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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR056999 | 56,999 | Phage zinc binding protein, tailed bacteriophages | Phage_zn_bind | Family | 172 | false | false | This entry represents a group of small uncharacterised tailed bacteriophage proteins with a domain that covers the whole length of the protein. Structure prediction shows that this domain adopts a four stranded β-meander fold and is likely zinc binding, with an N-terminal conserved CXXC motif and more central CXXXXC mo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23895"
] | [
"Phage_zn_bind"
] | [
172
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
4,
168
] | 2 | [] | [] | 0 | true | Family | Phage zinc binding protein, tailed bacteriophages | Phage zinc binding protein, tailed bacteriophages | Phage_zn_bind | 1 |
IPR057000 | 57,000 | Smacovirus capsid protein | Smaco_capsid | Family | 281 | false | false | This entry represents probable capsid proteins found mainly in smacoviruses, a family of small, circular single-stranded DNA viruses. This capsid protein is typically around 300-400 amino acids in length. Smacoviruses have been identified in the fecal matter of a variety of mammals, including humans, non-human primates... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23784"
] | [
"Smaco_capsid"
] | [
281
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Viruses",
"uncultured prokaryote"
] | [
2,
276,
3
] | 3 | [] | [] | 0 | true | Family | Smacovirus capsid protein | Smacovirus capsid protein | Smaco_capsid | 5 |
IPR057001 | 57,001 | RYYR-CCHC domain | RYYR-CCHC | Domain | 433 | false | false | This domain is found in uncharacterised proteins from nematodes. It is named after its conserved sequence motifs. It contains a semi-conserved RxY(x)nYR motif and two invariant CxxC and HxxxC motifs. This domain is predicted to adopt a globular structure with significant similarity to FLYWCH-type zinc finger, in partic... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23674"
] | [
"RYYR-CCHC"
] | [
433
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Ecdysozoa"
] | [
433
] | 1 | [] | [] | 0 | true | Domain | RYYR-CCHC domain | RYYR-CCHC domain | RYYR-CCHC | 1 |
IPR057002 | 57,002 | YdgV | YdgV | Family | 319 | false | false | This protein family includes YdgV from Escherichia coli and similar sequences from gammaproteobacteria. YdgV is a 33-residues micropeptide encoded by a small open reading frame (smORF). Proteins 50 or fewer residues-long have been shown to regulate the functions of larger proteins in a variety of organisms [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23502"
] | [
"YdgV"
] | [
319
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105763"
] | [
"30837344"
] | [
"Identifying Small Proteins by Ribosome Profiling with Stalled Initiation Complexes."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
319
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | YdgV | YdgV | YdgV | 5 |
IPR057003 | 57,003 | Phage tail termination protein, tailed bacteriophages | Phage_tail_terminator_2 | Family | 718 | false | false | This entry represents probable phage tail terminator proteins found in some bacteriophages that infect Actinobacteria. These proteins are likely located in the tail region and act as a terminator or cap the end of the tail. They are around 130-170 amino acids in length. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23841"
] | [
"Phage_tail_terminator_2"
] | [
718
] | 1 | [] | [] | [] | 0 | [
"8zdj",
"8zdl",
"9d94"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
306,
412
] | 2 | [] | [] | 0 | true | Family | Phage tail termination protein, tailed bacteriophages | Phage tail termination protein, tailed bacteriophages | Phage_tail_terminator_2 | 1 |
IPR057004 | 57,004 | Gp90-like protein, tailed bacteriophages | Gp90-like | Family | 194 | false | false | This family represents the Gp90-like protein from Synechococcus phages. Sequences in the family are typically around 110 residues in length. Gp90 homologues are found in a variety of different tailed bacteriophages. The function of Gp90 is currently unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23790"
] | [
"Kyano_Gp96"
] | [
194
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses",
"metagenomes"
] | [
6,
169,
19
] | 3 | [] | [] | 0 | true | Family | Gp90-like protein, tailed bacteriophages | Gp90-like protein, tailed bacteriophages | Gp90-like | 1 |
IPR057005 | 57,005 | Phage tail assembly chaperone, tailed bacteriophages | Phage_TAC_17 | Family | 156 | false | false | This family represents proteins found in tailed bacteriophages with structural similarity to the phage tail assembly chaperone proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23803"
] | [
"Phage_TAC_17"
] | [
156
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Caudoviricetes",
"metagenomes"
] | [
35,
119,
2
] | 3 | [] | [] | 0 | true | Family | Phage tail assembly chaperone, tailed bacteriophages | Phage tail assembly chaperone, tailed bacteriophages | Phage_TAC_17 | 4 |
IPR057006 | 57,006 | Phage tail chaperone protein-like | Phage_TAC_19 | Domain | 1,231 | false | false | This entry represents a family of proteins structurally similar to phage tail chaperone proteins and found in viruses and bacteria. The family contains proteins between 50-164 amino acids in length. Phage tail chaperone proteins play a role in the assembly of the phage tail apparatus. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF047360",
"PF23857"
] | [
"tail_chap_PVL",
"Phage_TAC_19"
] | [
1200,
1217
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00159571"
] | [
"15469818"
] | [
"Conserved translational frameshift in dsDNA bacteriophage tail assembly genes."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Halobaculum halobium",
"Viruses",
"metagenomes"
] | [
1039,
1,
188,
3
] | 4 | [] | [] | 0 | true | Domain | Phage tail chaperone protein-like | Phage tail chaperone protein-like | Phage_TAC_19 | 6 |
IPR057007 | 57,007 | Type III Secretion system protein OrgC | OrgC | Family | 448 | false | false | This entry represents the type III Secretion system protein OrgC from Salmonella Typhimurium and related proteins from proteobacteria. OrgC is a protein encoded within the T3SS gene cluster that is secreted by the T3SS. It interacts with the needle filament subunit PrgI and accelerates its polymerization into filaments... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF011849",
"PF24687"
] | [
"PRK15321.1",
"OrgC"
] | [
438,
448
] | 2 | [] | [] | [] | 0 | [
"6cjd"
] | 1 | [
"PUB00155775"
] | [
"30015613"
] | [
"A protein secreted by the <i>Salmonella</i> type III secretion system controls needle filament assembly."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
448
] | 1 | [] | [] | 0 | true | Family | Type III Secretion system protein OrgC | Type III Secretion system protein OrgC | OrgC | 2 |
IPR057008 | 57,008 | SpoVR-like, C-terminal | SpoVR-like_C | Domain | 7,746 | false | false | This entry represents a presumed domain found at the C-terminal of Stage V sporulation protein R from Bacillus subtilis (SpoVR), the uncharacterised protein YcgB from E.coli and related sequences from proteobacteria. SpoVR appears to be involved in spore cortex formation. This region may adopt a fold consisting of four... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24755"
] | [
"SpoVR_C"
] | [
7746
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteria",
"metagenomes",
"uncultured marine phage"
] | [
7407,
7,
297,
34,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | SpoVR-like, C-terminal | SpoVR-like, C-terminal | SpoVR-like_C | 4 |
IPR057009 | 57,009 | Fimbrial adhesin MrpH, N-terminal domain | MrpH_N | Domain | 234 | false | false | This entry represents the N-terminal domain of fimbrial adhesin MrpH and related proteins from bacteria. This protein is associated with strain virulence and is involved in surface adherence, biofilm formation and autoaggregation, essential for bladder and kidney colonization [ ]. This domain binds to surface receptor ... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF24222",
"cd22566"
] | [
"MrpH_N",
"MrpH-like"
] | [
234,
187
] | 2 | [] | [] | [] | 0 | [
"6y4e",
"6y4f"
] | 2 | [
"PUB00150666",
"PUB00150667",
"PUB00150668",
"PUB00150669",
"PUB00150670",
"PUB00155749"
] | [
"32780778",
"26605246",
"17714491",
"26542036",
"25853778",
"28017513"
] | [
"MrpH, a new class of metal-binding adhesin, requires zinc to mediate biofilm formation.",
"In silico design of fusion protein of FimH from uropathogenic Escherichia coli and MrpH from Proteus mirabilis against urinary tract infections.",
"Aggregative adherence of uropathogenic Proteus mirabilis to cultured epi... | [
2020,
2015,
2007,
2015,
2015,
2017
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
234
] | 1 | [] | [] | 0 | true | Domain | Fimbrial adhesin MrpH, N-terminal domain | Fimbrial adhesin MrpH, N-terminal domain | MrpH_N | 8 |
IPR057010 | 57,010 | Fimbrial adhesin MrpH, C-terminal domain | MrpH_C | Domain | 720 | false | false | This entry represents the C-terminal domain of fimbrial adhesin MrpH and related proteins from bacteria. MrpH is associated to strain virulence and is involved in surface adherence, biofilm formation and autoaggregation, essential for bladder and kidney colonization [ ]. This domain attaches to bacterial fimbrial tip [... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24223"
] | [
"MrpH_C"
] | [
720
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00150666",
"PUB00155749",
"PUB00155750"
] | [
"32780778",
"28017513",
"29536829"
] | [
"MrpH, a new class of metal-binding adhesin, requires zinc to mediate biofilm formation.",
"From Catheter to Kidney Stone: The Uropathogenic Lifestyle of Proteus mirabilis.",
"Pili Assembled by the Chaperone/Usher Pathway in <i>Escherichia coli</i> and <i>Salmonella</i>."
] | [
2020,
2017,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Puccinia striiformis f. sp. tritici PST-78"
] | [
719,
1
] | 2 | [] | [] | 0 | true | Domain | Fimbrial adhesin MrpH, C-terminal domain | Fimbrial adhesin MrpH, C-terminal domain | MrpH_C | 9 |
IPR057011 | 57,011 | ULTRAPETALA1/2, SAND domain | ULT1/2_SAND | Domain | 1,115 | false | false | This domain is found in the family of ULTRAPETALA proteins ULT1/2 from Arabidopsis thaliana and related plant proteins. This domain is predicted to adopt a globular structure with significant similarity to SAND domains. It also contains several highly conserved cysteine residues that could be involved in metal coordina... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23292"
] | [
"SAND_ULT1"
] | [
1115
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00052440",
"PUB00155833"
] | [
"15673576",
"23632855"
] | [
"ULTRAPETALA1 encodes a SAND domain putative transcriptional regulator that controls shoot and floral meristem activity in Arabidopsis.",
"EMBRYONIC FLOWER1 and ULTRAPETALA1 Act Antagonistically on Arabidopsis Development and Stress Response."
] | [
2005,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Streptophyta"
] | [
1115
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
5,
7
] | 3 | true | Domain | ULTRAPETALA1/2, SAND domain | ULTRAPETALA1/2, SAND domain | ULT1/2_SAND | 5 |
IPR057012 | 57,012 | ULTRAPETALA1/2, zinc finger domain | ULT1/2_Znf | Domain | 1,063 | false | false | This domain is found C-terminal in the family of ULTRAPETALA proteins ULT1/2 from Arabidopsis thaliana and related plant proteins. This domain contains several highly conserved cysteine and histidine residues that could be involved in metal coordination. In the core part, this domain shares similarity with CW-type zinc... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23293"
] | [
"zf_ULT1"
] | [
1063
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00052440",
"PUB00155833"
] | [
"15673576",
"23632855"
] | [
"ULTRAPETALA1 encodes a SAND domain putative transcriptional regulator that controls shoot and floral meristem activity in Arabidopsis.",
"EMBRYONIC FLOWER1 and ULTRAPETALA1 Act Antagonistically on Arabidopsis Development and Stress Response."
] | [
2005,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Streptophyta"
] | [
1063
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
4,
7
] | 3 | true | Domain | ULTRAPETALA1/2, zinc finger domain | ULTRAPETALA1/2, zinc finger domain | ULT1/2_Znf | 7 |
IPR057013 | 57,013 | EGF-like domain-containing protein ComC, LRR domain | LRR_ComC | Domain | 377 | false | false | This entry represents the N-terminal region of EGF-like domain containing protein ComC from Dictyostelium discoideum and similar sequences from amoebas and some plant species. ComC regulates aggregation, inhibiting lagC and activating lagD expression [ ]. The function of this domain, which is predicted to consist of le... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24141"
] | [
"LRR_ComC"
] | [
377
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154458"
] | [
"14651934"
] | [
"A cell-adhesion pathway regulates intercellular communication during Dictyostelium development."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Subsaximicrobium wynnwilliamsii"
] | [
376,
1
] | 2 | [
"Arabidopsis thaliana"
] | [
2
] | 1 | true | Domain | EGF-like domain-containing protein ComC, LRR domain | EGF-like domain-containing protein ComC, LRR domain | LRR_ComC | 3 |
IPR057014 | 57,014 | EGF-like domain-containing protein ComC, first beta-sandwich | B-sand_ComC_1st | Domain | 42 | false | false | This entry represents the first β-sandwich domain found in EGF-like domain containing protein ComC from amoebas. This protein regulates aggregation, inhibiting lagC and activating lagD expression [ ]. The function of this domain is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24142"
] | [
"Beta-sand_ComC_1st"
] | [
42
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154458"
] | [
"14651934"
] | [
"A cell-adhesion pathway regulates intercellular communication during Dictyostelium development."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Dictyostelium"
] | [
42
] | 1 | [] | [] | 0 | true | Domain | EGF-like domain-containing protein ComC, first beta-sandwich | EGF-like domain-containing protein ComC, first beta-sandwich | B-sand_ComC_1st | 5 |
IPR057016 | 57,016 | Endo-beta-N-acetylglucosaminidase EndoS/F2-like, TIM-barrel domain | EndoS_F2-like_TIM-barrel | Domain | 490 | false | false | This entry represents the TIM barrel domain found in Endo-beta-N-acetylglucosaminidase EndoS from Streptococcus spp., Endo-beta-N-acetylglucosaminidase F2 from Elizabethkingia meningoseptica and similar bacterial proteins. This domain binds to complex-type N-glycans and has an enzymatic activity [ , ]. EndoS is a secre... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23916"
] | [
"TIM-barrel_EndoS"
] | [
490
] | 1 | [
"EC"
] | [
"3.2.1.96"
] | [
"EC:3.2.1.96"
] | 1 | [
"1eok",
"1eom",
"4nuy",
"4nuz",
"6e58",
"6en3",
"6kpl",
"6kpm",
"6kpn",
"6kpo",
"6mds",
"6mdv",
"7puj",
"7puk",
"8a49",
"8a64",
"8q5u",
"8uen",
"8ura",
"8uro",
"8w4g",
"8w4i",
"8w4n",
"8x8g"
] | 24 | [
"PUB00120398",
"PUB00151608",
"PUB00151610",
"PUB00155713",
"PUB00160953"
] | [
"11406581",
"24753590",
"29760474",
"12438337",
"35241669"
] | [
"EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG.",
"Crystal structure of Streptococcus pyogenes EndoS, an immunomodulatory endoglycosidase specific for human IgG antibodies.",
"Structural basis for the recognition of complex-type N-glycans by Endoglycosida... | [
2001,
2014,
2018,
2002,
2022
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"bioreactor metagenome"
] | [
440,
48,
1,
1
] | 4 | [] | [] | 0 | true | Domain | Endo-beta-N-acetylglucosaminidase EndoS/F2-like, TIM-barrel domain | Endo-beta-N-acetylglucosaminidase EndoS/F2-like, TIM-barrel domain | EndoS_F2-like_TIM-barrel | 1 |
IPR057017 | 57,017 | F54D1.6-like, C-terminal Sushi-like domain | F54D1_6-like_C | Domain | 328 | false | false | This domain is found towards the C-terminal end of the uncharacterised protein F54D1.6 from Caenorhabditis elegans and similar sequences from worms. It is often found associated to . This domain has a detectable similarity to Sushi domains and is predicted to adopt a similar structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24469"
] | [
"F54D1_6_C"
] | [
328
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Nematoda"
] | [
328
] | 1 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Domain | F54D1.6-like, C-terminal Sushi-like domain | F54D1.6-like, C-terminal Sushi-like domain | F54D1_6-like_C | 3 |
IPR057018 | 57,018 | F54D1.6-like, Ig-like domain | F54D1_6-like_Ig-like | Domain | 360 | false | false | This is an immunoglobulin-like domain of the uncharacterised protein F54D1.6 from Caenorhabditis elegans and similar worm sequences. It is often found associated to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24462"
] | [
"Ig_F54D1_6"
] | [
360
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Protostomia"
] | [
360
] | 1 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Domain | F54D1.6-like, Ig-like domain | F54D1.6-like, Ig-like domain | F54D1_6-like_Ig-like | 5 |
IPR057019 | 57,019 | F54D1.6-like, second Ig-like domain | F54D1_6-like_Ig-like_2 | Domain | 367 | false | false | This is an immunoglobulin-like domain of the uncharacterised protein F54D1.6 from Caenorhabditis elegans and similar worm sequences. It is often found associated to and . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24464"
] | [
"Ig_F54D1_6_2"
] | [
367
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Nematoda"
] | [
367
] | 1 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Domain | F54D1.6-like, second Ig-like domain | F54D1.6-like, second Ig-like domain | F54D1_6-like_Ig-like_2 | 6 |
IPR057020 | 57,020 | Follistatin-related protein 1, EF-hand domain pair | EF-hand_FSTL1 | Domain | 1,642 | false | false | This is the EF-hand domain pair found in human Follistatin -like protein 1 (FSTL1), a secreted glycoprotein involved in angiogenesis, regulation of the immune response, cell proliferation and differentiation [ , ]. EF-hands tend to occur in pairs or higher copy numbers. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23564"
] | [
"EF-hand_FSTL1"
] | [
1642
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-201451",
"R-BTA-381426",
"R-BTA-8957275",
"R-HSA-201451",
"R-HSA-381426",
"R-HSA-8957275",
"R-MMU-201451",
"R-MMU-381426",
"R-MMU-8957275",
"R-RNO-201451",
"R-RNO-381426",
"R-RNO-8957275"
] | [
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-201451",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-201451",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-8957275",
"REACTOME:R-RNO-201451",
"REACTOME:R-RNO-381426",
"REACTOME:R-RNO-... | 12 | [] | 0 | [
"PUB00157905",
"PUB00160030"
] | [
"29212066",
"22265692"
] | [
"Fstl1 Promotes Glioma Growth Through the BMP4/Smad1/5/8 Signaling Pathway.",
"Follistatin-related protein/follistatin-like 1 evokes an innate immune response via CD14 and toll-like receptor 4."
] | [
2017,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
3,
1639
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
3,
1,
7
] | 4 | true | Domain | Follistatin-related protein 1, EF-hand domain pair | Follistatin-related protein 1, EF-hand domain pair | EF-hand_FSTL1 | 1 |
IPR057021 | 57,021 | STRA8, bHLH domain | bHLH_STRA8 | Domain | 563 | false | false | This bHLH domain is found in the family of Stimulated by retinoic acid gene 8 protein (STRA8). This protein is required for the transition into meiosis for both female and male germ cells [ , ]. In female germ cells, it acts as a key effector of the meiotic program and is required for premeiotic DNA replication and sub... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23175"
] | [
"bHLH_STRA8"
] | [
563
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00079035",
"PUB00079036",
"PUB00155559"
] | [
"16461896",
"17115059",
"32054698"
] | [
"Retinoic acid regulates sex-specific timing of meiotic initiation in mice.",
"In germ cells of mouse embryonic ovaries, the decision to enter meiosis precedes premeiotic DNA replication.",
"ZGLP1 is a determinant for the oogenic fate in mice."
] | [
2006,
2006,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"Chordata"
] | [
563
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
2
] | 3 | true | Domain | STRA8, bHLH domain | STRA8, bHLH domain | bHLH_STRA8 | 9 |
IPR057022 | 57,022 | PF0610-like, rubredoxin-like zinc beta-ribbon, C-terminal domain | PF0610-like_Zn_ribbon_C | Domain | 573 | false | false | This domain is found C-terminal in PF0610 protein from Pyrococcus furiosus ( ) and related homologous proteins. This protein has a Zn-ribbon embedded in winged HTH fold. This entry represents the C-terminal domain, which is composed of a rubredoxin-like zinc beta-ribbon domain with two CXXC sequence elements [ ]. The f... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23470"
] | [
"Zn_ribbon_PF0610"
] | [
573
] | 1 | [] | [] | [] | 0 | [
"2gmg"
] | 1 | [
"PUB00041110"
] | [
"17223696"
] | [
"PF0610, a novel winged helix-turn-helix variant possessing a rubredoxin-like Zn ribbon motif from the hyperthermophilic archaeon, Pyrococcus furiosus."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"groundwater metagenome"
] | [
470,
101,
2
] | 3 | [] | [] | 0 | true | Domain | PF0610-like, rubredoxin-like zinc beta-ribbon, C-terminal domain | PF0610-like, rubredoxin-like zinc beta-ribbon, C-terminal domain | PF0610-like_Zn_ribbon_C | 4 |
IPR057024 | 57,024 | FORGETTER1, first zinc ribbon domain | Znr_FGT1_1 | Domain | 1,042 | false | false | This domain is found in the Arabidopsis FORGETTER1 (FGT1) and related plant proteins. The domain represented by this entry is predicted to adopt a zinc ribbon fold and it is the first of the predicted pair of two. FGT1 mediates stress-induced chromatin memory by modulating nucleosome occupancy [ ]. This protein interac... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23547"
] | [
"Zn_ribbon_FGT1_1"
] | [
1042
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00083119"
] | [
"27680998"
] | [
"Arabidopsis FORGETTER1 mediates stress-induced chromatin memory through nucleosome remodeling."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1042
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
13,
15
] | 3 | true | Domain | FORGETTER1, first zinc ribbon domain | FORGETTER1, first zinc ribbon domain | Znr_FGT1_1 | 4 |
IPR057025 | 57,025 | FORGETTER1, second zinc ribbon domain | Znr_FGT1_2 | Domain | 1,156 | false | false | This domain is found in the Arabidopsis FORGETTER1 (FGT1) and related proteins from plants and some bacterial species. It is predicted to adopt a zinc ribbon fold and it is the second of the predicted pair of two. FGT1 mediates stress-induced chromatin memory by modulating nucleosome occupancy [ ]. This protein interac... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23548"
] | [
"Zn_ribbon_FGT1_2"
] | [
1156
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00083119"
] | [
"27680998"
] | [
"Arabidopsis FORGETTER1 mediates stress-induced chromatin memory through nucleosome remodeling."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
37,
1119
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
12,
15
] | 3 | true | Domain | FORGETTER1, second zinc ribbon domain | FORGETTER1, second zinc ribbon domain | Znr_FGT1_2 | 3 |
IPR057026 | 57,026 | C2H2-type zinc finger, ascomycetes | Znf-C2H2_ascomycetes | Domain | 1,296 | false | false | This is a presumed C2H2-type zinc finger domain found in a group of uncharacterised proteins from ascomycetes. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24537"
] | [
"zf-C2H2_fungi"
] | [
1296
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1296
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | C2H2-type zinc finger, ascomycetes | C2H2-type zinc finger, ascomycetes | Znf-C2H2_ascomycetes | 7 |
IPR057027 | 57,027 | Mitochondrial 15S rRNA processing factor CCM1-like, TPR repeats | CCM1-like_TPR | Domain | 12,098 | false | false | This entry represents a predicted region of tetratricopeptide repeats (TPR) found in a group of eukaryotic proteins, including mouse Leucine-rich PPR motif-containing protein, mitochondrial (Lrpprc) and Mitochondrial 15S rRNA processing factor CCM1 from Candida albicans. Lrpprc may play a role in RNA metabolism in both... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23276"
] | [
"TPR_24"
] | [
12098
] | 1 | [] | [] | [] | 0 | [
"8r5o",
"8r6s",
"8ras",
"8rdj",
"9epc",
"9evs",
"9gyt"
] | 7 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
6,
12092
] | 2 | [
"Arabidopsis thaliana",
"Drosophila melanogaster",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
48,
5,
1,
2,
40,
5,
1,
68
] | 8 | true | Domain | Mitochondrial 15S rRNA processing factor CCM1-like, TPR repeats | Mitochondrial 15S rRNA processing factor CCM1-like, TPR repeats | CCM1-like_TPR | 4 |
IPR057029 | 57,029 | Tetratricopeptide repeats, fungi 2 | TPR_fung_2 | Domain | 34 | false | false | These predicted tetratricopeptide repeats (TPR) are found in a group of uncharacterised fungal proteins. This domain is often found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23279"
] | [
"TPR_25"
] | [
34
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Sordariomycetes"
] | [
34
] | 1 | [] | [] | 0 | true | Domain | Tetratricopeptide repeats, fungi 2 | Tetratricopeptide repeats, fungi 2 | TPR_fung_2 | 6 |
IPR057030 | 57,030 | E3 ubiquitin-protein ligase listerin, tetratricopeptide repeats region | TPR_Rkr-1 | Domain | 652 | false | false | This region of predicted tetratricopeptide repeats (TPR) is found in E3 ubiquitin-protein ligase listerin from Neurospora crassa (Rkr-1) and similar fungal proteins. Rkr-1 is a component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incomplet... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23280"
] | [
"TPR_26"
] | [
652
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154051"
] | [
"27385828"
] | [
"Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Pezizomycotina"
] | [
652
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | E3 ubiquitin-protein ligase listerin, tetratricopeptide repeats region | E3 ubiquitin-protein ligase listerin, tetratricopeptide repeats region | TPR_Rkr-1 | 4 |
IPR057031 | 57,031 | SFR19-like, C-terminal domain | SFR19-like_C | Domain | 5,077 | false | false | This domain is found at the C-terminal end of human protein SCAF11, SFR19, SCAF1 and PHD and RING finger domain-containing protein 1. These proteins play a role in pre-mRNA alternative splicing by regulating spliceosome assembly [ ]. The SCAF1 C-terminal domain binds to the CTD domain of RNA polymerase II, helping to c... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23030"
] | [
"SCAF11-like_C"
] | [
5077
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00160048",
"PUB00160050"
] | [
"8692929",
"15992770"
] | [
"The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins.",
"Expression of the C-terminal domain of novel human SR-A1 protein: interaction with the CTD domain of RNA polymerase II."
] | [
1996,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
5076,
1
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
5,
27,
2,
18,
14,
10,
9,
8
] | 8 | true | Domain | SFR19-like, C-terminal domain | SFR19-like, C-terminal domain | SFR19-like_C | 5 |
IPR057032 | 57,032 | MBTPS1, fourth domain | MBTPS1_4th | Domain | 2,946 | false | false | This domain is found in the family of serine proteases such as MBTPS1 and SBT6.1 that are involved in regulated intramembrane proteolysis (RIP) of various substrates, playing a crucial role in cellular signalling and regulation. This domain is predicted to fold into a globular structure with significant similarity to d... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23090"
] | [
"MBTPS1_4th"
] | [
2946
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.112",
"R-HSA-1655829",
"R-HSA-381033",
"R-HSA-381426",
"R-HSA-8874177",
"R-HSA-8874211",
"R-HSA-8957275",
"R-HSA-8963889",
"R-MMU-1655829",
"R-MMU-381033",
"R-MMU-381426",
"R-MMU-8874177",
"R-MMU-8874211",
"R-MMU-8957275",
"R-RNO-1655829",
"R-RNO-381033",
"R-RNO-381426",
"R... | [
"EC:3.4.21.112",
"REACTOME:R-HSA-1655829",
"REACTOME:R-HSA-381033",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8874177",
"REACTOME:R-HSA-8874211",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-8963889",
"REACTOME:R-MMU-1655829",
"REACTOME:R-MMU-381033",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-88741... | 20 | [
"8uw8",
"8uwc",
"9csd"
] | 3 | [
"PUB00154941",
"PUB00155736",
"PUB00155737"
] | [
"12782636",
"10644685",
"17662035"
] | [
"A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6.",
"Biosynthesis and enzymatic characterization of human SKI-1/S1P and the processing of its inhibitory prosegment.",
"Salt stress responses in Arabidopsis utiliz... | [
2003,
2000,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mesotoga prima"
] | [
2945,
1
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
1,
3,
4,
2,
3,
11
] | 8 | true | Domain | MBTPS1, fourth domain | MBTPS1, fourth domain | MBTPS1_4th | 1 |
IPR057033 | 57,033 | Isoleucine--tRNA ligase, cytoplasmic, ubiquitin-like domain | Ubiquitin_IARS1 | Domain | 1,785 | false | false | This domain is found in two copies toward the C-terminal end of human Isoleucine--tRNA ligase, cytoplasmic (IARS1) and similar sequences predominantly found in vertebrates. IARS1 catalyses the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23567"
] | [
"Ubiquitin_IARS1"
] | [
1785
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-9856649",
"R-MMU-9856649"
] | [
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649"
] | 4 | [
"7wrs"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1785
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
12,
1,
3
] | 4 | true | Domain | Isoleucine--tRNA ligase, cytoplasmic, ubiquitin-like domain | Isoleucine--tRNA ligase, cytoplasmic, ubiquitin-like domain | Ubiquitin_IARS1 | 1 |
IPR057034 | 57,034 | FNG domain | FNG | Domain | 35 | false | false | This entry shows a β-sandwich structure that has similarity to known carbohydrate binding domain families CBM61 and CBM70. This domain is found at the N-terminal of proteins that contain repeated domains, suggesting these proteins may act as carbohydrate binding adhesins. This domain contains a conserved FNG sequence a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24424"
] | [
"FNG"
] | [
35
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
35
] | 1 | [] | [] | 0 | true | Domain | FNG domain | FNG domain | FNG | 8 |
IPR057035 | 57,035 | FmdE-like, treble clef zinc finger | Znf-Tbcl_FmdE | Domain | 160 | false | false | This treble clef zinc finger is found C-terminal in some members of FmdE family that are implicated in microbial methanogenesis, including from Syntrophus aciditrophicus [ ]. This domain follows the α/β core domain ( ) and contains four invariant cysteine residues that coordinate the zinc atom. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23475"
] | [
"zf-Tbcl_FmdE"
] | [
160
] | 1 | [] | [] | [] | 0 | [
"3d00"
] | 1 | [
"PUB00065983"
] | [
"20944230"
] | [
"Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc finger."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Aduncisulcus paluster",
"Bacteria",
"Methanomada group",
"ecological metagenomes"
] | [
1,
151,
3,
5
] | 4 | [] | [] | 0 | true | Domain | FmdE-like, treble clef zinc finger | FmdE-like, treble clef zinc finger | Znf-Tbcl_FmdE | 5 |
IPR057036 | 57,036 | Endo-acting ulvan lyase, beta-trefoil domain | Beta-tre_PLH30 | Domain | 99 | false | false | This entry represents the β-trefoil domain found in endo-acting ulvan lyase mainly found in bacteroidota. Ulvan lyases degrade the main polysaccharide component of green seaweed cell walls [ , ]. This domain binds to ulvan [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24208"
] | [
"Beta-tre_PLH30"
] | [
99
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00093668",
"PUB00155552",
"PUB00155553"
] | [
"31285597",
"29948117",
"28327560"
] | [
"A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan.",
"Biochemical characterization of an ulvan lyase from the marine flavobacterium Formosa agariphila KMM 3901<sup>T</sup>.",
"Revised domain structure of ulvan lyase and characterization of the first ulvan binding domain."
] | [
2019,
2018,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
99
] | 1 | [] | [] | 0 | true | Domain | Endo-acting ulvan lyase, beta-trefoil domain | Endo-acting ulvan lyase, beta-trefoil domain | Beta-tre_PLH30 | 9 |
IPR057037 | 57,037 | TPR repeat domain, actinomycetes | TPR_rep_actino | Domain | 649 | false | false | These predicted tetratrico peptide repeats (TPR) are found in a group of uncharacterised proteins from actinomycetes. This entry is found C-terminal to in some sequences. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23275"
] | [
"TPR_23"
] | [
649
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
649
] | 1 | [] | [] | 0 | true | Domain | TPR repeat domain, actinomycetes | TPR repeat domain, actinomycetes | TPR_rep_actino | 2 |
IPR057038 | 57,038 | FBX41/ZN365, C2H2-type zinc finger | FBX41/ZN365_Znf-C2H2 | Domain | 1,785 | false | false | This classical C2H2 zinc finger domain is found in F-box only protein 41 (FBX41) and related proteins. including ZN365. Members of the F-box protein family, such as FBX41, are characterised by an approximately 40-amino acid F-box motif. These proteins are substrate recognition component of the SCF complexes. They inter... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23165"
] | [
"zf-C2H2_FBX41"
] | [
1785
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-8951664",
"R-HSA-983168",
"R-MMU-8951664",
"R-MMU-983168"
] | [
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-8951664",
"REACTOME:R-MMU-983168"
] | 4 | [] | 0 | [
"PUB00111886",
"PUB00155931",
"PUB00155932"
] | [
"15520277",
"23966166",
"23776040"
] | [
"Systematic analysis and nomenclature of mammalian F-box proteins.",
"ZNF365 promotes stalled replication forks recovery to maintain genome stability.",
"ZNF365 promotes stability of fragile sites and telomeres."
] | [
2004,
2013,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Shewanella xiamenensis",
"ecological metagenomes"
] | [
5,
1777,
1,
2
] | 4 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
3,
4,
8
] | 4 | true | Domain | FBX41/ZN365, C2H2-type zinc finger | FBX41/ZN365, C2H2-type zinc finger | FBX41/ZN365_Znf-C2H2 | 1 |
IPR057039 | 57,039 | F-box protein At5g52880-like, ARM repeats region | At5g52880_ARM | Domain | 659 | false | false | This domain is found N-terminal in Arabidopsis thaliana F-box protein At5g52880 and related plant proteins. It usually precedes F-box . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24104"
] | [
"At5g52880_ARM"
] | [
659
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Viridiplantae"
] | [
659
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
4,
8
] | 3 | true | Domain | F-box protein At5g52880-like, ARM repeats region | F-box protein At5g52880-like, ARM repeats region | At5g52880_ARM | 1 |
IPR057040 | 57,040 | FAKV Clamp protein | FAKV_Clamp | Family | 3 | false | false | This entry represents the Fako virus (FAKV) Clamp protein ( ) and related sequences. It folds into a complex α/β structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24159"
] | [
"FAKV_Clamp"
] | [
3
] | 1 | [] | [] | [] | 0 | [
"6djy"
] | 1 | [
"PUB00155623"
] | [
"32049031"
] | [
"Arrangement of the Polymerase Complexes inside a Nine-Segmented dsRNA Virus."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Dinovernavirus"
] | [
3
] | 1 | [] | [] | 0 | true | Family | FAKV Clamp protein | FAKV Clamp protein | FAKV_Clamp | 9 |
IPR057041 | 57,041 | SCAP, N-terminal | SCAP_N | Domain | 1,847 | false | false | This entry represents a domain found at the N-terminal of SCAP (Sterol regulatory element-binding protein cleavage-activating protein) and similar animal proteins. This domain is the luminal domain of SCAP, which binds cholesterol [ , , , , ]. SCAP is a key player in the sterol regulatory element-binding protein (SREBP... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24006"
] | [
"SCAP_N"
] | [
1847
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1655829",
"R-MMU-1655829",
"R-RNO-1655829"
] | [
"REACTOME:R-HSA-1655829",
"REACTOME:R-MMU-1655829",
"REACTOME:R-RNO-1655829"
] | 3 | [
"6m49",
"7etw",
"7lkf",
"7lkh"
] | 4 | [
"PUB00062075",
"PUB00062076",
"PUB00062077",
"PUB00062078",
"PUB00062079",
"PUB00071990",
"PUB00109796",
"PUB00155542",
"PUB00155543",
"PUB00160032",
"PUB00160033"
] | [
"12482938",
"10497220",
"15899885",
"15728349",
"17428919",
"21454655",
"9488713",
"34192549",
"33446483",
"15260976",
"27068746"
] | [
"Three mutations in sterol-sensing domain of SCAP block interaction with insig and render SREBP cleavage insensitive to sterols.",
"Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating p... | [
2002,
1999,
2005,
2005,
2007,
2011,
1998,
2021,
2021,
2004,
2016
] | 11 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1847
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
2,
3,
3,
2
] | 6 | true | Domain | SCAP, N-terminal | SCAP, N-terminal | SCAP_N | 2 |
IPR057042 | 57,042 | SCAP, beta-propeller | Beta-prop_SCAP | Domain | 1,531 | false | false | This entry represents the β-propeller domain found at the C-terminal of SCAP (Sterol regulatory element-binding protein cleavage-activating protein). This domain is involved in the interaction with SREBP [ , ]. Members of this entry are specific to animals. SCAP is a key player in the sterol regulatory element-binding ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24017"
] | [
"Beta-prop_SCAP"
] | [
1531
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1655829",
"R-MMU-1655829",
"R-RNO-1655829"
] | [
"REACTOME:R-HSA-1655829",
"REACTOME:R-MMU-1655829",
"REACTOME:R-RNO-1655829"
] | 3 | [
"7lkf",
"7lkh"
] | 2 | [
"PUB00062075",
"PUB00062076",
"PUB00062077",
"PUB00062078",
"PUB00071990",
"PUB00155542",
"PUB00155543",
"PUB00160032",
"PUB00160033"
] | [
"12482938",
"10497220",
"15899885",
"15728349",
"21454655",
"34192549",
"33446483",
"15260976",
"27068746"
] | [
"Three mutations in sterol-sensing domain of SCAP block interaction with insig and render SREBP cleavage insensitive to sterols.",
"Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating p... | [
2002,
1999,
2005,
2005,
2011,
2021,
2021,
2004,
2016
] | 9 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"bird metagenome"
] | [
1530,
1
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
3,
1,
1
] | 5 | true | Domain | SCAP, beta-propeller | SCAP, beta-propeller | Beta-prop_SCAP | 3 |
IPR057043 | 57,043 | PARP14, second type I KH domain | PARP14_KH_2 | Domain | 1,712 | false | false | This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found second in human PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is invol... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23248"
] | [
"KH_PARP14_2"
] | [
1712
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 3 | [] | 0 | [
"PUB00083477",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"Family-wide analysis of poly(ADP-ribose) polymerase activity.",
"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation."
] | [
2005,
2014,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
1712
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
17,
2,
2,
1
] | 4 | true | Domain | PARP14, second type I KH domain | PARP14, second type I KH domain | PARP14_KH_2 | 3 |
IPR057044 | 57,044 | PARP14, first type I KH domain | PARP14_KH_1 | Domain | 1,891 | false | false | This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. It is a KH domain found first in human PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is invol... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23084"
] | [
"KH_PARP14_1"
] | [
1891
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 3 | [] | 0 | [
"PUB00083477",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"Family-wide analysis of poly(ADP-ribose) polymerase activity.",
"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation."
] | [
2005,
2014,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Campylobacter",
"Eumetazoa"
] | [
7,
1884
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
2,
1
] | 4 | true | Domain | PARP14, first type I KH domain | PARP14, first type I KH domain | PARP14_KH_1 | 2 |
IPR057045 | 57,045 | PARP14, third type I KH domain | PARP14_KH_3 | Domain | 1,643 | false | false | This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. It is a KH domain found third in PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23249"
] | [
"KH_PARP14_3"
] | [
1643
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 3 | [] | 0 | [
"PUB00083477",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"Family-wide analysis of poly(ADP-ribose) polymerase activity.",
"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation."
] | [
2005,
2014,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
1643
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
2,
1
] | 4 | true | Domain | PARP14, third type I KH domain | PARP14, third type I KH domain | PARP14_KH_3 | 6 |
IPR057046 | 57,046 | PARP14, fourth type I KH domain | PARP14_KH_4 | Domain | 1,609 | false | false | This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found fourth in PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23251"
] | [
"KH_PARP14_4"
] | [
1609
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 3 | [] | 0 | [
"PUB00083477",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"Family-wide analysis of poly(ADP-ribose) polymerase activity.",
"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation."
] | [
2005,
2014,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
1609
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
2,
1
] | 4 | true | Domain | PARP14, fourth type I KH domain | PARP14, fourth type I KH domain | PARP14_KH_4 | 8 |
IPR057048 | 57,048 | PARP14, sixth type I KH domain | PARP14_KH_6 | Domain | 1,592 | false | false | This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. It is a KH domain found sixth in PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved in ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23253"
] | [
"KH_PARP14_6"
] | [
1592
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 3 | [] | 0 | [
"PUB00083477",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"Family-wide analysis of poly(ADP-ribose) polymerase activity.",
"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation."
] | [
2005,
2014,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1592
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
2,
1
] | 4 | true | Domain | PARP14, sixth type I KH domain | PARP14, sixth type I KH domain | PARP14_KH_6 | 9 |
IPR057049 | 57,049 | PARP14-like, eighth type I KH domain | PARP14_KH_8 | Domain | 2,381 | false | false | This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins including mono-ADP-ribosyltransferase PARP9. It is a KH domain found eighth in PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23254"
] | [
"KH_PARP14_8"
] | [
2381
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.4.2.-",
"PWY-5381",
"PWY-5800",
"PWY-6148",
"PWY-6720",
"PWY-7018",
"PWY-7025",
"PWY-7450",
"PWY-7817",
"PWY-7981",
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"EC:2.4.2.-",
"METACYC:PWY-5381",
"METACYC:PWY-5800",
"METACYC:PWY-6148",
"METACYC:PWY-6720",
"METACYC:PWY-7018",
"METACYC:PWY-7025",
"METACYC:PWY-7450",
"METACYC:PWY-7817",
"METACYC:PWY-7981",
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 13 | [] | 0 | [
"PUB00083477",
"PUB00083478",
"PUB00083479",
"PUB00116104",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"23230272",
"16809771",
"27796300",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8.",
"BAL1 and BBAP ar... | [
2005,
2013,
2006,
2016,
2014,
2008
] | 6 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2381
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
9,
4,
2
] | 4 | true | Domain | PARP14-like, eighth type I KH domain | PARP14-like, eighth type I KH domain | PARP14_KH_8 | 7 |
IPR057050 | 57,050 | PARP14, second RRM domain | RRM_PARP14_2 | Domain | 1,944 | false | false | This domain is found in human Protein mono-ADP- ribosyltransferase PARP14 and related proteins. It is an RRM domain found second in PARP14. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23245"
] | [
"RRM_PARP14_2"
] | [
1944
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631"
] | 3 | [] | 0 | [
"PUB00083477",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"Family-wide analysis of poly(ADP-ribose) polymerase activity.",
"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation."
] | [
2005,
2014,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Deuterostomia"
] | [
1944
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
3,
3,
2
] | 4 | true | Domain | PARP14, second RRM domain | PARP14, second RRM domain | RRM_PARP14_2 | 3 |
IPR057051 | 57,051 | PAR14-like, first RRM domain | PARP14_RPM_1 | Domain | 2,788 | false | false | This domain is found at the N-terminal of proteins homologous to human mono-ADP-ribosyltransferase PARP14. It is also present in E3 ubiquitin-protein ligase DTX3L and RRM containing proteins. It shares significant sequence similarity with NID domain found in IFP35 and Nmi. These domains are predicted to adopt similar s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23222"
] | [
"RRM_PARP14_1"
] | [
2788
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196807",
"R-HSA-9683610",
"R-HSA-9694631",
"R-HSA-983168",
"R-MMU-983168"
] | [
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-983168"
] | 5 | [] | 0 | [
"PUB00083477",
"PUB00089592",
"PUB00116103",
"PUB00116104",
"PUB00124895",
"PUB00146699",
"PUB00155694"
] | [
"16061477",
"12670957",
"26479788",
"27796300",
"19818714",
"25043379",
"18851833"
] | [
"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.",
"The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity.",
"PARP9-DTX3L ubiquitin ligase targets host histone H2... | [
2005,
2003,
2015,
2016,
2009,
2014,
2008
] | 7 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2788
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
17,
4,
7,
5
] | 4 | true | Domain | PAR14-like, first RRM domain | PAR14-like, first RRM domain | PARP14_RPM_1 | 2 |
IPR057053 | 57,053 | ZMYND11/ZMYD8, MYND zinc finger | MYND_ZMYND11_ZMYD8 | Domain | 6,982 | false | false | This entry represents the MYND zinc finger from ZMYND11 and ZMYND8 from human and related sequences. These are chromatin readers that recognise methylated histones; ZMYND11 recognises H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. ZMYND8 recognises histone H3.1 dimethylated at '... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24324"
] | [
"MYND_ZMYND11_ZMYD8"
] | [
6982
] | 1 | [] | [] | [] | 0 | [
"5hda",
"5mq4",
"9wv4"
] | 3 | [
"PUB00085454",
"PUB00103632",
"PUB00103633",
"PUB00155752"
] | [
"27477906",
"36064715",
"31965980",
"26845565"
] | [
"ZMYND8 Reads the Dual Histone Mark H3K4me1-H3K14ac to Antagonize the Expression of Metastasis-Linked Genes.",
"ZMYND8 suppresses MAPT213 LncRNA transcription to promote neuronal differentiation.",
"A novel role of tumor suppressor ZMYND8 in inducing differentiation of breast cancer cells through its dual-histo... | [
2016,
2022,
2020,
2016
] | 4 | [
"IPR002893"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
6982
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
28,
2,
19,
21,
22
] | 6 | true | Domain | ZMYND11/ZMYD8, MYND zinc finger | ZMYND11/ZMYD8, MYND zinc finger | MYND_ZMYND11_ZMYD8 | 9 |
IPR057054 | 57,054 | ZMYND11, coiled-coil | ZMYND11_CC | Domain | 2,294 | false | false | This entry represents a coiled-coil domain that self associates to form a dimeric arrangement found in animal ZMYND11 proteins. This domain is adjacent to a MYND zinc finger [ ]. The Zinc finger MYND domain-containing protein 11 family functions as a chromatin reader, specifically recognising and binding to histone H3.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23461"
] | [
"ZMYND11_CC"
] | [
2294
] | 1 | [] | [] | [] | 0 | [
"5hda"
] | 1 | [
"PUB00015108",
"PUB00085456",
"PUB00102401",
"PUB00102402",
"PUB00155752"
] | [
"10734313",
"24675531",
"24590075",
"16565076",
"26845565"
] | [
"The adenovirus E1A binding protein BS69 is a corepressor of transcription through recruitment of N-CoR.",
"Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome binding.",
"ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression.",
"New insights in... | [
2000,
2014,
2014,
2006,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2294
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
15,
9,
15
] | 4 | true | Domain | ZMYND11, coiled-coil | ZMYND11, coiled-coil | ZMYND11_CC | 3 |
IPR057055 | 57,055 | PRTase associated wHTH domain | wHTH-PRTase_assoc | Domain | 322 | false | false | This entry represents a wHTH domain found at the C-terminal of proteins containing PRTase-CE ( ) domain in the retron antiviral immunity system [ ] and in similar uncharacterised prokaryotic sequences. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24409"
] | [
"wHTH-PRTase_assc"
] | [
322
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155486"
] | [
"37889040"
] | [
"Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
36,
284,
2
] | 3 | [] | [] | 0 | true | Domain | PRTase associated wHTH domain | PRTase associated wHTH domain | wHTH-PRTase_assoc | 8 |
IPR057056 | 57,056 | OLD-like TOPRIM domain | OLD-like_TOPRIM_dom | Domain | 16 | false | false | This entry represents a Toprim domain predicted to act as a nuclease like those seen in the OLD systems [ ]. It is found associated with | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24395"
] | [
"OLD-like_TOPRIM_1"
] | [
16
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155486"
] | [
"37889040"
] | [
"Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
16
] | 1 | [] | [] | 0 | true | Domain | OLD-like TOPRIM domain | OLD-like TOPRIM domain | OLD-like_TOPRIM_dom | 5 |
IPR057057 | 57,057 | Nesprin-1, spectrin repeats region | Spectrin_SYNE1 | Domain | 4,082 | false | false | This entry represents a region of spectrin repeats found in human Nesprin-1/2 (SYNE1/2) and its animal homologues, including Muscle-specific protein 300 kDa from Drosophila melanogaster (Msp300). SYNE1 is a a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to m... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25034"
] | [
"Spectrin_SYNE1"
] | [
4082
] | 1 | [
"REACTOME"
] | [
"R-HSA-1221632"
] | [
"REACTOME:R-HSA-1221632"
] | 1 | [] | 0 | [
"PUB00072122",
"PUB00100207",
"PUB00160005",
"PUB00160043"
] | [
"19596800",
"22927463",
"20724637",
"32066907"
] | [
"Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton.",
"Organelle positioning in muscles requires cooperation between two KASH proteins and microtubules.",
"Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement.",
"A pe... | [
2009,
2012,
2010,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
4082
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
34,
7,
21,
13,
17
] | 5 | true | Domain | Nesprin-1, spectrin repeats region | Nesprin-1, spectrin repeats region | Spectrin_SYNE1 | 2 |
IPR057058 | 57,058 | LTI65/LTI78, NYQTKV repeat | LTI65_LTI78_NYQTKV | Domain | 592 | false | false | This entry represents a disordered region found in LTI78 and LTI65 from Arabidopsis and related plant proteins. This region consists of repeats containing the conserved sequence NYQTKV. It is found N-terminal of the CAP160 repeat ( ). LTI78 and LTI65 are involved in responses to abiotic stress [ , , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23402"
] | [
"LTI65_LTI78_NYQTKV"
] | [
592
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016445",
"PUB00087049",
"PUB00155722"
] | [
"9536054",
"21374086",
"8437577"
] | [
"Characterization of a gene for spinach CAP160 and expression of two spinach cold-acclimation proteins in tobacco.",
"Characterization of abiotic stress-responsive Arabidopsis thaliana RD29A and RD29B genes and evaluation of transgenes.",
"Characterization of the expression of a desiccation-responsive rd29 gene... | [
1998,
2011,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Spermatophyta"
] | [
592
] | 1 | [
"Arabidopsis thaliana"
] | [
16
] | 1 | true | Domain | LTI65/LTI78, NYQTKV repeat | LTI65/LTI78, NYQTKV repeat | LTI65_LTI78_NYQTKV | 8 |
IPR057059 | 57,059 | LTI65/LTI78, PGEED repeat | LTI65/LTI78_PGEED | Domain | 1,345 | false | false | This entry represents a disordered region found in LTI78/LTI65 from Arabidopsis thaliana and related plant proteins. This region consists of repeats containing the conserved PGEED sequence and is located C-terminal of the CAP160 repeat ( ). LTI78 and LTI65 are involved in responses to abiotic stress [ , , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23399"
] | [
"LTI65_PGEED"
] | [
1345
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016445",
"PUB00087049",
"PUB00155722",
"PUB00155723"
] | [
"9536054",
"21374086",
"8437577",
"19470100"
] | [
"Characterization of a gene for spinach CAP160 and expression of two spinach cold-acclimation proteins in tobacco.",
"Characterization of abiotic stress-responsive Arabidopsis thaliana RD29A and RD29B genes and evaluation of transgenes.",
"Characterization of the expression of a desiccation-responsive rd29 gene... | [
1998,
2011,
1993,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Spermatophyta"
] | [
1345
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
22,
10,
17
] | 3 | true | Domain | LTI65/LTI78, PGEED repeat | LTI65/LTI78, PGEED repeat | LTI65/LTI78_PGEED | 2 |
IPR057060 | 57,060 | MBTPS1, third domain | MBTPS1_3rd | Domain | 2,835 | false | false | This domain is found in the family of serine proteases such as MBTPS1 and SBT6.1 that are involved in regulated intramembrane proteolysis (RIP) of various substrates, playing a crucial role in cellular signalling and regulation. This domain is predicted to fold into a globular structure with an Ig-like fold. MBTPS1 pro... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23094"
] | [
"MBTPS1_3rd"
] | [
2835
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21.112",
"R-HSA-1655829",
"R-HSA-381033",
"R-HSA-381426",
"R-HSA-8874177",
"R-HSA-8874211",
"R-HSA-8957275",
"R-HSA-8963889",
"R-MMU-1655829",
"R-MMU-381033",
"R-MMU-381426",
"R-MMU-8874177",
"R-MMU-8874211",
"R-MMU-8957275",
"R-RNO-1655829",
"R-RNO-381033",
"R-RNO-381426",
"R... | [
"EC:3.4.21.112",
"REACTOME:R-HSA-1655829",
"REACTOME:R-HSA-381033",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8874177",
"REACTOME:R-HSA-8874211",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-8963889",
"REACTOME:R-MMU-1655829",
"REACTOME:R-MMU-381033",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-88741... | 20 | [
"8uw8",
"8uwc",
"9csd"
] | 3 | [
"PUB00154941",
"PUB00155736",
"PUB00155737"
] | [
"12782636",
"10644685",
"17662035"
] | [
"A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6.",
"Biosynthesis and enzymatic characterization of human SKI-1/S1P and the processing of its inhibitory prosegment.",
"Salt stress responses in Arabidopsis utiliz... | [
2003,
2000,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2835
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
2,
2,
4,
2,
3,
11
] | 8 | true | Domain | MBTPS1, third domain | MBTPS1, third domain | MBTPS1_3rd | 7 |
IPR057061 | 57,061 | PLCG, EF-hand domain 2 | PLCG_EF-hand_2 | Domain | 3,840 | false | false | This entry represents an EF-hand like domain found in animal 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma proteins (PLCG). PLCG1 plays a role in actin reorganisation and cell migration [ ]. PLGC1 has a critical role in maintaining immune homeostasis [ ]. PLCG2 is a crucial enzyme in transmembrane sig... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23583"
] | [
"EF_HAND_2_PLCG"
] | [
3840
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.4.11",
"PWY-6351",
"PWY-6367",
"PWY-7039",
"PWY-8052",
"R-CEL-1855204",
"R-HSA-114604",
"R-HSA-1169408",
"R-HSA-1236382",
"R-HSA-1251932",
"R-HSA-1489509",
"R-HSA-166016",
"R-HSA-167021",
"R-HSA-1855204",
"R-HSA-186763",
"R-HSA-201556",
"R-HSA-202433",
"R-HSA-2029485",
"R-HS... | [
"EC:3.1.4.11",
"METACYC:PWY-6351",
"METACYC:PWY-6367",
"METACYC:PWY-7039",
"METACYC:PWY-8052",
"REACTOME:R-CEL-1855204",
"REACTOME:R-HSA-114604",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-1236382",
"REACTOME:R-HSA-1251932",
"REACTOME:R-HSA-1489509",
"REACTOME:R-HSA-166016",
"REACTOME:R-HSA-1... | 96 | [
"6pbc",
"7t8t",
"7z3j",
"8jqg",
"8jqh",
"8jqi",
"8qju",
"8t7c",
"9qb7"
] | 9 | [
"PUB00068259",
"PUB00068851",
"PUB00082318",
"PUB00155618",
"PUB00159010",
"PUB00160055",
"PUB00160056",
"PUB00160057"
] | [
"17229814",
"23000145",
"15194811",
"31889510",
"37422272",
"31918402",
"33929486",
"37371495"
] | [
"Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration.",
"A hypermorphic missense mutation in PLCG2, encoding phospholipase Cγ2, causes a dominantly inherited autoinflammatory disease with immunodeficiency.",
"Inositol 1,4,5-trisphosphate signaling regulates rhythmic contract... | [
2007,
2012,
2004,
2019,
2023,
2020,
2021,
2023
] | 8 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3840
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
8,
2,
8,
6,
10
] | 6 | true | Domain | PLCG, EF-hand domain 2 | PLCG, EF-hand domain 2 | PLCG_EF-hand_2 | 6 |
IPR057062 | 57,062 | Immunity protein TriTu | TriTu | Family | 185 | false | false | This entry represents the immunity protein TriTu from Salmonella enterica and related batcerial proteins. TriTu is a part of the TreTu/TriTu toxin/antitoxin system. TriTu immunity protein neutralises TreTu activity by acting like a lid that closes the TreTu catalytic site and traps the NAD+ [ ]. TriTu is composed of a ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24689"
] | [
"TriTu"
] | [
185
] | 1 | [] | [] | [] | 0 | [
"7zhm"
] | 1 | [
"PUB00155886"
] | [
"36484105"
] | [
"Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
185
] | 1 | [] | [] | 0 | true | Family | Immunity protein TriTu | Immunity protein TriTu | TriTu | 1 |
IPR057063 | 57,063 | Inactive Sirtuin | iSirtuin | Domain | 18 | false | false | This entry represents an inactive sirtuin domain found mainly in proteobacteria [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24403"
] | [
"iSirtuin"
] | [
18
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155486"
] | [
"37889040"
] | [
"Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"mine drainage metagenome"
] | [
16,
2
] | 2 | [] | [] | 0 | true | Domain | Inactive Sirtuin | Inactive Sirtuin | iSirtuin | 5 |
IPR057064 | 57,064 | p53, central conserved site | P53_central_site | Conserved_site | 4,705 | false | false | This entry represents a conserved stretch of 13 residues located in the central region of the p53. This region, known as domain IV in [ ], is involved (along with an adjacent region) in the binding of the large T antigen of SV40. In homo sapiens, this region is the focus of a variety of point mutations in cancerous tum... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00348"
] | [
"P53"
] | [
4705
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-2559580",
"R-BTA-2559586",
"R-BTA-349425",
"R-BTA-5689880",
"R-BTA-5689896",
"R-BTA-5693565",
"R-BTA-6804754",
"R-BTA-6804756",
"R-BTA-6804757",
"R-BTA-6804758",
"R-BTA-6804759",
"R-BTA-6804760",
"R-BTA-6811555",
"R-BTA-69473",
"R-BTA-69481",
"R-BTA-69541",
"R-BTA-69895",
"R... | [
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-349425",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-5689896",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-6804754",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6804757",
"REACTOME:R-BTA-6804758",
"REACTOME:R-BTA-6804759",
"REACTOME... | 150 | [
"1gzh",
"1hu8",
"1kzy",
"1tsr",
"1tup",
"1ycs",
"2ac0",
"2ady",
"2ahi",
"2ata",
"2fej",
"2geq",
"2h1l",
"2ioi",
"2iom",
"2ioo",
"2mej",
"2ocj",
"2p52",
"2pcx",
"2rmn",
"2xwc",
"2xwr",
"2ybg",
"3exj",
"3exl",
"3igl",
"3kmd",
"3kz8",
"3q01",
"3q05",
"3q06"... | 119 | [
"PUB00000596",
"PUB00001893",
"PUB00002729",
"PUB00004096",
"PUB00004490",
"PUB00017914"
] | [
"2142001",
"2137806",
"1639769",
"2046748",
"2142762",
"10203277"
] | [
"Tumor suppressor genes: the p53 and retinoblastoma sensitivity genes and gene products.",
"p53: oncogene or anti-oncogene?",
"The p53 tumor suppressor protein, a modulator of cell proliferation.",
"The p53 tumour suppressor gene.",
"Structural aspects of the p53 protein in relation to gene evolution.",
"... | [
1990,
1990,
1992,
1991,
1990,
1999
] | 6 | [] | [] | 0 | 0 | null | [
"Vertebrata",
"bird metagenome"
] | [
4704,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
69,
91,
23,
16
] | 4 | true | Conserved_site | p53, central conserved site | p53, central conserved site | P53_central_site | 2 |
IPR057066 | 57,066 | ILCR1, Ig-like domain | Ig_ILCR1 | Domain | 437 | false | false | This domain is found in ILCR1 from Caenorhabditis elegans and related proteins. The domain represented by this entry is predicted to adopt a β-sandwich with an Ig-like topology. Interleukin cytokine receptor-related protein 1 (ILCR1) forms a receptor complex together with receptor ILCR2, which upon activation acts as a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23608"
] | [
"Ig_ILCR1"
] | [
437
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00090974",
"PUB00160427"
] | [
"28099418",
"28329701"
] | [
"IL-17 is a neuromodulator of Caenorhabditis elegans sensory responses.",
"Interleukin-17: Why the Worms Squirm."
] | [
2017,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Bilateria"
] | [
2,
435
] | 2 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Domain | ILCR1, Ig-like domain | ILCR1, Ig-like domain | Ig_ILCR1 | 3 |
IPR057067 | 57,067 | Partner of xrn-2 protein 1-like, C-terminal | Paxt-1-like_C | Domain | 74 | false | false | This domain is found at the C-terminal end of Partner of xrn-2 protein 1 from Caenorhabditis elegans (Paxt-1) and similar sequences from worms. Paxt-1 plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA in complex with the exoribonuclease xrn-2 [ ].... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24799"
] | [
"Paxt-1_C"
] | [
74
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075685",
"PUB00087111"
] | [
"24462208",
"26779609"
] | [
"PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain.",
"Structural basis and function of XRN2 binding by XTB domains."
] | [
2014,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
74
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | Partner of xrn-2 protein 1-like, C-terminal | Partner of xrn-2 protein 1-like, C-terminal | Paxt-1-like_C | 4 |
IPR057068 | 57,068 | IML1, N-terminal, fungi | IML1_N_fung | Domain | 491 | false | false | This entry represents the N-terminal double-psi β-barrel domain found in vacuolar membrane-associated IML1 proteins from fungi. In Saccharomyces cerevisiae, Iml1 is a GAP subunit of both the SEA (Seh1-associated) and Iml1 complexes (Iml1-Npr2-Npr3). SEA complex is associated dynamically with the vacuole and is involved... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24438"
] | [
"IML1_N_fung"
] | [
491
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00063317",
"PUB00063318",
"PUB00087311",
"PUB00092863"
] | [
"21454883",
"21900499",
"23716719",
"25457612"
] | [
"A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae.",
"Selective regulation of autophagy by the Iml1-Npr2-Npr3 complex in the absence of nitrogen starvation.",
"Amino acid deprivation inhibits TORC1 through a GTPase-activating prot... | [
2011,
2011,
2013,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
491
] | 1 | [
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1
] | 1 | true | Domain | IML1, N-terminal, fungi | IML1, N-terminal, fungi | IML1_N_fung | 2 |
IPR057069 | 57,069 | Immunoglobulin A1 protease autotransporter, domain 2 | IgA0_D2 | Domain | 84 | false | false | This entry represents what has been called domain 2 of the immunoglobulin A1 protease autotransporter (IgA0) from proteobacteria. These proteases serve as virulence factors by cleaving IgA in humans and great apes [ ]. This domain has been suggested to be involved in protein-protein interactions and may contribute to s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24077"
] | [
"IgA0_D2"
] | [
84
] | 1 | [
"EC"
] | [
"3.4.21.72"
] | [
"EC:3.4.21.72"
] | 1 | [
"3h09"
] | 1 | [
"PUB00052228",
"PUB00155667"
] | [
"19393662",
"2105953"
] | [
"Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease the structure of haemophilus influenzae immunoglobulin A1 protease.",
"Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids."
] | [
2009,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
84
] | 1 | [] | [] | 0 | true | Domain | Immunoglobulin A1 protease autotransporter, domain 2 | Immunoglobulin A1 protease autotransporter, domain 2 | IgA0_D2 | 4 |
IPR057070 | 57,070 | Inactive HKD-Rease | HKD_inactive | Domain | 15 | false | false | This entry represents an inactive HKD-REase domain typically fused to the ParB-CE domain [ ] and predicted to be involved in conflict [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24402"
] | [
"iHKD"
] | [
15
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155486"
] | [
"37889040"
] | [
"Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
15
] | 1 | [] | [] | 0 | true | Domain | Inactive HKD-Rease | Inactive HKD-Rease | HKD_inactive | 5 |
IPR057071 | 57,071 | INO2 bHLH domain | bHLH_INO2 | Domain | 86 | false | false | The founding member of this family is the bHLH domain of yeast protein INO2. It is mainly found in saccharomycetales and pichiales yeast. This protein is a positive regulatory factor involved in the transcriptional regulation of phospholipid biosynthetic genes. INO2 forms a heterodimer with INO4 and this complex specif... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23179"
] | [
"bHLH_INO2"
] | [
86
] | 1 | [] | [] | [] | 0 | [
"7xq5"
] | 1 | [
"PUB00155555"
] | [
"35886947"
] | [
"Structural Analysis of Ino2p/Ino4p Mutual Interactions and Their Binding Interface with Promoter DNA."
] | [
2022
] | 1 | [
"IPR011598"
] | [] | 1 | 0 | 1 | [
"Saccharomycotina"
] | [
86
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | INO2 bHLH domain | INO2 bHLH domain | bHLH_INO2 | 6 |
IPR057072 | 57,072 | INO4, bHLH domain | bHLH_INO4 | Domain | 506 | false | false | The founding member of this family is the bHLH domain of yeast protein INO4. This protein is a positive regulatory factor involved in the transcriptional regulation of phospholipid biosynthetic genes. INO4 forms a heterodimer with INO2 and this complex specifically recognises the inositol/choline-responsive element, fo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23181"
] | [
"bHLH_INO4"
] | [
506
] | 1 | [] | [] | [] | 0 | [
"7xq5"
] | 1 | [
"PUB00155555"
] | [
"35886947"
] | [
"Structural Analysis of Ino2p/Ino4p Mutual Interactions and Their Binding Interface with Promoter DNA."
] | [
2022
] | 1 | [
"IPR011598"
] | [] | 1 | 0 | 1 | [
"Fungi"
] | [
506
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | INO4, bHLH domain | INO4, bHLH domain | bHLH_INO4 | 5 |
IPR057073 | 57,073 | Integrin beta, epidermal growth factor-like domain 2 | EGF_integrin_2 | Domain | 12,939 | false | false | This entry represents the second EGF-like domain that is found in several integrin beta proteins, including integrin beta-1/2/3/5/6/8. This domain has two characteristically long loops. EGF-like domains in beta subunits contain three disulphide groups with the same connectivity as in other EGF domains. The disulphide b... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23105"
] | [
"EGF_integrin"
] | [
12939
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1566948",
"R-BTA-166016",
"R-BTA-198933",
"R-BTA-202733",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA-2173789",
"R-BTA-3000178",
"R-BTA-6798695",
"R-CEL-114608",
"R-CEL-1236973",
"R-CEL-1566977",
"R-CEL-198933",
"R-CEL-202733",
"R-CEL-210991",
"R-CEL-2129379",
"R-CEL-216083",
"R... | [
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-3000178",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-1236973",
"REACTOME:R-C... | 166 | [
"1jv2",
"1l5g",
"1m1x",
"1u8c",
"2p26",
"2p28",
"3fcs",
"3ije",
"3k6s",
"3k71",
"3k72",
"4cak",
"4g1e",
"4g1m",
"4mmx",
"4mmy",
"4mmz",
"4neh",
"4nen",
"4o02",
"4um8",
"5e6w",
"5e6x",
"5es4",
"6avq",
"6avr",
"6avu",
"6bxb",
"6bxf",
"6bxj",
"6ckb",
"6djp"... | 76 | [
"PUB00006148",
"PUB00009789",
"PUB00015915",
"PUB00015985",
"PUB00026539",
"PUB00035000",
"PUB00035002",
"PUB00048597",
"PUB00051936",
"PUB00054805",
"PUB00057248",
"PUB00152567",
"PUB00160072",
"PUB00160425",
"PUB00160426"
] | [
"9009218",
"12297042",
"14689578",
"2467745",
"11546839",
"12361595",
"12234368",
"17673459",
"19111664",
"20033057",
"12388743",
"19704023",
"11572973",
"28510180",
"22308022"
] | [
"A structure prediction for the ligand-binding region of the integrin beta subunit: evidence for the presence of a von Willebrand factor A domain.",
"Integrins: bidirectional, allosteric signaling machines.",
"Integrin clipping: a novel adhesion switch?",
"A novel vitronectin receptor integrin (alpha v beta x... | [
1997,
2002,
2004,
1989,
2001,
2002,
2002,
2007,
2008,
2010,
2002,
2009,
2001,
2014,
2012
] | 15 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
12939
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
34,
5,
33,
18,
30
] | 6 | true | Domain | Integrin beta, epidermal growth factor-like domain 2 | Integrin beta, epidermal growth factor-like domain 2 | EGF_integrin_2 | 3 |
IPR057074 | 57,074 | Ionotropic receptor 75a/84a, N-terminal | IR75A/84a_N | Domain | 1,541 | false | false | This entry represents the N-terminal domain of the Ionotropic receptor 75a (IR75A), 84a (IR84A) from Drosophila melanogaster and related sequences from arthropods. IR75A is an odorant receptor for acetic and propionic acid. It functions as part of an olfactory receptor complex including the ionotropic receptor corecept... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24576"
] | [
"IR75A_N"
] | [
1541
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00072716",
"PUB00072717",
"PUB00155688",
"PUB00163352",
"PUB00163353"
] | [
"21220098",
"19135896",
"27776356",
"21964331",
"38114448"
] | [
"Functional architecture of olfactory ionotropic glutamate receptors.",
"Variant ionotropic glutamate receptors as chemosensory receptors in Drosophila.",
"Olfactory receptor pseudo-pseudogenes.",
"An olfactory receptor for food-derived odours promotes male courtship in Drosophila.",
"Ionotropic receptors m... | [
2011,
2009,
2016,
2011,
2024
] | 5 | [] | [] | 0 | 0 | null | [
"Pancrustacea"
] | [
1541
] | 1 | [
"Drosophila melanogaster"
] | [
9
] | 1 | true | Domain | Ionotropic receptor 75a/84a, N-terminal | Ionotropic receptor 75a/84a, N-terminal | IR75A/84a_N | 2 |
IPR057075 | 57,075 | Iron-related transcription factor 3, bHLH domain | bHLH_IRO3 | Domain | 5,410 | false | false | This entry represents the bHLH domain of iron-related transcription factor 3 from Oryza sativa and similar plant proteins. This transcription factor acts as a negative regulator of the iron deficiency response and plays an important role for iron homeostasis in rice [ ]. This domain is also found in a number of plant t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23177"
] | [
"bHLH_IRO3"
] | [
5410
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00096487",
"PUB00155556",
"PUB00160073",
"PUB00160074"
] | [
"31962167",
"20699001",
"25617318",
"36787175"
] | [
"bHLH121 Functions as a Direct Link that Facilitates the Activation of FIT by bHLH IVc Transcription Factors for Maintaining Fe Homeostasis in Arabidopsis.",
"Identification of a novel iron regulated basic helix-loop-helix protein involved in Fe homeostasis in Oryza sativa.",
"OsJAZ9 acts as a transcriptional r... | [
2020,
2010,
2015,
2023
] | 4 | [
"IPR011598"
] | [] | 1 | 0 | 1 | [
"Ectobacillus ponti",
"Eukaryota"
] | [
1,
5409
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
38,
19,
63
] | 3 | true | Domain | Iron-related transcription factor 3, bHLH domain | Iron-related transcription factor 3, bHLH domain | bHLH_IRO3 | 5 |
IPR057076 | 57,076 | HTH-like domain, caenorhabditis | HTH_71 | Domain | 19 | false | false | This presumed domain is found towards the N-terminal end of a group of uncharacterised proteins from Caenorhabditis. It shares significant sequence similarity to the HTH 3-helical bundle domains and it is predicted to adopt a similar structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23737"
] | [
"HTH_71"
] | [
19
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Caenorhabditis"
] | [
19
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | HTH-like domain, caenorhabditis | HTH-like domain, caenorhabditis | HTH_71 | 7 |
IPR057077 | 57,077 | HTH-like domain 2, caenorhabditis | HTH_72 | Domain | 24 | false | false | This domain is found C-terminal to in uncharacterised proteins from Caenorhabditis. It shares sequence similarity to the HTH 3-helical bundle domains and it is predicted to adopt a similar structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23739"
] | [
"HTH_72"
] | [
24
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Caenorhabditis"
] | [
24
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | HTH-like domain 2, caenorhabditis | HTH-like domain 2, caenorhabditis | HTH_72 | 2 |
IPR057078 | 57,078 | HYR-like domain | HYR-4C | Domain | 739 | false | false | This domain is found sometimes in tandem arrays in bacterial cell surface proteins. It contains four cysteines that appear to be likely to form two disulphide bridges between adjacent pairs of domains. It seems likely that these domains form rigid stalks. These domains show sequence similarity to HYR domains. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23237"
] | [
"HYR_4C"
] | [
739
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
731,
4,
4
] | 3 | [] | [] | 0 | true | Domain | HYR-like domain | HYR-like domain | HYR-4C | 2 |
IPR057079 | 57,079 | Type 4 adapter protein IcmW-like | IcmW-like | Family | 184 | false | false | This entry represent the type 4 adapter protein IcmW from Legionella pneumophila and related proteins found mainly in Gammaproteobacteria. IcmW is a component of Type 4B secretion (T4BS) system that translocates over 300 effectors into the host cell during infection. This protein is part of a subcomplex which recruits ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23130"
] | [
"IcmW"
] | [
184
] | 1 | [] | [] | [] | 0 | [
"5x1e",
"5x90",
"5xnb",
"7bwk"
] | 4 | [
"PUB00020742",
"PUB00100787",
"PUB00153340"
] | [
"15661013",
"32513920",
"18069892"
] | [
"The Legionella IcmS-IcmW protein complex is important for Dot/Icm-mediated protein translocation.",
"Mechanism of effector capture and delivery by the type IV secretion system from Legionella pneumophila.",
"The Legionella pneumophila IcmSW complex interacts with multiple Dot/Icm effectors to facilitate type I... | [
2005,
2020,
2007
] | 3 | [] | [
"IPR049919"
] | 0 | 1 | 0 | [
"Pseudomonadati",
"marine sediment metagenome"
] | [
182,
2
] | 2 | [] | [] | 0 | true | Family | Type 4 adapter protein IcmW-like | Type 4 adapter protein IcmW-like | IcmW-like | 9 |
IPR057080 | 57,080 | SMP domain-containing protein, PH domain | PH_SMPa | Domain | 967 | false | false | This entry represents a PH-like domain found at the N-terminal end of a group of uncharacterised plant proteins that contain an SMP domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23065"
] | [
"PH_SMPa"
] | [
967
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
967
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
1,
7
] | 3 | true | Domain | SMP domain-containing protein, PH domain | SMP domain-containing protein, PH domain | PH_SMPa | 3 |
IPR057081 | 57,081 | PH domain, N-terminal, fungi | PH_N | Domain | 937 | false | false | This PH domain is found at the N-terminal one of a pair of PH domains that is found in a group of uncharacterised fungal proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23074"
] | [
"PH_FT_N"
] | [
937
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pezizomycotina"
] | [
937
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Domain | PH domain, N-terminal, fungi | PH domain, N-terminal, fungi | PH_N | 5 |
IPR057082 | 57,082 | PH domain, C-terminal, fungi | PH_C | Domain | 943 | false | false | This PH domain is found as the C-terminal one of a pair of PH domains that is found in a group of uncharacterised fungal proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23076"
] | [
"PH_FT_C"
] | [
943
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pezizomycotina"
] | [
943
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Domain | PH domain, C-terminal, fungi | PH domain, C-terminal, fungi | PH_C | 9 |
IPR057084 | 57,084 | Phage integrase, N-terminal domain | Int_N | Domain | 4,009 | false | false | This domain is found at the N-terminal end of phage integrases, including the member from Escherichia phage P2. This protein is necessary for integration of the phage into the host genome by site-specific recombination [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24624"
] | [
"Int_N"
] | [
4009
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.-",
"PWY-6322",
"PWY-6626",
"PWY-6749",
"PWY-6955",
"PWY-6998",
"PWY-7127",
"PWY-7419",
"PWY-7529",
"PWY-7706",
"PWY-7719",
"PWY-7735",
"PWY-7737",
"PWY-7769",
"PWY-7888",
"PWY-7904",
"PWY-8117",
"PWY-8179"
] | [
"EC:2.7.7.-",
"METACYC:PWY-6322",
"METACYC:PWY-6626",
"METACYC:PWY-6749",
"METACYC:PWY-6955",
"METACYC:PWY-6998",
"METACYC:PWY-7127",
"METACYC:PWY-7419",
"METACYC:PWY-7529",
"METACYC:PWY-7706",
"METACYC:PWY-7719",
"METACYC:PWY-7735",
"METACYC:PWY-7737",
"METACYC:PWY-7769",
"METACYC:PWY-7... | 18 | [
"5c6k"
] | 1 | [
"PUB00155683"
] | [
"26453836"
] | [
"Crystal structure of the bacteriophage P2 integrase catalytic domain."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"Viruses",
"metagenomes"
] | [
3852,
4,
114,
39
] | 4 | [] | [] | 0 | true | Domain | Phage integrase, N-terminal domain | Phage integrase, N-terminal domain | Int_N | 5 |
IPR057086 | 57,086 | Irg-7, N-terminal galactose binding domain | GBD_Irg-7_N | Domain | 223 | false | false | This domain is found N-terminal in the nematode Irg-7 protein and related proteins. The domain is predicted to fold into a β-sandwich with topology similar to galactose-binding domains. Irg-7 is known as mediator of longevity in germlineless animals. It plays a role in the innate immunity, probably via the atf-7 pathwa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23623"
] | [
"GBD_IRG7_N"
] | [
223
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155634"
] | [
"28196094"
] | [
"Innate immunity mediated longevity and longevity induced by germ cell removal converge on the C-type lectin domain protein IRG-7."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
223
] | 1 | [
"Caenorhabditis elegans"
] | [
4
] | 1 | true | Domain | Irg-7, N-terminal galactose binding domain | Irg-7, N-terminal galactose binding domain | GBD_Irg-7_N | 4 |
IPR057087 | 57,087 | Phage neck terminator protein gp12-like | Gp12-like | Domain | 2,335 | false | false | This entry represents the neck terminator protein gp12 from cyanophage Pam3 [ ]. Six gp12 subunits form a hexameric ring that terminates neck assembly and links to the tail tube/sheath. Each subunit has an N-terminal loop, a conserved globular domain, and a protruding β-sheet domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23961"
] | [
"Phage_tail_terminator_9"
] | [
2335
] | 1 | [] | [] | [] | 0 | [
"7kjk",
"8hdr",
"9c39",
"9cc7",
"9mjn"
] | 5 | [
"PUB00154413"
] | [
"36656854"
] | [
"Fine structure and assembly pattern of a minimal myophage Pam3."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18)",
"Bacteria",
"Opisthokonta",
"Viruses",
"metagenomes"
] | [
1,
1700,
6,
609,
19
] | 5 | [] | [] | 0 | true | Domain | Phage neck terminator protein gp12-like | Phage neck terminator protein gp12-like | Gp12-like | 2 |
IPR057089 | 57,089 | T-cell immunomodulatory protein TIP, C2 domain | C2_TIP | Domain | 2,643 | false | false | This entry represents the N-terminal C2 domain present in T-cell immunomodulatory protein TIP proteins (enconded by gene ITFG1). In mammals, TIP promotes the adhesion between neighbouring cells through its extracellular domain and regulates microtubule dynamics through its intracellular domain [ ]. In parasites, it may... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23122"
] | [
"C2_ITFG1"
] | [
2643
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00033903",
"PUB00056730",
"PUB00076894",
"PUB00160423"
] | [
"12368864",
"12833085",
"25437307",
"1236886"
] | [
"Genome sequence of the human malaria parasite Plasmodium falciparum.",
"A TIP on malaria (genomics).",
"LINKIN, a new transmembrane protein necessary for cell adhesion.",
"[First trials with the cockscomb candidiasis test as an in vitro screening model for antifungal agents]."
] | [
2002,
2003,
2014,
1975
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2643
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
6,
6,
1,
6
] | 6 | true | Domain | T-cell immunomodulatory protein TIP, C2 domain | T-cell immunomodulatory protein TIP, C2 domain | C2_TIP | 6 |
IPR057090 | 57,090 | Kinesin-like protein KIF26A/B, helical domain | HTH_KIF26A_B_1st | Domain | 1,828 | false | false | This domain is found in the kinesin-like protein KIF26A/B from Mus musculus and similar sequences mainly found in vertebrates. KIF26A plays a key role in enteric neurone development, while KIF26B is essential for embryonic kidney development [ ]. This domain is predicted to form an α-helical bundle. Kinesin [ , , ] is ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23081"
] | [
"HTH_KIF26A_B_1st"
] | [
1828
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2132295",
"R-HSA-6811434",
"R-HSA-983189",
"R-MMU-2132295",
"R-MMU-6811434",
"R-MMU-983189"
] | [
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-6811434",
"REACTOME:R-HSA-983189",
"REACTOME:R-MMU-2132295",
"REACTOME:R-MMU-6811434",
"REACTOME:R-MMU-983189"
] | 6 | [] | 0 | [
"PUB00000075",
"PUB00004968",
"PUB00005510",
"PUB00160076"
] | [
"2142876",
"8542443",
"14732151",
"36228617"
] | [
"Motor proteins of cytoplasmic microtubules.",
"Motor proteins 1: kinesins.",
"A kinesin medley: biochemical and functional heterogeneity.",
"Loss of non-motor kinesin KIF26A causes congenital brain malformations via dysregulated neuronal migration and axonal growth as well as apoptosis."
] | [
1990,
1995,
1995,
2022
] | 4 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
1828
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
7,
4,
4
] | 4 | true | Domain | Kinesin-like protein KIF26A/B, helical domain | Kinesin-like protein KIF26A/B, helical domain | HTH_KIF26A_B_1st | 1 |
IPR057091 | 57,091 | Kinetochore protein NDC80 loop region | NDC80_loop | Domain | 2,027 | false | false | This entry represents the so-called NDC80 'loop' structure found at the coiled coil C-terminal of kinetochore protein NDC80. NDC80 is a conserved coiled-coil protein that forms the mitotic spindle, which is required for kinetochore integrity and the organisation of stable microtubule binding sites in the outer plate of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24487"
] | [
"NDC80_loop"
] | [
2027
] | 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-GGA-141444",
"R-GGA-2467813",
"R-GGA-2500257",
"R-GGA-5663220",
"R-GGA-9648025",
"R-HSA-141444",
"R-HSA-2467813",
"R-HSA-2500257",
"R-HSA-5663220",
"R-HSA-68877",
"R-HSA-9648025",
"R-MMU-141444",
"R-MMU-2467813",
"R-MMU-2500257",
"R-MMU-5663220",
"R-MMU-68877",
"R-MMU-9648025",
... | [
"REACTOME:R-GGA-141444",
"REACTOME:R-GGA-2467813",
"REACTOME:R-GGA-2500257",
"REACTOME:R-GGA-5663220",
"REACTOME:R-GGA-9648025",
"REACTOME:R-HSA-141444",
"REACTOME:R-HSA-2467813",
"REACTOME:R-HSA-2500257",
"REACTOME:R-HSA-5663220",
"REACTOME:R-HSA-68877",
"REACTOME:R-HSA-9648025",
"REACTOME:R-... | 23 | [
"8g0p"
] | 1 | [
"PUB00154936",
"PUB00154937"
] | [
"30409912",
"36883282"
] | [
"Dynamic acetylation of the kinetochore-associated protein HEC1 ensures accurate microtubule-kinetochore attachment.",
"Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface."
] | [
2019,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine sediment metagenome"
] | [
2026,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
4,
2,
1,
3,
1
] | 6 | true | Domain | Kinetochore protein NDC80 loop region | Kinetochore protein NDC80 loop region | NDC80_loop | 4 |
IPR057092 | 57,092 | Kinase D-interacting substrate of 220 kDa-like, SAM domain | SAM_KIDINS220 | Domain | 4,080 | false | false | This is the predicted Sterile alpha motif (SAM) domain of human Kinase D-interacting substrate of 220 kDa (KIDINS220) and similar animal and insect proteins. KIDINS220 promotes a prolonged MAP -kinase signalling by neurotrophins and is involved in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosom... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23307"
] | [
"SAM_KIDINS220"
] | [
4080
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-170984",
"R-DRE-9696270",
"R-DRE-9696273",
"R-HSA-170984",
"R-HSA-9696270",
"R-HSA-9696273",
"R-RNO-170984",
"R-RNO-9696270",
"R-RNO-9696273"
] | [
"REACTOME:R-DRE-170984",
"REACTOME:R-DRE-9696270",
"REACTOME:R-DRE-9696273",
"REACTOME:R-HSA-170984",
"REACTOME:R-HSA-9696270",
"REACTOME:R-HSA-9696273",
"REACTOME:R-RNO-170984",
"REACTOME:R-RNO-9696270",
"REACTOME:R-RNO-9696273"
] | 9 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
4080
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
20,
17,
19,
15,
17
] | 6 | true | Domain | Kinase D-interacting substrate of 220 kDa-like, SAM domain | Kinase D-interacting substrate of 220 kDa-like, SAM domain | SAM_KIDINS220 | 4 |
IPR057094 | 57,094 | K1 capsule-specific polysaccharide lyase, N-terminal domain | K1-lyase_N | Domain | 15 | false | false | This entry represents the N-terminal domain of K1 capsule-specific polysaccharide lyase and related proteins. The N-terminal domain is known as a particle-binding domain. It folds into an open β-barrel structure the curvature of which is completed by an α-helix. Structurally, this domain is very similar to collagen XVI... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24145"
] | [
"K1-lyase_N"
] | [
15
] | 1 | [] | [] | [] | 0 | [
"7w1c",
"7w1d",
"7w1e"
] | 3 | [
"PUB00155689"
] | [
"35130876"
] | [
"Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Caudoviricetes"
] | [
15
] | 1 | [] | [] | 0 | true | Domain | K1 capsule-specific polysaccharide lyase, N-terminal domain | K1 capsule-specific polysaccharide lyase, N-terminal domain | K1-lyase_N | 6 |
IPR057095 | 57,095 | K1 capsule-specific polysaccharide lyase, rider domain | K1-lyase_rider | Domain | 21 | false | false | This entry represents the so-called rider domain of K1 capsule-specific polysaccharide lyase and related proteins. The rider domain folds into a β-barrel, participates in polysaccharide binding to both carbohydrate-binding sites of the enzyme and makes an important contribution to the structural stability of the trimer... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24149"
] | [
"K1-lyase_Rider"
] | [
21
] | 1 | [] | [] | [] | 0 | [
"7w1c",
"7w1d",
"7w1e"
] | 3 | [
"PUB00155689"
] | [
"35130876"
] | [
"Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes"
] | [
3,
18
] | 2 | [] | [] | 0 | true | Domain | K1 capsule-specific polysaccharide lyase, rider domain | K1 capsule-specific polysaccharide lyase, rider domain | K1-lyase_rider | 6 |
IPR057096 | 57,096 | KRIT1/FRMD8, FERM domain C-lobe | KRIT1_FRMD8_FERM_C | Domain | 2,638 | false | false | KRIT1, also known as CCM1, a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins [ ]. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins whose mutations are found in cerebral cavernous malformations, char... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24522"
] | [
"KRIT1_FRMD8_FERM_C"
] | [
2638
] | 1 | [] | [] | [] | 0 | [
"3u7d",
"4dxa",
"4hdo",
"4hdq",
"5d68",
"5mv7",
"5mv8",
"5xbf",
"6oq3",
"6oq4",
"6uzk",
"8su8",
"8t09",
"8t7v"
] | 14 | [
"PUB00062547",
"PUB00091843",
"PUB00091844",
"PUB00154949",
"PUB00154950",
"PUB00160422"
] | [
"23007647",
"17954608",
"22577140",
"29897333",
"29897336",
"38296350"
] | [
"Structural basis of the junctional anchorage of the cerebral cavernous malformations complex.",
"KRIT-1/CCM1 is a Rap1 effector that regulates endothelial cell cell junctions.",
"Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapp... | [
2012,
2007,
2012,
2018,
2018,
2024
] | 6 | [
"IPR000299"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2638
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
2,
5,
4,
7
] | 6 | true | Domain | KRIT1/FRMD8, FERM domain C-lobe | KRIT1/FRMD8, FERM domain C-lobe | KRIT1_FRMD8_FERM_C | 6 |
IPR057097 | 57,097 | LYK3/RLK10-like, LysM domain | LysM_RLK3/10 | Domain | 1,626 | false | false | This entry represents a set of LysM domains found in LysM domain receptor-like kinase family LYRK3, RLK10 ( ) and similar receptors. Plant receptor-like kinases and receptor-like proteins (RLKs or LYRK) ( ) are involved in innate immunity and symbiotic interactions in plants. Members of this family function as cell sur... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23577"
] | [
"LysM_RLK"
] | [
1626
] | 1 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [
"4eby",
"4ebz",
"5ls2",
"6xwe",
"7vs7",
"9h24",
"9h3b",
"9h6v",
"9qrs"
] | 9 | [
"PUB00097130",
"PUB00097131",
"PUB00097132",
"PUB00160418",
"PUB00160419",
"PUB00160420",
"PUB00160421"
] | [
"21070404",
"24964058",
"22891159",
"17586690",
"20971894",
"2947035",
"23498959"
] | [
"Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice.",
"Targeted gene disruption of OsCERK1 reveals its indispensable role in chitin perception and involvement in the peptidoglycan response and immunity in rice.",
"Functional characterization of CEBiP and CE... | [
2010,
2014,
2012,
2007,
2010,
1986,
2013
] | 7 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
1626
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
6,
10
] | 3 | true | Domain | LYK3/RLK10-like, LysM domain | LYK3/RLK10-like, LysM domain | LysM_RLK3/10 | 8 |
IPR057098 | 57,098 | Macrodomain effector MavL | MavL | Domain | 71 | false | false | This entry represents the Legionella macrodomain effector MavL, an ADP-ribosyl hydrolase that reverses the arginine ADP-ribosylation, to minimise potential detrimental effects caused by the modified ubiquitin. Legionella pneumophila mediates atypical ubiquitination of host targets using the SidE effector family [ ]. Th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24754"
] | [
"MavL"
] | [
71
] | 1 | [] | [] | [] | 0 | [
"6omi",
"8dmp",
"8dmq",
"8dmr",
"8dms",
"8ipj",
"8ipw",
"8xep"
] | 8 | [
"PUB00155313"
] | [
"38503748"
] | [
"Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain."
] | [
2024
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
61,
10
] | 2 | [] | [] | 0 | true | Domain | Macrodomain effector MavL | Macrodomain effector MavL | MavL | 7 |
IPR057100 | 57,100 | MAX effector | MAX_effector | Domain | 8 | false | false | This entry represents a family of MAX effectors (for Magnaporthe Avrs and ToxB like) from Magnaporthe oryzae (rice blast fungus). MAX effectors share a conserved β-sandwich structure ( ), despite sharing low sequence similarity between them [ ] They also contain two highly conserved cysteines. Effectors are small and v... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23364"
] | [
"MAX_effector"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"7zjy"
] | 1 | [
"PUB00155735",
"PUB00160413"
] | [
"35657473",
"24586116"
] | [
"<sup>1</sup>H, <sup>13</sup>C, <sup>15</sup> N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae.",
"How do filamentous pathogens deliver effector proteins into plant cells?"
] | [
2022,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Sordariomycetes"
] | [
8
] | 1 | [] | [] | 0 | true | Domain | MAX effector | MAX effector | MAX_effector | 3 |
IPR057101 | 57,101 | Mitochondrial microtubule binder MBB1 | MBB1 | Family | 14 | false | false | This protein family includes the uncharacterised protein mitochondrial microtubule binder MBB1 from Saccharomyces cerevisiae and similar fungal sequences. MBB1 is a small protein that may be involved in metabolic processes [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23508"
] | [
"MBB1"
] | [
14
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00088508",
"PUB00155509"
] | [
"14566057",
"29897761"
] | [
"Predicting protein functions from redundancies in large-scale protein interaction networks.",
"Enrichment-Based Proteogenomics Identifies Microproteins, Missing Proteins, and Novel smORFs in Saccharomyces cerevisiae."
] | [
2003,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Ascomycota"
] | [
14
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Mitochondrial microtubule binder MBB1 | Mitochondrial microtubule binder MBB1 | MBB1 | 5 |
IPR057102 | 57,102 | Non-contractile tail sheath, N-terminal domain | NCTSP_N | Domain | 546 | false | false | This entry represents the N-terminal domain found in the non-contractile tail sheath protein (NCTSP) from Bacteriophage N4 (BPN4). This protein is essential for BPN4 infectivity and it is hypothesized that it mediates binding with target cell receptors [ ]. The function of this domain is unknown. This entry also includ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23844"
] | [
"NCTSP_N"
] | [
546
] | 1 | [] | [] | [] | 0 | [
"9lc0"
] | 1 | [
"PUB00106835"
] | [
"18374942"
] | [
"Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Diploscapter pachys",
"Methanobrevibacter thaueri",
"Viruses",
"hydrothermal vent metagenome"
] | [
433,
1,
1,
107,
4
] | 5 | [] | [] | 0 | true | Domain | Non-contractile tail sheath, N-terminal domain | Non-contractile tail sheath, N-terminal domain | NCTSP_N | 7 |
IPR057103 | 57,103 | NTCP5/P3, N-terminal domain | NTCP5_P3_N | Domain | 600 | false | false | This entry represents the N-terminal domain of Sodium/bile acid cotransporter 5 (NTCP5) and protein P3 from animals, which may have bile acid:sodium symporter activity. This domain is predicted to adopt a β-sandwich fold. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24690"
] | [
"NTCP5_P3_N"
] | [
600
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
600
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
4,
4
] | 4 | true | Domain | NTCP5/P3, N-terminal domain | NTCP5/P3, N-terminal domain | NTCP5_P3_N | 5 |
IPR057104 | 57,104 | Phage putative PDDEXK endonuclease | PDDEXK_14 | Family | 65 | false | false | This entry represents a small family of phage proteins that are structurally related to the PD-(D/E)XK nuclease superfamily. The highest structural similarity is to Holliday junction resolvase Hjc proteins and tRNA-splicing endonucleases from archaebacteria. The exact function of this protein family, which also include... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24579"
] | [
"PDDEXK_14"
] | [
65
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobellus rarus",
"Viruses",
"marine sediment metagenome"
] | [
2,
1,
60,
2
] | 4 | [] | [] | 0 | true | Family | Phage putative PDDEXK endonuclease | Phage putative PDDEXK endonuclease | PDDEXK_14 | 4 |
IPR057105 | 57,105 | Phage ACT-like containing protein | ACT-containing_phage | Family | 91 | false | false | This entry represents an uncharacterised phage protein family. It contains an N-terminal domain that looks like an ACT domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24021"
] | [
"ACT_phage"
] | [
91
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Caudoviricetes"
] | [
91
] | 1 | [] | [] | 0 | true | Family | Phage ACT-like containing protein | Phage ACT-like containing protein | ACT-containing_phage | 9 |
IPR057106 | 57,106 | NXPE, C-terminal | NXPE4_C | Domain | 5,739 | false | false | This domain is found at the C-terminal of NXPE and similar proteins, mainly from animals. This domain is predicted to adopt an α/β structure with similarity to hydrolase domains. Neurexophilins (NXPE) are secreted neuropeptide-like glycoproteins originally discovered as alpha-neurexin ligands and later found to bind to... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24536"
] | [
"NXPE4_C"
] | [
5739
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00160078"
] | [
"31566781"
] | [
"Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5739
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
29,
14,
18,
28
] | 4 | true | Domain | NXPE, C-terminal | NXPE, C-terminal | NXPE4_C | 8 |
IPR057107 | 57,107 | ORF20A | ORF20A | Family | 7 | false | false | This protein family includes ORF20A from Fowl aviadenovirus 4 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23684"
] | [
"ORF20A"
] | [
7
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155774"
] | [
"36851744"
] | [
"Analysis of Fowl Adenovirus 4 Transcriptome by De Novo ORF Prediction Based on Corrected Nanopore Full-Length cDNA Sequencing Data."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Fowl aviadenovirus C"
] | [
7
] | 1 | [] | [] | 0 | true | Family | ORF20A | ORF20A | ORF20A | 2 |
IPR057108 | 57,108 | ORF28 | ORF28 | Family | 6 | false | false | This protein family includes ORF28 from Fowl aviadenovirus 4 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23682"
] | [
"ORF28"
] | [
6
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155774"
] | [
"36851744"
] | [
"Analysis of Fowl Adenovirus 4 Transcriptome by De Novo ORF Prediction Based on Corrected Nanopore Full-Length cDNA Sequencing Data."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Fowl aviadenovirus C"
] | [
6
] | 1 | [] | [] | 0 | true | Family | ORF28 | ORF28 | ORF28 | 2 |
IPR057110 | 57,110 | ORF68, C-terminal | ORF68_C | Domain | 66 | false | false | This entry describes the C-terminal domain in ORF68 from Staphylococcus phage K and similar viral proteins. This domain adopts an all-β configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23624"
] | [
"ORF68_C"
] | [
66
] | 1 | [] | [] | [] | 0 | [
"5m9f",
"9euf",
"9eui"
] | 3 | [
"PUB00160079",
"PUB00160080"
] | [
"35435752",
"24591378"
] | [
"Global Transcriptomic Analysis of Bacteriophage-Host Interactions between a Kayvirus Therapeutic Phage and Staphylococcus aureus.",
"In silico analysis of AHJD-like viruses, Staphylococcus aureus phages S24-1 and S13', and study of phage S24-1 adsorption."
] | [
2022,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
66
] | 1 | [] | [] | 0 | true | Domain | ORF68, C-terminal | ORF68, C-terminal | ORF68_C | 2 |
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