interpro_id string | interpro_numeric_id int64 | name string | short_name string | entry_type string | protein_count int64 | is_llm bool | is_llm_reviewed bool | abstract string | go_ids list | go_terms list | go_categories list | go_count int64 | member_databases list | member_accessions list | member_names list | member_protein_counts list | member_count int64 | external_databases list | external_accessions list | external_xrefs list | external_xref_count int64 | pdb_ids list | structure_count int64 | publication_ids list | pubmed_ids list | publication_titles list | publication_years list | publication_count int64 | parent_ids list | child_ids list | parent_count int64 | child_count int64 | tree_depth float64 | taxonomy_names list | taxonomy_protein_counts list | taxonomy_count int64 | key_species_names list | key_species_protein_counts list | key_species_count int64 | in_entry_list bool | entry_list_type string | entry_list_name string | names_dat_name string | short_names_dat_name string | split_bucket int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR054023 | 54,023 | Spike protein P1, C-terminal | Phage_spike_P1_C | Domain | 4 | false | false | This entry represents the C-terminal receptor binding domain of Spike protein P1 ( ) from Pseudoalteromonas phage PM2 [ ] and related prophages [ , , ]. The Spike protein P1, also known as Protein I, is a key component of the Pseudoalteromonas phage PM2 (Bacteriophage PM2). This protein is responsible for receptor bind... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22188"
] | [
"Phage_spike_P1"
] | [
4
] | 1 | [] | [] | [] | 0 | [
"2vvd",
"2vve",
"2w0c"
] | 3 | [
"PUB00049918",
"PUB00161734",
"PUB00161735"
] | [
"18775333",
"17634101",
"29798916"
] | [
"Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2.",
"Putative prophages related to lytic tailless marine dsDNA phage PM2 are widespread in the genomes of aquatic bacteria.",
"Genome Sequence of PM2-Like Phage Cr39582, Induced from a Pseud... | [
2008,
2007,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudoalteromonas",
"Pseudoalteromonas phage PM2"
] | [
3,
1
] | 2 | [] | [] | 0 | true | Domain | Spike protein P1, C-terminal | Spike protein P1, C-terminal | Phage_spike_P1_C | 9 |
IPR054024 | 54,024 | Domain of unknown function DUF6946 | DUF6946 | Domain | 196 | false | false | This domain is found in uncharacterised bacterial proteins either standalone or in combination with other domains. It is distantly related to the type II restriction endonucleases with predicted similar active site architecture. These proteins are most likely endonucleases based on the strict conservation of the putati... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22187"
] | [
"DUF6946"
] | [
196
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
184,
12
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6946 | Domain of unknown function DUF6946 | DUF6946 | 8 |
IPR054025 | 54,025 | Uncharacterized protein AF_0924 | AF_0924 | Domain | 4 | false | false | This entry represents the AF_0924 protein from Archaeoglobus fulgidus. The structure of this protein ( ) is composed of three α-helices and three β-strands. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22185"
] | [
"AF_0924"
] | [
4
] | 1 | [] | [] | [] | 0 | [
"3dt5"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
4
] | 1 | [] | [] | 0 | true | Domain | Uncharacterized protein AF_0924 | Uncharacterized protein AF_0924 | AF_0924 | 2 |
IPR054026 | 54,026 | Atadenovirus fibre, head domain | Fibre_HD | Domain | 2 | false | false | This entry represents the carboxy-terminal virus-distal fibre head domain present in Atadenovirus. This domain is putatively responsible for primary receptor recognition. Atadenovirus fibre head domains has a similar β-sandwich propeller topology found in other adenovirus fibre proteins ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22183"
] | [
"Fibre_HD"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"4d0u",
"4d0v",
"4d1f",
"4d1g",
"4umi"
] | 5 | [
"PUB00153945"
] | [
"25486282"
] | [
"Crystal structure of the fibre head domain of the Atadenovirus Snake Adenovirus 1."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Barthadenovirus"
] | [
2
] | 1 | [] | [] | 0 | true | Domain | Atadenovirus fibre, head domain | Atadenovirus fibre, head domain | Fibre_HD | 9 |
IPR054028 | 54,028 | TarS/TarP, linker domain | TarS/TarP_linker | Domain | 2,113 | false | false | TarS is an enzyme responsible for the glycosylation of wall teichoic acid polymers of the S. aureus cell wall, a process that has been shown to contribute for methicillin resistance in MRSA. TarS consist of three domains: catalytic, linker and trimerisation [ ]. This entry represents the linker domain that bridges the ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22181"
] | [
"TarS_linker"
] | [
2113
] | 1 | [] | [] | [] | 0 | [
"5tz8",
"5tze",
"5tzi",
"5tzj",
"5tzk",
"5u02",
"6h1j",
"6h21",
"6h2n",
"6h4f",
"6h4m",
"6hnq",
"8bz4",
"8bz5",
"8bz6",
"8bz7",
"8bz8",
"9gzj",
"9gzk"
] | 19 | [
"PUB00091409",
"PUB00154261"
] | [
"27973583",
"30464342"
] | [
"Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance.",
"Methicillin-resistant Staphylococcus aureus alters cell wall glycosylation to evade immunity."
] | [
2016,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Staphylococcus phage Sebago"
] | [
2112,
1
] | 2 | [] | [] | 0 | true | Domain | TarS/TarP, linker domain | TarS/TarP, linker domain | TarS/TarP_linker | 4 |
IPR054030 | 54,030 | Gp5/Type VI secretion system Vgr, C-terminal trimerisation domain | Gp5_Vgr_C | Domain | 12,494 | false | false | This entry represents the C-terminal trimerisation domain found in Type VI secretion system spike protein VgrG(1-5, A,B) and Gp5. This domain associates to form a triple-stranded β-helix that forms an equilateral triangular prism, which acts as a membrane-puncturing needle [ ]. The interior of the β-helix has an increa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22178"
] | [
"Gp5_trimer_C"
] | [
12494
] | 1 | [] | [] | [] | 0 | [
"4jiv",
"4jiw",
"4jj2",
"4ku0",
"4mtk",
"4osd",
"4uhv",
"6h3l",
"6h3n",
"6p1z",
"6p22",
"7q5p",
"8qja",
"9f4a",
"9f4b"
] | 15 | [
"PUB00012803",
"PUB00029807",
"PUB00032318",
"PUB00050212",
"PUB00054456",
"PUB00094751",
"PUB00098812",
"PUB00153988"
] | [
"11823865",
"12923574",
"15701513",
"18098245",
"20661999",
"30177742",
"26894532",
"26894531"
] | [
"Structure of the cell-puncturing device of bacteriophage T4.",
"Three-dimensional structure of bacteriophage T4 baseplate.",
"Control of bacteriophage T4 tail lysozyme activity during the infection process.",
"Molecular design of heteroprotein assemblies providing a bionanocup as a chemical reactor.",
"Con... | [
2002,
2003,
2005,
2008,
2010,
2018,
2016,
2016
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
12305,
66,
67,
56
] | 4 | [] | [] | 0 | true | Domain | Gp5/Type VI secretion system Vgr, C-terminal trimerisation domain | Gp5/Type VI secretion system Vgr, C-terminal trimerisation domain | Gp5_Vgr_C | 2 |
IPR054031 | 54,031 | Xylose operon regulatory protein, N-terminal domain | XylR_PBP1 | Domain | 2,644 | false | false | This entry represents the N-terminal domain of Xylose operon regulatory protein (XylR), an atypical AraC protein. This D-xylose-binding domain contains a periplasmic-binding protein (PBP) fold, similar to LacI/GalR transcription regulators, and mediates dimerisation [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22177"
] | [
"PBP1_XylR"
] | [
2644
] | 1 | [] | [] | [] | 0 | [
"4fe4",
"4fe7"
] | 2 | [
"PUB00065111"
] | [
"23241389"
] | [
"Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domain."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2636,
5,
3
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Xylose operon regulatory protein, N-terminal domain | Xylose operon regulatory protein, N-terminal domain | XylR_PBP1 | 4 |
IPR054034 | 54,034 | Tail protein NMB1110-like, C-terminal domain | NMB1110-like_C | Domain | 388 | false | false | This domain is found at the C-terminal end of Tail protein, 43 kDa Neisseria meningitidis (NMB1110) and similar sequences found in tailed bacteriophages and prophages from proteobacteria. This domain is usually found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22174"
] | [
"NMB1110-like_C"
] | [
388
] | 1 | [] | [] | [] | 0 | [
"3d37"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Caudoviricetes",
"Glossina brevipalpis",
"Pseudomonadati",
"ecological metagenomes"
] | [
4,
1,
381,
2
] | 4 | [] | [] | 0 | true | Domain | Tail protein NMB1110-like, C-terminal domain | Tail protein NMB1110-like, C-terminal domain | NMB1110-like_C | 5 |
IPR054035 | 54,035 | Acylamino-acid-releasing enzyme-like, N-terminal domain | APH-like_N | Domain | 40 | false | false | This domain is found at the N-terminal of Acylamino-acid-releasing enzyme from Aeropyrum pernix (APH) and similar archaeal sequences. APH catalyses the removal of an N-acylated amino acid from peptides. This domain folds as a regular seven-bladed β-propeller [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22173"
] | [
"APH-like_N"
] | [
40
] | 1 | [] | [] | [] | 0 | [
"1ve6",
"1ve7",
"2hu5",
"2hu7",
"2hu8",
"2qr5",
"2qzp",
"3o4g",
"3o4h",
"3o4i",
"3o4j",
"4re5",
"4re6",
"9s6b"
] | 14 | [
"PUB00032065",
"PUB00041506",
"PUB00049114",
"PUB00058773",
"PUB00153820"
] | [
"15296741",
"17350041",
"18325786",
"21084296",
"25760596"
] | [
"Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1.",
"The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity.",
"Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl... | [
2004,
2007,
2008,
2011,
2015
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
40
] | 1 | [] | [] | 0 | true | Domain | Acylamino-acid-releasing enzyme-like, N-terminal domain | Acylamino-acid-releasing enzyme-like, N-terminal domain | APH-like_N | 1 |
IPR054037 | 54,037 | Phosphocholine transferase AnkX, insertion domain | AnkX_ins | Domain | 21 | false | false | This entry represents the insertion domain of AnkX, a Legionella pneumophila PC transferase that mediates the recruitment of Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). It is a virulence factor that modifies host RAB1 (RAB1A, RAB1B, or RAB1C) and RAB35 leading to the displacement of GDP diss... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22170"
] | [
"AnkX_ins"
] | [
21
] | 1 | [] | [] | [] | 0 | [
"4bep",
"4ber",
"4bes",
"4bet",
"6sku"
] | 5 | [
"PUB00067149",
"PUB00153814"
] | [
"23572077",
"32440549"
] | [
"Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain.",
"<i>Legionella</i> effector AnkX displaces the switch II region for Rab1b phosphocholination."
] | [
2013,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Legionellaceae"
] | [
21
] | 1 | [] | [] | 0 | true | Domain | Phosphocholine transferase AnkX, insertion domain | Phosphocholine transferase AnkX, insertion domain | AnkX_ins | 1 |
IPR054038 | 54,038 | AP205 coat protein | AP205_coat | Domain | 6 | false | false | AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence that is not similar to any other known single-stranded RNA phage protein. The AP205 coat protein forms a dimer which adopts the conserved Leviviridae coat protein core fold with the exception of the N-terminal region. This coat protein has a ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22169"
] | [
"AP205_coat"
] | [
6
] | 1 | [] | [] | [] | 0 | [
"5fs4",
"5jzr",
"5lqp",
"6yfs",
"8toc",
"8tw2",
"8twc"
] | 7 | [
"PUB00153816",
"PUB00153817"
] | [
"27591890",
"27489348"
] | [
"Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.",
"Structure of fully protonated proteins by proton-detected magic-angle spinning NMR."
] | [
2016,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Norzivirales"
] | [
6
] | 1 | [] | [] | 0 | true | Domain | AP205 coat protein | AP205 coat protein | AP205_coat | 7 |
IPR054040 | 54,040 | ArnR1-like, winged-helix domain | WHD_ArnR1 | Domain | 878 | false | false | This entry represents a WH-like domain present in ArnR1-like putative DNA binding protein. ArnR1-like transcription factors have been implicated in regulating the expression of components found in both the archaeal adhesive pilus and UV-inducible pili systems [ , ]. This domain is also found in many uncharacterised bac... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22166"
] | [
"WHD_ArnR1"
] | [
878
] | 1 | [] | [] | [] | 0 | [
"2pg4"
] | 1 | [
"PUB00088324",
"PUB00153824"
] | [
"23461567",
"30828487"
] | [
"The one-component system ArnR: a membrane-bound activator of the crenarchaeal archaellum.",
"Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in <i>Sulfolobus acidocaldarius</i>."
] | [
2013,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
11,
863,
4
] | 3 | [] | [] | 0 | true | Domain | ArnR1-like, winged-helix domain | ArnR1-like, winged-helix domain | WHD_ArnR1 | 9 |
IPR054041 | 54,041 | SSO1393-like, winged-helix domain | WHD_SSO1393 | Domain | 16 | false | false | This entry represents a winged-helix (WH)-like domain found in CRISPR system ring nuclease SSO1393 from Sulfolobus solfataricus ( ) and similar archaeal sequences. This protein has been described as a component of the CRISPR system [ ]. SSO1393 has been described as a component of the CRISPR system [ ]. CRISPR (cluster... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22165"
] | [
"WHD_SSO1393"
] | [
16
] | 1 | [] | [] | [] | 0 | [
"3qyf",
"7pq2",
"7pq3",
"7pq6",
"7pqa"
] | 5 | [
"PUB00091682",
"PUB00154244"
] | [
"30232454",
"30444997"
] | [
"Ring nucleases deactivate type III CRISPR ribonucleases by degrading cyclic oligoadenylate.",
"If You'd Like to Stop a Type III CRISPR Ribonuclease, Then You Should Put a Ring (Nuclease) on It."
] | [
2018,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
16
] | 1 | [] | [] | 0 | true | Domain | SSO1393-like, winged-helix domain | SSO1393-like, winged-helix domain | WHD_SSO1393 | 4 |
IPR054042 | 54,042 | Dark, winged-helix domain | WHD_Dark | Domain | 54 | false | false | This entry represents the winged-helix (WH)-like found in Apaf-1/CED-4-related caspase activator Dapaf-1S from Drosophila melanogaster (Dark) and similar Dark (Drosophila Apaf-1-related killer) proteins from insects. Dark protein is part of the apoptosome complex and plays a key role in procaspases activation and apopt... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22164"
] | [
"WHD_Dark"
] | [
54
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-111458",
"R-DME-111459",
"R-DME-6798695",
"R-DME-9627069"
] | [
"REACTOME:R-DME-111458",
"REACTOME:R-DME-111459",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-9627069"
] | 4 | [
"3j9k",
"3j9l",
"4v4l",
"5jul",
"8y6p",
"8y6q"
] | 6 | [
"PUB00153900",
"PUB00153901"
] | [
"21220123",
"27916517"
] | [
"Structure of the Drosophila apoptosome at 6.9 a resolution.",
"A Near-Atomic Structure of the Dark Apoptosome Provides Insight into Assembly and Activation."
] | [
2011,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Diptera"
] | [
54
] | 1 | [
"Drosophila melanogaster"
] | [
3
] | 1 | true | Domain | Dark, winged-helix domain | Dark, winged-helix domain | WHD_Dark | 8 |
IPR054043 | 54,043 | Cell invasion protein SipA, C-terminal actin binding domain | SipA_C | Domain | 730 | false | false | This domain is found at the C-terminal end of Cell invasion protein SipA (Salmonella Invasion protein A) from Salmonella typhimurium. SipA actin-binding protein that interferes with host cell actin cytoskeleton, and reduce the critical concentration for the formation of F-actin, contributing to bacterial invasion. This... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22163"
] | [
"SipA_2nd"
] | [
730
] | 1 | [] | [] | [] | 0 | [
"1q5z",
"8c4c",
"8c4e",
"8uee",
"8vfm"
] | 5 | [
"PUB00030139",
"PUB00035463"
] | [
"14512630",
"16507363"
] | [
"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms.",
"A common structural motif in the binding of virulence factors to bacterial secretion chaperones."
] | [
2003,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
730
] | 1 | [] | [] | 0 | true | Domain | Cell invasion protein SipA, C-terminal actin binding domain | Cell invasion protein SipA, C-terminal actin binding domain | SipA_C | 8 |
IPR054044 | 54,044 | Plasmid Fertility inhibition factor | PFIN | Family | 431 | false | false | FiwA-like proteins are fertility inhibition factors (FIN), which are employed by plasmids to block import of rival plasmids [ , ]. FiwA is encoded by plasmid RP1 and blocks the transfer of plasmid R388 [ ]. A FiwA-like protein called Osa (oncogenic suppressive activity) inhibits the oncogenic properties of Agrobacteriu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22162"
] | [
"PFIN"
] | [
431
] | 1 | [] | [] | [] | 0 | [
"4o7k",
"4ovb"
] | 2 | [
"PUB00085711",
"PUB00085712",
"PUB00085713",
"PUB00085714",
"PUB00085716",
"PUB00154164"
] | [
"25358815",
"15489437",
"1832152",
"2559940",
"16194240",
"9864329"
] | [
"Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids.",
"Osa protein constitutes a strong oncogenic suppression system that can block vir-dependent transfer of IncQ plasmids between Agrobacterium cells and the establishment of IncQ plasmids in plant cells.",
... | [
2014,
2004,
1991,
1989,
2005,
1999
] | 6 | [] | [
"IPR035615"
] | 0 | 1 | 0 | [
"Bacteria",
"Birmingham IncP-alpha plasmid",
"Eukaryota"
] | [
428,
1,
2
] | 3 | [] | [] | 0 | true | Family | Plasmid Fertility inhibition factor | Plasmid Fertility inhibition factor | PFIN | 1 |
IPR054045 | 54,045 | Mre11, C-terminal domain | Mre11_C | Domain | 5 | false | false | This entry represents the helix-turn-helix domain of Mre11 from Thermotoga maritima and similar proteins [ ]. Mre11, together with Rad50, form the MR protein complex involved in DNA double-strand break repair [ , ]. This domain binds Rad50 and attaches flexibly to the nuclease domain which allows large conformational c... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22161"
] | [
"Mre11_C_bact"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"3qf7",
"3qg5",
"3tho",
"4w9m"
] | 4 | [
"PUB00055796",
"PUB00154076"
] | [
"21458667",
"20122942"
] | [
"The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair.",
"Crystal structure of the first eubacterial Mre11 nuclease reveals novel features that may discriminate substrates during DNA repair."
] | [
2011,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Thermotoga"
] | [
5
] | 1 | [] | [] | 0 | true | Domain | Mre11, C-terminal domain | Mre11, C-terminal domain | Mre11_C | 3 |
IPR054046 | 54,046 | Gycoside hydrolase/deacetylase, C-terminal domain | Gyco_hydrolase/deacetylase_C | Domain | 45 | false | false | This entry represents the C-terminal domain of a group of predicted glycoside hydrolase/deacetylases from Thermococcales. This enzyme is predicted to have two domains: an N-terminal domain with a typical glycoside hydrolase 57 family (β/α)7-barrel fold ( ) and a C-terminal domain mainly composed of α-helical bundles. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22160"
] | [
"PSMA-like_C"
] | [
45
] | 1 | [] | [] | [] | 0 | [
"4cmr"
] | 1 | [
"PUB00154184",
"PUB00154185"
] | [
"24914977",
"23884203"
] | [
"Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04.",
"Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04."
] | [
2014,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Sumerlaea chitinivorans",
"Thermococcaceae"
] | [
1,
44
] | 2 | [] | [] | 0 | true | Domain | Gycoside hydrolase/deacetylase, C-terminal domain | Gycoside hydrolase/deacetylase, C-terminal domain | Gyco_hydrolase/deacetylase_C | 7 |
IPR054047 | 54,047 | Gycoside hydrolase/deacetylase, N-terminal domain | Gyco_hydrolase/deacetylase_N | Domain | 45 | false | false | This entry represents the N-terminal domain of a group of predicted glycoside hydrolase/deacetylases from Thermococcales. This enzyme is predicted to have two domains: an N-terminal domain with a typical glycoside hydrolase 57 family (β/α)7-barrel fold (this entry) and a C-terminal domain composed of α-helical bundles ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22159"
] | [
"PSMA-like_N"
] | [
45
] | 1 | [] | [] | [] | 0 | [
"4cmr"
] | 1 | [
"PUB00154184",
"PUB00154185"
] | [
"24914977",
"23884203"
] | [
"Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04.",
"Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04."
] | [
2014,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Sumerlaea chitinivorans",
"Thermococcaceae"
] | [
1,
44
] | 2 | [] | [] | 0 | true | Domain | Gycoside hydrolase/deacetylase, N-terminal domain | Gycoside hydrolase/deacetylase, N-terminal domain | Gyco_hydrolase/deacetylase_N | 6 |
IPR054048 | 54,048 | M152, N-terminal domain | M152_N | Domain | 86 | false | false | This domain is found at the N-terminal of M152 from Murid herpesvirus 1 ( ), a glycoprotein that shows structural similarity to m153 and m157 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22158"
] | [
"M157_N_1"
] | [
86
] | 1 | [] | [] | [] | 0 | [
"2o5n",
"4g59"
] | 2 | [
"PUB00064063",
"PUB00154052"
] | [
"23169621",
"17897947"
] | [
"Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1γ reveals a paradigm for MHC/MHC interaction in immune evasion.",
"Cellular expression and crystal structure of the murine cytomegalovirus major histocompatibility complex class I-like glycoprotein, m153."
] | [
2012,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Muromegalovirus"
] | [
86
] | 1 | [] | [] | 0 | true | Domain | M152, N-terminal domain | M152, N-terminal domain | M152_N | 2 |
IPR054049 | 54,049 | Sucrose hydrolase-like, C-terminal domain | SupH-like_C | Domain | 1,647 | false | false | This domain is found at the C-terminal end of Sucrose hydrolase from Xanthomonas campestris (SupH, ) and similar bacterial sequences. SupH shows a central domain that consists of an eight-stranded α/β barrel ( ). This β-stranded domain is located on a side of the barrel fold [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22157"
] | [
"SupH-like_C"
] | [
1647
] | 1 | [] | [] | [] | 0 | [
"2wpg",
"3cze",
"3czg",
"3czk",
"3czl"
] | 5 | [
"PUB00128509"
] | [
"19966417"
] | [
"The apo structure of sucrose hydrolase from Xanthomonas campestris pv. campestris shows an open active-site groove."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteriales",
"metagenomes"
] | [
1637,
6,
4
] | 3 | [] | [] | 0 | true | Domain | Sucrose hydrolase-like, C-terminal domain | Sucrose hydrolase-like, C-terminal domain | SupH-like_C | 8 |
IPR054051 | 54,051 | Mucin-20 repeat | MUC-20_rpt | Repeat | 60 | false | false | This entry represents a short repeat found in human Mucin-20 (MUC-20) and similar sequences from primates. MUC-20 may regulate the MET signalling cascade and seems to decrease the hepatocyte growth factor (HGF)-induced transient MAPK activation [ ]. This repeat is predicted to form a β-solenoid structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21824"
] | [
"MUC20"
] | [
60
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5083625",
"R-HSA-5083632",
"R-HSA-5083636",
"R-HSA-5621480",
"R-HSA-8851805",
"R-HSA-913709",
"R-HSA-977068"
] | [
"REACTOME:R-HSA-5083625",
"REACTOME:R-HSA-5083632",
"REACTOME:R-HSA-5083636",
"REACTOME:R-HSA-5621480",
"REACTOME:R-HSA-8851805",
"REACTOME:R-HSA-913709",
"REACTOME:R-HSA-977068"
] | 7 | [] | 0 | [
"PUB00052449"
] | [
"15314156"
] | [
"MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by binding to a multifunctional docking site of met."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Euteleostomi"
] | [
60
] | 1 | [
"Homo sapiens"
] | [
16
] | 1 | true | Repeat | Mucin-20 repeat | Mucin-20 repeat | MUC-20_rpt | 7 |
IPR054052 | 54,052 | Y16Q-like | Y16Q-like | Family | 875 | false | false | This entry represents a family of proteins that are present in crAss phage such as , including Uncharacterized 7.5 kDa protein in denB-rIIB intergenic region from Enterobacteria phage T4. AlphaFold predicts these short proteins to adopt an α helical hairpin structure. These proteins bind the immune signalling molecule ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21825"
] | [
"Sequestin"
] | [
875
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00156031",
"PUB00156032",
"PUB00162462"
] | [
"36174646",
"39478223",
"39083849"
] | [
"Viruses inhibit TIR gcADPR signalling to overcome bacterial defence.",
"Single phage proteins sequester signals from TIR and cGAS-like enzymes.",
"Nucleotide Immune Signaling in CBASS, Pycsar, Thoeris, and CRISPR Antiphage Defense."
] | [
2022,
2024,
2024
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
479,
3,
383,
10
] | 4 | [] | [] | 0 | true | Family | Y16Q-like | Y16Q-like | Y16Q-like | 8 |
IPR054053 | 54,053 | Protein of unknown function DUF6887 | DUF6887 | Family | 825 | false | false | This entry represents a family of uncharacterised cyanobacterial proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21826"
] | [
"DUF6887"
] | [
825
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Natrinema hispanicum"
] | [
824,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF6887 | Protein of unknown function DUF6887 | DUF6887 | 8 |
IPR054054 | 54,054 | New-glue 1-3-like | Ng_1-3-like | Family | 370 | false | false | This entry represents new glue proteins which are mucin-like proteins found mainly in arthropods. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21827"
] | [
"New_glue"
] | [
370
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154101"
] | [
"36005360"
] | [
"Drosophila Glue: A Promising Model for Bioadhesion."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"hydrothermal vent metagenome"
] | [
32,
335,
2,
1
] | 4 | [
"Drosophila melanogaster"
] | [
27
] | 1 | true | Family | New-glue 1-3-like | New-glue 1-3-like | Ng_1-3-like | 9 |
IPR054055 | 54,055 | YpzH protein family | YpzH | Family | 1,029 | false | false | This entry contains a family of small protein of unknown function. Proteins in this family are found in Firmicutes. These proteins adopt a β-sheet structure with four strands with an α-helix packed on one face between the second and third strands. Using AlphaFold we can identify a likely hexameric ring complex. Additio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21835"
] | [
"YIEGIA_cap"
] | [
1029
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota",
"ecological metagenomes"
] | [
1018,
11
] | 2 | [] | [] | 0 | true | Family | YpzH protein family | YpzH protein family | YpzH | 7 |
IPR054056 | 54,056 | ESX-1 secretion-associated protein EspB, PPE domain | EspB_PPE | Domain | 297 | false | false | This entry represents the PPE domain of ESX-1 secretion-associated protein EspB, a member of the PE/PPE family and the only one described to date to form higher-order oligomers [ , , ]. It contains PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21856"
] | [
"EspB_PPE"
] | [
297
] | 1 | [] | [] | [] | 0 | [
"3j83",
"4wj1",
"4wj2",
"4xwp",
"4xxn",
"4xxx",
"4xy3",
"6xzc",
"7p0z",
"7p13",
"8ako"
] | 11 | [
"PUB00103932",
"PUB00103933",
"PUB00103934"
] | [
"32875288",
"34337436",
"36463964"
] | [
"High resolution CryoEM structure of the ring-shaped virulence factor EspB from <i>Mycobacterium tuberculosis</i>.",
"Priming mycobacterial ESX-secreted protein B to form a channel-like structure.",
"The crystal structure of the EspB-EspK virulence factor-chaperone complex suggests an additional type VII secret... | [
2020,
2021,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Mycobacteriales"
] | [
297
] | 1 | [] | [] | 0 | true | Domain | ESX-1 secretion-associated protein EspB, PPE domain | ESX-1 secretion-associated protein EspB, PPE domain | EspB_PPE | 2 |
IPR054057 | 54,057 | Campylobacter invasion antigen D, C-terminal | CiaD_C | Domain | 325 | false | false | This entry represents the C-terminal domain of Campylobacter invasion antigen D from Campylobacter jejuni (CiaD) and similar sequences mainly found in Campylobacterales. C. jejuni utilizes a cell binding and effector delivery mechanism to invade host cells. The Cia proteins (effectors) are exported from the bacterium's... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21862"
] | [
"CiaD"
] | [
325
] | 1 | [] | [] | [] | 0 | [
"8swd",
"8uz8"
] | 2 | [
"PUB00153870"
] | [
"36671522"
] | [
"The Missing Pieces: The Role of Secretion Systems in <i>Campylobacter jejuni</i> Virulence."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Epsilonproteobacteria",
"hydrothermal vent metagenome"
] | [
317,
8
] | 2 | [] | [] | 0 | true | Domain | Campylobacter invasion antigen D, C-terminal | Campylobacter invasion antigen D, C-terminal | CiaD_C | 5 |
IPR054059 | 54,059 | MORF/ORRM1/DAG-like, MORF domain | MORF/ORRM1/DAG-like_MORF | Domain | 5,165 | false | false | This domain is found in Multiple organellar RNA editing factor 1 (MORF1) and ORRM1 from Arabidopsis thaliana, DAG protein from Antirrhinum majus, and similar proteins from plants involved in organellar RNA editing in mitochondria. This conserved domain, termed MORF domain, plays a role in the multimerization of MORF pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21864"
] | [
"MORF_dom"
] | [
5165
] | 1 | [] | [] | [] | 0 | [
"5gi0",
"5iwb",
"5iww",
"5mpw",
"5mpx",
"5mpy",
"5ydg"
] | 7 | [
"PUB00089297",
"PUB00153873",
"PUB00154073",
"PUB00154074"
] | [
"22411807",
"28394309",
"28201607",
"29229384"
] | [
"Multiple organellar RNA editing factor (MORF) family proteins are required for RNA editing in mitochondria and plastids of plants.",
"MORF9 increases the RNA-binding activity of PLS-type pentatricopeptide repeat protein in plastid RNA editing.",
"Crystal structures of the Arabidopsis thaliana organellar RNA ed... | [
2012,
2017,
2017,
2018
] | 4 | [] | [] | 0 | 0 | null | [
"Spermatophyta"
] | [
5165
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
46,
21,
39
] | 3 | true | Domain | MORF/ORRM1/DAG-like, MORF domain | MORF/ORRM1/DAG-like, MORF domain | MORF/ORRM1/DAG-like_MORF | 1 |
IPR054060 | 54,060 | Talin 1-like, rod-segment domain | TLN1-like_RS | Domain | 5,176 | false | false | This domain is found repeated in human Talin-1 (TLN1) and similar proteins mainly from animals. Talin is an essential component in focal adhesions (FAs), intracellular protein assemblies that serve as tension-sensing anchoring points to link cells to the extracellular environment [ , , ]. This protein plays a key regul... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21865"
] | [
"TLN1-like_RS"
] | [
5176
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-DDI-114608",
"R-HSA-114608",
"R-HSA-354192",
"R-HSA-354194",
"R-HSA-372708",
"R-HSA-381038",
"R-HSA-399955",
"R-HSA-445355",
"R-HSA-5674135",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955",
"R-HSA-9649948",
"R-HSA-9656223",
"R-HSA-9856530",
"R-MMU-114608",
"R... | [
"REACTOME:R-DDI-114608",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-354192",
"REACTOME:R-HSA-354194",
"REACTOME:R-HSA-372708",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-399955",
"REACTOME:R-HSA-445355",
"REACTOME:R-HSA-5674135",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802948",
"REACTOME:R-HSA-... | 23 | [
"2kbb",
"2kgx",
"2l10",
"3dyj",
"3fyq",
"4f7g",
"5ic0",
"5ic1",
"6r9t",
"8vdo",
"8vdp",
"8vdq",
"8vdr",
"9qn7"
] | 14 | [
"PUB00048304",
"PUB00066006",
"PUB00093617",
"PUB00154285",
"PUB00154286"
] | [
"19297334",
"23389036",
"20610383",
"31539492",
"25520155"
] | [
"The structure of an interdomain complex that regulates talin activity.",
"RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover.",
"Central region of talin has a unique fold that binds vinculin and actin.",
"The Architecture of Talin1 Reveals an Autoinhibition ... | [
2009,
2013,
2010,
2019,
2014
] | 5 | [] | [
"IPR037438"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
5176
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
17,
6,
7,
14,
15
] | 6 | true | Domain | Talin 1-like, rod-segment domain | Talin 1-like, rod-segment domain | TLN1-like_RS | 6 |
IPR054061 | 54,061 | Domain of unknown function DUF6915 | DUF6915 | Domain | 757 | false | false | This family of proteins is primarily found mainly in proteobacteria. Proteins in this family are typically between 124 and 153 amino acids in length. Proteins in this family have several conserved histidine residues that may form zinc-binding sites. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21866"
] | [
"DUF6915"
] | [
757
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Blyttiomyces helicus",
"Caudoviricetes",
"ecological metagenomes"
] | [
704,
1,
44,
8
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6915 | Domain of unknown function DUF6915 | DUF6915 | 2 |
IPR054062 | 54,062 | Virion DNA-directed RNA polymerase domain 2 | vRNAP_dom2 | Domain | 148 | false | false | This domain is found in Virion DNA-directed RNA polymerase from Bacteriophage N4 (vRNAP), which is injected into the host upon infection and transcribes the phage early genes from promoters that have a 5-bp stem-3 nt loop hairpin structure. This entry represents a region located C-terminal to the mini-vRNAP, which poss... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21867"
] | [
"vRNAP_dom_2"
] | [
148
] | 1 | [] | [] | [] | 0 | [
"2po4",
"3c2p",
"3c3l",
"3c46",
"3q0a",
"3q22",
"3q23",
"3q24",
"4ff1",
"4ff2",
"4ff3",
"4ff4"
] | 12 | [
"PUB00048738",
"PUB00050871",
"PUB00055751"
] | [
"18362338",
"19061645",
"21321236"
] | [
"X-ray crystal structure of the polymerase domain of the bacteriophage N4 virion RNA polymerase.",
"Structural basis for DNA-hairpin promoter recognition by the bacteriophage N4 virion RNA polymerase.",
"X-ray crystal structures elucidate the nucleotidyl transfer reaction of transcript initiation using two nucl... | [
2008,
2008,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Lucilia cuprina",
"Pseudomonadati",
"Viruses",
"marine metagenome"
] | [
1,
9,
137,
1
] | 4 | [] | [] | 0 | true | Domain | Virion DNA-directed RNA polymerase domain 2 | Virion DNA-directed RNA polymerase domain 2 | vRNAP_dom2 | 8 |
IPR054063 | 54,063 | GlcNAc-binding protein A, third domain | GbpA_D3 | Domain | 912 | false | false | This entry represents the third domain D3 of GlcNAc-binding protein A from Vibrio cholerae (GbpA), which is thought to promote attachment to both epithelial cell surfaces and marine chitin. GbpA contains four domains. D3 binds to the surface of the bacteria. It shows distant structural similarity to bacterial surface p... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21868"
] | [
"GbpA_D3"
] | [
912
] | 1 | [] | [] | [] | 0 | [
"2xwx",
"8gul",
"8gum"
] | 3 | [
"PUB00091406"
] | [
"22253590"
] | [
"The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Anopheles melas",
"Bacteria"
] | [
1,
911
] | 2 | [] | [] | 0 | true | Domain | GlcNAc-binding protein A, third domain | GlcNAc-binding protein A, third domain | GbpA_D3 | 3 |
IPR054064 | 54,064 | Distal tail component, second carbohydrate binding domain | Dit-like_CBM2 | Domain | 76 | false | false | This entry represents the second putative carbohydrate binding domain (CBM2) of the distal tail component from Lactobacillus phage J-1 ( , Dit), which is involved in host recognition. This domain folds into a β-sandwich with two β-sheets gathering 12 β-strands [ ]. It usually appears associated to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21869"
] | [
"Dit-like_CBM2"
] | [
76
] | 1 | [] | [] | [] | 0 | [
"5ly8"
] | 1 | [
"PUB00153908"
] | [
"28196397"
] | [
"Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Caudoviricetes",
"Lactobacillales"
] | [
37,
39
] | 2 | [] | [] | 0 | true | Domain | Distal tail component, second carbohydrate binding domain | Distal tail component, second carbohydrate binding domain | Dit-like_CBM2 | 6 |
IPR054066 | 54,066 | SAM domain-like | SAM_5 | Domain | 2 | false | false | This entry corresponds to the most N-terminal SAM domain found in topoisomerase V proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21872"
] | [
"SAM_5"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"2csb",
"2csd",
"3m6k",
"3m6z",
"3m7d",
"4gfj",
"5hm5",
"8df7",
"8df8",
"8df9",
"8dfb"
] | 11 | [
"PUB00040090",
"PUB00055625",
"PUB00064037",
"PUB00151856"
] | [
"16395333",
"20637419",
"23125368",
"26908655"
] | [
"Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases.",
"Structures of minimal catalytic fragments of topoisomerase V reveals conformational changes relevant for DNA binding.",
"Identification of one of the apurinic/apyrimidinic lyase active sites of topoisomerase V by... | [
2006,
2010,
2013,
2016
] | 4 | [] | [] | 0 | 0 | null | [
"Methanopyrus kandleri"
] | [
2
] | 1 | [] | [] | 0 | true | Domain | SAM domain-like | SAM domain-like | SAM_5 | 1 |
IPR054067 | 54,067 | SSO1120-like, N-terminal thioredoxin-like domain | SSO1120-like_N | Domain | 48 | false | false | This entry represents a thioredoxin domain found at the N-terminal of a group of archaeal proteins, including the protein disulfide oxidoreductase (PDO) SSO1120 from the hyperthermophilic archaeon Sulfolobus solfataricus ( ). This domain, a non-canonical thioredoxin fold, is composed of four β-strands and three α-helic... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21873"
] | [
"Thioredoxin_17"
] | [
48
] | 1 | [] | [] | [] | 0 | [
"4mnn"
] | 1 | [
"PUB00154282"
] | [
"24306780"
] | [
"Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
48
] | 1 | [] | [] | 0 | true | Domain | SSO1120-like, N-terminal thioredoxin-like domain | SSO1120-like, N-terminal thioredoxin-like domain | SSO1120-like_N | 8 |
IPR054068 | 54,068 | CofJ | CofJ | Family | 8 | false | false | This entry represents CofJ from Escherichia coli ( ) and similar sequences from Enterobacterales. CofJ is a soluble protein secreted via the CFA/III apparatus in Enterotoxigenic Escherichia coli (ETEC), which colonize the human gut causing severe diarrhoea. CofJ is a single-domain protein of 326 residues, comprised of ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21874"
] | [
"CofJ"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"4ijy",
"5yq0"
] | 2 | [
"PUB00153879",
"PUB00154417"
] | [
"24106767",
"29941571"
] | [
"Structure and secretion of CofJ, a putative colonization factor of enterotoxigenic Escherichia coli.",
"Interplay of a secreted protein with type IVb pilus for efficient enterotoxigenic <i>Escherichia coli</i> colonization."
] | [
2013,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Enterobacteriaceae"
] | [
8
] | 1 | [] | [] | 0 | true | Family | CofJ | CofJ | CofJ | 4 |
IPR054069 | 54,069 | Calpain-3/13-like, C-terminal EF-hand | CAPN3/13-like_C_EFh | Domain | 2,379 | false | false | This domain is found at the C-terminal end of human Calpain-13 (CAPN13) , Calpain-3 (CAPN3) and similar sequences from vertebrates. CAPN13 is thought to be a non-lysosomal thiol-protease. CAPN3 is a calcium-regulated non-lysosomal thiol-protease that cleaves proteolytically CTBP1 at 'His-409'. It mediates, with UTP25, ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21875"
] | [
"CAPN13-like_C_EFh"
] | [
2379
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.22.54",
"R-HSA-1474228",
"R-MMU-1474228",
"R-RNO-1474228"
] | [
"EC:3.4.22.54",
"REACTOME:R-HSA-1474228",
"REACTOME:R-MMU-1474228",
"REACTOME:R-RNO-1474228"
] | 4 | [
"2i7a",
"4okh"
] | 2 | [
"PUB00018210",
"PUB00023348",
"PUB00023370",
"PUB00026718",
"PUB00029174",
"PUB00097921",
"PUB00097922",
"PUB00137014"
] | [
"10601010",
"9228945",
"9228946",
"10639123",
"14579356",
"27657329",
"23357851",
"24846670"
] | [
"Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.",
"Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes.",
"Crystal structure of calcium bound domain VI of calpain a... | [
1999,
1997,
1997,
2000,
2003,
2016,
2013,
2014
] | 8 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
2379
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
22,
15,
13
] | 4 | true | Domain | Calpain-3/13-like, C-terminal EF-hand | Calpain-3/13-like, C-terminal EF-hand | CAPN3/13-like_C_EFh | 5 |
IPR054071 | 54,071 | Neurofibromin, PH domain-like | PH_NF1 | Domain | 3,141 | false | false | This entry represents the pleckstrin homology (PH)-like domain of neurofibromin (NF1) and similar sequences from animals and fungi. Neurofibromin is a Ras-specific GTPase-activating protein (RasGAP). Mutations in the gene encoding this protein cause neurofibromatosis type 1 (NF1). This domain forms a bipartite module w... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21877"
] | [
"PH_NF1"
] | [
3141
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5658442",
"R-HSA-6802953",
"R-MMU-5658442",
"R-RNO-5658442"
] | [
"REACTOME:R-HSA-5658442",
"REACTOME:R-HSA-6802953",
"REACTOME:R-MMU-5658442",
"REACTOME:R-RNO-5658442"
] | 4 | [
"2d4q",
"2e2x",
"3p7z",
"3peg",
"3pg7",
"7moc",
"7mp5",
"7mp6",
"7pgp",
"7pgq",
"7pgr",
"7pgs",
"7pgt",
"7pgu",
"7r03",
"7r04",
"8e20",
"8edl",
"8edm",
"8edn",
"8edo"
] | 21 | [
"PUB00040189",
"PUB00047322",
"PUB00113159",
"PUB00154167"
] | [
"16397625",
"17187824",
"21089070",
"34707296"
] | [
"A novel bipartite phospholipid-binding module in the neurofibromatosis type 1 protein.",
"The sec14 homology module of neurofibromin binds cellular glycerophospholipids: mass spectrometry and structure of a lipid complex.",
"Structural and biochemical consequences of NF1 associated nontruncating mutations in t... | [
2006,
2007,
2011,
2021
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3141
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
8,
5,
2,
7
] | 5 | true | Domain | Neurofibromin, PH domain-like | Neurofibromin, PH domain-like | PH_NF1 | 7 |
IPR054072 | 54,072 | C381 turret protein, N-terminal | C381_turret_N | Domain | 2 | false | false | This entry represents the N-terminal jelly roll domain of the Sulfolobus turreted icosahedral virus (STIV) turret protein. The C381 turret protein is a component of the STIV virion vertex complex, which orchestrates virion assembly by coordinating interactions of the membrane and various protein components involved. Th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21878"
] | [
"STIV_turret_1st"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"3j31",
"4ind"
] | 2 | [
"PUB00154247"
] | [
"23520050"
] | [
"Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobus acidocaldarius",
"Sulfolobus turreted icosahedral virus 1"
] | [
1,
1
] | 2 | [] | [] | 0 | true | Domain | C381 turret protein, N-terminal | C381 turret protein, N-terminal | C381_turret_N | 4 |
IPR054073 | 54,073 | C381 turret protein, C-terminal | C381_turret_C | Domain | 2 | false | false | This entry represents the C-termina jelly roll domain of the Sulfolobus turreted icosahedral virus (STIV) turret protein. The C381 turret protein is a component of the STIV virion vertex complex, which orchestrates virion assembly by coordinating interactions of the membrane and various protein components involved. The... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21879"
] | [
"STIV_turret_3rd"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"3j31",
"4ind"
] | 2 | [
"PUB00154247"
] | [
"23520050"
] | [
"Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobus acidocaldarius",
"Sulfolobus turreted icosahedral virus 1"
] | [
1,
1
] | 2 | [] | [] | 0 | true | Domain | C381 turret protein, C-terminal | C381 turret protein, C-terminal | C381_turret_C | 2 |
IPR054074 | 54,074 | A223 penton protein, C-terminal | A223_penton_C | Domain | 2 | false | false | This entry represents the C-terminal second jelly roll domain of the Sulfolobus turreted icosahedral virus (STIV) penton protein ( , ). STIV is a virus that infects the archaeon Sulfolobus solfataricus and was isolated in acidic hot springs. The virus has a unique architecture based on a pseudo T = 31d capsid symmetry ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21881"
] | [
"STIV_penton_2nd"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"3j31",
"4il7",
"6bo3"
] | 3 | [
"PUB00154247"
] | [
"23520050"
] | [
"Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobus acidocaldarius",
"Sulfolobus turreted icosahedral virus 1"
] | [
1,
1
] | 2 | [] | [] | 0 | true | Domain | A223 penton protein, C-terminal | A223 penton protein, C-terminal | A223_penton_C | 1 |
IPR054075 | 54,075 | Putative tail fiber protein gp53-like, C-terminal | Gp53-like_C | Domain | 3,018 | false | false | This entry represents a domain found at the C-terminal end of putative tail fiber protein gp53 from Acinetobacter phage AP22 ( , , gp53) and similar uncharacterised sequences from tailed bacteriophages and prophages mainly found in proteobacteria. It shows structural similarities to other phage/virus host cell-binding ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21882"
] | [
"Gp53-like_C"
] | [
3018
] | 1 | [] | [] | [] | 0 | [
"4mtm",
"6cl5",
"6cl6",
"6ct8",
"6cu2",
"6cxb"
] | 6 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)",
"Viruses",
"metagenomes"
] | [
2799,
21,
1,
175,
22
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Putative tail fiber protein gp53-like, C-terminal | Putative tail fiber protein gp53-like, C-terminal | Gp53-like_C | 4 |
IPR054076 | 54,076 | Zuotin-like, zuotin homology domain | ZUO1-like_ZHD | Domain | 9,378 | false | false | This domain is found in Zuotin from Saccharomyces cerevisiae (ZUO1) and in similar eukaryotic sequences. ZUO1 is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in the regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21884"
] | [
"ZUO1-like_ZHD"
] | [
9378
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-3371453",
"R-DRE-3371453",
"R-HSA-3371453",
"R-MMU-3371453",
"R-RNO-3371453",
"R-SCE-3371453",
"R-SPO-3371453",
"R-XTR-3371453"
] | [
"REACTOME:R-BTA-3371453",
"REACTOME:R-DRE-3371453",
"REACTOME:R-HSA-3371453",
"REACTOME:R-MMU-3371453",
"REACTOME:R-RNO-3371453",
"REACTOME:R-SCE-3371453",
"REACTOME:R-SPO-3371453",
"REACTOME:R-XTR-3371453"
] | 8 | [
"5dje",
"7x3k",
"7z3n",
"7z3o"
] | 4 | [
"PUB00096580"
] | [
"27669034"
] | [
"Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9378
] | 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... | [
10,
2,
2,
3,
8,
8,
3,
4,
13,
2,
2,
19
] | 12 | true | Domain | Zuotin-like, zuotin homology domain | Zuotin-like, zuotin homology domain | ZUO1-like_ZHD | 7 |
IPR054077 | 54,077 | TMEM181, GOLD domain | TMEM181_GOLD | Domain | 1,569 | false | false | This is the N-terminal domain of TMEM181, also known as a Golgi-dynamics (GOLD) domain [ ]. TMEM181 mediates action of cytolethal distending toxins (CDT), which are secreted by many pathogenic bacteria [ ]. It is homologous to GPR180, TMEM145, and WLS which, together with TMEM87A/B, GPR107 and GPR108, they have been gr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21885"
] | [
"TMEM181_GOLD"
] | [
1569
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00090927",
"PUB00151072"
] | [
"19965467",
"36373655"
] | [
"Haploid genetic screens in human cells identify host factors used by pathogens.",
"Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A."
] | [
2009,
2022
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1569
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
9,
5,
7
] | 5 | true | Domain | TMEM181, GOLD domain | TMEM181, GOLD domain | TMEM181_GOLD | 9 |
IPR054078 | 54,078 | BRF2-like, C-terminal | BRF2-like_C | Domain | 1,207 | false | false | This domain is found in human Transcription factor IIIB 50 kDa subunit (BRF2) and similar sequences mainly found in eukaryotes. BRF2 is a general activator of RNA polymerase III transcription. This protein consists of an N-terminal zinc ribbon ( ), a core domain consisting of two cyclin fold imperfect repeats and a C-t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21886"
] | [
"BRF2-like_C_cyclin_rpt"
] | [
1207
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-76071",
"R-HSA-749476",
"R-HSA-76071",
"R-MMU-76071",
"R-RNO-76071"
] | [
"REACTOME:R-BTA-76071",
"REACTOME:R-HSA-749476",
"REACTOME:R-HSA-76071",
"REACTOME:R-MMU-76071",
"REACTOME:R-RNO-76071"
] | 5 | [
"4roc",
"4rod",
"4roe",
"5n9g",
"8ity",
"8iue",
"8iuh",
"9fso",
"9fsp",
"9fsq",
"9fsr",
"9fss",
"9k2g",
"9k36",
"9k38",
"9k39",
"9k3b",
"9k3u",
"9k3v",
"9lkt",
"9lxn",
"9lxo"
] | 22 | [
"PUB00108581",
"PUB00153836",
"PUB00153837",
"PUB00154397"
] | [
"26638071",
"28743884",
"29345637",
"23713077"
] | [
"Redox Signaling by the RNA Polymerase III TFIIB-Related Factor Brf2.",
"Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation.",
"Structural basis of RNA polymerase III transcription initiation.",
"Pollen-expressed transcription factor 2 encodes a novel plant-specifi... | [
2015,
2017,
2018,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1207
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
2,
2,
4
] | 5 | true | Domain | BRF2-like, C-terminal | BRF2-like, C-terminal | BRF2-like_C | 9 |
IPR054079 | 54,079 | RhiE, branching domain | RhiE_branching_dom | Domain | 35 | false | false | This entry represents the branching domain of RhiE, part of a non-canonical polyketide synthase (PKS) module found in Mycetohabitans rhizoxinica ( , ), and in similar sequences from proteobacteria. Unlike typical PKS modules, RhiE catalyses a Michael-type acetyl addition to generate a branch in the carbon chain, expand... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21887"
] | [
"RhiE_B"
] | [
35
] | 1 | [] | [] | [] | 0 | [
"4kc5",
"8oii"
] | 2 | [
"PUB00153896"
] | [
"24048471"
] | [
"Vinylogous chain branching catalysed by a dedicated polyketide synthase module."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
35
] | 1 | [] | [] | 0 | true | Domain | RhiE, branching domain | RhiE, branching domain | RhiE_branching_dom | 7 |
IPR054080 | 54,080 | TPR1-like, CTLH-containing domain | TPR1-like_2nd | Domain | 6,159 | false | false | This domain is found in Protein TPR1 from Oryza sativa, also known as Topless-related protein 1/2, and in similar sequences predominantly found in plants and some fungal species. TPR1 is thought to be a downstream regulator of strigolactones signalling. This entry represents the second part of the N-terminal domain of ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21889"
] | [
"TPR1-like_2nd"
] | [
6159
] | 1 | [] | [] | [] | 0 | [
"4zhe",
"5c6q",
"5c6v",
"5c7e",
"5c7f",
"5j9k",
"5ja5",
"5jgc",
"5jhp",
"5nqs",
"5nqv"
] | 11 | [
"PUB00090272",
"PUB00138298",
"PUB00151950",
"PUB00151951",
"PUB00154294"
] | [
"28781166",
"26601214",
"28630893",
"28698367",
"31076555"
] | [
"Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.",
"Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors.",
"A D53 repression motif induces oligomerization of TOPLESS corepressors and promotes assembly of a corepressor-nucleos... | [
2017,
2015,
2017,
2017,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6159
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
35,
3,
78
] | 3 | true | Domain | TPR1-like, CTLH-containing domain | TPR1-like, CTLH-containing domain | TPR1-like_2nd | 1 |
IPR054082 | 54,082 | Talin, IBS2B domain | Talin_IBS2B | Domain | 6,337 | false | false | Talin is an adaptor protein that activates integrin family of cell adhesion molecules and couples them to the actin cytoskeleton. The integrin activation is known to involve binding of the Talin FERM domain to membrane proximal sequences in the cytoplasmic domain of the integrin beta-subunit. IBS2 is a second integrin-... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21896"
] | [
"Talin_IBS2B"
] | [
6337
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-DDI-114608",
"R-HSA-114608",
"R-HSA-354192",
"R-HSA-354194",
"R-HSA-372708",
"R-HSA-381038",
"R-HSA-399955",
"R-HSA-445355",
"R-HSA-5674135",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955",
"R-HSA-9649948",
"R-HSA-9656223",
"R-HSA-9856530",
"R-MMU-114608",
"R... | [
"REACTOME:R-DDI-114608",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-354192",
"REACTOME:R-HSA-354194",
"REACTOME:R-HSA-372708",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-399955",
"REACTOME:R-HSA-445355",
"REACTOME:R-HSA-5674135",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802948",
"REACTOME:R-HSA-... | 23 | [
"1sj8",
"2l7n",
"2x0c",
"3dyj",
"3s90",
"4w8p",
"5fzt",
"5ic0",
"5ic1",
"6r9t",
"6twn",
"6xz3",
"6xz4",
"7v1a",
"7zw4",
"8as9",
"8vdo",
"8vdp",
"8vdq",
"8vdr",
"9qn7"
] | 21 | [
"PUB00051543"
] | [
"19176533"
] | [
"Structural determinants of integrin binding to the talin rod."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6337
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
19,
6,
6,
17,
20
] | 6 | true | Domain | Talin, IBS2B domain | Talin, IBS2B domain | Talin_IBS2B | 2 |
IPR054083 | 54,083 | Sarcolamban A/B | SclA/B | Family | 8 | false | false | This entry represents Sarcolamban A and B from Drosophila melanogaster (SclA/B) and similar sequences from Drosophila species. SclA and SclB play an essential role in the regulation of calcium transport at the sarcoplasmic reticulum (SR), which is secondarily required for regular muscle contraction [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21898"
] | [
"Sarcolamban"
] | [
8
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00135473",
"PUB00143561",
"PUB00143562"
] | [
"23970561",
"24385504",
"27923914"
] | [
"Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames.",
"Small open reading frames pack a big punch in cardiac calcium regulation.",
"Widespread control of calcium signaling by a family of SERCA-inhibiting micropeptides."
] | [
2013,
2014,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Endopterygota"
] | [
8
] | 1 | [
"Drosophila melanogaster"
] | [
2
] | 1 | true | Family | Sarcolamban A/B | Sarcolamban A/B | SclA/B | 9 |
IPR054084 | 54,084 | Tarsal-less AA | Tal-AA | Family | 19 | false | false | This entry represents Peptide tarsal-less AA from Drosophila melanogaster and simal sequences from Drosophilidae. This protein is required in early stages of leg development for the intercalation of the tarsal segments during the mid-third instar stage and later for tarsal joint formation [ , , ]. It is one of four pep... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF21899",
"cd20258"
] | [
"Tal_Pri",
"Tal_Pri"
] | [
19,
16
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00089033",
"PUB00143925",
"PUB00143926",
"PUB00143927",
"PUB00143928",
"PUB00143929",
"PUB00143930",
"PUB00143931",
"PUB00154398"
] | [
"26383956",
"21527259",
"25344753",
"17486114",
"15809421",
"17439302",
"16901788",
"30896406",
"18801356"
] | [
"Pri sORF peptides induce selective proteasome-mediated protein processing.",
"Tarsal-less peptides control Notch signalling through the Shavenbaby transcription factor.",
"Pri peptides are mediators of ecdysone for the temporal control of development.",
"Small peptide regulators of actin-based cell morphogen... | [
2015,
2011,
2014,
2007,
2005,
2007,
2006,
2019,
2008
] | 9 | [] | [] | 0 | 0 | null | [
"Drosophilinae"
] | [
19
] | 1 | [
"Drosophila melanogaster"
] | [
2
] | 1 | true | Family | Tarsal-less AA | Tarsal-less AA | Tal-AA | 6 |
IPR054085 | 54,085 | Cep192-like, domain 1 | Cep192-like_D1 | Domain | 1,120 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22060"
] | [
"Cep192_D1"
] | [
1120
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [] | 0 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural and Functional Analy... | [
2008,
2014,
2014,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1120
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
9,
3,
4
] | 4 | true | Domain | Cep192-like, domain 1 | Cep192-like, domain 1 | Cep192-like_D1 | 3 |
IPR054086 | 54,086 | Cep192-like, domain 2 | Cep192-like_D2 | Domain | 1,218 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22064"
] | [
"Cep192_D2"
] | [
1218
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [] | 0 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural and Functional Analy... | [
2008,
2014,
2014,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1218
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
7,
3,
4
] | 4 | true | Domain | Cep192-like, domain 2 | Cep192-like, domain 2 | Cep192-like_D2 | 8 |
IPR054087 | 54,087 | Cep192-like, domain 7 | Cep192-like_D7 | Domain | 1,224 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22065"
] | [
"Cep192_D7"
] | [
1224
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [
"6fvi"
] | 1 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural and Functional Analy... | [
2008,
2014,
2014,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1224
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
8,
5,
3
] | 4 | true | Domain | Cep192-like, domain 7 | Cep192-like, domain 7 | Cep192-like_D7 | 9 |
IPR054088 | 54,088 | Cep192-like, domain 8 | Cep192-like_D8 | Domain | 1,241 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22066"
] | [
"Cep192_D8"
] | [
1241
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [] | 0 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural and Functional Analy... | [
2008,
2014,
2014,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Archangium lansingense",
"Eukaryota"
] | [
1,
1240
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
6,
5,
3
] | 4 | true | Domain | Cep192-like, domain 8 | Cep192-like, domain 8 | Cep192-like_D8 | 2 |
IPR054089 | 54,089 | Cep192-like, domain 3 | Cep192-like_D3 | Domain | 1,921 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22067"
] | [
"Cep192_D3"
] | [
1921
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [] | 0 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural and Functional Analy... | [
2008,
2014,
2014,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermofilum pendens"
] | [
17,
1903,
1
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
8,
3,
4
] | 4 | true | Domain | Cep192-like, domain 3 | Cep192-like, domain 3 | Cep192-like_D3 | 6 |
IPR054090 | 54,090 | Cep192/Spd-2-like domain | Cep192_Spd-2-like_dom | Domain | 2,014 | false | false | Human Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a b... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22073"
] | [
"Cep192_D4"
] | [
2014
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [
"7ptb",
"9fh8",
"9fu8"
] | 3 | [
"PUB00056085",
"PUB00068670",
"PUB00075915",
"PUB00088934",
"PUB00148286",
"PUB00148294",
"PUB00153863",
"PUB00154404"
] | [
"19081077",
"18207742",
"15068791",
"15186742",
"24997597",
"25042804",
"35383272",
"32433990"
] | [
"The conserved protein SZY-20 opposes the Plk4-related kinase ZYG-1 to limit centrosome size.",
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Centrosome maturation and duplication in C. elegans require the coiled-coil protein SPD-2.",
"The Caenorhabditis elegans centrosomal protein ... | [
2008,
2008,
2004,
2004,
2014,
2014,
2022,
2020
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
8,
299,
1702,
5
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
21,
1,
7,
5,
3
] | 6 | true | Domain | Cep192/Spd-2-like domain | Cep192/Spd-2-like domain | Cep192_Spd-2-like_dom | 9 |
IPR054091 | 54,091 | Cep192-like, domain 5 | Cep192-like_D5 | Domain | 1,580 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains. These are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22074"
] | [
"Cep192_D5"
] | [
1580
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [
"7ptb",
"9fh8"
] | 2 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00153863",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"35383272",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural validation and asses... | [
2008,
2014,
2014,
2022,
2020
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1580
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
1,
9,
6,
3
] | 5 | true | Domain | Cep192-like, domain 5 | Cep192-like, domain 5 | Cep192-like_D5 | 7 |
IPR054092 | 54,092 | Cep192-like, domain 6 | Cep192-like_D6 | Domain | 1,303 | false | false | Cep192 is a centrosomal protein with key roles in centriole duplication and pericentriolar material recruitment, organisation and regulation [ , ]. Most of the metazoan Cep192 homologues consist of eight ASH/PapD-like domains, which are located at the C-terminal part of the proteins and are likely arranged in a beads-o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22076"
] | [
"Cep192_D6"
] | [
1303
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518"
] | [
"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-8854518"
] | 7 | [
"9c72"
] | 1 | [
"PUB00068670",
"PUB00148286",
"PUB00148294",
"PUB00154404"
] | [
"18207742",
"24997597",
"25042804",
"32433990"
] | [
"The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.",
"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.",
"The Cep192-organized aurora A-Plk1 cascade is essential for centrosome cycle and bipolar spindle assembly.",
"Structural and Functional Analy... | [
2008,
2014,
2014,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1303
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
1,
8,
6,
3
] | 5 | true | Domain | Cep192-like, domain 6 | Cep192-like, domain 6 | Cep192-like_D6 | 9 |
IPR054093 | 54,093 | Androglobin, domain II | Androglobin_II | Domain | 1,296 | false | false | Androglobin is a protein with a key role in spermatogenesis. It is required for sperm flagellum formation and maturation of elongating spermatids, both essential for male fertility. Androglobin contains an N-terminal cysteine protease domain that lacks the catalytic cysteine, a tandem of three β-sandwich domains (domai... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22068"
] | [
"Androglobin_II"
] | [
1296
] | 1 | [] | [] | [] | 0 | [
"7n6g",
"7sqc"
] | 2 | [
"PUB00095962",
"PUB00154403"
] | [
"22115833",
"36995441"
] | [
"Androglobin: a chimeric globin in metazoans that is preferentially expressed in Mammalian testes.",
"ADGB variants cause asthenozoospermia and male infertility."
] | [
2012,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1296
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
4,
3,
5
] | 4 | true | Domain | Androglobin, domain II | Androglobin, domain II | Androglobin_II | 1 |
IPR054094 | 54,094 | Androglobin, domain IV | Androglobin_IV | Domain | 1,277 | false | false | Androglobin is a protein with a key role in spermatogenesis. It is required for sperm flagellum formation and maturation of elongating spermatids, both essential for male fertility. Androglobin contains an N-terminal cysteine protease domain that lacks the catalytic cysteine, a tandem of three β-sandwich domains (domai... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22069"
] | [
"Androglobin_IV"
] | [
1277
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00095962",
"PUB00154403"
] | [
"22115833",
"36995441"
] | [
"Androglobin: a chimeric globin in metazoans that is preferentially expressed in Mammalian testes.",
"ADGB variants cause asthenozoospermia and male infertility."
] | [
2012,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1277
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
6,
2,
4
] | 4 | true | Domain | Androglobin, domain IV | Androglobin, domain IV | Androglobin_IV | 2 |
IPR054095 | 54,095 | Androglobin, domain V | Androglobin_V | Domain | 1,247 | false | false | Androglobin is a protein with a key role in spermatogenesis. It is required for sperm flagellum formation and maturation of elongating spermatids, both essential for male fertility. Androglobin contains an N-terminal cysteine protease domain that lacks the catalytic cysteine, a tandem of three β-sandwich domains (domai... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22070"
] | [
"Androglobin_V"
] | [
1247
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00095962",
"PUB00154403"
] | [
"22115833",
"36995441"
] | [
"Androglobin: a chimeric globin in metazoans that is preferentially expressed in Mammalian testes.",
"ADGB variants cause asthenozoospermia and male infertility."
] | [
2012,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1247
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
8,
2,
5
] | 4 | true | Domain | Androglobin, domain V | Androglobin, domain V | Androglobin_V | 1 |
IPR054096 | 54,096 | FAP42-like, domain B2 | FAP42-like_B2 | Domain | 43 | false | false | FAP42 is a large protein that forms the peripheral 'beam' of the C1b projection of the ciliary central apparatus (CA). This protein forms a complex with FAP413 and FAP246, which is essential for a stable assembly of the C1b, C1f and C2b projections, and loss of these proteins leads to ciliary motility defects. FAP42 st... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22071"
] | [
"FAP42_B2"
] | [
43
] | 1 | [] | [] | [] | 0 | [
"7n6g",
"7sqc"
] | 2 | [
"PUB00153933",
"PUB00153934"
] | [
"35578023",
"35578022"
] | [
"Ciliary central apparatus structure reveals mechanisms of microtubule patterning.",
"Cryo-EM structure of an active central apparatus."
] | [
2022,
2022
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
43
] | 1 | [] | [] | 0 | true | Domain | FAP42-like, domain B2 | FAP42-like, domain B2 | FAP42-like_B2 | 5 |
IPR054098 | 54,098 | HvfC, C-terminal domain | HvfC_C | Domain | 1,773 | false | false | This entry describes the C-terminal domain in Uncharacterized protein HvfC ( ), NGO_1945 ( , ) and various other proteins partnered with MNIO family peptide modification enzymes. HvfC, as described in Haemophilus influenzae, is a partner protein to the multinuclear nonheme iron-dependent oxidase (MNIO) enzyme HvfB , an... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22106"
] | [
"NGO1945_C"
] | [
1773
] | 1 | [] | [] | [] | 0 | [
"3dee"
] | 1 | [
"PUB00057687",
"PUB00161749",
"PUB00161768",
"PUB00161769"
] | [
"20944208",
"39602266",
"31427451",
"38968106"
] | [
"The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation.",
"A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress.",
"Discovery and Contribution of Nontypeable Hae... | [
2010,
2024,
2019,
2024
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"ecological metagenomes"
] | [
1753,
2,
18
] | 3 | [] | [] | 0 | true | Domain | HvfC, C-terminal domain | HvfC, C-terminal domain | HvfC_C | 5 |
IPR054099 | 54,099 | Oxygen-evolving enhancer protein 3, plants | PSII_PsbQ_pln | Family | 2,587 | false | false | In PSII, the oxygen-evolving complex (OEC) is responsible for catalysing the splitting of water to O(2) and 4H+. The OEC is composed of a cluster of manganese, calcium and chloride ions bound to extrinsic proteins. In cyanobacteria there are five extrinsic proteins in OEC (PsbO, PsbP-like, PsbQ-like, PsbU and PsbV), wh... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR33399"
] | [
""
] | [
2587
] | 1 | [] | [] | [] | 0 | [
"1nze",
"1vyk",
"2mwq",
"3jcu",
"5xnl",
"6kac",
"7eu3",
"7f9o",
"7wff",
"7wg5",
"8bd3",
"8z9d",
"9grx",
"9hd7"
] | 14 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015369",
"PUB00015372",
"PUB00097583",
"PUB00152828"
] | [
"12518057",
"15100025",
"14871485",
"15258264",
"12949587",
"30076221",
"33846594"
] | [
"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.",
"The evolutionary development of the protein complement of photosystem 2.",
"The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.",
"Homologs of plant PsbP and PsbQ prot... | [
2003,
2004,
2004,
2004,
2003,
2018,
2021
] | 7 | [
"IPR008797"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
4,
2583
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
18,
15,
35
] | 3 | true | Family | Oxygen-evolving enhancer protein 3, plants | Oxygen-evolving enhancer protein 3, plants | PSII_PsbQ_pln | 8 |
IPR054100 | 54,100 | Membrane protein of 12 TMs, archaea | 12TM_1_arc | Family | 50 | false | false | This entry represents a family of archaeal proteins that carry twelve transmembrane regions. It does not have any characteristic nucleotide-binding-domains of the GxSGSGKST type, so it may not be an ATP-binding cassette transporter. However, it may well be a transporter of some description. ABC transporters always have... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF018875"
] | [
"UCP018875_ABC_perm"
] | [
50
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR018646"
] | [] | 1 | 0 | 1 | [
"Methanobacteriati"
] | [
50
] | 1 | [] | [] | 0 | true | Family | Membrane protein of 12 TMs, archaea | Membrane protein of 12 TMs, archaea | 12TM_1_arc | 6 |
IPR054102 | 54,102 | BDI_0842-like | BDI_0842-like | Domain | 15 | false | false | This entry represents the C-terminal region of BDI_0842 from Parabacteroides distasonis and similar sequences, for which there is a known structure . The structure has similarity to the alpha-lytic protease prodomain-like fold. Proteins in this family have an N-terminal lipoprotein attachment motif. The function of the... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21903"
] | [
"BDI_0842"
] | [
15
] | 1 | [] | [] | [] | 0 | [
"4jm1"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroidota",
"Myoviridae sp. ctcPl3"
] | [
14,
1
] | 2 | [] | [] | 0 | true | Domain | BDI_0842-like | BDI_0842-like | BDI_0842-like | 3 |
IPR054103 | 54,103 | CAND6/7, N-terminal domain | CAND6-7_N | Domain | 2,603 | false | false | This entry represents the N-terminal domain found in CAND6/7 from Arabidopsis and related sequences. These proteins have been predicted to be G-protein coupled receptors that play a role in plant and microbe interactions [ , ]. They consist of two domains, a GOLD-like domain represented in this entry and a seven transm... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21904"
] | [
"CAND6-7_N"
] | [
2603
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00093390",
"PUB00093391",
"PUB00151072"
] | [
"22206669",
"18671868",
"36373655"
] | [
"Two G-protein-coupled-receptor candidates, Cand2 and Cand7, are involved in Arabidopsis root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones.",
"Whole proteome identification of plant candidate G-protein coupled receptors in Arabidopsis, rice, and poplar: computational predicti... | [
2012,
2008,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2603
] | 1 | [
"Arabidopsis thaliana",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
17,
1,
4,
12,
26
] | 5 | true | Domain | CAND6/7, N-terminal domain | CAND6/7, N-terminal domain | CAND6-7_N | 4 |
IPR054104 | 54,104 | Nsp1alpha, N-terminal zinc finger | Nsp1alpha_Znf | Domain | 1,282 | false | false | Porcine reproductive and respiratory syndrome (PRRS) virus (PRRSV), a positive-strand RNA virus that belongs to the Arteriviridae family of Nidovirales, has been identified as the causative agent of PRRS. Nsp1alpha is the amino (N)-terminal protein in a polyprotein encoded by the PRRSV genome and is reported to be cruc... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21905"
] | [
"Zf-Nsp1alpha"
] | [
1282
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC"
] | [
"2.7.7.48",
"3.4.19.12",
"3.4.21.-",
"3.4.22.-",
"3.6.4.12",
"3.6.4.13",
"4.6.1.-",
"PWY-7884"
] | [
"EC:2.7.7.48",
"EC:3.4.19.12",
"EC:3.4.21.-",
"EC:3.4.22.-",
"EC:3.6.4.12",
"EC:3.6.4.13",
"EC:4.6.1.-",
"METACYC:PWY-7884"
] | 8 | [
"3ifu"
] | 1 | [
"PUB00057983"
] | [
"19706710"
] | [
"Crystal structure of porcine reproductive and respiratory syndrome virus leader protease Nsp1alpha."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"unclassified Arteriviridae"
] | [
1282
] | 1 | [] | [] | 0 | true | Domain | Nsp1alpha, N-terminal zinc finger | Nsp1alpha, N-terminal zinc finger | Nsp1alpha_Znf | 8 |
IPR054105 | 54,105 | NrtR, DNA-binding winged helix domain | WHD_NrtR | Domain | 15,009 | false | false | This entry represents the C-terminal DNA-binding domain of transcriptional regulator NrtR from Acinetobacter baylyi and similar bacterial proteins. NrtR is involved in regulating the transcription of NAD biosynthetic genes. This domain has a winged helix-turn-helix structure [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21906"
] | [
"WHD_NrtR"
] | [
15009
] | 1 | [] | [] | [] | 0 | [
"2fml",
"3gz5",
"3gz6",
"5bs6",
"5dd4",
"5ddg",
"5deq",
"7q91",
"7q92",
"7q93",
"7q94"
] | 11 | [
"PUB00052992",
"PUB00099062"
] | [
"19604474",
"26438537"
] | [
"Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism.",
"A novel transcriptional regulator of L-arabinose utilization in human gut bacteria."
] | [
2009,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillus phage G",
"Bacteria",
"Candidatus Methanoplasma termitum",
"Eukaryota",
"unclassified sequences"
] | [
1,
14860,
1,
8,
139
] | 5 | [] | [] | 0 | true | Domain | NrtR, DNA-binding winged helix domain | NrtR, DNA-binding winged helix domain | WHD_NrtR | 9 |
IPR054106 | 54,106 | CEP-1, C-terminal SAM domain | CEP-1_C | Domain | 68 | false | false | This entry represents the C-terminal domain of the CEP-1 protein which is a p53 homologue found in C. elegans [ ]. The CEP-1 C-terminal is composed of two sub-domains, an oligomerisation domain (OD) followed by a SAM domain (this entry) that closely interacts with the oligomerisation. The OD domain of CEP-1 forms a dim... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21907"
] | [
"SAM_CEP-1_C"
] | [
68
] | 1 | [] | [] | [] | 0 | [
"2rp5"
] | 1 | [
"PUB00049456"
] | [
"17581633"
] | [
"Structural evolution of C-terminal domains in the p53 family."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Rhabditida"
] | [
68
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | CEP-1, C-terminal SAM domain | CEP-1, C-terminal SAM domain | CEP-1_C | 1 |
IPR054107 | 54,107 | Cel124-like, catalytic domain | Cel124_cat | Domain | 22 | false | false | This entry represents the catalytic domain of endo-acting cellulase Cel124 ( ), found at its C-terminal, and related proteins. The active site architecture of this cellulase shares significant structural similarity to GH23 enzymes, a family that contains inverting lysozymes and lytic transglycosylases [ , ]. These prot... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21908"
] | [
"Cel124_C"
] | [
22
] | 1 | [] | [] | [] | 0 | [
"2xqo",
"6g1g",
"6g1i"
] | 3 | [
"PUB00066150",
"PUB00153862"
] | [
"21393568",
"30084399"
] | [
"Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis.",
"Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum."
] | [
2011,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Neocallimastigaceae"
] | [
16,
6
] | 2 | [] | [] | 0 | true | Domain | Cel124-like, catalytic domain | Cel124-like, catalytic domain | Cel124_cat | 7 |
IPR054108 | 54,108 | Ubiquitin carboxyl-terminal hydrolase 25/28, UIM | USP25/28_UIM | Conserved_site | 2,941 | false | false | This entry represents the N-terminal ubiquitin-interacting motif (UIM) found in ubiquitin carboxyl-terminal hydrolase 25 and 28, which are ubiquitin-specific proteases (USP) [ ]. This domain provides a structural basis for the recognition and recruitment of ubiquitin substrates, potentially conferring USP display of ca... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21909"
] | [
"USP_UIM_N"
] | [
2941
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.19.12",
"R-HSA-5689880",
"R-MMU-5689880",
"R-RNO-5689880"
] | [
"EC:3.4.19.12",
"REACTOME:R-HSA-5689880",
"REACTOME:R-MMU-5689880",
"REACTOME:R-RNO-5689880"
] | 4 | [
"2lva",
"2muu",
"2mux",
"5o71"
] | 4 | [
"PUB00102041",
"PUB00134011",
"PUB00144227",
"PUB00149611",
"PUB00149743",
"PUB00154318",
"PUB00154428",
"PUB00154429",
"PUB00154430"
] | [
"24623306",
"16901786",
"30926243",
"28619731",
"30478318",
"26268556",
"29518389",
"37339955",
"37683630"
] | [
"A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype.",
"A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response.",
"Differential Oligomerization of the Deubiquitinases USP25 and USP28 Regulates Their Activities.",
"USP25 regulates Wnt... | [
2014,
2006,
2019,
2017,
2018,
2015,
2018,
2023,
2023
] | 9 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2941
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
38,
8,
7,
13
] | 4 | true | Conserved_site | Ubiquitin carboxyl-terminal hydrolase 25/28, UIM | Ubiquitin carboxyl-terminal hydrolase 25/28, UIM | USP25/28_UIM | 5 |
IPR054109 | 54,109 | UBA-like domain | UBA_8 | Domain | 6,770 | false | false | This entry represents a UBA-like domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22566"
] | [
"UBA_8"
] | [
6770
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6798695",
"R-BTA-8980692",
"R-HSA-5689880",
"R-HSA-6798695",
"R-HSA-8951664",
"R-HSA-8980692",
"R-HSA-9755511",
"R-MMU-5689880",
"R-MMU-6798695",
"R-MMU-8951664",
"R-MMU-8980692",
"R-MMU-9755511",
"R-RNO-5689880",
"R-XTR-6798695",
"R-XTR-8980692"
] | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8980692",
"REACTOME:R-HSA-5689880",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9755511",
"REACTOME:R-MMU-5689880",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-8951664",
"REACTOME:R-MMU-8980692",
"REACTOM... | 15 | [
"1vdl",
"2dal",
"2dam",
"2dzl",
"2l4e",
"2l4f",
"2lva",
"2muu",
"2mux",
"3bq3",
"4f1i",
"4gew",
"5o71"
] | 13 | [
"PUB00022822",
"PUB00040923",
"PUB00050725",
"PUB00065883",
"PUB00154318"
] | [
"15029246",
"16563434",
"18206966",
"23104058",
"26268556"
] | [
"Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.",
"Structural basis for monoubiquitin recognition by the Ede1 UBA domain.",
"Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation.",
"Structural basis for recognition of 5'-phosphotyrosine adducts by Tdp2.",
... | [
2004,
2006,
2008,
2012,
2015
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
42,
6728
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
46,
2,
21,
16,
28,
1
] | 7 | true | Domain | UBA-like domain | UBA-like domain | UBA_8 | 4 |
IPR054110 | 54,110 | Endo-beta-N-acetylglucosaminidase D-like, D2 domain | EndoD-like_D2 | Domain | 1,054 | false | false | This entry represents the D2 domain of Endo-beta-N-acetylglucosaminidase D (EndoD, ) from Streptococcus pneumoniae and similar sequences, which belong to family 85 of glycoside hydrolases (GH85 endohexosaminidases). These enzymes cleave the glycosidic linkage between the two N-acetylglucosamine units that make up the c... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21910"
] | [
"GH85_C"
] | [
1054
] | 1 | [] | [] | [] | 0 | [
"2vtf",
"2w91",
"2w92",
"3fha",
"3fhq",
"3gdb"
] | 6 | [
"PUB00050077"
] | [
"19181667"
] | [
"Streptococcus pneumoniae endohexosaminidase D, structural and mechanistic insight into substrate-assisted catalysis in family 85 glycoside hydrolases."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Phytophthora kernoviae 00238/432",
"metagenomes"
] | [
1050,
1,
3
] | 3 | [] | [] | 0 | true | Domain | Endo-beta-N-acetylglucosaminidase D-like, D2 domain | Endo-beta-N-acetylglucosaminidase D-like, D2 domain | EndoD-like_D2 | 5 |
IPR054111 | 54,111 | PG_1098, N-terminal domain | PG_1098_N | Domain | 25 | false | false | This small α-helical domain is found at the N-terminal of putative methyltransferase proteins. The structure of a member has been determined . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21911"
] | [
"PG_1098_N"
] | [
25
] | 1 | [] | [] | [] | 0 | [
"3ll7"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Porphyromonadaceae"
] | [
25
] | 1 | [] | [] | 0 | true | Domain | PG_1098, N-terminal domain | PG_1098, N-terminal domain | PG_1098_N | 2 |
IPR054112 | 54,112 | Glycosyltransferase 99, N-terminal domain | Glyco_transf_99_N | Domain | 71 | false | false | This entry represents the N-terminal domain found in a new family of glycosyltransferases (GTs) assigned as family Glycosyltransferase 99 (GT99) in the CAZy database [ ]. The GT99 family includes a prototype beta-Kdo GT from WbbB ([swissprot Q6U8B0]), a modular protein participating in lipopolysaccharide (LPS) O-antige... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21912"
] | [
"Glyco_transf_99"
] | [
71
] | 1 | [] | [] | [] | 0 | [
"5fa0",
"5fa1",
"8csb",
"8csc",
"8csd",
"8cse",
"8csf"
] | 7 | [
"PUB00153983"
] | [
"27199480"
] | [
"Bacterial β-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99)."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"hydrocarbon metagenome"
] | [
70,
1
] | 2 | [] | [] | 0 | true | Domain | Glycosyltransferase 99, N-terminal domain | Glycosyltransferase 99, N-terminal domain | Glyco_transf_99_N | 9 |
IPR054114 | 54,114 | Major tropism determinant, second domain | Mtd_2nd | Domain | 136 | false | false | This entry represents the second domain of major tropism determinant (Mtd). Mtd, the receptor-binding protein of Bordetella bacteriophage, varies greatly in sequence [ ]. It is the tail fibre protein located at the distal ends of the fibres that binds to the adhesion receptors on the host surface, thereby determining t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21916"
] | [
"mtd_2nd"
] | [
136
] | 1 | [] | [] | [] | 0 | [
"1yu0",
"1yu1",
"1yu2",
"1yu3",
"1yu4",
"2iou"
] | 6 | [
"PUB00038630",
"PUB00047723",
"PUB00091539"
] | [
"16170324",
"18532877",
"15386016"
] | [
"The C-type lectin fold as an evolutionary solution for massive sequence variation.",
"Selective ligand recognition by a diversity-generating retroelement variable protein.",
"Tropism switching in Bordetella bacteriophage defines a family of diversity-generating retroelements."
] | [
2005,
2008,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacterium spitsbergense",
"Viruses",
"viral metagenome"
] | [
125,
1,
5,
5
] | 4 | [] | [] | 0 | true | Domain | Major tropism determinant, second domain | Major tropism determinant, second domain | Mtd_2nd | 4 |
IPR054115 | 54,115 | Magnesium and cobalt efflux protein CorC, N-terminal domain | CorC_N | Domain | 5,558 | false | false | This entry represents a pair of helices found at the N-terminal of some CBS domain proteins. A pair of these regions dimerise to form a four helical bundle. Proteins in this family have this region followed by two CBS domains and a Transporter-associated domain ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21917"
] | [
"NMB0537_N"
] | [
5558
] | 1 | [] | [] | [] | 0 | [
"3oi8",
"4hg0"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5470,
10,
78
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Magnesium and cobalt efflux protein CorC, N-terminal domain | Magnesium and cobalt efflux protein CorC, N-terminal domain | CorC_N | 5 |
IPR054116 | 54,116 | Cas12a, REC2 domain | Cas12a_REC2 | Domain | 129 | false | false | This entry represents the REC2 domain found in Cpf1, also known as CRISPR-associated endonuclease Cas12a. Cpf1 is an RNA-guided endonuclease of a type V CRISPR-Cas system that has been harnessed for genome editing. The REC2 domain is a part of the REC lobe of the bilobed architecture of Cpf1, which consists of both REC... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21918"
] | [
"cas_Cpf1_2nd"
] | [
129
] | 1 | [] | [] | [] | 0 | [
"5b43",
"5id6",
"5kk5",
"5mga",
"5nfv",
"5ng6",
"5xh6",
"5xh7",
"5xus",
"5xut",
"5xuu",
"5xuz",
"6gtc",
"6gtd",
"6gte",
"6gtf",
"6gtg",
"6i1k",
"6i1l",
"6iv6",
"6kl9",
"6klb",
"6nm9",
"6nma",
"6nmc",
"6nmd",
"6nme",
"6omv",
"6p7m",
"6p7n",
"8h9d",
"8i54"... | 60 | [
"PUB00087324",
"PUB00087325",
"PUB00091266",
"PUB00153855",
"PUB00153856"
] | [
"28431230",
"28562584",
"27114038",
"27096363",
"27444870"
] | [
"Structural Basis for Guide RNA Processing and Seed-Dependent DNA Targeting by CRISPR-Cas12a.",
"Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage.",
"Crystal Structure of Cpf1 in Complex with Guide RNA and Target DNA.",
"The crystal structure of Cpf1 in complex with CRISPR RNA.",
... | [
2017,
2017,
2016,
2016,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomassiliicoccales",
"Potamilus streckersoni"
] | [
122,
3,
4
] | 3 | [] | [] | 0 | true | Domain | Cas12a, REC2 domain | Cas12a, REC2 domain | Cas12a_REC2 | 9 |
IPR054117 | 54,117 | Thermus phage P23-45 portal protein | P23-45_portal | Family | 5 | false | false | This entry represents the Thermus phage P23-45 portal protein. The portal protein is a key component of many double-stranded DNA viruses, governing capsid assembly and genome packaging. Twelve subunits of the portal protein define a tunnel, through which DNA is translocated into the capsid [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21919"
] | [
"P23-45_portal_barrel"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"4zjn",
"5ngd",
"6ibg",
"6qjt"
] | 4 | [
"PUB00095684",
"PUB00154143"
] | [
"30737287",
"32286226"
] | [
"Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with supersized T=7 capsids.",
"Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss."
] | [
2019,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Oshimavirus"
] | [
2,
3
] | 2 | [] | [] | 0 | true | Family | Thermus phage P23-45 portal protein | Thermus phage P23-45 portal protein | P23-45_portal | 1 |
IPR054118 | 54,118 | Ski7, domain III | Ski7_3rd | Domain | 19 | false | false | This entry represents the third domain (domain III) of the Superkiller protein 7 (Ski7), a cofactor of the cytoplasmic exosome that functions in mRNA turnover and non-stop decay (NSD). The C-terminal region of these proteins is organised into three domains, with domain I adopting the α/β fold of GTP-binding domains, an... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21920"
] | [
"Ski7_3rd"
] | [
19
] | 1 | [] | [] | [] | 0 | [
"4zkd",
"4zke",
"5g06"
] | 3 | [
"PUB00152002",
"PUB00154234"
] | [
"27174052",
"26051716"
] | [
"CryoEM structure of yeast cytoplasmic exosome complex.",
"Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases."
] | [
2016,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomyces"
] | [
19
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Ski7, domain III | Ski7, domain III | Ski7_3rd | 4 |
IPR054119 | 54,119 | Ski7, domain II | Ski7_2nd | Domain | 19 | false | false | This entry represents the second domain (domain II) of the Superkiller protein 7 (Ski7), a cofactor of the cytoplasmic exosome that functions in mRNA turnover and non-stop decay (NSD). The C-terminal region of these proteins is organised into three domains, with domain I adopting the α/β fold of GTP-binding domains, an... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21921"
] | [
"Ski7_2nd"
] | [
19
] | 1 | [] | [] | [] | 0 | [
"4zkd",
"4zke",
"5g06"
] | 3 | [
"PUB00152002",
"PUB00154234"
] | [
"27174052",
"26051716"
] | [
"CryoEM structure of yeast cytoplasmic exosome complex.",
"Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases."
] | [
2016,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomyces"
] | [
19
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Ski7, domain II | Ski7, domain II | Ski7_2nd | 5 |
IPR054120 | 54,120 | Penicillin binding protein A, dimerisation domain | PBPA_dimer | Domain | 7,929 | false | false | This domain is found in peptidoglycan D,D-transpeptidase also known as penicillin-binding protein A (PBPA). This domain consists of a four-stranded mixed β-sheet with three short helices packed on one side [ , ]. Compared to the N-terminal domains of other class B High Molecular Mass (HMM) PBPs, the NTD of PBPA is rela... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21922"
] | [
"PBP_dimer_2"
] | [
7929
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.4.16.4",
"PWY-5265",
"PWY-6471"
] | [
"EC:3.4.16.4",
"METACYC:PWY-5265",
"METACYC:PWY-6471"
] | 3 | [
"3lo7",
"3un7",
"3upn",
"3upo",
"3upp",
"4jbf",
"4mnr",
"4n1x",
"4qjg",
"4r0q",
"4r1g",
"4r23",
"4r3j",
"4ra7",
"7onn",
"7ono",
"8gpw"
] | 17 | [
"PUB00154148",
"PUB00154149",
"PUB00154150"
] | [
"22365933",
"20206184",
"34356681"
] | [
"The role of the β5-α11 loop in the active-site dynamics of acylated penicillin-binding protein A from Mycobacterium tuberculosis.",
"Unusual conformation of the SxN motif in the crystal structure of penicillin-binding protein A from Mycobacterium tuberculosis.",
"Interaction Mode of the Novel Monobactam AIC499... | [
2012,
2010,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhynchospora breviuscula",
"metagenomes"
] | [
7825,
1,
103
] | 3 | [] | [] | 0 | true | Domain | Penicillin binding protein A, dimerisation domain | Penicillin binding protein A, dimerisation domain | PBPA_dimer | 9 |
IPR054121 | 54,121 | Peptidoglycan-binding protein ArfA, BON-like domain | ArfA_BON-like | Domain | 284 | false | false | This entry represents BON-like domain found in Peptidoglycan-binding protein ArfA from Mycobacterium tuberculosis, which appears to lack the first α-helix of the classical BON domain structure. ArfA is thought to play a role in ammonia secretion, although it does not play a direct role in ammonia transport. This domain... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21923"
] | [
"BON_like"
] | [
284
] | 1 | [] | [] | [] | 0 | [
"2kgs",
"2ksm",
"2l26"
] | 3 | [
"PUB00054320",
"PUB00054622",
"PUB00057081"
] | [
"20199110",
"21117233",
"22108166"
] | [
"Mycobacterium tuberculosis Rv0899 adopts a mixed alpha/beta-structure and does not form a transmembrane beta-barrel.",
"Structure of the Mycobacterium tuberculosis OmpATb protein: a model of an oligomeric channel in the mycobacterial cell wall.",
"Structural Studies of Mycobacterium tuberculosis Rv0899 Reveal ... | [
2010,
2011,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
284
] | 1 | [] | [] | 0 | true | Domain | Peptidoglycan-binding protein ArfA, BON-like domain | Peptidoglycan-binding protein ArfA, BON-like domain | ArfA_BON-like | 1 |
IPR054123 | 54,123 | CT0912-like, N-terminal domain | CT0912-like_N | Domain | 28 | false | false | This domain is found in from Chlorobaculum tepidum and similar bacterial proteins. It adopts an α-β configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21931"
] | [
"ABM-like"
] | [
28
] | 1 | [] | [] | [] | 0 | [
"3gn6"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"mine drainage metagenome"
] | [
27,
1
] | 2 | [] | [] | 0 | true | Domain | CT0912-like, N-terminal domain | CT0912-like, N-terminal domain | CT0912-like_N | 9 |
IPR054125 | 54,125 | MCM5, C-terminal domain | MCM5_C | Domain | 4,200 | false | false | This entry represents the C-terminal domain of MCM5 from humans and its homologues [ ]. MCM5 is part of the MCM2-7 complex. This is a HTH domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21933"
] | [
"MCM5_C"
] | [
4200
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.4.12",
"R-CEL-68867",
"R-CEL-68949",
"R-CEL-68962",
"R-CEL-69052",
"R-DDI-68867",
"R-DDI-68962",
"R-DDI-69052",
"R-DME-176187",
"R-DME-68867",
"R-DME-68949",
"R-DME-68962",
"R-DME-69052",
"R-HSA-176187",
"R-HSA-176974",
"R-HSA-68867",
"R-HSA-68949",
"R-HSA-68962",
"R-HSA-690... | [
"EC:3.6.4.12",
"REACTOME:R-CEL-68867",
"REACTOME:R-CEL-68949",
"REACTOME:R-CEL-68962",
"REACTOME:R-CEL-69052",
"REACTOME:R-DDI-68867",
"REACTOME:R-DDI-68962",
"REACTOME:R-DDI-69052",
"REACTOME:R-DME-176187",
"REACTOME:R-DME-68867",
"REACTOME:R-DME-68949",
"REACTOME:R-DME-68962",
"REACTOME:R-... | 38 | [
"3ja8",
"3jc5",
"3jc6",
"3jc7",
"5bk4",
"5u8s",
"5u8t",
"5v8f",
"5xf8",
"6eyc",
"6f0l",
"6hv9",
"6ptj",
"6ptn",
"6pto",
"6raw",
"6rax",
"6ray",
"6raz",
"6rqc",
"6skl",
"6sko",
"6wgf",
"6wgg",
"6wgi",
"6xtx",
"6xty",
"7p30",
"7p5z",
"7pfo",
"7plo",
"7pmk"... | 81 | [
"PUB00154055"
] | [
"32453425"
] | [
"CryoEM structures of human CMG-ATPγS-DNA and CMG-AND-1 complexes."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4200
] | 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,
1,
7,
3,
1,
1,
5,
1,
1,
17
] | 12 | true | Domain | MCM5, C-terminal domain | MCM5, C-terminal domain | MCM5_C | 7 |
IPR054127 | 54,127 | Pcf11, C-terminal domain | Pcf11_C | Domain | 2,929 | false | false | This entry represents the C-terminal domain of Pcf11, a CCHC zinc-finger domain which contains a conserved interface for potential binding partners. Mutational studies revealed that mutations in key residues in this conserved region disrupt 3'-end processing [ , ]. Pfc11 is a highly conserved multidomain protein that l... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21936"
] | [
"Pcf11_C"
] | [
2929
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6807505",
"R-HSA-72187",
"R-HSA-72203",
"R-HSA-73856",
"R-HSA-77595",
"R-MMU-6807505",
"R-MMU-72187",
"R-MMU-72203",
"R-MMU-73856",
"R-MMU-77595"
] | [
"REACTOME:R-HSA-6807505",
"REACTOME:R-HSA-72187",
"REACTOME:R-HSA-72203",
"REACTOME:R-HSA-73856",
"REACTOME:R-HSA-77595",
"REACTOME:R-MMU-6807505",
"REACTOME:R-MMU-72187",
"REACTOME:R-MMU-72203",
"REACTOME:R-MMU-73856",
"REACTOME:R-MMU-77595"
] | 10 | [
"2nax",
"5m9z"
] | 2 | [
"PUB00154152",
"PUB00154153"
] | [
"27780845",
"28973460"
] | [
"The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'-end processing.",
"Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing."
] | [
2017,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Ectocarpus siliculosus virus 1 (isolate New Zealand/Kaikoura/1988)",
"Eukaryota"
] | [
1,
2928
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
4,
2,
2,
1,
1,
1,
1
] | 8 | true | Domain | Pcf11, C-terminal domain | Pcf11, C-terminal domain | Pcf11_C | 4 |
IPR054128 | 54,128 | Pfc11, Rna14/15 interacting domain | Pfc11_Rna14/15-ID | Domain | 59 | false | false | This entry represents the Rna14/15 interacting domain (Rna14/15-ID) of Pfc11 from yeast [ ]. Pfc11 is a multidomain protein that links transcriptional elongation, 3'-end processing, and transcription termination. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21940"
] | [
"Pfc11_Rna14-15-ID"
] | [
59
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154152"
] | [
"27780845"
] | [
"The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'-end processing."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycetes"
] | [
59
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Pfc11, Rna14/15 interacting domain | Pfc11, Rna14/15 interacting domain | Pfc11_Rna14/15-ID | 5 |
IPR054129 | 54,129 | DesT tetracyclin repressor-like, C-terminal domain | DesT_TetR_C | Domain | 14,076 | false | false | This domain is found at the C-terminal end of DesT from Pseudomonas aeruginosa ( ) and similar bacterial transcriptional regulators such as the HTH-type transcriptional repressor FabR. DesT is involved in the control of the unsaturated:saturated fatty acid ratio available for membrane lipid synthesis. This region folds... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21943"
] | [
"TetR_C_46"
] | [
14076
] | 1 | [] | [] | [] | 0 | [
"2qib",
"3f1b",
"3lsj",
"3lsp",
"3lsr",
"6o6n",
"6o6o",
"6o6p"
] | 8 | [
"PUB00061581",
"PUB00154272"
] | [
"20639888",
"32710080"
] | [
"Structural basis for the transcriptional regulation of membrane lipid homeostasis.",
"Mycobacterium tuberculosis FasR senses long fatty acyl-CoA through a tunnel and a hydrophobic transmission spine."
] | [
2010,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
13978,
3,
95
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | DesT tetracyclin repressor-like, C-terminal domain | DesT tetracyclin repressor-like, C-terminal domain | DesT_TetR_C | 2 |
IPR054130 | 54,130 | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | Family | 2 | false | false | This protein family represents human Mitochondrial-derived peptide MOTS-c (MT-RNR1), a 16-residue peptide that regulates insulin sensitivity and metabolic homeostasis [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21945"
] | [
"MT-RNR1"
] | [
2
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154085"
] | [
"25738459"
] | [
"The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Euteleostomi"
] | [
2
] | 1 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Mitochondrial-derived peptide MOTS-c | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | 1 |
IPR054133 | 54,133 | T-cell receptor gamma alternate reading frame protein | TARP | Family | 15 | false | false | This protein family includes human T-cell receptor gamma alternate reading frame protein (TARP) and similar sequences from vertebrates. TARP is a 7kDa protein with five leucine residues in heptad repeats followed by a basic region. It is expressed at higher levels in several types of cancerous cells [ , , , , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21951"
] | [
"TARP"
] | [
15
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154256",
"PUB00154257",
"PUB00154258",
"PUB00154259",
"PUB00154260"
] | [
"10931945",
"15150260",
"31371409",
"24238509",
"28153567"
] | [
"TARP: a nuclear protein expressed in prostate and breast cancer cells derived from an alternate reading frame of the T cell receptor gamma chain locus.",
"The T cell receptor gamma chain alternate reading frame protein (TARP), a prostate-specific protein localized in mitochondria.",
"TARP is an immunotherapeut... | [
2000,
2004,
2020,
2013,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Boreoeutheria"
] | [
15
] | 1 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | T-cell receptor gamma alternate reading frame protein | T-cell receptor gamma alternate reading frame protein | TARP | 5 |
IPR054134 | 54,134 | Protein PAXX, N-terminal domain | PAXX_N | Domain | 482 | false | false | Protein PAXX (also known as Paralog of XRCC4 and XLF) is a paralog of X-ray repair cross-complementing protein 4 (XRCC4) and XRCC4-like factor (XLF) that is involved in non-homologous end joining (NHEJ), a major pathway to repair double-strand breaks (DSBs) in DNA. It may act as a scaffold required to stabilise the DSB... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd22286"
] | [
"HD_PAXX_N"
] | [
482
] | 1 | [] | [] | [] | 0 | [
"3wtd",
"3wtf",
"4wja",
"7zwa",
"7zyg",
"8bh3",
"8bhv",
"8bhy",
"8eza",
"8ezb",
"9cq3",
"9cq6",
"9cqc",
"9g9l",
"9gd7",
"9n81",
"9n82",
"9n83"
] | 18 | [
"PUB00074304",
"PUB00110097",
"PUB00140191",
"PUB00147230",
"PUB00147243"
] | [
"25574025",
"32375023",
"25941166",
"25670504",
"31399561"
] | [
"DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair.",
"CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.",
"XLS (c9orf142) is a new component of mammalian DNA double-stranded break repair.",
"Interactome analysis identifies a new paralogue... | [
2015,
2020,
2015,
2015,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
482
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
2,
2
] | 4 | true | Domain | Protein PAXX, N-terminal domain | Protein PAXX, N-terminal domain | PAXX_N | 5 |
IPR054135 | 54,135 | Dermonecrotic toxin, barrel-like domain | ToxA_barrel | Domain | 15 | false | false | Dermonecrotic toxin (ToxA), also known as Pasteurella multocida toxin (PMT), inhibits osteoblastic differentiation in mammals and birds. It consists of an N-terminal domain that binds to target cells, and a large C-terminal domain. This entry represents a presumed barrel-like domain found between the N- and C-terminal ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22771"
] | [
"ToxA_barrel"
] | [
15
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
15
] | 1 | [] | [] | 0 | true | Domain | Dermonecrotic toxin, barrel-like domain | Dermonecrotic toxin, barrel-like domain | ToxA_barrel | 8 |
IPR054136 | 54,136 | Gp49, pectin lyase-like domain | Gp49_pectate_lyase-like | Domain | 32 | false | false | This entry represents the β-helix repeats from the catalytic domain of tailspike Gp49 from phage LKA1 ( ) [ ]. Gp49 binds and cleaves B-band LPS of Pseudomonas aeruginosa, reducing its virulence [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22442"
] | [
"Gp49_Pectate_lyase_like"
] | [
32
] | 1 | [] | [] | [] | 0 | [
"4ru4",
"4ru5",
"4y9v"
] | 3 | [
"PUB00152607"
] | [
"29176754"
] | [
"The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
23,
9
] | 2 | [] | [] | 0 | true | Domain | Gp49, pectin lyase-like domain | Gp49, pectin lyase-like domain | Gp49_pectate_lyase-like | 9 |
IPR054137 | 54,137 | PRKCH upstream open reading frame 2 | PRKCH_uORF2 | Family | 1 | false | false | This entry represents human PRKCH upstream open reading frame 2 (PRKCH_uORF2), also known as Protein uPEP2, the product of an upstream open reading frame (uORF). PRKCH_uORF2 exhibits kinase inhibitory functions. It possesses the typical PKC pseudosubstrate motif present in all PKCs that autoinhibits their kinase activi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21952"
] | [
"PRKCH_uORF2"
] | [
1
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154182"
] | [
"34593629"
] | [
"Unraveling the hidden role of a uORF-encoded peptide as a kinase inhibitor of PKCs."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Homo sapiens"
] | [
1
] | 1 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | PRKCH upstream open reading frame 2 | PRKCH upstream open reading frame 2 | PRKCH_uORF2 | 5 |
IPR054138 | 54,138 | TUNAR | TUNAR | Family | 303 | false | false | This protein family includes the human protein TUNAR and similar sequences from vertebrates. TUNAR is a 48-amino-acid micropeptide with a single-pass transmembrane domain involved in the regulation of intracellular calcium levels in neurons and in the endoplasmic reticulum of pancreatic beta cells, where it also enhanc... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21954"
] | [
"TUNAR"
] | [
303
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154311"
] | [
"34513312"
] | [
"A putative long noncoding RNA-encoded micropeptide maintains cellular homeostasis in pancreatic β cells."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
303
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
1,
2
] | 4 | true | Family | TUNAR | TUNAR | TUNAR | 2 |
IPR054139 | 54,139 | Carbapenem resistance protein CarG-like | CarG-like | Family | 132 | false | false | This entry represents the carbapenem resistance protein CarG from Serratia sp. and similar sequences mainly found in proteobacteria. CarG shows a unique β-sandwich fold with short terminal α-helices, displaying close structural homology with bacterial inhibitors of invertebrate lysozyme ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21955"
] | [
"CarG-like"
] | [
132
] | 1 | [] | [] | [] | 0 | [
"4o7j"
] | 1 | [
"PUB00153850"
] | [
"24583229"
] | [
"Crystal structure of the carbapenem intrinsic resistance protein CarG."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"hot springs metagenome"
] | [
131,
1
] | 2 | [] | [] | 0 | true | Family | Carbapenem resistance protein CarG-like | Carbapenem resistance protein CarG-like | CarG-like | 9 |
IPR054140 | 54,140 | AppA, four helical bundle | AppA_4HB | Domain | 31 | false | false | This domain is found in AppA protein from Rhodobacter sphaeroides and similar sequences from alphaproteobacteria. AppA is a light-sensing antirepressor involved in oxygen and light control of photosynthesis-gene expression. This protein senses blue-light via its N-terminal sensor of blue-light using FAD (BLUF) domain (... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21961"
] | [
"AppA_4HB"
] | [
31
] | 1 | [] | [] | [] | 0 | [
"4heh",
"4hh0",
"4hh1",
"4hh3"
] | 4 | [
"PUB00153821",
"PUB00153822"
] | [
"23982072",
"23728293"
] | [
"Redox and light control the heme-sensing activity of AppA.",
"A ternary AppA-PpsR-DNA complex mediates light regulation of photosynthesis-related gene expression."
] | [
2013,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Alphaproteobacteria"
] | [
31
] | 1 | [] | [] | 0 | true | Domain | AppA, four helical bundle | AppA, four helical bundle | AppA_4HB | 7 |
IPR054141 | 54,141 | TcdA1, receptor binding domain 2 | TcdA1_RBD_2 | Domain | 96 | false | false | This domain is found in TcdA1 from Photorhabdus luminescens and similar sequences mainly from gammaproteobacteria. TcdA1 is one of the three subunits of the Tc toxins. TcdA1 acts as an injecting device responsible for translocating the actual toxic component into host cells. TcA has four receptor-binding domains. This ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21963"
] | [
"TcdA1_RBD_2"
] | [
96
] | 1 | [] | [] | [] | 0 | [
"4o9y",
"5lkh",
"5lki",
"6h6e",
"6h6f",
"6l7e",
"6rw6",
"6rwa",
"6sue",
"6suf",
"8cpz",
"8cq0",
"8cq2",
"8tqe",
"8tv0",
"9mlg",
"9mlh",
"9mli"
] | 18 | [
"PUB00091290",
"PUB00154263"
] | [
"24572368",
"31663026"
] | [
"Mechanism of Tc toxin action revealed in molecular detail.",
"Common architecture of Tc toxins from human and insect pathogenic bacteria."
] | [
2014,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
96
] | 1 | [] | [] | 0 | true | Domain | TcdA1, receptor binding domain 2 | TcdA1, receptor binding domain 2 | TcdA1_RBD_2 | 6 |
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