[ 2008, 2021 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Phage sp. ctrsQ3", "unclassified sequences" ]

[ 861, 10670, 2512, 1, 173 ]

5

[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 7, 1, 3, 1, 1, 9 ]

6

true

Domain

MrfA-like Zn-binding domain

MZB

8

IPR018974

18,974

Tex-like protein, N-terminal

Tex-like_N

Domain

21,571

false

This presumed domain is found at the N terminus of . This protein defines a novel family of prokaryotic transcriptional accessory factors [ ].

[]

0

[ "PFAM" ]

[ "PF09371" ]

[ "Tex_N" ]

[ 21571 ]

1

[]

0

[ "2oce", "3bzc", "3bzk" ]

3

[ "PUB00044514" ]

[ "8755871" ]

[ "A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins." ]

[ 1996 ]

1

[]

0

null

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

[ 65, 19444, 1940, 122 ]

4

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

[ 1, 8, 1, 1, 2, 2, 6 ]

7

true

Domain

Tex-like protein, N-terminal

Tex-like_N

6

IPR018975

18,975

Pseudomurein-binding repeat

Pseudomurein-binding_repeat

Repeat

381

false

Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum) is a methanogenic Gram-positive microorganism with a cell wall consisting of pseudomurein. This repeat specifically binds to pseudomurein. This repeat is found at the N-terminal of PeiW and PeiP which are pseudomurein binding phage proteins.

[]

0

[ "PFAM" ]

[ "PF09373" ]

[ "PMBR" ]

[ 381 ]

1

[]

0

[ "8z4f" ]

1

[]

0

[]

0

null

[ "Bacteria", "Methanobacteriales", "Methanobavirales", "ecological metagenomes" ]

[ 88, 280, 3, 10 ]

4

[]

0

true

Repeat

Pseudomurein-binding repeat

Pseudomurein-binding_repeat

4

IPR018976

18,976

Imelysin-like domain

Imelysin-like

Domain

14,728

false

EfeO is an essential component of the EfeUOB operon which is highly conserved in bacteria. However, its biochemical function is unknown. EfeO contains an N-terminal cupredoxin (CUP)-like domain and C-terminal imelysin-like domain that may bind iron [ ]. Algp7, a member of the EfeO family of proteins from Sphingomonas s...

[]

0

[ "PFAM" ]

[ "PF09375" ]

[ "Peptidase_M75" ]

[ 14728 ]

1

[ "REACTOME" ]

[ "R-HSA-9638482" ]

[ "REACTOME:R-HSA-9638482" ]

1

[ "3at7", "3n8u", "3oyv", "3pf0", "3wsc", "4ecg", "5y4c", "6jbo", "7q1g", "7wgu", "7xrx" ]

11

[ "PUB00065473", "PUB00084773", "PUB00084780", "PUB00084781" ]

[ "21799754", "21238429", "19701722", "18803672" ]

[ "Structural and sequence analysis of imelysin-like proteins implicated in bacterial iron uptake.", "Crystal structure of bacterial cell-surface alginate-binding protein with an M75 peptidase motif.", "EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport.", "...

[ 2011, 2011, 2010, 2008 ]

4

[]

[ "IPR034981", "IPR034982", "IPR034984" ]

0

3

0

[ "Bacteria", "Candidatus Nitrosopumilus sediminis", "Eukaryota", "metagenomes" ]

[ 14608, 1, 32, 87 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Imelysin-like domain

Imelysin-like

9

IPR018977

18,977

NurA domain

NurA_domain

Domain

2,462

false

This domain is found in several uncharacterised proteins and in NurA, a nuclease exhibiting both single-stranded endonuclease activity and 5'-3' exonuclease activity on single-stranded and double-stranded DNA from the hyperthermophilic archaeon Sulfolobus acidocaldarius [ ].

[]

0

[ "PFAM", "SMART" ]

[ "PF09376", "SM00933" ]

[ "NurA", "NurA" ]

[ 2407, 2117 ]

2

[]

0

[ "1zup", "2ygk", "3tai", "3tal", "3taz", "7f6d" ]

6

[ "PUB00044410" ]

[ "12052775" ]

[ "NurA, a novel 5'-3' nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea." ]

[ 2002 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Metazoa", "metagenomes" ]

[ 1356, 1043, 2, 61 ]

4

[]

0

true

Domain

NurA domain

NurA_domain

1

IPR018978

18,978

Ribosome maturation protein SDO1/SBDS, central domain

SDO1/SBDS_central

Domain

6,008

false

This entry represents the central domain of proteins that are highly conserved in species ranging from archaea to vertebrates and plants [ ]. This entry contains several Shwachman-Bodian-Diamond syndrome (SBDS) proteins from both mouse and humans. Shwachman-Diamond syndrome (OMIM 260400) is an autosomal recessive disor...

[ "GO:0042254" ]

[ "ribosome biogenesis" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF09377" ]

[ "SBDS_domain_II" ]

[ 6008 ]

1

[]

0

[ "1p9q", "1t95", "2kdo", "2l9n", "2wbm", "5an9", "5anb", "5anc", "6fsw", "6qkl", "6skg" ]

11

[ "PUB00020303", "PUB00020304", "PUB00020305", "PUB00045126", "PUB00076340" ]

[ "12496757", "15701634", "15701631", "17353896", "21536732" ]

[ "Mutations in SBDS are associated with Shwachman-Diamond syndrome.", "The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.", "Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome.", "The Shwachman-Bodian-D...

[ 2003, 2005, 2005, 2007, 2011 ]

5

[]

0

null

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

[ 906, 2, 5056, 44 ]

4

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

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

12

true

Domain

Ribosome maturation protein SDO1/SBDS, central domain

SDO1/SBDS_central

1

IPR018979

18,979

FERM, N-terminal

FERM_N

Domain

53,911

false

This domain is the N-terminal ubiquitin-like structural domain of the FERM domain. The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane [ ]. FERM domains are found in a number of cytoskeletal-associated pro...

[]

0

[ "PFAM" ]

[ "PF09379" ]

[ "FERM_N" ]

[ 53911 ]

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-373752", "R-BTA-6794361", "R-CEL-182971", "R-CEL-5675221", "R-DDI-114608", "R-DME-2029482", "R-DME-373752", "R-DME-5627123", "R-DME-6794361", "R-DRE-983168", "R-HSA-166016", "R-HSA-1660499", "R-HSA-182971", "R-HSA-2029482", "R-HSA-373752", "R-HSA-399719", "R-HSA-399955", "R-...

[ "REACTOME:R-BTA-373752", "REACTOME:R-BTA-6794361", "REACTOME:R-CEL-182971", "REACTOME:R-CEL-5675221", "REACTOME:R-DDI-114608", "REACTOME:R-DME-2029482", "REACTOME:R-DME-373752", "REACTOME:R-DME-5627123", "REACTOME:R-DME-6794361", "REACTOME:R-DRE-983168", "REACTOME:R-HSA-166016", "REACTOME:R-HS...

69

[ "1e5w", "1ef1", "1gc6", "1gc7", "1gg3", "1h4r", "1isn", "1j19", "1ni2", "1sgh", "2d10", "2d11", "2d2q", "2ems", "2emt", "2he7", "2i1j", "2i1k", "2kma", "2yvc", "2zpy", "3bin", "3ivf", "3qij", "3u8z", "3wa0", "3x23", "4p7i", "4rm8", "4rm9", "4rma", "4yl8"...

117

[ "PUB00005484", "PUB00013213", "PUB00017978" ]

[ "9757824", "10847681", "10970839" ]

[ "The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.", "Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.", "Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domai...

[ 1998, 2000, 2000 ]

3

[]

[ "IPR021187", "IPR030691", "IPR030696", "IPR030698" ]

0

4

0

[ "Eukaryota" ]

[ 53911 ]

1

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

[ 1, 30, 381, 32, 137, 134, 156 ]

7

true

Domain

FERM, N-terminal

FERM_N

8

IPR018980

18,980

FERM, C-terminal PH-like domain

FERM_PH-like_C

Domain

57,703

false

This entry represents the PH-like domain found at the C terminus of the FERM domain. The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane [ ]. FERM domains are found in a number of cytoskeletal-associated p...

[]

0

[ "PFAM", "SMART" ]

[ "PF09380", "SM01196" ]

[ "FERM_C", "FERM_C" ]

[ 57018, 56809 ]

2

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

[ "R-BTA-373752", "R-BTA-6794361", "R-CEL-182971", "R-CEL-5675221", "R-DME-2029482", "R-DME-373752", "R-DME-451806", "R-DME-5627123", "R-DME-6794361", "R-DRE-983168", "R-HSA-166016", "R-HSA-1660499", "R-HSA-182971", "R-HSA-2029482", "R-HSA-373752", "R-HSA-399719", "R-HSA-399955", "R-...

[ "REACTOME:R-BTA-373752", "REACTOME:R-BTA-6794361", "REACTOME:R-CEL-182971", "REACTOME:R-CEL-5675221", "REACTOME:R-DME-2029482", "REACTOME:R-DME-373752", "REACTOME:R-DME-451806", "REACTOME:R-DME-5627123", "REACTOME:R-DME-6794361", "REACTOME:R-DRE-983168", "REACTOME:R-HSA-166016", "REACTOME:R-HS...

69

[ "1e5w", "1ef1", "1gc6", "1gc7", "1gg3", "1h4r", "1isn", "1j19", "1ni2", "1sgh", "2d10", "2d11", "2d2q", "2ems", "2emt", "2he7", "2i1j", "2i1k", "2yvc", "2zpy", "3bin", "3qij", "3u8z", "3wa0", "3x23", "4p7i", "4rm8", "4rm9", "4rma", "4yl8", "4zri", "4zrj"...

107

[ "PUB00005484", "PUB00013213", "PUB00017978" ]

[ "9757824", "10847681", "10970839" ]

[ "The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.", "Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.", "Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domai...

[ 1998, 2000, 2000 ]

3

[]

[ "IPR041781", "IPR041782", "IPR041783", "IPR041785", "IPR041788", "IPR041789", "IPR041790" ]

0

7

0

[ "Eukaryota", "Tepidibacter hydrothermalis" ]

[ 57702, 1 ]

2

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

[ 1, 35, 401, 36, 143, 125, 156 ]

7

true

Domain

FERM, C-terminal PH-like domain

FERM_PH-like_C

9

IPR018981

18,981

Outer membrane porin G

Outer_membrane_porin_G

Family

419

false

Porins are channel proteins in the outer membrane of Gram-negative bacteria which mediate the uptake of molecules required for growth and survival. Escherichia coli OmpG forms a 14 stranded β-barrel and in contrast to most porins, appears to function as a monomer [ ]. The central pore of OmpG is wider than other E. col...

[]

0

[ "PFAM" ]

[ "PF09381" ]

[ "Porin_OmpG" ]

[ 419 ]

1

[]

0

[ "2f1c", "2iwv", "2iww", "2jqy", "2wvp", "2x9k", "4ctd", "5mwv", "6oqh", "7q5c" ]

10

[ "PUB00040490" ]

[ "16797588" ]

[ "Crystal structure of the monomeric porin OmpG." ]

[ 2006 ]

1

[]

0

null

[ "Bacteria" ]

[ 419 ]

1

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Outer membrane porin G

Outer_membrane_porin_G

5

IPR018982

18,982

RQC domain

RQC_domain

Domain

27,995

false

This entry represents the RQC domain, which is a DNA-binding domain found only in RecQ family enzymes [ ]. RecQ family helicases can unwind G4 DNA, and play important roles at G-rich domains of the genome, including the telomeres, rDNA, and immunoglobulin switch regions. This domain has a helix-turn-helix structure and...

[ "GO:0043138", "GO:0006260", "GO:0006281" ]

[ "3'-5' DNA helicase activity", "DNA replication", "DNA repair" ]

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

3

[ "PFAM", "SMART" ]

[ "PF09382", "SM00956" ]

[ "RQC", "RQC" ]

[ 27673, 27084 ]

2

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

[ "5.6.2.4", "R-CEL-5693607", "R-DME-3108214", "R-DME-5693607", "R-DME-6804756", "R-DME-69473", "R-HSA-174414", "R-HSA-174437", "R-HSA-3108214", "R-HSA-5685938", "R-HSA-5685942", "R-HSA-5693554", "R-HSA-5693568", "R-HSA-5693579", "R-HSA-5693607", "R-HSA-5693616", "R-HSA-6804756", "R-...

[ "EC:5.6.2.4", "REACTOME:R-CEL-5693607", "REACTOME:R-DME-3108214", "REACTOME:R-DME-5693607", "REACTOME:R-DME-6804756", "REACTOME:R-DME-69473", "REACTOME:R-HSA-174414", "REACTOME:R-HSA-174437", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-5685938", "REACTOME:R-HSA-5685942", "REACTOME:R-HSA-5693554"...

35

[ "1oyw", "1oyy", "2axl", "2mh9", "3aaf", "3we2", "3we3", "4cdg", "4cgz", "4o3m", "4q47", "4q48", "4tmu", "6crm", "6jtz", "6yhr" ]

16

[ "PUB00044472", "PUB00101132" ]

[ "16530788", "25901030" ]

[ "A conserved G4 DNA binding domain in RecQ family helicases.", "Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes." ]

[ 2006, 2015 ]

2

[]

0

null

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

[ 138, 20199, 7403, 42, 213 ]

5

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

[ 17, 2, 11, 1, 1, 9, 7, 1, 8, 8, 1, 1, 21 ]

13

true

Domain

RQC domain

RQC_domain

9

IPR018983

18,983

U3 small nucleolar RNA-associated protein 15, C-terminal

U3_snoRNA-assocProt_15_C

Domain

4,414

false

This entry represents the C-terminal domain of the U3 small nucleolar RNA-associated protein 15 (UTP15). This protein is involved in nucleolar processing of pre-18S ribosomal RNA, and is required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcrip...

[ "GO:0006364", "GO:0005730" ]

[ "rRNA processing", "nucleolus" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09384" ]

[ "UTP15_C" ]

[ 4414 ]

1

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

[ "R-BTA-6791226", "R-GGA-6791226", "R-HSA-6790901", "R-HSA-6791226", "R-MMU-6791226", "R-RNO-6791226", "R-SCE-6791226", "R-SPO-6791226" ]

[ "REACTOME:R-BTA-6791226", "REACTOME:R-GGA-6791226", "REACTOME:R-HSA-6790901", "REACTOME:R-HSA-6791226", "REACTOME:R-MMU-6791226", "REACTOME:R-RNO-6791226", "REACTOME:R-SCE-6791226", "REACTOME:R-SPO-6791226" ]

8

[ "5oql", "5wlc", "6ke6", "6l3q", "6lqp", "6lqq", "6lqr", "6lqs", "6lqt", "6lqu", "6lqv", "6nd4", "6rxt", "6rxu", "6rxv", "6rxx", "6rxy", "6rxz", "6zqa", "6zqb", "6zqc", "6zqd", "6zqe", "7ajt", "7aju", "7d4i", "7d5s", "7d63", "7mq8", "7mq9", "7mqa", "7suk"...

46

[ "PUB00008496", "PUB00035836", "PUB00035837" ]

[ "12068309", "15590835", "15489292" ]

[ "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis.", "The small-subunit processome is a ribosome assembly intermediate.", "RNA polymerase I transcription and pre-rRNA processing are linked by specific SSU processome components." ]

[ 2002, 2004, 2004 ]

3

[]

0

null

[ "Eukaryota" ]

[ 4414 ]

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, 1, 2, 2, 2, 1, 5, 5, 1, 1, 2 ]

12

true

Domain

U3 small nucleolar RNA-associated protein 15, C-terminal

U3_snoRNA-assocProt_15_C

6

IPR018984

18,984

Histidine kinase, N-terminal

Histidine_kinase_N

Domain

529

false

This domain is found at the N-terminal of sensor histidine kinase proteins.

[]

0

[ "PFAM" ]

[ "PF09385" ]

[ "HisK_N" ]

[ 529 ]

1

[]

0

[ "3pmc", "3pmd" ]

2

[]

0

[]

0

null

[ "Bacteria" ]

[ 529 ]

1

[]

0

true

Domain

Histidine kinase, N-terminal

Histidine_kinase_N

8

IPR018987

18,987

Protein of unknown function DUF1999

DUF1999

Family

119

false

This family contains a putative Fe-S binding reductase ( ) whose structure adopts an α and β fold.

[]

0

[ "PFAM" ]

[ "PF09390" ]

[ "DUF1999" ]

[ 119 ]

1

[]

0

[ "2d4o", "2d4p" ]

2

[]

0

[]

0

null

[ "Deinococci", "Methanomassiliicoccales" ]

[ 114, 5 ]

2

[]

0

true

Family

Protein of unknown function DUF1999

DUF1999

3

IPR018988

18,988

Protein of unknown function DUF2000

DUF2000

Family

4,111

false

This is a family of proteins of unknown function. The structure of one of the proteins in this family has been shown to adopt an α β fold.

[]

0

[ "PFAM" ]

[ "PF09391" ]

[ "DUF2000" ]

[ 4111 ]

1

[]

0

[ "2gax" ]

1

[]

0

[]

[ "IPR017021" ]

0

1

0

[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "unclassified sequences" ]

[ 4089, 1, 3, 18 ]

4

[]

0

true

Family

Protein of unknown function DUF2000

DUF2000

9

IPR018989

18,989

Phage tail tube protein

DUF2001

Family

1,497

false

This is a family of phage tail tube proteins including protein XkdM from phage-like element PBSX protein ( ) whose structure adopts a β barrel flanked with α helical regions [ ].

[]

0

[ "PFAM" ]

[ "PF09393" ]

[ "DUF2001" ]

[ 1497 ]

1

[]

0

[ "2guj", "5li2", "6gkx", "8v3t", "8v3w", "8v3x", "8v3z", "8v40", "9g8s", "9gb1", "9gb2", "9gb5", "9gb7" ]

13

[ "PUB00075454" ]

[ "23542344" ]

[ "A conserved spiral structure for highly diverged phage tail assembly chaperones." ]

[ 2013 ]

1

[]

0

null

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

[ 1369, 5, 2, 112, 9 ]

5

[]

0

true

Family

Phage tail tube protein

DUF2001

5

IPR018990

18,990

Proteinase inhibitor I42, chagasin

Prot_inh_I42_chagasin

Domain

3,102

false

Chagasin is a reversible inhibitor of papain-like cysteine proteases [ ]. Chagasin has a β-barrel structure, which is a unique variant of the immunoglobulin fold with homology to human CD8alpha [ , ].

[]

0

[ "PFAM" ]

[ "PF09394" ]

[ "Inhibitor_I42" ]

[ 3102 ]

1

[]

0

[ "2c34", "2cio", "2fo8", "2h7w", "2nnr", "2nqd", "2oul", "2wgn", "3cbj", "3cbk", "3e1z", "3m86", "3m88", "5swk", "6cjz" ]

15

[ "PUB00041307", "PUB00044196", "PUB00045297" ]

[ "17011790", "11719560", "17502099" ]

[ "Crystal structure of chagasin, the endogenous cysteine-protease inhibitor from Trypanosoma cruzi.", "Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi.", "The structure of chagasin in complex with a cysteine protease clarifies the bi...

[ 2007, 2001, 2007 ]

3

[]

0

null

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

[ 2519, 197, 315, 71 ]

4

[]

0

true

Domain

Proteinase inhibitor I42, chagasin

Prot_inh_I42_chagasin

9

IPR018992

18,992

Thrombin light chain

Thrombin_light_chain

Domain

1,176

false

Thrombin is a Na+-activated, allosteric serine protease that functions in blood homeostasis, inflammation and wound healing [ ]. Thrombin (or coagulation factor II) is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, and (in complex with thrombomodulin) p...

[ "GO:0004252", "GO:0006508", "GO:0007596", "GO:0005576" ]

[ "serine-type endopeptidase activity", "proteolysis", "blood coagulation", "extracellular region" ]

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

4

[ "PFAM" ]

[ "PF09396" ]

[ "Thrombin_light" ]

[ 1176 ]

1

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

[ "3.4.21.5", "R-HSA-140837", "R-HSA-140875", "R-HSA-159740", "R-HSA-159763", "R-HSA-159782", "R-HSA-202733", "R-HSA-375276", "R-HSA-381426", "R-HSA-416476", "R-HSA-456926", "R-HSA-76009", "R-HSA-9657688", "R-HSA-9672391", "R-HSA-977606", "R-MMU-140837", "R-MMU-140875", "R-MMU-159740...

[ "EC:3.4.21.5", "REACTOME:R-HSA-140837", "REACTOME:R-HSA-140875", "REACTOME:R-HSA-159740", "REACTOME:R-HSA-159763", "REACTOME:R-HSA-159782", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-456926", "REACTOME:R-HSA-76009", "RE...

38

[ "1a0h", "1a2c", "1a3b", "1a3e", "1a46", "1a4w", "1a5g", "1a61", "1abi", "1abj", "1ad8", "1ae8", "1afe", "1aht", "1ai8", "1aix", "1avg", "1awf", "1awh", "1ay6", "1b5g", "1b7x", "1ba8", "1bb0", "1bbr", "1bcu", "1bhx", "1bmm", "1bmn", "1bth", "1c1u", "1c1v"...

503

[ "PUB00045293", "PUB00045294", "PUB00045295" ]

[ "18329094", "18282807", "15656349" ]

[ "Thrombin.", "Thrombin generation, fibrin clot formation and hemostasis.", "Thrombin: a paradigm for enzymes allosterically activated by monovalent cations." ]

[ 2008, 2008, 2004 ]

3

[]

0

null

[ "Vertebrata" ]

[ 1176 ]

1

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

[ 2, 4, 3, 4 ]

4

true

Domain

Thrombin light chain

Thrombin_light_chain

1

IPR018993

18,993

FGFR1 oncogene partner (FOP), N-terminal dimerisation domain

FOP_dimerisation-dom_N

Domain

3,525

false

Fibroblast growth factor receptor 1 (FGFR1) oncogene partner (FOP) is a centrosomal protein that is involved in anchoring microtubules to centrosomes. This domain includes a Lis-homology motif. It forms an α-helical bundle and is involved in dimerisation [ ].

[ "GO:0034453", "GO:0005815" ]

[ "microtubule anchoring", "microtubule organizing center" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09398" ]

[ "FOP_dimer" ]

[ 3525 ]

1

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

[ "R-HSA-1839117", "R-HSA-2565942", "R-HSA-380259", "R-HSA-380270", "R-HSA-380284", "R-HSA-380320", "R-HSA-5620912", "R-HSA-5655302", "R-HSA-8854518", "R-MMU-2565942", "R-MMU-380259", "R-MMU-380270", "R-MMU-380284", "R-MMU-380320", "R-MMU-5620912", "R-MMU-8854518", "R-RNO-2565942", "...

[ "REACTOME:R-HSA-1839117", "REACTOME:R-HSA-2565942", "REACTOME:R-HSA-380259", "REACTOME:R-HSA-380270", "REACTOME:R-HSA-380284", "REACTOME:R-HSA-380320", "REACTOME:R-HSA-5620912", "REACTOME:R-HSA-5655302", "REACTOME:R-HSA-8854518", "REACTOME:R-MMU-2565942", "REACTOME:R-MMU-380259", "REACTOME:R-M...

23

[ "2d68" ]

1

[ "PUB00040195" ]

[ "16690081" ]

[ "Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization." ]

[ 2006 ]

1

[]

0

null

[ "Eukaryota" ]

[ 3525 ]

1

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

[ 21, 25, 4, 5 ]

4

true

Domain

FGFR1 oncogene partner (FOP), N-terminal dimerisation domain

FOP_dimerisation-dom_N

7

IPR018994

18,994

Protein of unknown function DUF2002

DUF2002

Family

938

false

This entry represents a group of putative cytoplasmic proteins. The structure of these proteins form an antiparallel β sheet and contain some α helical regions.

[]

0

[ "NCBIFAM", "PFAM" ]

[ "NF007845", "PF09400" ]

[ "PRK10556.1-3", "DUF2002" ]

[ 873, 938 ]

2

[]

0

[ "2g7j" ]

1

[]

0

[]

0

null

[ "Opisthokonta", "Pseudomonadota" ]

[ 4, 934 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Protein of unknown function DUF2002

DUF2002

2

IPR018995

18,995

RNA synthesis protein NSP10, coronavirus

RNA_synth_NSP10_CoV

Domain

7,749

false

Non-structural protein NSP10 is involved in RNA synthesis. It is synthesised as part of a replicase polyprotein, whose cleavage generates many non-structural proteins [ ]. NSP10 has a mixed α/β fold comprised of five α-helices contains, one 3(10)-helix, and three β-strands ( ) and it is rich in cysteines, featuring two...

[ "GO:0003723", "GO:0008270", "GO:0019079" ]

[ "RNA binding", "zinc ion binding", "viral genome replication" ]

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

3

[ "PFAM", "PROFILE" ]

[ "PF09401", "PS51952" ]

[ "CoV_NSP10", "COV_EXON_MTASE_COACT" ]

[ 7748, 7529 ]

2

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

[ "2.7.7.50", "3.4.19.12", "3.4.22.-", "GenProp1009", "PWY-7375", "R-HSA-191859", "R-HSA-918233", "R-HSA-9679504", "R-HSA-9682706", "R-HSA-9682708", "R-HSA-9683439", "R-HSA-9684325", "R-HSA-9692916", "R-HSA-9694271", "R-HSA-9694301", "R-HSA-9694676", "R-HSA-9694686", "R-HSA-9694786",...

[ "EC:2.7.7.50", "EC:3.4.19.12", "EC:3.4.22.-", "GP:GenProp1009", "METACYC:PWY-7375", "REACTOME:R-HSA-191859", "REACTOME:R-HSA-918233", "REACTOME:R-HSA-9679504", "REACTOME:R-HSA-9682706", "REACTOME:R-HSA-9682708", "REACTOME:R-HSA-9683439", "REACTOME:R-HSA-9684325", "REACTOME:R-HSA-9692916", ...

21

[ "2fyg", "2g9t", "2ga6", "2xyq", "2xyr", "2xyv", "3r24", "5c8s", "5c8t", "5c8u", "5nfy", "5yn5", "5yn6", "5yn8", "5ynb", "5ynf", "5yni", "5ynj", "5ynm", "5ynn", "5yno", "5ynp", "5ynq", "6w4h", "6w61", "6w75", "6wjt", "6wkq", "6wks", "6wq3", "6wrz", "6wvn"...

137

[ "PUB00040863", "PUB00045296", "PUB00094087", "PUB00094105", "PUB00094106", "PUB00099876", "PUB00099890", "PUB00100898" ]

[ "16873246", "17634238", "27712628", "29279395", "25074927", "34580920", "32994211", "33036230" ]

[ "Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs.", "Processing of open reading frame 1a replicase proteins nsp7 to nsp10 in murine hepatitis virus strain A59 replication.", "The Nonstructural Proteins Directi...

[ 2006, 2007, 2016, 2018, 2014, 2021, 2020, 2020 ]

8

[]

0

null

[ "Nidovirales" ]

[ 7749 ]

1

[]

0

true

Domain

RNA synthesis protein NSP10, coronavirus

RNA_synth_NSP10_CoV

1

IPR018996

18,996

Man1/Src1-like, C-terminal

Man1/Src1-like_C

Domain

4,840

false

MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organisation. The C-terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad [ ]. This C-terminal tail is also found in S. cerevisiae and is thought to consist of th...

[]

0

[ "PFAM" ]

[ "PF09402" ]

[ "MSC" ]

[ 4840 ]

1

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

[ "R-HSA-2980766", "R-HSA-2995383", "R-HSA-4419969", "R-HSA-9013149", "R-HSA-9013404", "R-HSA-9013405", "R-HSA-9013408", "R-HSA-9013423", "R-HSA-9668328", "R-HSA-9696264", "R-HSA-9696270", "R-HSA-9696273", "R-SCE-9668328", "R-SPO-9668328" ]

[ "REACTOME:R-HSA-2980766", "REACTOME:R-HSA-2995383", "REACTOME:R-HSA-4419969", "REACTOME:R-HSA-9013149", "REACTOME:R-HSA-9013404", "REACTOME:R-HSA-9013405", "REACTOME:R-HSA-9013408", "REACTOME:R-HSA-9013423", "REACTOME:R-HSA-9668328", "REACTOME:R-HSA-9696264", "REACTOME:R-HSA-9696270", "REACTOM...

14

[ "2ch0" ]

1

[ "PUB00040011", "PUB00057231" ]

[ "16648637", "15611647" ]

[ "The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain.", "Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex." ]

[ 2006, 2004 ]

2

[]

0

null

[ "Eukaryota" ]

[ 4840 ]

1

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

[ 6, 1, 5, 4, 2, 1, 7, 2, 2, 8 ]

10

true

Domain

Man1/Src1-like, C-terminal

Man1/Src1-like_C

2

IPR018997

18,997

PUB domain

PUB_domain

Domain

8,783

false

The PUB (also known as PUG) domain is found in peptide N-glycanase where it functions as a AAA ATPase binding domain [ , ]. This domain is also found on other proteins linked to the ubiquitin-proteasome system. It has α(2)-β-α(2)-α(2)-α fold. It is composed of a cluster of helices with a small antiparallel β-sheet on o...

[]

0

[ "PFAM" ]

[ "PF09409" ]

[ "PUB" ]

[ 8783 ]

1

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

[ "R-DME-532668", "R-DRE-532668", "R-HSA-532668", "R-HSA-5357786", "R-HSA-5357905", "R-HSA-5357956", "R-MMU-532668", "R-MMU-5357786", "R-MMU-5357905", "R-MMU-5357956", "R-RNO-532668" ]

[ "REACTOME:R-DME-532668", "REACTOME:R-DRE-532668", "REACTOME:R-HSA-532668", "REACTOME:R-HSA-5357786", "REACTOME:R-HSA-5357905", "REACTOME:R-HSA-5357956", "REACTOME:R-MMU-532668", "REACTOME:R-MMU-5357786", "REACTOME:R-MMU-5357905", "REACTOME:R-MMU-5357956", "REACTOME:R-RNO-532668" ]

11

[ "2ccq", "2cm0", "2d5u", "2hpj", "2hpl", "4juy", "4oyj", "4oyk", "4p09", "4p0a", "4p0b", "5ljn", "6sap", "7uy2", "7uyj", "8fcl", "8fcm", "8fcn", "8fco", "8fcp", "8fcq", "8fcr", "8fct", "8z30", "8z36" ]

25

[ "PUB00039970", "PUB00103872" ]

[ "16807242", "31847414" ]

[ "The PUB domain functions as a p97 binding module in human peptide N-glycanase.", "Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase." ]

[ 2006, 2019 ]

2

[]

[ "IPR042774" ]

0

1

0

[ "Eukaryota", "Klosneuvirinae" ]

[ 8781, 2 ]

2

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

[ 25, 1, 5, 2, 15, 7, 12, 11, 26 ]

9

true

Domain

PUB domain

PUB_domain

8

IPR018998

18,998

EndoU ribonuclease, C-terminal

EndoU_C

Domain

5,066

false

This entry represents the EndoU domain found at the C-terminal of EndoU endoribonucleases, which carries out a conserved RNA processing function. The EndoU domain cleaves RNA at uridylates and release 2',3'-cyclic phosphodiester ends. The EndoU domain is an α/β domain, that contains nine α-helices and three antiparalle...

[ "GO:0004521" ]

[ "RNA endonuclease activity" ]

[ "molecular_function" ]

1

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

[ "PF09412", "PS51959", "cd21159" ]

[ "XendoU", "ENDOU", "XendoU" ]

[ 5034, 5032, 4684 ]

3

[ "EC" ]

[ "4.6.1.-" ]

[ "EC:4.6.1.-" ]

1

[ "2c1w", "9ftw" ]

2

[ "PUB00039850", "PUB00086626", "PUB00086627", "PUB00086628", "PUB00100908", "PUB00100909", "PUB00100910", "PUB00100911", "PUB00100912", "PUB00100913" ]

[ "16895992", "18936097", "15755742", "28610924", "32284351", "25287301", "28139767", "32049015", "21805647", "24344237" ]

[ "The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.", "The tumor marker human placental protein 11 is an endoribonuclease.", "Functional characterization of XendoU, the endoribonuclease involved in small nucleolar RNA b...

[ 2006, 2008, 2005, 2017, 2020, 2014, 2017, 2020, 2011, 2014 ]

10

[]

0

null

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

[ 81, 4984, 1 ]

3

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

[ 5, 2, 6, 2, 3, 1, 5, 8, 17 ]

9

true

Domain

EndoU ribonuclease, C-terminal

EndoU_C

4

IPR019002

19,002

Ribosome biogenesis protein Nop16

Ribosome_biogenesis_Nop16

Family

4,252

false

Nucleolar protein 16 (Nop16) is a protein involved in the biogenesis of the 60S ribosomal subunit.

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09420", "PTHR13243" ]

[ "Nop16", "" ]

[ 4193, 4076 ]

2

[]

0

[ "6c0f", "6cb1", "6elz", "6em1", "6em3", "6em4", "6em5", "7nac", "7ohp", "7ohr", "7ohs", "7ohv", "7ohw", "7ohx", "7r6q", "7r7a", "8esq", "8esr", "8etg", "8eth", "8eti", "8eup", "8euy", "8ev3", "8fkp", "8fkq", "8fkr", "8fks", "8fkt", "8fku", "8fkv", "8fkw"...

46

[]

0

[]

0

null

[ "Eukaryota" ]

[ 4252 ]

1

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

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

12

true

Family

Ribosome biogenesis protein Nop16

Ribosome_biogenesis_Nop16

1

IPR019003

19,003

APC membrane recruitment protein

AMER

Family

2,475

false

This entry includes APC membrane recruitment protein 1/2/3 (Amer1/2/3). Amer1, also known as WTX, binds to the tumour suppressor adenomatous polyposis coli and acts as an inhibitor of Wnt signaling by inducing beta-catenin degradation [ ]. Amer2 is a negative regulator of Wnt/beta-catenin signaling involved in neuroect...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09422", "PTHR22237" ]

[ "AMER", "" ]

[ 2461, 2465 ]

2

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

[ "R-HSA-195253", "R-HSA-196299", "R-HSA-4641262", "R-HSA-5339716", "R-HSA-5358747", "R-HSA-5358749", "R-HSA-5358751", "R-HSA-5358752", "R-HSA-5467337", "R-HSA-5467340", "R-HSA-5467348", "R-HSA-8951664", "R-HSA-9755511", "R-MMU-195253", "R-MMU-196299", "R-MMU-4641262" ]

[ "REACTOME:R-HSA-195253", "REACTOME:R-HSA-196299", "REACTOME:R-HSA-4641262", "REACTOME:R-HSA-5339716", "REACTOME:R-HSA-5358747", "REACTOME:R-HSA-5358749", "REACTOME:R-HSA-5358751", "REACTOME:R-HSA-5358752", "REACTOME:R-HSA-5467337", "REACTOME:R-HSA-5467340", "REACTOME:R-HSA-5467348", "REACTOME:...

16

[]

0

[ "PUB00088520", "PUB00088521", "PUB00088522" ]

[ "21498506", "22128170", "20843316" ]

[ "Structural and functional characterization of the Wnt inhibitor APC membrane recruitment 1 (Amer1).", "Amer2 protein is a novel negative regulator of Wnt/β-catenin signaling involved in neuroectodermal patterning.", "The WTX/AMER1 gene family: evolution, signature and function." ]

[ 2011, 2012, 2010 ]

3

[]

0

null

[ "Vertebrata" ]

[ 2475 ]

1

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

[ 5, 6, 5, 5 ]

4

true

Family

APC membrane recruitment protein

AMER

8

IPR019004

19,004

Uncharacterised protein YqeY/Aim41

YqeY/Aim41

Family

20,034

false

This entry consist of uncharacterised proteins from bacteria, such as YqeY from Bacillus subtilis, and Aim41/YOR215C from yeast. Altered inheritance of mitochondria protein 41 (Aim41/YOR215C) is a protein of unknown function. It was detected in highly purified mitochondria in high-throughput studies, and null mutant di...

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09424", "PTHR28055" ]

[ "YqeY", "" ]

[ 19898, 19873 ]

2

[]

0

[ "1ng6", "8xje", "8xjg", "9ihq", "9ihr" ]

5

[ "PUB00057438" ]

[ "19300474" ]

[ "Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis." ]

[ 2009 ]

1

[]

0

null

[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 17778, 1, 1699, 87, 469 ]

5

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

[ 1, 1, 1 ]

3

true

Family

Uncharacterised protein YqeY/Aim41

YqeY/Aim41

9

IPR019005

19,005

Vacuolar R-SNARE Nyv1, longin domain

Vacuolar_R-SNAR_Nyv1_longi_dom

Domain

59

false

SNARE-mediated fusion typically results in the formation a complex consisting of three Q-SNAREs and one R-SNARE. R-SNAREs that contain a profilin-like fold in their N-terminal domains have been termed longins. The genome of the yeast Saccharomyces cerevisiae encodes five R-SNAREs of which three (Sec22, Ykt6, and Nyv1) ...

[]

0

[ "PFAM" ]

[ "PF09426" ]

[ "Nyv1_longin" ]

[ 59 ]

1

[ "REACTOME" ]

[ "R-SCE-199992" ]

[ "REACTOME:R-SCE-199992" ]

1

[ "2fz0" ]

1

[ "PUB00040873" ]

[ "16855025" ]

[ "Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein." ]

[ 2006 ]

1

[]

0

null

[ "Saccharomycetes" ]

[ 59 ]

1

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

[ 1 ]

1

true

Domain

Vacuolar R-SNARE Nyv1, longin domain

Vacuolar_R-SNAR_Nyv1_longi_dom

2

IPR019006

19,006

Sterol regulatory element-binding protein 1, C-terminal

Sre1_C

Domain

1,085

false

This entry represents the C-terminal domain of the sterol regulatory element-binding protein 1 (Sre1). Sre1 is a transcriptional activator required for transcription of genes required for adaptation to anaerobic growth like those implicated in the nonrespiratory oxygen-consumptive biosynthetic pathways of sterol, heme,...

[ "GO:0032933", "GO:0045944" ]

[ "SREBP signaling pathway", "positive regulation of transcription by RNA polymerase II" ]

[ "biological_process", "biological_process" ]

2

[ "PFAM" ]

[ "PF09427" ]

[ "DUF2014" ]

[ 1085 ]

1

[]

0

[ "5gpd", "5grs" ]

2

[ "PUB00044954", "PUB00078787" ]

[ "15797383", "16537923" ]

[ "SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast.", "Sterol regulatory element binding protein is a principal regulator of anaerobic gene expression in fission yeast." ]

[ 2005, 2006 ]

2

[]

0

null

[ "Eukaryota" ]

[ 1085 ]

1

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

[ 1, 1 ]

2

true

Domain

Sterol regulatory element-binding protein 1, C-terminal

Sre1_C

9

IPR019007

19,007

Wbp11/ELF5/Saf1, N-terminal domain

Wbp11/ELF5/Saf1_N

Domain

3,951

false

This entry represents WW domain-binding protein 11 (or Saf1 in Schizosaccharomyces pombe), which may play a role in the regulation of pre-mRNA processing and EARLY FLOWERING 5, which acts as a repressor of flowering in Arabidopsis thaliana [ ]. The WW domain is a short conserved region in a number of unrelated proteins...

[ "GO:0006396" ]

[ "RNA processing" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF09429" ]

[ "Wbp11" ]

[ 3951 ]

1

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

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

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

4

[ "7abf", "7abg" ]

2

[ "PUB00000239", "PUB00001680", "PUB00001690", "PUB00004872", "PUB00005431", "PUB00007124", "PUB00090956" ]

[ "7802651", "7828727", "7641887", "7644498", "7846762", "11911877", "15125772" ]

[ "WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65.", "The rsp5-domain is shared by proteins of diverse functions.", "Characterization of a novel protein-binding module--the WW domain.", "The WW domain of ...

[ 1994, 1995, 1995, 1995, 1994, 2002, 2004 ]

7

[]

0

null

[ "Eukaryota" ]

[ 3951 ]

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...

[ 4, 1, 1, 2, 5, 7, 1, 4, 8, 1, 13 ]

11

true

Domain

Wbp11/ELF5/Saf1, N-terminal domain

Wbp11/ELF5/Saf1_N

4

IPR019008

19,008

ER membrane protein complex subunit 7, beta-sandwich domain

Beta_sandwich_EMC7

Domain

5,216

false

This is the β-sandwich domain found in ER membrane protein complex subunit 7 (EMC7) [ , ], which is an integral membrane component of the EMC. EMC is widely conserved and involved in membrane protein biogenesis. It mediates the insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins in an ...

[]

0

[ "PFAM" ]

[ "PF09430" ]

[ "EMC7_beta-sandw" ]

[ 5216 ]

1

[]

0

[ "6ww7", "6z3w", "7ado", "8eoi", "8j0n", "8j0o", "8s9s", "9c7v" ]

8

[ "PUB00054165", "PUB00096678", "PUB00096679", "PUB00096681", "PUB00096682" ]

[ "15257293", "30415835", "29809151", "32459176", "32439656" ]

[ "Nicalin and its binding partner Nomo are novel Nodal signaling antagonists.", "EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.", "The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.", "The architecture of EMC reveals a path for m...

[ 2004, 2018, 2018, 2020, 2020 ]

5

[]

0

null

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

[ 28, 5187, 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", "Schizosaccharomyces pombe (stra...

[ 6, 1, 6, 2, 3, 2, 1, 3, 4, 1, 18 ]

11

true

Domain

ER membrane protein complex subunit 7, beta-sandwich domain

Beta_sandwich_EMC7

9

IPR019009

19,009

Signal recognition particle receptor, beta subunit

SRP_receptor_beta_su

Family

4,781

false

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

[]

0

[ "PFAM", "CDD" ]

[ "PF09439", "cd04105" ]

[ "SRPRB", "SR_beta" ]

[ 4781, 3060 ]

2

[ "REACTOME", "REACTOME" ]

[ "R-HSA-1799339", "R-HSA-381038" ]

[ "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-381038" ]

2

[ "1nrj", "2fh5", "2ged", "2go5", "5ck3", "5ck4", "5ck5", "6frk", "7nfx", "7obq" ]

10

[ "PUB00022264", "PUB00028143", "PUB00035998", "PUB00035999", "PUB00036002", "PUB00036003", "PUB00041125", "PUB00053948", "PUB00063486", "PUB00100261" ]

[ "12654246", "16469117", "17622352", "17507650", "7844142", "10859309", "16675701", "12364595", "12605305", "34020957" ]

[ "Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.", "Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.", "X-ray structures of the signal recognition particle receptor reveal targeting...

[ 2003, 2006, 2007, 2007, 1995, 2000, 2006, 2002, 2003, 2021 ]

10

[ "IPR024156" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4781 ]

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...

[ 9, 1, 1, 2, 4, 3, 1, 4, 6, 1, 1, 4 ]

12

true

Family

Signal recognition particle receptor, beta subunit

SRP_receptor_beta_su

5

IPR019011

19,011

Cryptic/Cripto, CFC domain

Cryptic/Cripto_CFC-dom

Domain

1,137

false

This entry represents the CFC domain found in the membrane protein Cripto (or teratocarcinoma-derived growth factor) and Cryptic proteins. CFC is approximately 40 residues long, compacted by three internal disulphide bridges, and binds Alk4 via a hydrophobic patch. CFC is structurally homologous to the VWFC-like domain...

[]

0

[ "PFAM" ]

[ "PF09443" ]

[ "CFC" ]

[ 1137 ]

1

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

[ "R-HSA-1181150", "R-HSA-1433617", "R-HSA-2892247" ]

[ "REACTOME:R-HSA-1181150", "REACTOME:R-HSA-1433617", "REACTOME:R-HSA-2892247" ]

3

[ "2j5h" ]

1

[ "PUB00012246", "PUB00041880", "PUB00044195", "PUB00045289" ]

[ "11062482", "17125258", "12919325", "19035567" ]

[ "Loss-of-function mutations in the EGF-CFC gene CFC1 are associated with human left-right laterality defects.", "Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala.", "The CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto. Functional and structural insights through disulfide struct...

[ 2000, 2006, 2003, 2009 ]

4

[]

0

null

[ "Bilateria" ]

[ 1137 ]

1

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

[ 2, 7, 4, 5 ]

4

true

Domain

Cryptic/Cripto, CFC domain

Cryptic/Cripto_CFC-dom

6

IPR019012

19,012

RNA cap guanine-N2 methyltransferase

RNA_cap_Gua-N2-MeTrfase

Family

6,416

false

RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe (Fission yeast) trimethylguanosine synthase (Tgs1) and Giardia lamblia (Giardia intestinalis) Tgs2, catalyse the methylation step(s) for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m...

[ "GO:0008168", "GO:0001510", "GO:0036261" ]

[ "methyltransferase activity", "RNA methylation", "7-methylguanosine cap hypermethylation" ]

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

3

[ "PFAM" ]

[ "PF09445" ]

[ "Methyltransf_15" ]

[ 6416 ]

1

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

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

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

163

[ "3egi", "3gdh" ]

2

[ "PUB00044360", "PUB00045320", "PUB00045321" ]

[ "17284461", "18840651", "15590684" ]

[ "Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe.", "Hypermethylation of yeast telomerase RNA by the snRNA and snoRNA methyltransferase Tgs1.", "Specificity and mechanism of RNA cap guanine-N2 methyltransferase (Tgs1)." ]

[ 2007, 2008, 2005 ]

3

[]

0

null

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

[ 100, 655, 5550, 52, 59 ]

5

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

[ 15, 2, 4, 2, 3, 2, 1, 6, 3, 1, 1, 12 ]

12

true

Family

RNA cap guanine-N2 methyltransferase

RNA_cap_Gua-N2-MeTrfase

8

IPR019013

19,013

Vacuolar ATPase assembly integral membrane protein Vma21

Vma21

Family

4,041

false

The vacuolar ATPase assembly integral membrane protein Vma21 is required for the assembly of the integral membrane sector (V0 component) of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum [ ].

[ "GO:0070072" ]

[ "vacuolar proton-transporting V-type ATPase complex assembly" ]

[ "biological_process" ]

1

[ "HAMAP", "PFAM", "PANTHER" ]

[ "MF_03058", "PF09446", "PTHR31792" ]

[ "VMA21", "VMA21", "" ]

[ 2819, 4028, 3295 ]

3

[]

0

[ "8eau" ]

1

[ "PUB00044535" ]

[ "15356264" ]

[ "Role of Vma21p in assembly and transport of the yeast vacuolar ATPase." ]

[ 2004 ]

1

[]

0

null

[ "Blautia", "Eukaryota" ]

[ 2, 4039 ]

2

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

[ 6, 2, 1, 5, 2, 5, 1, 2, 5, 1, 1, 9 ]

12

true

Family

Vacuolar ATPase assembly integral membrane protein Vma21

Vma21

9

IPR019014

19,014

Multivesicular body sorting factor 12

Mvb12

Domain

62

false

Mvb12 is a subunit of the ESCRT-I core complex involved in ubiquitin-dependent sorting of proteins into the endosome. Mvb12 may regulate the interactions of ESCRT-I with cargo and other proteins of the ESCRT machinery to efficiently coordinate cargo sorting and release of ESCRT-I from the multivesicular body [ ]. The m...

[ "GO:0043130", "GO:0032509", "GO:0000813" ]

[ "ubiquitin binding", "endosome transport via multivesicular body sorting pathway", "ESCRT I complex" ]

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

3

[ "PFAM" ]

[ "PF09452" ]

[ "Mvb12" ]

[ 62 ]

1

[]

0

[ "2p22" ]

1

[ "PUB00035959", "PUB00039953", "PUB00074619", "PUB00087727" ]

[ "17215868", "16615893", "17135292", "17450176" ]

[ "Structural insight into the ESCRT-I/-II link and its role in MVB trafficking.", "ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes.", "Efficient cargo sorting by ESCRT-I and the subsequent release of ESCRT-I from multivesicular bodies requires the subunit...

[ 2007, 2006, 2007, 2007 ]

4

[]

0

null

[ "Saccharomycetes" ]

[ 62 ]

1

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

[ 1 ]

1

true

Domain

Multivesicular body sorting factor 12

Mvb12

1

IPR019016

19,016

CRISPR system endoribonuclease Csx1-like, HEPN domain

Csx1-like_HEPN

Domain

195

false

CRISPR system endoribonuclease Csx1 is a metal-independent, endoribonuclease that acts selectively on ssRNA and cleaves specifically after adenosines, as part of the type III-B CRISP-Cas system and it is homologous to Csm6 [ , , ], sharing the same domain domain architecture consisting of a CARF domain at the N-termina...

[]

0

[ "PFAM" ]

[ "PF09455" ]

[ "Csx1_HEPN" ]

[ 195 ]

1

[]

0

[ "2i71", "4eog" ]

2

[ "PUB00020781", "PUB00091682", "PUB00153894" ]

[ "16292354", "30232454", "26647461" ]

[ "A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes.", "Ring nucleases deactivate type III CRISPR ribonucleases by degrading cyclic oligoadenylate.", "The CRISPR-associated Csx1 protein of Pyrococcus furiosus is an adenosine-specific endoribonucl...

[ 2005, 2018, 2016 ]

3

[]

0

null

[ "Archaea", "Bacteria" ]

[ 138, 57 ]

2

[]

0

true

Domain

CRISPR system endoribonuclease Csx1-like, HEPN domain

Csx1-like_HEPN

3

IPR019017

19,017

Signal transduction histidine kinase RcsC, alpha-beta loop, C-terminal

Sig_transdc_His_kin_a/b-loop_C

Domain

1,688

false

This domain is found in the C terminus of the signal transduction response regulator (phospho-relay) kinase RcsC, between the ATP-binding region ( ) and the receiver region ( ). This domain forms a discrete α/β/loop structure [ ]. The Rcs signalling pathway controls a variety of physiological functions like capsule syn...

[ "GO:0004673", "GO:0005524", "GO:0000160", "GO:0006355", "GO:0018106", "GO:0005886", "GO:0016020" ]

[ "protein histidine kinase activity", "ATP binding", "phosphorelay signal transduction system", "regulation of DNA-templated transcription", "peptidyl-histidine phosphorylation", "plasma membrane", "membrane" ]

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

7

[ "PFAM", "PROFILE" ]

[ "PF09456", "PS51426" ]

[ "RcsC", "ABL" ]

[ 1614, 1688 ]

2

[ "EC" ]

[ "2.7.13.3" ]

[ "EC:2.7.13.3" ]

1

[ "2ayx", "2ayy" ]

2

[ "PUB00039457" ]

[ "17005198" ]

[ "A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains." ]

[ 2006 ]

1

[]

0

null

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

[ 1661, 25, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Signal transduction histidine kinase RcsC, alpha-beta loop, C-terminal

Sig_transdc_His_kin_a/b-loop_C

8

IPR019018

19,018

Rab-binding domain FIP-RBD

Rab-bd_FIP-RBD

Domain

9,395

false

The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognise the active form of Rab11. FIPs are diverse in sequence length and composi...

[]

0

[ "PFAM", "PROFILE" ]

[ "PF09457", "PS51511" ]

[ "RBD-FIP", "FIP_RBD" ]

[ 9160, 9327 ]

2

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

[ "R-DRE-5620916", "R-HSA-432040", "R-HSA-5620916", "R-MMU-432040", "R-MMU-5620916" ]

[ "REACTOME:R-DRE-5620916", "REACTOME:R-HSA-432040", "REACTOME:R-HSA-5620916", "REACTOME:R-MMU-432040", "REACTOME:R-MMU-5620916" ]

5

[ "2d7c", "2gzd", "2gzh", "2hv8", "2k6s", "3tso", "4c4p", "4d0g", "4d0m", "4uj3", "4uj4", "6s8x" ]

12

[ "PUB00041224", "PUB00041514", "PUB00044456", "PUB00045288", "PUB00055535", "PUB00055536" ]

[ "16905101", "17007872", "17030804", "19119858", "15218148", "11929610" ]

[ "Crystal structure of rab11 in complex with rab11 family interacting protein 2.", "Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes.", "Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.", "Disorder and struct...

[ 2006, 2006, 2006, 2009, 2004, 2002 ]

6

[]

0

null

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

[ 3, 9391, 1 ]

3

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

[ 6, 32, 20, 15, 16, 26 ]

6

true

Domain

Rab-binding domain FIP-RBD

Rab-bd_FIP-RBD

3

IPR019019

19,019

H-type lectin domain

H-type_lectin_domain

Domain

2,768

false

The H-type lectin domain is a unit of six beta chains, combined into a homo-hexamer. It is involved in self/non-self recognition of cells, through binding with carbohydrates [ ]. It is sometimes found in association with the C-terminal domain of coagulation factor F5/8 ( ).

[ "GO:0030246", "GO:0007155" ]

[ "carbohydrate binding", "cell adhesion" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09458" ]

[ "H_lectin" ]

[ 2768 ]

1

[]

0

[ "2ccv", "2ce6", "2cgy", "2cgz", "2vm9", "2vmc", "2vmd", "2vme", "2w94", "2w95", "2wn2", "2wn3", "3wmp", "3wmq", "4q56", "5x4a" ]

16

[ "PUB00044309" ]

[ "16704980" ]

[ "Biochemical and structural analysis of Helix pomatia agglutinin. A hexameric lectin with a novel fold." ]

[ 2006 ]

1

[]

0

null

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

[ 736, 90, 1923, 2, 17 ]

5

[]

0

true

Domain

H-type lectin domain

H-type_lectin_domain

9

IPR019020

19,020

Cytochrome c-552/DMSO reductase-like, haem-binding domain

Cyt-c552/DMSO_Rdtase_haem-bd

Domain

1,951

false

This entry represents a haem-binding domain found in cytochromes b558/566 (subunit A), c-551 and c-552, as well as in members of the type-II members of the microbial dimethyl sulphoxide (DMSO) reductase family. The DMSO reductase family is a large and rapidly expanding group of enzymes found in bacteria and archaea tha...

[ "GO:0020037" ]

[ "heme binding" ]

[ "molecular_function" ]

1

[ "PFAM", "SMART" ]

[ "PF09459", "SM00887" ]

[ "EB_dh", "EB_dh" ]

[ 1934, 1482 ]

2

[]

0

[ "2ivf", "7b04" ]

2

[ "PUB00041792", "PUB00042991", "PUB00042992", "PUB00042993", "PUB00042994", "PUB00045286" ]

[ "16962969", "15866716", "11294876", "12067345", "15311335", "16030201" ]

[ "Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum.", "The C subunit of Ideonella dechloratans chlorate reductase: expression, purification, refolding, and heme reconstitution.", "Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing molybdenum/iron-sulfur/heme enzyme.", "Molecul...

[ 2006, 2005, 2001, 2002, 2004, 2005 ]

6

[]

0

null

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

[ 246, 968, 647, 90 ]

4

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

[ 7, 3, 5 ]

3

true

Domain

Cytochrome c-552/DMSO reductase-like, haem-binding domain

Cyt-c552/DMSO_Rdtase_haem-bd

4

IPR019021

19,021

E3 ubiquitin-protein ligase substrate receptor Mms22

Mms22

Family

1,602

false

This entry includes methyl methanesulphonate-sensitivity protein 22 (Mms22) from fungi. Mms22 functions to resolve replication intermediates or to prevent damage caused by blocked replication forks [ ]. Saccharomyces cerevisiae Mms22 is a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase ...

[ "GO:0006281", "GO:0006974", "GO:0031297", "GO:0005634" ]

[ "DNA repair", "DNA damage response", "replication fork processing", "nucleus" ]

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

4

[ "PFAM", "PANTHER" ]

[ "PF09462", "PTHR28122" ]

[ "Mus7", "" ]

[ 1544, 1530 ]

2

[]

0

[]

0

[ "PUB00074932", "PUB00074933", "PUB00074934", "PUB00075368" ]

[ "20139071", "21593207", "18704118", "19819763" ]

[ "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage response and transcriptional silencing.", "Mms1 and Mms22 stabilize the replisome during replication stress.", "Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA.", "...

[ 2010, 2011, 2008, 2009 ]

4

[]

[ "IPR013220" ]

0

1

0

[ "Fungi" ]

[ 1602 ]

1

[ "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

Family

E3 ubiquitin-protein ligase substrate receptor Mms22

Mms22

3

IPR019023

19,023

Lamin-B receptor of TUDOR domain

Lamin-B_rcpt_of_tudor

Domain

1,358

false

The Lamin-B receptor is a chromatin and lamin binding protein in the inner nuclear membrane. It is one of the integral inner nuclear envelope membrane proteins responsible for targeting nuclear membranes to chromatin, being a downstream effector of Ran, a small Ras-like nuclear GTPase which regulates NE assembly. Lamin...

[]

0

[ "PFAM", "CDD" ]

[ "PF09465", "cd20381" ]

[ "LBR_tudor", "Tudor_LBR" ]

[ 1354, 1108 ]

2

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

[ "1.3.1.70", "PWY-2541", "PWY-6074", "PWY-7154", "PWY-8026", "PWY-8191", "PWY-8238", "PWY-8239", "R-HSA-191273", "R-HSA-2995383", "R-HSA-8980692", "R-HSA-9013106", "R-HSA-9013148", "R-HSA-9013149", "R-HSA-9013404", "R-HSA-9013405", "R-HSA-9013408", "R-HSA-9013423", "R-HSA-9022692"...

[ "EC:1.3.1.70", "METACYC:PWY-2541", "METACYC:PWY-6074", "METACYC:PWY-7154", "METACYC:PWY-8026", "METACYC:PWY-8191", "METACYC:PWY-8238", "METACYC:PWY-8239", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-2995383", "REACTOME:R-HSA-8980692", "REACTOME:R-HSA-9013106", "REACTOME:R-HSA-9013148", "REACT...

30

[ "2dig", "2l8d" ]

2

[ "PUB00044329", "PUB00100217" ]

[ "17251381", "27336722" ]

[ "Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta.", "The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations." ]

[ 2007, 2016 ]

2

[]

0

null

[ "Candidatus Methanofastidiosum methylothiophilum", "Eukaryota" ]

[ 1, 1357 ]

2

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

[ 2, 5, 5, 2, 4, 20 ]

6

true

Domain

Lamin-B receptor of TUDOR domain

Lamin-B_rcpt_of_tudor

9

IPR019024

19,024

Ribonuclease H2 subunit B, wHTH domain

RNase_H2_suB_wHTH

Domain

4,316

false

Ribonuclease H2B is one of the three proteins of eukaryotic RNase H2 complex that is required for nucleic acid binding and hydrolysis. RNase H is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2/HII). ...

[]

0

[ "PFAM" ]

[ "PF09468" ]

[ "RNase_H2-Ydr279" ]

[ 4316 ]

1

[]

0

[ "3kio", "3p56", "3p5j", "3puf", "8yjz" ]

5

[ "PUB00044465", "PUB00079405", "PUB00079406" ]

[ "14734815", "19228198", "19923215" ]

[ "RNase H2 of Saccharomyces cerevisiae is a complex of three proteins.", "Ribonuclease H.", "The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction." ]

[ 2004, 2009, 2010 ]

3

[]

0

null

[ "Eukaryota" ]

[ 4316 ]

1

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

[ 6, 1, 1, 3, 24, 1, 1, 1, 10, 1, 1, 8 ]

12

true

Domain

Ribonuclease H2 subunit B, wHTH domain

RNase_H2_suB_wHTH

9

IPR019025

19,025

Cordon-bleu, ubiquitin-like domain

Cordon-bleu_ubiquitin_domain

Domain

3,861

false

The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node...

[]

0

[ "PFAM" ]

[ "PF09469" ]

[ "Cobl" ]

[ 3861 ]

1

[]

0

[ "2daj" ]

1

[ "PUB00044202" ]

[ "14512015" ]

[ "Cordon-bleu is a conserved gene involved in neural tube formation." ]

[ 2003 ]

1

[]

0

null

[ "Bilateria" ]

[ 3861 ]

1

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

[ 43, 14, 10, 19 ]

4

true

Domain

Cordon-bleu, ubiquitin-like domain

Cordon-bleu_ubiquitin_domain

2

IPR019026

19,026

Peptidase M64, IgA

Peptidase_M64_IgA

Family

3,204

false

This is a family of highly selective metallo-endopeptidases belonging to the MEROPS peptidase family M64 (IgA peptidase, clan MA). The primary structure of the Clostridium ramosum IgA peptidase shows no significant overall similarity to any other known metallo-endopeptidase [ ].

[]

0

[ "PFAM" ]

[ "PF09471" ]

[ "Peptidase_M64" ]

[ 3204 ]

1

[]

0

[ "3p1v", "4df9", "9ekk", "9ekm", "9ekn", "9i4z", "9qa6", "9qdh", "9qdi" ]

9

[ "PUB00044427" ]

[ "11815614" ]

[ "The Clostridium ramosum IgA proteinase represents a novel type of metalloendopeptidase." ]

[ 2002 ]

1

[]

0

null

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

[ 2640, 514, 50 ]

3

[]

0

true

Family

Peptidase M64, IgA

Peptidase_M64_IgA

8

IPR019027

19,027

Pilus biogenesis CpaD-related

Pilus_biogenesis_CpaD-related

Family

2,211

false

Proteins in this entry consist of a pilus biogenesis protein, CpaD, from Caulobacter, and homologues in other bacteria, including three in the root nodule bacterium Bradyrhizobium japonicum. The molecular function of the homologues is not known.

[]

0

[ "PFAM" ]

[ "PF09476" ]

[ "Pilus_CpaD" ]

[ 2211 ]

1

[]

0

[]

0

[]

0

[]

[ "IPR013361" ]

0

1

0

[ "Eukaryota", "Pseudomonadati", "unclassified sequences" ]

[ 3, 2181, 27 ]

3

[]

0

true

Family

Pilus biogenesis CpaD-related

Pilus_biogenesis_CpaD-related

8

IPR019028

19,028

Carbohydrate binding domain CBM49

CBM_49

Domain

2,088

false

A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare instances of independent putative CBMs. The requirement of CBMs existi...

[ "GO:0030246" ]

[ "carbohydrate binding" ]

[ "molecular_function" ]

1

[ "PFAM", "SMART" ]

[ "PF09478", "SM01063" ]

[ "CBM49", "CBM49" ]

[ 1928, 1976 ]

2

[ "EC", "METACYC" ]

[ "3.2.1.4", "PWY-6788" ]

[ "EC:3.2.1.4", "METACYC:PWY-6788" ]

2

[]

0

[ "PUB00044183", "PUB00054922", "PUB00054923", "PUB00054924" ]

[ "17322304", "3338453", "3134347", "15214846" ]

[ "A tomato endo-beta-1,4-glucanase, SlCel9C1, represents a distinct subclass with a new family of carbohydrate binding modules (CBM49).", "Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.", "Precise excision of the cel...

[ 2007, 1988, 1988, 2004 ]

4

[]

0

null

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

[ 115, 1970, 1, 2 ]

4

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

[ 20, 6, 10 ]

3

true

Domain

Carbohydrate binding domain CBM49

CBM_49

5

IPR019029

19,029

Type III secretion system, PrgH/EprH-like

T3SS_PrgH/EprH-like

Family

995

false

In Salmonella, the gene encoding this protein is part of a four-gene operon PrgHIJK, while in other organisms it is found in type III secretion operons. PrgH has been shown to be required for type III secretion and is a structural component of the needle complex, which is the core component of type III secretion system...

[ "GO:0016020" ]

[ "membrane" ]

[ "cellular_component" ]

1

[ "PFAM" ]

[ "PF09480" ]

[ "PrgH" ]

[ 995 ]

1

[]

0

[ "2xxs", "2y9j", "3gr0", "3gr1", "3j1w", "3j1x", "3j6d", "4a4y", "4g1i", "4g2s", "5tcp", "5tcr", "6duz", "6pem", "6pep", "6q14", "6q15", "6q16", "6rwk", "6rwx", "6uot", "6uov", "7ah9", "7ahi", "8axn" ]

25

[]

0

[]

[ "IPR013387" ]

0

1

0

[ "Bacteria", "human gut metagenome" ]

[ 993, 2 ]

2

[]

0

true

Family

Type III secretion system, PrgH/EprH-like

T3SS_PrgH/EprH-like

5

IPR019034

19,034

Uncharacterised protein family UPF0390

UPF0390

Family

3,067

false

This protein family is highly conserved, but its exact function is unknown. Included in this entry is Leydig cell tumor 10 kDa protein homolog from human which may have a potential role in hypercalcemia of malignancy [ ].

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09495", "PTHR16967" ]

[ "DUF2462", "" ]

[ 3060, 1023 ]

2

[]

0

[ "8fla", "8flb", "8flc", "8idt", "8idy", "8ine", "8inf" ]

7

[ "PUB00044959" ]

[ "15635413" ]

[ "Nucleolar proteome dynamics." ]

[ 2005 ]

1

[]

0

null

[ "Eukaryota" ]

[ 3067 ]

1

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

[ 2, 1, 1, 2, 5, 1, 1, 1, 4, 1, 1, 2 ]

12

true

Family

Uncharacterised protein family UPF0390

UPF0390

7

IPR019035

19,035

Mediator complex, subunit Med12

Mediator_Med12

Domain

5,650

false

The Mediator complex is a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact confor...

[ "GO:0003712", "GO:0006357", "GO:0016592" ]

[ "transcription coregulator activity", "regulation of transcription by RNA polymerase II", "mediator complex" ]

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

3

[ "PFAM", "SMART" ]

[ "PF09497", "SM01281" ]

[ "Med12", "Med12" ]

[ 5630, 5621 ]

2

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

[ "R-DME-9841922", "R-HSA-1989781", "R-HSA-212436", "R-HSA-381340", "R-HSA-9833110", "R-HSA-9841922" ]

[ "REACTOME:R-DME-9841922", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-212436", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-9833110", "REACTOME:R-HSA-9841922" ]

6

[ "7kpv", "7kpw", "7kpx", "8tq2", "8tqc", "8tqw" ]

6

[ "PUB00045284", "PUB00045285" ]

[ "17088561", "18394596" ]

[ "A subunit of the mediator complex regulates vertebrate neuronal development.", "Multiple roles for Med12 in vertebrate endoderm development." ]

[ 2006, 2008 ]

2

[]

0

null

[ "Eukaryota" ]

[ 5650 ]

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...

[ 5, 1, 5, 2, 15, 5, 2, 6, 12, 1, 2, 28 ]

12

true

Domain

Mediator complex, subunit Med12

Mediator_Med12

5

IPR019036

19,036

Restriction endonuclease, type II, ApaLI

Restrct_endonuc_II_ApaLI

Family

144

false

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

[]

0

[ "PFAM" ]

[ "PF09499" ]

[ "RE_ApaLI" ]

[ 144 ]

1

[]

0

[]

0

[ "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707", "PUB00045097" ]

[ "15770420", "14576294", "11827971", "11557805", "15121719", "12665693", "9862476" ]

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

[ 2005, 2003, 2002, 2001, 2004, 2003, 1998 ]

7

[]

0

null

[ "Bacteria", "Halosimplex rubrum", "Shirahamavirus PTm1", "ecological metagenomes" ]

[ 137, 1, 2, 4 ]

4

[]

0

true

Family

Restriction endonuclease, type II, ApaLI

Restrct_endonuc_II_ApaLI

7

IPR019037

19,037

Restriction endonuclease, type II, Bsp6I

Restrct_endonuc_II_Bsp6I

Family

89

false

This entry includes the restriction endonuclease Bsp6I, which recognises and cleaves the double-stranded sequence GC^NGC [ ]. There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to giv...

[]

0

[ "PFAM" ]

[ "PF09504" ]

[ "RE_Bsp6I" ]

[ 89 ]

1

[]

0

[]

0

[ "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707", "PUB00099965" ]

[ "15770420", "14576294", "11827971", "11557805", "15121719", "12665693", "12654995" ]

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

7

[]

0

null

[ "Bacteria", "Glomeromycetes", "Methanobacteriaceae", "Viruses", "metagenomes" ]

[ 68, 2, 2, 3, 14 ]

5

[]

0

true

Family

Restriction endonuclease, type II, Bsp6I

Restrct_endonuc_II_Bsp6I

2

IPR019038

19,038

DNA polymerase delta subunit 3

POLD3

Family

4,322

false

POLD3 is a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. It is required for optimal Pol-delta activity [ , , , , ].

[ "GO:0006260", "GO:0005634", "GO:0043625" ]

[ "DNA replication", "nucleus", "delta DNA polymerase complex" ]

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

3

[ "PFAM", "PANTHER" ]

[ "PF09507", "PTHR17598" ]

[ "CDC27", "" ]

[ 4063, 4085 ]

2

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

[ "R-BTA-110314", "R-BTA-174411", "R-BTA-174414", "R-BTA-174417", "R-BTA-174437", "R-BTA-5358565", "R-BTA-5358606", "R-BTA-5651801", "R-BTA-5656169", "R-BTA-5685942", "R-BTA-5696397", "R-BTA-5696400", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-69091", "R-BTA-69166", "R-BTA-69183", "R-G...

[ "REACTOME:R-BTA-110314", "REACTOME:R-BTA-174411", "REACTOME:R-BTA-174414", "REACTOME:R-BTA-174417", "REACTOME:R-BTA-174437", "REACTOME:R-BTA-5358565", "REACTOME:R-BTA-5358606", "REACTOME:R-BTA-5651801", "REACTOME:R-BTA-5656169", "REACTOME:R-BTA-5685942", "REACTOME:R-BTA-5696397", "REACTOME:R-B...

65

[ "3e0j", "6s1m", "6s1n", "6s1o", "6tny", "6tnz", "9ekb" ]

7

[ "PUB00092479", "PUB00092480", "PUB00092481", "PUB00092482", "PUB00092483" ]

[ "10219083", "10852724", "11595739", "16510448", "24035200" ]

[ "Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts.", "Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 prote...

[ 1999, 2000, 2001, 2006, 2013 ]

5

[]

0

null

[ "Eukaryota" ]

[ 4322 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "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...

[ 6, 1, 2, 12, 8, 1, 3, 5, 1, 40 ]

10

true

Family

DNA polymerase delta subunit 3

POLD3

6

IPR019041

19,041

SSXRD motif

SSXRD_motif

Conserved_site

815

false

Protein SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N terminus. However, from the analysis of these deletion constructs further repression activity was found at the C terminus of SSX1. Which has been called the SSXRD (SSX Repression D...

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

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

[ "biological_process", "cellular_component" ]

2

[ "PFAM" ]

[ "PF09514" ]

[ "SSXRD" ]

[ 815 ]

1

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

[ "R-HSA-212436", "R-HSA-3214841", "R-HSA-912446", "R-MMU-3214841", "R-RNO-3214841" ]

[ "REACTOME:R-HSA-212436", "REACTOME:R-HSA-3214841", "REACTOME:R-HSA-912446", "REACTOME:R-MMU-3214841", "REACTOME:R-RNO-3214841" ]

5

[ "8hqy" ]

1

[ "PUB00007560" ]

[ "9788446" ]

[ "A KRAB-related domain and a novel transcription repression domain in proteins encoded by SSX genes that are disrupted in human sarcomas." ]

[ 1998 ]

1

[]

0

null

[ "Amniota" ]

[ 815 ]

1

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

[ 21, 26, 4 ]

3

true

Conserved_site

SSXRD motif

SSXRD_motif

2

IPR019042

19,042

Restriction endonuclease, type II, CfrBI

Restrct_endonuc_II_CfrBI

Family

164

false

This entry includes the CfrBI restriction endonuclease which recognises and cleaves C^CWWGG [ ]. Type II restriction endonucleases ( ) are components of prokaryotic DNA restriction-modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonuc...

[]

0

[ "PFAM" ]

[ "PF09516" ]

[ "RE_CfrBI" ]

[ 164 ]

1

[]

0

[]

0

[ "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00045100" ]

[ "15770420", "14576294", "11827971", "11557805", "8335262" ]

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "Clo...

[ 2005, 2003, 2002, 2001, 1993 ]

5

[]

0

null

[ "Bacteria", "Candidatus Syntropharchaeum caldarium", "Eukaryota", "metagenomes" ]

[ 156, 1, 2, 5 ]

4

[]

0

true

Family

Restriction endonuclease, type II, CfrBI

Restrct_endonuc_II_CfrBI

5

IPR019043

19,043

Restriction endonuclease, type II, HindIII

Restrct_endonuc_II_HindIII

Family

109

false

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

[]

0

[ "PFAM" ]

[ "PF09518" ]

[ "RE_HindIII" ]

[ 109 ]

1

[]

0

[ "2e52", "3a4k", "3wvg", "3wvh", "3wvi", "3wvk", "3wvp" ]

7

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Potamilus streckersoni", "metagenomes" ]

[ 104, 1, 4 ]

3

[]

0

true

Family

Restriction endonuclease, type II, HindIII

Restrct_endonuc_II_HindIII

1

IPR019044

19,044

Restriction endonuclease, type II, HindVP

Restrct_endonuc_II_HindVP

Family

185

false

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

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

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

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

3

[ "PFAM" ]

[ "PF09519" ]

[ "RE_HindVP" ]

[ 185 ]

1

[ "EC" ]

[ "3.1.21.4" ]

[ "EC:3.1.21.4" ]

1

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Viruses", "human gut metagenome" ]

[ 181, 3, 1 ]

3

[]

0

true

Family

Restriction endonuclease, type II, HindVP

Restrct_endonuc_II_HindVP

5

IPR019045

19,045

Restriction endonuclease, type II, HinfI-like

Restrct_endonuc_II_HinfI

Family

601

false

This entry includes the restriction endonuclease HinfI, which recognises the double-stranded sequence 5'-GANTC-3' and cleaves after G-1 [ ]. It also includes other Type II restriction enzymes that recognise and cleave at GGNCC sites such as MjaII as well as HgiEI, HgiBI, HgiCII that recognise the double-stranded sequen...

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

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

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

3

[ "PFAM" ]

[ "PF09520" ]

[ "HinfI" ]

[ 601 ]

1

[ "EC" ]

[ "3.1.21.4" ]

[ "EC:3.1.21.4" ]

1

[]

0

[ "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707", "PUB00099965", "PUB00154748", "PUB00161587", "PUB00161588" ]

[ "15770420", "14576294", "11827971", "11557805", "15121719", "12665693", "12654995", "3063606", "1644308", "7607523" ]

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

[ 2005, 2003, 2002, 2001, 2004, 2003, 2003, 1988, 1992, 1995 ]

10

[]

[ "IPR054785" ]

0

1

0

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

[ 30, 537, 34 ]

3

[]

0

true

Family

Restriction endonuclease, type II, HinfI-like

Restrct_endonuc_II_HinfI

4

IPR019046

19,046

Restriction endonuclease, type II, NgoPII

Restrct_endonuc_II_NgoPII

Family

195

false

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

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

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

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

3

[ "PFAM" ]

[ "PF09521" ]

[ "RE_NgoPII" ]

[ 195 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

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

[ 7, 185, 3 ]

3

[]

0

true

Family

Restriction endonuclease, type II, NgoPII

Restrct_endonuc_II_NgoPII

6

IPR019049

19,049

Nucleoporin protein Ndc1-Nup

Nucleoporin_prot_Ndc1/Nup

Family

4,426

false

Ndc1 is a nucleoporin protein that is a component of the Nuclear Pore Complex, and, in fungi, also of the Spindle Pole Body. It consists of six transmembrane segments, three luminal loops, both concentrated at the N terminus and cytoplasmic domains largely at the C terminus, all of which are well conserved.

[]

0

[ "PFAM", "PANTHER" ]

[ "PF09531", "PTHR13269" ]

[ "Ndc1_Nup", "" ]

[ 4241, 4291 ]

2

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

[ "R-DME-159227", "R-DME-159230", "R-DME-159231", "R-DME-159236", "R-DME-170822", "R-DME-3108214", "R-DME-3301854", "R-DME-4085377", "R-DME-4551638", "R-DME-4615885", "R-DME-5578749", "R-DME-9615933", "R-HSA-1169408", "R-HSA-159227", "R-HSA-159230", "R-HSA-159231", "R-HSA-159236", "R...

[ "REACTOME:R-DME-159227", "REACTOME:R-DME-159230", "REACTOME:R-DME-159231", "REACTOME:R-DME-159236", "REACTOME:R-DME-170822", "REACTOME:R-DME-3108214", "REACTOME:R-DME-3301854", "REACTOME:R-DME-4085377", "REACTOME:R-DME-4551638", "REACTOME:R-DME-4615885", "REACTOME:R-DME-5578749", "REACTOME:R-D...

89

[ "7r5j", "7r5k", "7wkk", "9sob" ]

4

[]

0

[]

0

null

[ "Eukaryota" ]

[ 4426 ]

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...

[ 5, 1, 2, 1, 2, 2, 1, 3, 5, 1, 1, 9 ]

12

true

Family

Nucleoporin protein Ndc1-Nup

Nucleoporin_prot_Ndc1/Nup

3

IPR019050

19,050

FDF domain

FDF_dom

Domain

10,802

false

The FDF domain, so called because of the conserved FDF at its N termini, is an entirely α-helical domain with multiple exposed hydrophilic loops [ ]. It is found at the C terminus of Scd6p-like SM domains [ , ]. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is fou...

[]

0

[ "PFAM", "SMART" ]

[ "PF09532", "SM01199" ]

[ "FDF", "FDF" ]

[ 9149, 10706 ]

2

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

[ "R-DME-430039", "R-DRE-430039", "R-HSA-430039", "R-MMU-430039", "R-SCE-430039" ]

[ "REACTOME:R-DME-430039", "REACTOME:R-DRE-430039", "REACTOME:R-HSA-430039", "REACTOME:R-MMU-430039", "REACTOME:R-SCE-430039" ]

5

[ "2wax", "2way", "3d3j", "3d3k", "4a53", "6f9s", "6s8s" ]

7

[ "PUB00043768", "PUB00044226" ]

[ "15257761", "15225602" ]

[ "Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability.", "Novel Sm-like proteins with long C-terminal tails and associated methyltransferases." ]

[ 2004, 2004 ]

2

[]

0

null

[ "Eukaryota" ]

[ 10802 ]

1

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

[ 8, 1, 16, 10, 11, 8, 2, 6, 13, 2, 2, 26 ]

12

true

Domain

FDF domain

FDF_dom

5

IPR019051

19,051

Trp biosynthesis associated, transmembrane protein, Oprn/Chp

Trp_biosyn_TM_oprn/chp

Family

4,105

false

Members of this family are predicted transmembrane proteins with four membrane-spanning helices. Members are found in the Actinobacteria (Mycobacterium, Corynebacterium, Streptomyces), always associated with genes for tryptophan biosynthesis.

[]

0

[ "PFAM" ]

[ "PF09534" ]

[ "Trp_oprn_chp" ]

[ 4105 ]

1

[]

0

[]

0

[]

0

[]

[ "IPR011746" ]

0

1

0

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

[ 4063, 2, 40 ]

3

[]

0

true

Family

Trp biosynthesis associated, transmembrane protein, Oprn/Chp

Trp_biosyn_TM_oprn/chp

1

IPR019052

19,052

Domain of unknown function DUF2383

DUF2383

Domain

6,036

false

This entry represents a domain found in uncharacterised proteins predominantly found in bacteria that includes DUF2383 domain-containing protein from Pseudomonas aeruginosa ( ). This protein shows a ferritin-like topology with a four-helix-bundle fold that lacks metal-ion-binding site typical of the ferritin family but...

[]

0

[ "PFAM" ]

[ "PF09537" ]

[ "DUF2383" ]

[ 6036 ]

1

[]

0

[ "4etr" ]

1

[ "PUB00065044" ]

[ "23295481" ]

[ "The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic studies for assessment of potential targets in early-stage drug discovery." ]

[ 2013 ]

1

[]

0

null

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

[ 5964, 50, 22 ]

3

[]

0

true

Domain

Domain of unknown function DUF2383

DUF2383

9

IPR019054

19,054

Restriction endonuclease, type II, AccI

Restrct_endonuc_II_AccI

Family

74

false

This entry includes the restriction endonuclease AccI, which recognises and cleaves the double-stranded sequence GT^MKAC. There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give sp...

[]

0

[ "PFAM" ]

[ "PF09545" ]

[ "RE_AccI" ]

[ 74 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Archaea", "Bacteria", "marine sediment metagenome" ]

[ 5, 67, 2 ]

3

[]

0

true

Family

Restriction endonuclease, type II, AccI

Restrct_endonuc_II_AccI

3

IPR019056

19,056

Phage tail assembly chaperone protein, TAC6

Phage_TAC_6

Family

1,622

false

This is a family of phage tail assembly chaperone proteins largely derived from the Rhodobacter species viral agent GTA (gene transfer agent) gp10 [ ].

[]

0

[ "PFAM" ]

[ "PF09550" ]

[ "Phage_TAC_6" ]

[ 1622 ]

1

[]

0

[]

0

[ "PUB00075454" ]

[ "23542344" ]

[ "A conserved spiral structure for highly diverged phage tail assembly chaperones." ]

[ 2013 ]

1

[]

[ "IPR011739" ]

0

1

0

[ "Bacteria", "Diploscapter pachys", "Viruses", "metagenomes" ]

[ 1603, 1, 5, 13 ]

4

[]

0

true

Family

Phage tail assembly chaperone protein, TAC6

Phage_TAC_6

7

IPR019057

19,057

Restriction endonuclease, type II, Eco47II

Restrct_endonuc_II_Eco47II

Family

371

false

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

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

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

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

3

[ "PFAM" ]

[ "PF09553" ]

[ "RE_Eco47II" ]

[ 371 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

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

[ 8, 348, 3, 12 ]

4

[]

0

true

Family

Restriction endonuclease, type II, Eco47II

Restrct_endonuc_II_Eco47II

9

IPR019058

19,058

Restriction endonuclease, type II, HaeII

Restrct_endonuc_II_HaeII

Family

79

false

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

[]

0

[ "PFAM" ]

[ "PF09554" ]

[ "RE_HaeII" ]

[ 79 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Haloferacaceae" ]

[ 76, 3 ]

2

[]

0

true

Family

Restriction endonuclease, type II, HaeII

Restrct_endonuc_II_HaeII

7

IPR019059

19,059

Restriction endonuclease, type II, HaeIII

Restrct_endonuc_II_HaeIII

Family

254

false

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

[]

0

[ "PFAM" ]

[ "PF09556" ]

[ "RE_HaeIII" ]

[ 254 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobrevibacter arboriphilus", "metagenomes" ]

[ 244, 3, 1, 6 ]

4

[]

0

true

Family

Restriction endonuclease, type II, HaeIII

Restrct_endonuc_II_HaeIII

6

IPR019062

19,062

Restriction endonuclease, type II, HpaII

Restrct_endonuc_II_HpaII

Family

531

false

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

[]

0

[ "PFAM" ]

[ "PF09561" ]

[ "RE_HpaII" ]

[ 531 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

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

[ 520, 3, 8 ]

3

[]

0

true

Family

Restriction endonuclease, type II, HpaII

Restrct_endonuc_II_HpaII

7

IPR019063

19,063

Restriction endonuclease, type II, LlaMI

Restrct_endonuc_II_LlaMI

Family

31

false

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

[]

0

[ "PFAM" ]

[ "PF09562" ]

[ "RE_LlaMI" ]

[ 31 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Methanobrevibacter", "metagenomes" ]

[ 22, 2, 7 ]

3

[]

0

true

Family

Restriction endonuclease, type II, LlaMI

Restrct_endonuc_II_LlaMI

6

IPR019064

19,064

Type-2 restriction enzyme NlaIV

Restrct_endonuc_II_NlaIV

Family

122

false

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

[ "GO:0009036", "GO:0090304" ]

[ "type II site-specific deoxyribonuclease activity", "nucleic acid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM" ]

[ "PF09564" ]

[ "RE_NgoBV" ]

[ 122 ]

1

[]

0

[ "6qm2" ]

1

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Methanobacteriaceae", "organismal metagenomes" ]

[ 116, 2, 4 ]

3

[]

0

true

Family

Type-2 restriction enzyme NlaIV

Restrct_endonuc_II_NlaIV

3

IPR019065

19,065

Restriction endonuclease, type II, NgoFVII, N-terminal domain

RE_NgoFVII_N

Domain

586

false

This entry represents a N-terminal domain of the type II restriction enzyme NgoFVII, which recognises the double-stranded sequence GCSGC and cleaves after G-4 [ ]. 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 ...

[]

0

[ "PFAM" ]

[ "PF09565" ]

[ "RE_NgoFVII" ]

[ 586 ]

1

[]

0

[ "4rct" ]

1

[ "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707", "PUB00152066" ]

[ "15770420", "14576294", "11827971", "11557805", "15121719", "12665693", "25429979" ]

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

[ 2005, 2003, 2002, 2001, 2004, 2003, 2014 ]

7

[]

0

null

[ "Bacteria", "Methanobacteriati", "ecological metagenomes" ]

[ 568, 11, 7 ]

3

[]

0

true

Domain

Restriction endonuclease, type II, NgoFVII, N-terminal domain

RE_NgoFVII_N

8

IPR019066

19,066

Restriction endonuclease, type II, SacI

Restrct_endonuc_II_SacI

Family

200

false

This family includes the SacI restriction endonuclease, which recognises and cleaves GAGCT^C. There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragm...

[]

0

[ "PFAM" ]

[ "PF09566" ]

[ "RE_SacI" ]

[ 200 ]

1

[]

0

[ "7e8r", "7edb" ]

2

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Archaea", "Bacteria", "Peduovirus P2", "metagenomes" ]

[ 6, 191, 1, 2 ]

4

[]

0

true

Family

Restriction endonuclease, type II, SacI

Restrct_endonuc_II_SacI

2

IPR019067

19,067

Restriction endonuclease, type II, MamI

Restrct_endonuc_II_MamI

Family

36

false

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

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

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

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

3

[ "PFAM" ]

[ "PF09567" ]

[ "RE_MamI" ]

[ 36 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

[ "Bacteria", "Candidatus Micrarchaeum acidiphilum ARMAN-2", "Siphoviridae sp. ctkL423" ]

[ 33, 1, 2 ]

3

[]

0

true

Family

Restriction endonuclease, type II, MamI

Restrct_endonuc_II_MamI

9

IPR019068

19,068

Restriction endonuclease, type II, MjaI-like

Restrct_endonuc_II_MjaI-like

Family

303

false

This entry includes the MjaI restriction endonuclease and Type II restriction enzyme MthZI. There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragmen...

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

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

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

3

[ "PFAM" ]

[ "PF09568" ]

[ "RE_MjaI" ]

[ 303 ]

1

[]

0

[]

0

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

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

[ "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 endonucleases.", "Structure and function of type II restriction endonucleases.", "S-A...

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

6

[]

0

null

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

[ 43, 234, 8, 18 ]

4

[]

0

true

Family

Restriction endonuclease, type II, MjaI-like

Restrct_endonuc_II_MjaI-like

4