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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR054254 | 54,254 | Domain of unknown function DUF6985 | DUF6985 | Domain | 1,133 | false | false | This entry represents bacterial domain of unknown function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22481"
] | [
"DUF6985"
] | [
1133
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctkfK18",
"bioreactor metagenome"
] | [
1127,
4,
1,
1
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6985 | Domain of unknown function DUF6985 | DUF6985 | 1 |
IPR054255 | 54,255 | Protein of unknown function DUF6986 | DUF6986 | Family | 2,599 | false | false | This entry represents a family of bacterial TIM barrel proteins that are most closely related to . This strongly suggests that these proteins are enzymes with a possibly related function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22484"
] | [
"DUF6986"
] | [
2599
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2580,
2,
17
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF6986 | Protein of unknown function DUF6986 | DUF6986 | 3 |
IPR054256 | 54,256 | Domain of unknown function DUF6987 | DUF6987 | Domain | 1,417 | false | false | This α-helical domain is usually found at the C-terminal of proteins containing repeats of . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22485"
] | [
"DUF6987"
] | [
1417
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Fungi"
] | [
1417
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Domain of unknown function DUF6987 | Domain of unknown function DUF6987 | DUF6987 | 5 |
IPR054257 | 54,257 | Protein of unknown function DUF6988 | DUF6988 | Family | 490 | false | false | This family of uncharacterised proteins is found mainly in Proteobacteria. These proteins are predicted to adopt an α-helical structure. They contain a highly conserved RXXXE-motif and an invariant histidine that may have a functional role. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22491"
] | [
"DUF6988"
] | [
490
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadati",
"mine drainage metagenome"
] | [
4,
484,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF6988 | Protein of unknown function DUF6988 | DUF6988 | 1 |
IPR054259 | 54,259 | Protein of unknown function DUF6990 | DUF6990 | Family | 154 | false | false | This family of proteins is found in bacteria. Proteins in this family are typically between 185 and 199 amino acids in length. There are two semi-conserved sequence motifs: HLA and GFVPYI. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22499"
] | [
"DUF6990"
] | [
154
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
154
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF6990 | Protein of unknown function DUF6990 | DUF6990 | 1 |
IPR054260 | 54,260 | Domain of unknown function DUF6991 | DUF6991 | Domain | 172 | false | false | This entry represents a C-terminal domain of a functionally unknown conserved protein from Bacillus anthracis and related proteins from Bacillus. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22501"
] | [
"DUF6991"
] | [
172
] | 1 | [] | [] | [] | 0 | [
"4fca",
"5ev7"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
172
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6991 | Domain of unknown function DUF6991 | DUF6991 | 8 |
IPR054261 | 54,261 | Protein of unknown function DUF6992 | DUF6992 | Family | 525 | false | false | This is a family of uncharacterised bacterial proteins. They are enriched with hydrophobic residues and are likely associated with the membrane. These proteins contain two conserved motifs GLDxxYxxxG and FLxxFD. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22503"
] | [
"DUF6992"
] | [
525
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
516,
9
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF6992 | Protein of unknown function DUF6992 | DUF6992 | 7 |
IPR054262 | 54,262 | Domain of unknown function DUF6993 | DUF6993 | Domain | 633 | false | false | This entry represents a bacterial domain of unknown function. It is predicted to adopt α+β structure consisting of four-stranded atiparallel beta-shsheet and α-helix that packs on it. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22504"
] | [
"DUF6993"
] | [
633
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"freshwater metagenome"
] | [
623,
10
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6993 | Domain of unknown function DUF6993 | DUF6993 | 1 |
IPR054263 | 54,263 | Protein of unknown function DUF6994 | DUF6994 | Family | 280 | false | false | This is a family of uncharacterised bacterial proteins. They are probably remotely related to His-Me finger endonucleases. The conservation of the putative active site residues in this family is not strict, in particular the position of the catalytic histidine. The residues involved in metal coordination are conserved.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22507"
] | [
"DUF6994"
] | [
280
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriati",
"ecological metagenomes"
] | [
261,
7,
12
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF6994 | Protein of unknown function DUF6994 | DUF6994 | 4 |
IPR054264 | 54,264 | PolB1 binding protein 2 | PBP2 | Family | 110 | false | false | This is a family of archaeal proteins, previously known as DUF6995, representing homologues of PolB1 binding protein 2 (PBP2) such as . PBP2, is a subunit of PolB1 enzyme that is a member of the archaeal B-family of DNA polymerases. PBP2 along with PBP1, associate with distinct surfaces of the larger catalytic subunit ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22511"
] | [
"PBP2"
] | [
110
] | 1 | [] | [] | [] | 0 | [
"5n35",
"5n41"
] | 2 | [
"PUB00154412"
] | [
"28462924"
] | [
"Identification and characterization of a heterotrimeric archaeal DNA polymerase holoenzyme."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Thermoproteota"
] | [
110
] | 1 | [] | [] | 0 | true | Family | PolB1 binding protein 2 | PolB1 binding protein 2 | PBP2 | 4 |
IPR054265 | 54,265 | Domain of unknown function DUF6996 | DUF6996 | Domain | 450 | false | false | This domain is found N-terminal in a group of uncharacterised proteins. It is remotely related to AbiEi winged helix domain and it is predicted to adopt the same structure. This domain is usually associated with which is related to PD-(D/E)XK nucleases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22515"
] | [
"DUF6996"
] | [
450
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Potamilus streckersoni",
"metagenomes"
] | [
426,
9,
2,
13
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6996 | Domain of unknown function DUF6996 | DUF6996 | 5 |
IPR054266 | 54,266 | Domain of unknown function DUF6997 | DUF6997 | Domain | 498 | false | false | This domain is found C-terminal in a group of uncharacterised proteins mainly bacterial. It usually follows winged helix domain . This domain is related to PD-(D/E)XK nucleases and it is predicted to adopt the same structure with similar active site architecture. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22518"
] | [
"DUF6997"
] | [
498
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Potamilus streckersoni",
"metagenomes"
] | [
457,
25,
2,
14
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6997 | Domain of unknown function DUF6997 | DUF6997 | 5 |
IPR054267 | 54,267 | Domain of unknown function DUF6998 | DUF6998 | Domain | 767 | false | false | This domain is found in uncharacterised bacterial proteins either standalone or in combination with other domains. It shares significant sequence similarity with PvuII endonucleases ( ) and is predicted to adopt similar structure. The predicted structures, however, do not suggest similarity in the active site architect... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22522"
] | [
"DUF6998"
] | [
767
] | 1 | [] | [] | [] | 0 | [
"8q5m",
"8q5o"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3,
742,
2,
20
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6998 | Domain of unknown function DUF6998 | DUF6998 | 2 |
IPR054268 | 54,268 | Protein of unknown function DUF6999 | DUF6999 | Family | 517 | false | false | This is a family of uncharacterised prokaryotic proteins. They are predicted to adopt α-helical structure. These proteins contain several invariant histidines and aspartates that may have a functional role. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22523"
] | [
"DUF6999"
] | [
517
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"environmental samples",
"plant metagenome"
] | [
507,
2,
8
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF6999 | Protein of unknown function DUF6999 | DUF6999 | 9 |
IPR054269 | 54,269 | Domain of unknown function DUF7000 | DUF7000 | Domain | 227 | false | false | This domain is found in uncharacterised archaeal proteins. It is predicted to adopt an α/β structure consisting of a cradle-like β-sheet with α-helices pocked on the convex side of it. It contains a highly conserved GYMDFTYF sequence motif that may be of functional importance. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22526"
] | [
"DUF7000"
] | [
227
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"ecological metagenomes"
] | [
203,
8,
16
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7000 | Domain of unknown function DUF7000 | DUF7000 | 6 |
IPR054270 | 54,270 | Protein of unknown function DUF7001 | DUF7001 | Family | 156 | false | false | This is a family of uncharacterised proteins found in Archaea. They have sequence similarity to Zincin-like metalloproteases and are predicted to adopt the same structure. Only one of the two zinc binding sites are conserved suggesting that these proteins may possess different function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22529"
] | [
"DUF7001"
] | [
156
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Candidatus Hakubella thermalkaliphila",
"Methanobacteriota",
"marine sediment metagenome"
] | [
4,
150,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF7001 | Protein of unknown function DUF7001 | DUF7001 | 6 |
IPR054271 | 54,271 | Protein of unknown function DUF7002 | DUF7002 | Family | 366 | false | false | This is a family of uncharacterised bacterial proteins. They share some sequence similarity with DarT toxin ( ) and are likely to adopt the same structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22531"
] | [
"DUF7002"
] | [
366
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
362,
3,
1
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF7002 | Protein of unknown function DUF7002 | DUF7002 | 3 |
IPR054272 | 54,272 | Protein of unknown function DUF7003 | DUF7003 | Family | 386 | false | false | This is a family of uncharacterised bacterial proteins. It is predicted to adopt a globular α/β structure with a central antiparallel β-sheet and helices packed on it. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22535"
] | [
"DUF7003"
] | [
386
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
386
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF7003 | Protein of unknown function DUF7003 | DUF7003 | 2 |
IPR054273 | 54,273 | Protein of unknown function DUF7004 | DUF7004 | Family | 68 | false | false | This family of proteins is found in mainly bacteria. Proteins in this family are approximately 160 amino acids in length. They are predicted to adopt globular α/β structure. These proteins contain two highly conserved sequence motifs GxFDxWC and KRxKRLG that may be of functional importance. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22539"
] | [
"DUF7004"
] | [
68
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / SANAE)"
] | [
67,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF7004 | Protein of unknown function DUF7004 | DUF7004 | 1 |
IPR054274 | 54,274 | Protein of unknown function DUF7005 | DUF7005 | Family | 138 | false | false | This is a family of uncharacterised bacterial proteins. These proteins share partial sequence similarity to the collagenase catalytic core with invariant HExxH motif. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22541"
] | [
"DUF7005"
] | [
138
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
135,
3
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF7005 | Protein of unknown function DUF7005 | DUF7005 | 8 |
IPR054275 | 54,275 | Family of unknown function DUF7006 | DUF7006 | Family | 226 | false | false | Proteins in this family are found in Firmicutes. They are approximately 120 amino acids in length and are predicted to adopt an α-helical structure. Members of this family contain two highly conserved acid residues aspartate and glutamate. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22652"
] | [
"DUF7006"
] | [
226
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacilli",
"bioreactor metagenome"
] | [
225,
1
] | 2 | [] | [] | 0 | true | Family | Family of unknown function DUF7006 | Family of unknown function DUF7006 | DUF7006 | 7 |
IPR054276 | 54,276 | Domain of unknown function DUF7007 | DUF7007 | Domain | 684 | false | false | This domain is found in uncharacterised bacterial proteins. It is predicted to adopt a globular structure consisting of segregated α-helices and a five-stranded antiparallel β-sheet. This domain contains two highly conserved sequence motifs TxxHGG and YEED that may be of a functional importance. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22653"
] | [
"DUF7007"
] | [
684
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
666,
2,
14,
2
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7007 | Domain of unknown function DUF7007 | DUF7007 | 2 |
IPR054278 | 54,278 | Domain of unknown function DUF7012 | DUF7012 | Domain | 125 | false | false | This domain of unknown function is found in a group of proteins mainly from alphaproteobacteria. It is normally found N-terminal to . It is predicted to adopt a configuration formed mainly by β-strands. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22792"
] | [
"DUF7012"
] | [
125
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Alphaproteobacteria",
"Blyttiomyces helicus",
"mine drainage metagenome"
] | [
122,
1,
2
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7012 | Domain of unknown function DUF7012 | DUF7012 | 8 |
IPR054279 | 54,279 | Domain of unknown function DUF7013 | DUF7013 | Domain | 51 | false | false | This is a presumed domain found in combination with different domains of phage sequences. In some proteins, at the N-terminal, followed by FN3-like domain ( ) at the C-terminal. In others, flanked on both sides by an N-terminal domain ( ) and a C-terminal domain ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22793"
] | [
"DUF7013"
] | [
51
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
9,
42
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7013 | Domain of unknown function DUF7013 | DUF7013 | 9 |
IPR054281 | 54,281 | Domain of unknown function DUF7015 | DUF7015 | Domain | 28 | false | false | This domain of unknown function is found at the C terminus of a group of bacterial proteins and, according to structure predictions, it may adopt a β-barrel structure. It is often associated with an Ig-like domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22839"
] | [
"DUF7015"
] | [
28
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroidota"
] | [
28
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7015 | Domain of unknown function DUF7015 | DUF7015 | 9 |
IPR054282 | 54,282 | Domain of unknown function DUF7016 | DUF7016 | Domain | 1 | false | false | This entry represents an OB fold domain found in a group of uncharacterised proteins from bacteria which have a domain at the C-terminal which also represents OB-fold domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22858"
] | [
"DUF7016"
] | [
1
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Ellagibacter isourolithinifaciens"
] | [
1
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7016 | Domain of unknown function DUF7016 | DUF7016 | 2 |
IPR054283 | 54,283 | Domain of unknown function (DUF7017) | DUF7017 | Repeat | 388 | false | false | This entry represents a domain consisting of TPR repeats found at the N-terminal in a group of uncharacterised sequences predominantly from bacteria, which seems to be related to TOTE conflict systems as they are associated with and . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22860"
] | [
"DUF7017"
] | [
388
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
358,
15,
8,
7
] | 4 | [] | [] | 0 | true | Repeat | Domain of unknown function (DUF7017) | Domain of unknown function (DUF7017) | DUF7017 | 2 |
IPR054284 | 54,284 | Protein of unknown function DUF7019 | DUF7019 | Family | 298 | false | false | This is a family of uncharacterised proteins found mainly in actinomycetes. Their function is unknown. They are predicted to adopt OB fold ( ) with significant similarity to Rpa. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF040893",
"PF22880"
] | [
"SAVMC3_10250",
"DUF7019"
] | [
269,
259
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Opisthokonta"
] | [
2,
294,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF7019 | Protein of unknown function DUF7019 | DUF7019 | 3 |
IPR054285 | 54,285 | Protein of unknown function DUF7020 | DUF7020 | Family | 244 | false | false | This entry represents a family of phage proteins of unknown function. AlphaFold shows confident dimer interaction. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22885"
] | [
"DUF7020"
] | [
244
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
244
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF7020 | Protein of unknown function DUF7020 | DUF7020 | 7 |
IPR054286 | 54,286 | Domain of unknown function DUF7021 | DUF7021 | Domain | 509 | false | false | This entry represents a β-barrel domain from uncharacterised bacterial proteins which is found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22886"
] | [
"DUF7021"
] | [
509
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
508,
1
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7021 | Domain of unknown function DUF7021 | DUF7021 | 2 |
IPR054287 | 54,287 | Protein of unknown function DUF7022 | DUF7022 | Family | 240 | false | false | This family of uncharacterised proteins is found in the T5 bacteriophage and other viruses within the family Demerecviridae. The function of this protein is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22887"
] | [
"DUF7022"
] | [
240
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pyrolobus fumarii (strain DSM 11204 / 1A)",
"Viruses",
"marine sediment metagenome"
] | [
1,
236,
3
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF7022 | Protein of unknown function DUF7022 | DUF7022 | 5 |
IPR054288 | 54,288 | Domain of unknown function DUF7024 | DUF7024 | Domain | 1,692 | false | false | This domain has a structure that resembles the galactose-binding domain. This domain is often associated with a sulfatase like domain ( ). Suggesting that this domain may be part of an enzyme that modifies some kind of carbohydrate. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22895"
] | [
"DUF7024"
] | [
1692
] | 1 | [
"EC"
] | [
"2.7.8.20"
] | [
"EC:2.7.8.20"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"ecological metagenomes"
] | [
1685,
3,
4
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Domain of unknown function DUF7024 | Domain of unknown function DUF7024 | DUF7024 | 6 |
IPR054289 | 54,289 | UncB-like, DUF7025 | UncB-like_DUF7025 | Domain | 9,494 | false | false | This entry represents an SH3 barrel-like domain found in a large family of AAA proteins, including Isoindolinone tripeptide biosynthesis cluster protein B from Uncinocarpus reesii (UncB), part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B [ ]. The func... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22942"
] | [
"DUF7025"
] | [
9494
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00163349"
] | [
"40387549"
] | [
"Genome Mining of Isoindolinone-Containing Peptide Natural Products."
] | [
2025
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Paramagnetospirillum magnetotacticum MS-1",
"unclassified Klosneuvirinae"
] | [
9489,
1,
4
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
4
] | 1 | true | Domain | UncB-like, DUF7025 | UncB-like, DUF7025 | UncB-like_DUF7025 | 1 |
IPR054290 | 54,290 | Domain of unknown function DUF7026 | DUF7026 | Domain | 348 | false | false | This entry represents a helical domain found in plant proteins. The function of these proteins is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22950"
] | [
"DUF7026"
] | [
348
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Magnoliopsida"
] | [
348
] | 1 | [
"Arabidopsis thaliana"
] | [
4
] | 1 | true | Domain | Domain of unknown function DUF7026 | Domain of unknown function DUF7026 | DUF7026 | 5 |
IPR054291 | 54,291 | Domain of unknown function DUF7027 | DUF7027 | Domain | 497 | false | false | This is a domain of unknown function found in a group of uncharacterised proteins mainly from nematodes and arthropods. This is likely an α-helical transmembrane segment. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22954"
] | [
"DUF7027"
] | [
497
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
497
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | Domain of unknown function DUF7027 | Domain of unknown function DUF7027 | DUF7027 | 1 |
IPR054292 | 54,292 | Domain of unknown function DUF7028 | DUF7028 | Domain | 2,863 | false | false | This domain is found in a group of uncharacterised proteins mainly from plants. It is predicted to adopt a globular structure that has significant sequence and structural similarity to MBD domains. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22970"
] | [
"DUF7028"
] | [
2863
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2863
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
43,
9,
80
] | 3 | true | Domain | Domain of unknown function DUF7028 | Domain of unknown function DUF7028 | DUF7028 | 8 |
IPR054293 | 54,293 | Domain of unknown function DUF7029 | DUF7029 | Domain | 2,525 | false | false | This domain is found in uncharacterised proteins mainly from fungi. It is predicted to adopt a globular structure that has some similarity to SRA domain ( ). The function of this domain is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22974"
] | [
"DUF7029"
] | [
2525
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
2525
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7029 | Domain of unknown function DUF7029 | DUF7029 | 9 |
IPR054294 | 54,294 | Lysine-specific demethylase 3A/B-like, DUF7030 | KDM3A/B_DUF7030 | Domain | 2,160 | false | false | This domain of unknown function is found N-terminal in Lysine-specific demethylase 3A/B (KDM3A/B, also known as JmjC domain-containing histone demethylation protein 2A/B or JHDM2A/B) and related sequences. KDM3B is a histone demethylase that specifically demethylates lysine at position 9 of histone H3 [ ]. This enzyme ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22989"
] | [
"DUF7030"
] | [
2160
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.11.65",
"R-HSA-3214842",
"R-HSA-9029569",
"R-HSA-983231",
"R-MMU-3214842",
"R-MMU-983231"
] | [
"EC:1.14.11.65",
"REACTOME:R-HSA-3214842",
"REACTOME:R-HSA-9029569",
"REACTOME:R-HSA-983231",
"REACTOME:R-MMU-3214842",
"REACTOME:R-MMU-983231"
] | 6 | [] | 0 | [
"PUB00153916"
] | [
"16603237"
] | [
"JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2160
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
27,
7,
8,
10
] | 4 | true | Domain | Lysine-specific demethylase 3A/B-like, DUF7030 | Lysine-specific demethylase 3A/B-like, DUF7030 | KDM3A/B_DUF7030 | 3 |
IPR054296 | 54,296 | Domain of unknown function DUF7032 | DUF7032 | Domain | 2,822 | false | false | This domain is found N-terminal in a group of uncharacterised proteins mainly from plants. This domain is predicted to adopt a globular structure that folds into a four helical bundle and has a significant sequence and structural similarity to MLKL executioner domain ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23005"
] | [
"DUF7032"
] | [
2822
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
2822
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
21,
18,
24
] | 3 | true | Domain | Domain of unknown function DUF7032 | Domain of unknown function DUF7032 | DUF7032 | 2 |
IPR054297 | 54,297 | Domain of unknown function DUF7033 | DUF7033 | Domain | 1,295 | false | false | This uncharacterised domain is found in a group of polysaccharide deacetylases and similar proteins from bacteria. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23019"
] | [
"DUF7033"
] | [
1295
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Adineta steineri",
"Bacteria",
"ecological metagenomes"
] | [
1,
1275,
19
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF7033 | Domain of unknown function DUF7033 | DUF7033 | 1 |
IPR054298 | 54,298 | BACOVA_00961-like | BACOVA_00961-like | Family | 257 | false | false | This family represents BACOVA_00961 from Bacteroides ovatus ( ) and similar sequences mainly found in bacteroidetes. This protein shows an α/β configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22057"
] | [
"BACOVA_00961-like"
] | [
257
] | 1 | [] | [] | [] | 0 | [
"2ml5",
"2ml6",
"4r4k"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"metagenomes"
] | [
252,
5
] | 2 | [] | [] | 0 | true | Family | BACOVA_00961-like | BACOVA_00961-like | BACOVA_00961-like | 1 |
IPR054300 | 54,300 | DNA polymerase alpha subunit B, OB domain | OB_DPOA2 | Domain | 4,280 | false | false | This entry represents the OB domain of DNA polymerase alpha subunit B [ , , , ]. B subunits of DNA polymerases stabilize the catalytic subunit, playing a role in regulation of the DNA synthesis in a cell cycle-dependent manner and act as scaffolds mediating interactions with other components of the replication machiner... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22062"
] | [
"OB_DPOA2"
] | [
4280
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-113501",
"R-CEL-68952",
"R-CEL-68962",
"R-CEL-69091",
"R-CEL-69166",
"R-CEL-69183",
"R-DME-113501",
"R-DME-68952",
"R-DME-68962",
"R-DME-69091",
"R-DME-69166",
"R-DME-69183",
"R-HSA-113501",
"R-HSA-174411",
"R-HSA-174430",
"R-HSA-68952",
"R-HSA-68962",
"R-HSA-69091",
"R-HS... | [
"REACTOME:R-CEL-113501",
"REACTOME:R-CEL-68952",
"REACTOME:R-CEL-68962",
"REACTOME:R-CEL-69091",
"REACTOME:R-CEL-69166",
"REACTOME:R-CEL-69183",
"REACTOME:R-DME-113501",
"REACTOME:R-DME-68952",
"REACTOME:R-DME-68962",
"REACTOME:R-DME-69091",
"REACTOME:R-DME-69166",
"REACTOME:R-DME-69183",
"R... | 49 | [
"3flo",
"4y97",
"5exr",
"7opl",
"7u5c",
"7uy8",
"8b9a",
"8b9b",
"8b9c",
"8b9d",
"8d0b",
"8d0k",
"8d9d",
"8foc",
"8fod",
"8foe",
"8foh",
"8foj",
"8fok",
"8g99",
"8g9f",
"8qj7",
"8v5m",
"8v5n",
"8v5o",
"8v6g",
"8v6h",
"8v6i",
"8v6j",
"8vy3",
"9c8v"
] | 31 | [
"PUB00052915",
"PUB00153910",
"PUB00153911",
"PUB00153912"
] | [
"19494830",
"25847248",
"26975377",
"34719824"
] | [
"3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases.",
"Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit.",
"Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.",
"Structural bas... | [
2009,
2015,
2016,
2022
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
4279,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
2,
2,
5,
7,
1,
5,
6,
1,
1,
9
] | 12 | true | Domain | DNA polymerase alpha subunit B, OB domain | DNA polymerase alpha subunit B, OB domain | OB_DPOA2 | 6 |
IPR054301 | 54,301 | Pdc1, Ge1 domain | Pdc1_Ge1 | Domain | 7 | false | false | This entry represents the Ge1 domain of Pdc1 from S.pombe. Pdc1 is known to be related to metazoan Edc4 (also known asGe-1) family, although the sequence similarity is very low. EDC4 (enhancer of mRNA-decapping protein 4) is a regulator of mRNA decapping in cytoplasmic processing bodies (P-bodies) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22063"
] | [
"Pdc1_Ge1"
] | [
7
] | 1 | [] | [] | [] | 0 | [
"4q2s"
] | 1 | [
"PUB00154155"
] | [
"24862735"
] | [
"In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Schizosaccharomyces"
] | [
7
] | 1 | [
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1
] | 1 | true | Domain | Pdc1, Ge1 domain | Pdc1, Ge1 domain | Pdc1_Ge1 | 1 |
IPR054302 | 54,302 | Large ribosomal subunit protein bL9m, C-terminal domain | Ribosomal_bL9m_C | Domain | 823 | false | false | This entry represents a presumed domain found at the C-terminal of the large ribosomal subunit protein bL9m (mitochondrial) from animals. This domain may adopt a similar fold to that of prokaryotic large ribosomal subunit protein bL9. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all orga... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22078"
] | [
"Ribosomal_bL9m_C"
] | [
823
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383",
"R-RNO-5389840",
"R-RNO-5419276",
"R-RNO-9937383"
] | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOME:R-MMU-9937383",
"REACTOME:R-RNO-5389840",
"REACTOM... | 13 | [
"3j7y",
"3j9m",
"4ce4",
"4v19",
"5aj4",
"5ool",
"5oom",
"6gaw",
"6gb2",
"6i9r",
"6nu3",
"6vlz",
"6vmi",
"6ydp",
"6ydw",
"6zm5",
"6zm6",
"6zs9",
"6zsa",
"6zsb",
"6zsc",
"6zsd",
"6zse",
"6zsg",
"7a5f",
"7a5g",
"7a5h",
"7a5i",
"7a5j",
"7a5k",
"7l08",
"7l20"... | 89 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
823
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
4,
9
] | 4 | true | Domain | Large ribosomal subunit protein bL9m, C-terminal domain | Large ribosomal subunit protein bL9m, C-terminal domain | Ribosomal_bL9m_C | 7 |
IPR054303 | 54,303 | Type III effector protein HopBA1 | HopBA1 | Family | 24 | false | false | HopBA1 is a type III effector protein that triggers an RBA1-dependent cell-death response. It folds into an α/β structure that consists of a central mixed β-sheet packed on both sides with α-helices [ ]. HopBA1 is structurally similar to proteins members of EreA/ChaN-like superfamily. It contains a ψ-loop between stran... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22079"
] | [
"HopBA1"
] | [
24
] | 1 | [] | [] | [] | 0 | [
"5t09"
] | 1 | [
"PUB00154010"
] | [
"28137883"
] | [
"TIR-only protein RBA1 recognizes a pathogen effector to regulate cell death in <i>Arabidopsis</i>."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
24
] | 1 | [] | [] | 0 | true | Family | Type III effector protein HopBA1 | Type III effector protein HopBA1 | HopBA1 | 9 |
IPR054304 | 54,304 | Dark, CARD domain | Dark_CARD | Domain | 47 | false | false | This entry represents a caspase recruitment domain (CARD) present in a set of Dark (Drosophila Apaf-1-related killer) proteins from insects, including Apaf-1/CED-4-related caspase activator Dapaf-1S from Drosophila melanogaster (Dark). Dark protein is part of the apoptosome complex and plays a key role in procaspases a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22080"
] | [
"Dark_CARD"
] | [
47
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-111458",
"R-DME-111459",
"R-DME-6798695",
"R-DME-9627069"
] | [
"REACTOME:R-DME-111458",
"REACTOME:R-DME-111459",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-9627069"
] | 4 | [
"3j9k",
"3j9l",
"4v4l",
"5jul",
"8y6p",
"8y6q"
] | 6 | [
"PUB00153900",
"PUB00153901"
] | [
"21220123",
"27916517"
] | [
"Structure of the Drosophila apoptosome at 6.9 a resolution.",
"A Near-Atomic Structure of the Dark Apoptosome Provides Insight into Assembly and Activation."
] | [
2011,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Schizophora"
] | [
47
] | 1 | [
"Drosophila melanogaster"
] | [
3
] | 1 | true | Domain | Dark, CARD domain | Dark, CARD domain | Dark_CARD | 1 |
IPR054305 | 54,305 | SwaI restriction endonuclease | SwaI | Family | 18 | false | false | SwaI is a Type IIP restriction endonuclease that recognises a palindromic eight base pair symmetric sequence, 5'-ATTTAAAT-3', and cleaves this target sequence at its centre to generate blunt-ended DNA fragments. SwaI forms a dimeric α/β structure, with each subunit having a central cradle-like mixed β-sheet with two he... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22081"
] | [
"SwaI-like"
] | [
18
] | 1 | [] | [] | [] | 0 | [
"5tgq",
"5tgx",
"5th3"
] | 3 | [
"PUB00154249"
] | [
"28180307"
] | [
"DNA recognition by the SwaI restriction endonuclease involves unusual distortion of an 8 base pair A:T-rich target."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"hydrothermal vent metagenome"
] | [
17,
1
] | 2 | [] | [] | 0 | true | Family | SwaI restriction endonuclease | SwaI restriction endonuclease | SwaI | 7 |
IPR054306 | 54,306 | 2-thiouridine synthetase TtuA-like, N-terminal LIM domain | TtuA-like_LIM_N | Domain | 1,404 | false | false | TtuA is an oxygen-labile iron-sulfur protein that is involved in a post-transcriptional thiolation of RNA. The iron-sulfur cluster of TtuA is required for sulfurtransferase activity. The enzyme structure consists of three domains: a central catalytic domain and two Zn-fingers [ ]. This entry represents the N-terminal Z... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22082"
] | [
"TtuA_LIM_N"
] | [
1404
] | 1 | [] | [] | [] | 0 | [
"3vrh",
"5b4e",
"5b4f",
"5gha",
"5mko",
"5mkp",
"5mkq",
"5ztb",
"6scy"
] | 9 | [
"PUB00088041",
"PUB00154400"
] | [
"28439027",
"24906001"
] | [
"Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA.",
"Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is associated with ubiquitin-proteasome, translation, and RNA processing system homologs."
] | [
2017,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
887,
307,
155,
55
] | 4 | [] | [] | 0 | true | Domain | 2-thiouridine synthetase TtuA-like, N-terminal LIM domain | 2-thiouridine synthetase TtuA-like, N-terminal LIM domain | TtuA-like_LIM_N | 6 |
IPR054307 | 54,307 | DNA endonuclease I-HmuI-like, NUMOD-like domain | I-HmuI_NUMOD-like | Domain | 457 | false | false | This entry represents the C-terminal NUMOD1-like DNA-binding HTH domain present in a set of intron-encoded endonucleases (homing endonucleases) such as I-HmuI from Bacteriophage SP01 and similar proteins [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22083"
] | [
"I-HmuI_NUMOD-like"
] | [
457
] | 1 | [] | [] | [] | 0 | [
"1u3e"
] | 1 | [
"PUB00031655"
] | [
"15313606"
] | [
"DNA binding and cleavage by the HNH homing endonuclease I-HmuI."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
160,
58,
218,
21
] | 4 | [] | [] | 0 | true | Domain | DNA endonuclease I-HmuI-like, NUMOD-like domain | DNA endonuclease I-HmuI-like, NUMOD-like domain | I-HmuI_NUMOD-like | 8 |
IPR054308 | 54,308 | UFSP, N-terminal MPN domain | UFSP_MPN | Domain | 48 | false | false | This entry represents the MPN domain in UFSP proteins that forms an α/β globular structure with a central mixed β-sheet packed on both sides with helices and a pair of two strands and a helix. This domain modulates both substrate recognition and deufmylation activity. UFM1-specific isopeptidase 1 and 2 (UFSP1 and UFSP2... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22084"
] | [
"UfSP_MPN_N"
] | [
48
] | 1 | [] | [] | [] | 0 | [
"5ejj",
"5xda"
] | 2 | [
"PUB00034739",
"PUB00034740",
"PUB00151643",
"PUB00154319",
"PUB00154320"
] | [
"17182609",
"15071506",
"21228277",
"27240952",
"29251776"
] | [
"Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2.",
"A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier.",
"Structure of ubiquitin-fold modifier 1-specific protease UfSP2.",
"The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition a... | [
2007,
2004,
2011,
2016,
2018
] | 5 | [] | [] | 0 | 0 | null | [
"Rhabditomorpha"
] | [
48
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | UFSP, N-terminal MPN domain | UFSP, N-terminal MPN domain | UFSP_MPN | 5 |
IPR054309 | 54,309 | Nitric oxide reductase subunit B, cytochrome c-like domain | NorB_cytochrome_c-like | Domain | 2,816 | false | false | This domain is found in Nitric oxide reductase subunit B from Pseudomonas aeruginosa (NorB) and similar bacterial sequences. NorB is the large component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). This entry represents the cytochrome C-like domain of NorB, which has 12 α-... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22085"
] | [
"NorB_cytochrome_c-like"
] | [
2816
] | 1 | [] | [] | [] | 0 | [
"3ayf",
"3ayg",
"6fwf",
"6l1x",
"6l3h",
"6qq5",
"6qq6",
"6t6v",
"8bgw",
"8zgo",
"8zgp"
] | 11 | [
"PUB00138296",
"PUB00154109",
"PUB00154110",
"PUB00154112"
] | [
"31489376",
"21109633",
"22266822",
"29483528"
] | [
"Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy.",
"Structural basis of biological N2O generation by bacterial nitric oxide reductase.",
"Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus.",
"Characteri... | [
2019,
2010,
2012,
2018
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
237,
2538,
15,
26
] | 4 | [] | [] | 0 | true | Domain | Nitric oxide reductase subunit B, cytochrome c-like domain | Nitric oxide reductase subunit B, cytochrome c-like domain | NorB_cytochrome_c-like | 1 |
IPR054310 | 54,310 | CT0912-like, C-terminal domain | CT0912-like_C | Domain | 29 | false | false | This domain is found at the C-terminal end of from Chlorobaculum tepidum (CT0912), a functionally uncharacterised protein with a ferredoxin-like domain repeat. This domain shows an α-β configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22087"
] | [
"CT0912-like_C"
] | [
29
] | 1 | [] | [] | [] | 0 | [
"3gn6"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"mine drainage metagenome"
] | [
28,
1
] | 2 | [] | [] | 0 | true | Domain | CT0912-like, C-terminal domain | CT0912-like, C-terminal domain | CT0912-like_C | 7 |
IPR054312 | 54,312 | LPG0439, HIT-related | LPG0439_HIT-like | Domain | 60 | false | false | These are uncharacterised proteins that are related to proteins which are members of the HIT-like superfamily. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22088"
] | [
"HIT-like"
] | [
60
] | 1 | [] | [] | [] | 0 | [
"5l0l"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Legionellaceae",
"Orpheovirus IHUMI-LCC2"
] | [
37,
22,
1
] | 3 | [] | [] | 0 | true | Domain | LPG0439, HIT-related | LPG0439, HIT-related | LPG0439_HIT-like | 7 |
IPR054313 | 54,313 | DIP2116-like, N-terminal domain | DIP2116-like_N | Domain | 23 | false | false | This domain is found at the N-terminal of the putative membrane anchored protein DIP2116 from Corynebacterium diphtheriae ( ). It shows an immunoglobulin-like fold. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22089"
] | [
"DIP2116-like_N"
] | [
23
] | 1 | [] | [] | [] | 0 | [
"3lso"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Corynebacterium"
] | [
23
] | 1 | [] | [] | 0 | true | Domain | DIP2116-like, N-terminal domain | DIP2116-like, N-terminal domain | DIP2116-like_N | 5 |
IPR054314 | 54,314 | Gins51, C-terminal domain | Gins51_C | Domain | 488 | false | false | This domain is found at the C-terminal of the DNA replication complex GINS family protein TK0536 from Thermococcus kodakarensis (Gins51, ). Gins51 is composed of a large α-helical domain at the N-terminal, and a small β-stranded domain at the C-terminal. This mobile C-terminal domain acts as a hook to bind the archaeal... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22090"
] | [
"Gins51_C"
] | [
488
] | 1 | [] | [] | [] | 0 | [
"3anw",
"5ghr",
"5ghs",
"7e15"
] | 4 | [
"PUB00088351",
"PUB00147362",
"PUB00154176"
] | [
"21527023",
"27599844",
"34568951"
] | [
"Architectures of archaeal GINS complexes, essential DNA replication initiation factors.",
"Atomic structure of an archaeal GAN suggests its dual roles as an exonuclease in DNA repair and a CMG component in DNA replication.",
"Family D DNA polymerase interacts with GINS to promote CMG-helicase in the archaeal r... | [
2011,
2016,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
459,
2,
27
] | 3 | [] | [] | 0 | true | Domain | Gins51, C-terminal domain | Gins51, C-terminal domain | Gins51_C | 1 |
IPR054315 | 54,315 | T26-6p, immunoglobulin-like domain 1 | T26-6p_Ig-like_dom_1 | Domain | 56 | false | false | This domain is found at the N-terminal in T26-6p from Thermococcus and similar archaeal sequences. T26-6p has three domains: two β- sandwich with two sheets made of four antiparallel β-strands (this entry and ) and a bundle of five α-helices ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22092"
] | [
"T26-6p_Ig-like_dom"
] | [
56
] | 1 | [] | [] | [] | 0 | [
"2wb7"
] | 1 | [
"PUB00093664"
] | [
"19319959"
] | [
"A protein encoded by a new family of mobile elements from Euryarchaea exhibits three domains with novel folds."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Methanobacteriota"
] | [
56
] | 1 | [] | [] | 0 | true | Domain | T26-6p, immunoglobulin-like domain 1 | T26-6p, immunoglobulin-like domain 1 | T26-6p_Ig-like_dom_1 | 9 |
IPR054316 | 54,316 | T26-6p, second immunoglobulin-like domain | T26-6p_Ig-like_dom_2 | Domain | 61 | false | false | This domain is found in T26-6p from Thermococcus and similar archaeal sequences. T26-6p has three domains: two β- sandwich with two sheets made of four antiparallel β-strands ( and this entry) and a bundle of five α-helices ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22265"
] | [
"T26-6p_Ig-like_dom_2"
] | [
61
] | 1 | [] | [] | [] | 0 | [
"2wb7"
] | 1 | [
"PUB00093664"
] | [
"19319959"
] | [
"A protein encoded by a new family of mobile elements from Euryarchaea exhibits three domains with novel folds."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Methanobacteriota"
] | [
61
] | 1 | [] | [] | 0 | true | Domain | T26-6p, second immunoglobulin-like domain | T26-6p, second immunoglobulin-like domain | T26-6p_Ig-like_dom_2 | 3 |
IPR054317 | 54,317 | CED4, winged-helix domain | WHD_CED4 | Domain | 71 | false | false | This entry represents a winged-helix-like domain (WHD) found at the C-terminal of CED4 and similar proteins from nematodes. CDE4 together with EGL1, CED9, and CED3, forms a crucial component of the apoptotic signalling cascade necessary for triggering programmed cell death during both embryonic and postembryonic develo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22094"
] | [
"WHD_CED4"
] | [
71
] | 1 | [] | [] | [] | 0 | [
"2a5y",
"3lqq",
"3lqr",
"4m9s",
"4m9x",
"4m9y",
"4m9z",
"8jns",
"8jo0",
"8jol"
] | 10 | [
"PUB00039156",
"PUB00153860",
"PUB00153861"
] | [
"16208361",
"16239138",
"36541866"
] | [
"Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans.",
"The nematode death machine in 3D.",
"Molecular dynamics studies of CED-4/CED-9/EGL-1 ternary complex reveal CED-4 release mechanism in the linear apoptotic pathway of Caenorhabditis elegans."
] | [
2005,
2005,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Rhabditida"
] | [
71
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | CED4, winged-helix domain | CED4, winged-helix domain | WHD_CED4 | 7 |
IPR054318 | 54,318 | BT_3535-like | BT_3535-like | Family | 25 | false | false | This family represents the functionally uncharacterised protein BT_3535 from Bacteroides thetaiotaomicron ( ) and similar sequences found in bacteroidetes. This protein is organised into two domains. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22095"
] | [
"BT_3535-like"
] | [
25
] | 1 | [] | [] | [] | 0 | [
"3kny"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroidales"
] | [
25
] | 1 | [] | [] | 0 | true | Family | BT_3535-like | BT_3535-like | BT_3535-like | 1 |
IPR054319 | 54,319 | PspC-related, ToastRack domain | PspC-rel_ToastRack | Domain | 1,747 | false | false | This entry represents the ToastRack domain found at the C-terminal end of a group of proteins related to PspC [ ] predominantly found in firmicutes. This domain is often associated to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22744"
] | [
"Toast-rack_PspC-Cterm"
] | [
1747
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00158885"
] | [
"38809013"
] | [
"The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history."
] | [
2024
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"ecological metagenomes"
] | [
1739,
8
] | 2 | [] | [] | 0 | true | Domain | PspC-related, ToastRack domain | PspC-related, ToastRack domain | PspC-rel_ToastRack | 6 |
IPR054321 | 54,321 | PspC-related, transmembrane region | PspC-rel_TM | Domain | 2,232 | false | false | This entry represents the transmembrane region found in a group of proteins related to PspC predominantly found in firmicutes. This domain is often associated to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22571"
] | [
"LiaI-LiaF-TM_PspC"
] | [
2232
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Scylla paramamosain",
"metagenomes"
] | [
2204,
1,
27
] | 3 | [] | [] | 0 | true | Domain | PspC-related, transmembrane region | PspC-related, transmembrane region | PspC-rel_TM | 3 |
IPR054322 | 54,322 | Flagellar calcium-binding protein, EF-hand domain | FCABP_EF-hand | Domain | 316 | false | false | This entry represents a EF-hand domain found in Flagellar calcium-binding protein from Trypanosoma cruzi (FCABP) and similar sequences mainly found in lower eukaryotes. This protein contains two EF-hand domains, the first of which is represented by this entry. FCABP may contribute to the rapid motility of the trypanoso... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22592"
] | [
"FCaBP_EF-hand"
] | [
316
] | 1 | [] | [] | [] | 0 | [
"2lvv",
"3cs1"
] | 2 | [
"PUB00051109",
"PUB00064147",
"PUB00153939"
] | [
"18559337",
"23011904",
"23782698"
] | [
"Structural insights into membrane targeting by the flagellar calcium-binding protein (FCaBP), a myristoylated and palmitoylated calcium sensor in Trypanosoma cruzi.",
"NMR structure of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei.",
"Functional manipulation of a calcium-binding pr... | [
2008,
2012,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
316
] | 1 | [] | [] | 0 | true | Domain | Flagellar calcium-binding protein, EF-hand domain | Flagellar calcium-binding protein, EF-hand domain | FCABP_EF-hand | 1 |
IPR054323 | 54,323 | Sperm microtubule inner protein 1, C-terminal | SPMIP1_C | Domain | 1,062 | false | false | This entry represents the C-terminal region of human Sperm microtubule inner protein 1 (SPMIP1). SPMIP1 is a microtubule inner protein (MIP) part of the doublet microtubules (DMTs) in the sperm axoneme [ ]. It binds to protofilament B09 along with CFAP90 in the sperm DMTs. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22589"
] | [
"SPMIP1"
] | [
1062
] | 1 | [] | [] | [] | 0 | [
"8otz",
"8snb",
"9e2g",
"9e5c",
"9fqr"
] | 5 | [
"PUB00151496"
] | [
"37327785"
] | [
"Structural specializations of the sperm tail."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1062
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
1,
2,
3
] | 5 | true | Domain | Sperm microtubule inner protein 1, C-terminal | Sperm microtubule inner protein 1, C-terminal | SPMIP1_C | 8 |
IPR054324 | 54,324 | McpB, first HAMP domain | McpB_HAMP_1st | Domain | 26 | false | false | This entry represents the first of five HAMP domains of Methyl-accepting chemotaxis protein McpB from Pseudomonas aeruginosa and similar sequences mainly from gammaproteobacteria. McpB, also known as Aerotaxis transducer Aer2, is a chemoreceptor that plays a critical role in the virulence and pathogenesis of the bacter... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22097"
] | [
"McpB_HAMP_1st"
] | [
26
] | 1 | [] | [] | [] | 0 | [
"3lnr",
"4i3m",
"4i44"
] | 3 | [
"PUB00058629",
"PUB00065072"
] | [
"20399181",
"23424282"
] | [
"Structure of concatenated HAMP domains provides a mechanism for signal transduction.",
"HAMP Domain Conformers That Propagate Opposite Signals in Bacterial Chemoreceptors."
] | [
2010,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
26
] | 1 | [] | [] | 0 | true | Domain | McpB, first HAMP domain | McpB, first HAMP domain | McpB_HAMP_1st | 5 |
IPR054325 | 54,325 | VtrA, C-terminal periplasmic domain | VtrA_C | Domain | 23 | false | false | VtrA forms a complex with VtrC on the surface of the membrane that surrounds the bacterial cell. These two proteins create a platform that can bind to bile salts and trigger the release of bacterial toxins. This entry represents the C-terminal periplasmic domain of VtrA from Vibrio parahaemolyticus ( ), which interacts... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22100"
] | [
"VtrA_C"
] | [
23
] | 1 | [] | [] | [] | 0 | [
"5kev",
"5kew",
"8dml"
] | 3 | [
"PUB00154328"
] | [
"27377244"
] | [
"Bile salt receptor complex activates a pathogenic type III secretion system."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Vibrionaceae"
] | [
23
] | 1 | [] | [] | 0 | true | Domain | VtrA, C-terminal periplasmic domain | VtrA, C-terminal periplasmic domain | VtrA_C | 5 |
IPR054326 | 54,326 | Homoserine dehydrogenase, C-terminal domain | HSD_C | Domain | 134 | false | false | Homoserine dehydrogenase (HSD) coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The enzyme structure consists of three domains. This e... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22101"
] | [
"HSD_C"
] | [
134
] | 1 | [] | [] | [] | 0 | [
"4pg4",
"4pg5",
"4pg6",
"4pg7",
"4pg8"
] | 5 | [
"PUB00104234"
] | [
"25945586"
] | [
"Structural basis for the catalytic mechanism of homoserine dehydrogenase."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
134
] | 1 | [] | [] | 0 | true | Domain | Homoserine dehydrogenase, C-terminal domain | Homoserine dehydrogenase, C-terminal domain | HSD_C | 4 |
IPR054327 | 54,327 | Histidine kinase-like, sensor domain | His-kinase-like_sensor | Domain | 4,668 | false | false | This entry represents a sensor domain found in a group of predicted histidine kinases and diguanylate cyclases mainly from proteobacteria, including from Shewanella oneidensis. It folds into an α/β structure consisting of a curved β-sheet and an α-helix packed on the concave side of it [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22588"
] | [
"dCache_1_like"
] | [
4668
] | 1 | [] | [] | [] | 0 | [
"3lif"
] | 1 | [
"PUB00055196"
] | [
"20435045"
] | [
"Structural characterization of the predominant family of histidine kinase sensor domains."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4652,
3,
13
] | 3 | [] | [] | 0 | true | Domain | Histidine kinase-like, sensor domain | Histidine kinase-like, sensor domain | His-kinase-like_sensor | 1 |
IPR054328 | 54,328 | SseL-like, C-terminal domain | SseL-like_C | Domain | 1,393 | false | false | This entry represents the C-terminal catalytic domain from a group of CE proteases from human pathogens including SseL from Salmonella typhimurium [ , ], which are dedicated deubiquitinases (DUBs), proteases that reverse the addition of ubiquitin to substrates, and effectively hijacks the host's ubiquitination processe... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22102"
] | [
"ElaD-SseL-like_C"
] | [
1393
] | 1 | [
"EC"
] | [
"3.4.22.-"
] | [
"EC:3.4.22.-"
] | 1 | [
"5haf",
"5ubw"
] | 2 | [
"PUB00117515",
"PUB00153924"
] | [
"27425412",
"32109687"
] | [
"The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases.",
"Modification of the host ubiquitome by bacterial enzymes."
] | [
2016,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"human gut metagenome"
] | [
1392,
1
] | 2 | [] | [] | 0 | true | Domain | SseL-like, C-terminal domain | SseL-like, C-terminal domain | SseL-like_C | 4 |
IPR054329 | 54,329 | ElaD/SseL-like, N-terminal domain | ElaD/SseL-like_N | Domain | 1,271 | false | false | This entry represents the N-terminal helical domain found in a group of CE proteases from human pathogens, including ElaD from E.coli and SseL from Salmonella typhimurium [ , ], which are dedicated deubiquitinases (DUBs), proteases that reverse the addition of ubiquitin to substrates, and effectively hijacks the host's... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22103"
] | [
"ElaD_SseL-like_N"
] | [
1271
] | 1 | [
"EC"
] | [
"3.4.22.-"
] | [
"EC:3.4.22.-"
] | 1 | [
"5haf"
] | 1 | [
"PUB00117515",
"PUB00153924"
] | [
"27425412",
"32109687"
] | [
"The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases.",
"Modification of the host ubiquitome by bacterial enzymes."
] | [
2016,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
1271
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | ElaD/SseL-like, N-terminal domain | ElaD/SseL-like, N-terminal domain | ElaD/SseL-like_N | 5 |
IPR054331 | 54,331 | LiaF, transmembrane domain | LiaF_TM | Domain | 4,173 | false | false | This entry represents the transmembrane region (TM) found at the N-terminal of LiaF ( ), which is thought to be a sensory domain. It may tie into a two-component system to regulate the membrane integrity and permeability in response to the stress signal. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22570"
] | [
"LiaF-TM"
] | [
4173
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Tanacetum cinerariifolium",
"unclassified sequences"
] | [
93,
4020,
1,
59
] | 4 | [] | [] | 0 | true | Domain | LiaF, transmembrane domain | LiaF, transmembrane domain | LiaF_TM | 4 |
IPR054332 | 54,332 | Transcription factor IIB, C-terminal module 2 | TFIIB_C_2 | Domain | 45 | false | false | In the pathogenic trypanosome, Trypanosoma brucei, transcription factor IIB (tTFIIB) is essential for spliced leader (SL) RNA gene transcription and cell viability, but has a highly divergent primary sequence in comparison to TFIIB in other eukaryotes. Structure analysis of the C-terminal region of trypanosome TFIIB, r... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22108"
] | [
"TFIIB_C_2"
] | [
45
] | 1 | [] | [] | [] | 0 | [
"3h4c"
] | 1 | [
"PUB00053009"
] | [
"19666603"
] | [
"Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Trypanosomatidae"
] | [
45
] | 1 | [] | [] | 0 | true | Domain | Transcription factor IIB, C-terminal module 2 | Transcription factor IIB, C-terminal module 2 | TFIIB_C_2 | 9 |
IPR054333 | 54,333 | ARP associated Restriction Endonuclease | REase-ARP-assoc | Family | 378 | false | false | This entry represents a rapidly evolving Restriction Endonuclease (REase) family of bacterial proteins observed in host systems and predicted to counter the action of viral ribosylating toxins, associated with ARG and Rhodanese-Phosphatase domain (ARP). It potentially functions as an effector in these systems [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22558"
] | [
"REase-ARP"
] | [
378
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153825",
"PUB00153826"
] | [
"36146784",
"36968430"
] | [
"Apprehending the NAD<sup>+</sup>-ADPr-Dependent Systems in the Virus World.",
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2022,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
328,
50
] | 2 | [] | [] | 0 | true | Family | ARP associated Restriction Endonuclease | ARP associated Restriction Endonuclease | REase-ARP-assoc | 2 |
IPR054334 | 54,334 | Decaheme cytochrome c component MtrC/MtrF, domain I | MtrC-MtrF_dom_I | Domain | 192 | false | false | This entry represents the domain I (N-terminal) of the decaheme cytochrome c component MtrC from the MtrCAB complex and its homologue MtrF, which is part of the MtrFDE complex. In Shewanella oneidensis, these proteins are at bacterial cell surface at the termini of trans-outer-membrane electron transfer conduits and al... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22111"
] | [
"MtrC-MtrF_N"
] | [
192
] | 1 | [] | [] | [] | 0 | [
"3pmq",
"4lm8",
"6qyc",
"6r2q",
"7o7g",
"7qth",
"8qbq",
"8qbz",
"8qc9",
"9eov"
] | 10 | [
"PUB00065514",
"PUB00151187",
"PUB00151188",
"PUB00154087"
] | [
"21606337",
"34556577",
"32289252",
"26126857"
] | [
"Structure of a bacterial cell surface decaheme electron conduit.",
"Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme.",
"The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire.",
"Redox Linked Flavin ... | [
2011,
2021,
2020,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
192
] | 1 | [] | [] | 0 | true | Domain | Decaheme cytochrome c component MtrC/MtrF, domain I | Decaheme cytochrome c component MtrC/MtrF, domain I | MtrC-MtrF_dom_I | 2 |
IPR054335 | 54,335 | Dual OB-containing domain | DuOB_dom | Domain | 434 | false | false | This entry represents a region found in a group of prokaryotic proteins that contains two domain copies of the OB fold. There is nearly absolutely conserved cysteine, serine/threonine, arginine, and aspartate residues which are predicted to line a deep cleft formed at the interface of the two OB domains. The predicted ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22557"
] | [
"DuOB"
] | [
434
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153826"
] | [
"36968430"
] | [
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
404,
9,
6,
15
] | 4 | [] | [] | 0 | true | Domain | Dual OB-containing domain | Dual OB-containing domain | DuOB_dom | 7 |
IPR054336 | 54,336 | OmcA-like, N-terminal domain | OmcA-like_N | Domain | 250 | false | false | This entry represents the N-terminal domain of OmcA ( ) from Shewanella oneidensis and similar proteins. OmcA is a decaheme c-type cytochrome homologue of MtrF and MtrC [ , , , , ]. OmcA may be able to receive electrons from the MtrCAB or MtrFDE complexes through the interaction with MtrC or MtrF [ ]. OmcA, MtrF and Mt... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22112"
] | [
"OmcA-like_N"
] | [
250
] | 1 | [] | [] | [] | 0 | [
"3ucp",
"3ufh",
"3ufk",
"4lmh"
] | 4 | [
"PUB00065514",
"PUB00065704",
"PUB00151186",
"PUB00151187",
"PUB00151188",
"PUB00154087"
] | [
"21606337",
"22682743",
"20550916",
"34556577",
"32289252",
"26126857"
] | [
"Structure of a bacterial cell surface decaheme electron conduit.",
"The crystal structure of the extracellular 11-heme cytochrome UndA reveals a conserved 10-heme motif and defined binding site for soluble iron chelates.",
"Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite sur... | [
2011,
2012,
2010,
2021,
2020,
2015
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
250
] | 1 | [] | [] | 0 | true | Domain | OmcA-like, N-terminal domain | OmcA-like, N-terminal domain | OmcA-like_N | 7 |
IPR054337 | 54,337 | Outer membrane cytochrome MtrC/MtrF-like, domains II/IV | Mtrc-MtrF-like_dom_II/IV | Domain | 1,242 | false | false | This entry represents domains II and IV found in decaheme cytochrome c component MtrC from the MtrCAB complex and its homologues MtrF (which is part of the MtrFDE complex) and OmcA. In Shewanella oneidensis, these proteins are located at the bacterial cell surface at the termini of trans-outer-membrane electron transfe... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22113"
] | [
"Mtrc-MtrF_II-IV_dom"
] | [
1242
] | 1 | [] | [] | [] | 0 | [
"1gws",
"1h29",
"2cvc",
"3pmq",
"3ucp",
"3ufh",
"3ufk",
"4lm8",
"4lmh",
"6qyc",
"6r2q",
"7o7g",
"7qth",
"8qbq",
"8qbz",
"8qc9",
"9eov"
] | 17 | [
"PUB00014111",
"PUB00014116",
"PUB00023222",
"PUB00024318",
"PUB00065514",
"PUB00151186"
] | [
"11095707",
"11005826",
"10368280",
"11170457",
"21606337",
"20550916"
] | [
"Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.",
"Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described... | [
2000,
2000,
1999,
2001,
2011,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"ecological metagenomes"
] | [
1201,
11,
30
] | 3 | [] | [] | 0 | true | Domain | Outer membrane cytochrome MtrC/MtrF-like, domains II/IV | Outer membrane cytochrome MtrC/MtrF-like, domains II/IV | Mtrc-MtrF-like_dom_II/IV | 4 |
IPR054338 | 54,338 | Peptidoglycan muramidase Tse3, catalytic domain | Tse3_cat | Domain | 31 | false | false | This entry represents the catalytic domain found in Peptidoglycan muramidase Tse3. Tse3 is a toxin secreted by the H1 type VI (H1-T6SS) secretion system into the periplasm of recipient cells. This protein degrades peptidoglycan via muramidase activity. Tse3 is composed of a small N-terminal domain ( ) and a C-terminal ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22115"
] | [
"T6SS_Tse3_cat"
] | [
31
] | 1 | [] | [] | [] | 0 | [
"3wa5",
"4luq",
"4m5e",
"4m5f",
"4n7s",
"4n80",
"4n88"
] | 7 | [
"PUB00105729",
"PUB00105730",
"PUB00154253"
] | [
"24100309",
"24724564",
"24025333"
] | [
"Complex structure of type VI peptidoglycan muramidase effector and a cognate immunity protein.",
"Structural insights into the T6SS effector protein Tse3 and the Tse3-Tsi3 complex from Pseudomonas aeruginosa reveal a calcium-dependent membrane-binding mechanism.",
"Structural Insights on the bacteriolytic and ... | [
2013,
2014,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
31
] | 1 | [] | [] | 0 | true | Domain | Peptidoglycan muramidase Tse3, catalytic domain | Peptidoglycan muramidase Tse3, catalytic domain | Tse3_cat | 1 |
IPR054339 | 54,339 | GMT-like, wHTH domain | GMT_wHTH | Domain | 439 | false | false | This entry represents a rapidly-evolving wHTH domain C-terminally fused to Rossmann fold methylase specifically related to the guanine methylase (GMT). Often co-occurs on the genome across a broad range of bacterial phylogenies with a further gene encoding a RADICAL SAM enzyme ( ). This two-gene island is predicted to ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22560"
] | [
"GMT-wHTH"
] | [
439
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153826"
] | [
"36968430"
] | [
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Fungi incertae sedis",
"Methanobacteriota",
"metagenomes"
] | [
417,
2,
2,
10,
8
] | 5 | [] | [] | 0 | true | Domain | GMT-like, wHTH domain | GMT-like, wHTH domain | GMT_wHTH | 8 |
IPR054340 | 54,340 | GNAT-like, C-terminal domain, phage-lihe | GNAT-like_C_phage-like | Domain | 170 | false | false | This domain is found at the C-terminal of a group of proteins from tailed bacteriophages and bacterial prophages, including some predicted GNAT family N-acetyltransferase. It has been characterised as part of a nucleic acid modifying system in certain phages. This system may modify tRNAs that are encoded adjacent to th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22559"
] | [
"GNAT-phage-like"
] | [
170
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153826"
] | [
"36968430"
] | [
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses",
"marine sediment metagenome"
] | [
155,
13,
2
] | 3 | [] | [] | 0 | true | Domain | GNAT-like, C-terminal domain, phage-lihe | GNAT-like, C-terminal domain, phage-lihe | GNAT-like_C_phage-like | 1 |
IPR054341 | 54,341 | GNAT-like, N-terminal domain | GNAT-like_N | Domain | 165 | false | false | This domain is found at the N-terminal of a group of proteins from tailed bacteriophages and bacterial prophages, including some predicted GNAT family N-acetyltransferase. It has been characterised as part of a nucleic acid modifying system in certain phages. This system may modify tRNAs that are encoded adjacent to th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22555"
] | [
"DAM-like-phage1"
] | [
165
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153826"
] | [
"36968430"
] | [
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses",
"marine sediment metagenome"
] | [
154,
10,
1
] | 3 | [] | [] | 0 | true | Domain | GNAT-like, N-terminal domain | GNAT-like, N-terminal domain | GNAT-like_N | 1 |
IPR054342 | 54,342 | TY-Chap, C-terminal domain | TY-Chap_C | Domain | 311 | false | false | This entry represents a domain found at the C-terminal end of a group of T3SS (YopN, CesT) and YbjN peptide-binding chaperone 1 (TY-Chap) proteins from actinomycetes. Members are observed in host systems and predicted to counteract the action of viral ribosylating toxins. It is found C-terminal to the N-terminal ( ) an... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22554"
] | [
"Chap-C"
] | [
311
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153825",
"PUB00153869"
] | [
"36146784",
"36968434"
] | [
"Apprehending the NAD<sup>+</sup>-ADPr-Dependent Systems in the Virus World.",
"Separating Inner and Outer Membranes of <i>Escherichia coli</i> by EDTA-free Sucrose Gradient Centrifugation."
] | [
2022,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"freshwater metagenome"
] | [
309,
2
] | 2 | [] | [] | 0 | true | Domain | TY-Chap, C-terminal domain | TY-Chap, C-terminal domain | TY-Chap_C | 8 |
IPR054343 | 54,343 | TY-Chap, central domain | TY-Chap_M | Domain | 1,048 | false | false | This entry represents a domain found centrally located in a group of T3SS (YopN, CesT) and YbjN peptide-binding chaperone 1 (TY-Chap) proteins from bacteria. Members are observed in host systems and predicted to counteract the action of viral ribosylating toxins. It is found between the TY-Chap N-terminal ( ) and C-ter... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22551"
] | [
"TY-Chap1"
] | [
1048
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153825",
"PUB00153869",
"PUB00154312"
] | [
"36146784",
"36968434",
"36968431"
] | [
"Apprehending the NAD<sup>+</sup>-ADPr-Dependent Systems in the Virus World.",
"Separating Inner and Outer Membranes of <i>Escherichia coli</i> by EDTA-free Sucrose Gradient Centrifugation.",
"DiSiR: fast and robust method to identify ligand-receptor interactions at subunit level from single-cell RNA-sequencing... | [
2022,
2023,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanoculleus chikugoensis",
"ecological metagenomes"
] | [
1023,
1,
24
] | 3 | [] | [] | 0 | true | Domain | TY-Chap, central domain | TY-Chap, central domain | TY-Chap_M | 9 |
IPR054344 | 54,344 | TY-Chap, N-terminal domain | TY-Chap_N | Domain | 1,345 | false | false | This entry represents a domain found at the N-terminal end of a group of T3SS (YopN, CesT) and YbjN peptide-binding chaperone 1 (TY-Chap) proteins from bacteria. Members are observed in host systems and predicted to counteract the action of viral ribosylating toxins. It is found N-terminal to the central ( ) and C-term... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22552"
] | [
"TY-Chap3"
] | [
1345
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153825",
"PUB00153869",
"PUB00154314"
] | [
"36146784",
"36968434",
"36968433"
] | [
"Apprehending the NAD<sup>+</sup>-ADPr-Dependent Systems in the Virus World.",
"Separating Inner and Outer Membranes of <i>Escherichia coli</i> by EDTA-free Sucrose Gradient Centrifugation.",
"Cardiovascular disease and feminizing gender-affirming hormone therapy: Implications for the provision of safe and life... | [
2022,
2023,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
1327,
18
] | 2 | [] | [] | 0 | true | Domain | TY-Chap, N-terminal domain | TY-Chap, N-terminal domain | TY-Chap_N | 6 |
IPR054346 | 54,346 | ARG and Rhodanese-Phosphatase-superfamily-associated domain 2 | ARPP-2 | Domain | 465 | false | false | ARPP-2 (ARG and Rhodanese-Phosphatase-superfamily-associated Protein domain 2) shows a distinguishing group of absolutely conserved residues distinct from ARPP-1 ( ). ARPP-2 is typically found fused to a C-terminal HTH domain and adjacent to a Rot/TROVE domain fused to a vWA domain [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22549"
] | [
"ARPP-2"
] | [
465
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153825",
"PUB00153826"
] | [
"36146784",
"36968430"
] | [
"Apprehending the NAD<sup>+</sup>-ADPr-Dependent Systems in the Virus World.",
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2022,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"hydrothermal vent metagenome"
] | [
464,
1
] | 2 | [] | [] | 0 | true | Domain | ARG and Rhodanese-Phosphatase-superfamily-associated domain 2 | ARG and Rhodanese-Phosphatase-superfamily-associated domain 2 | ARPP-2 | 7 |
IPR054347 | 54,347 | TOTE conflict system, primase domain | TOTE_primase | Domain | 2,190 | false | false | This entry represents the presumed primase domain predicted to function as RNA polymerase in the TOTE (TPR, OB, TBP, Effector) conflict systems, potentially generating transcripts for hybrid duplex formation [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22548"
] | [
"AEP-TOTE"
] | [
2190
] | 1 | [] | [] | [] | 0 | [
"7nqd",
"7nqe",
"7nqf",
"7p9j",
"7qaz"
] | 5 | [
"PUB00153788",
"PUB00154401"
] | [
"35609893",
"35508653"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty.",
"Molecular basis for the initiation of DNA primer synthesis."
] | [
2022,
2022
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"metagenomes"
] | [
2034,
3,
18,
61,
74
] | 5 | [] | [] | 0 | true | Domain | TOTE conflict system, primase domain | TOTE conflict system, primase domain | TOTE_primase | 3 |
IPR054348 | 54,348 | Protein M, C-terminal | M_C | Domain | 5 | false | false | This domain is found in proteins from Mycoplasmaceae, including Uncharacterized protein MG281 from Mycoplasma genitalium, also known as protein M. This virulence protein consists of two domains and N- and C-terminal fragments. This entry represents the C-terminal region, which is probably disordered [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22806"
] | [
"M_C"
] | [
5
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00074319"
] | [
"24503852"
] | [
"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Mycoplasmoides"
] | [
5
] | 1 | [] | [] | 0 | true | Domain | Protein M, C-terminal | Protein M, C-terminal | M_C | 9 |
IPR054349 | 54,349 | Protein M, smaller domain | M_smaller_dom | Domain | 5 | false | false | This domain is found in proteins from Mycoplasmaceae, including Uncharacterized protein MG281 from Mycoplasma genitalium, also known as protein M. This virulence protein consists of two domains. The larger one ( ) binds the IgG light chain to block the binding of antibody to antigen and includes a leucine-rich repeat (... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22805"
] | [
"M_smaller_dom"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"4nzr",
"4nzt"
] | 2 | [
"PUB00074319"
] | [
"24503852"
] | [
"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Mycoplasmoides"
] | [
5
] | 1 | [] | [] | 0 | true | Domain | Protein M, smaller domain | Protein M, smaller domain | M_smaller_dom | 7 |
IPR054350 | 54,350 | PurT/PurK-like, preATP-grasp domain | PurT/PurK_preATP-grasp | Domain | 32,023 | false | false | This domain precedes the ATP-grasp domain in a number of ribonucleotide synthetases, such as PurT, PurK and Pur6 [ , , , , ]. PurT is involved in the de novo purine biosynthesis. PurK, N5-carboxyaminoimidazole ribonucleotide (N5_CAIR) synthetase, catalyses the conversion of 5-aminoimidazole ribonucleotide (AIR), ATP, a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22660"
] | [
"RS_preATP-grasp-like"
] | [
32023
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"6.3.1.21",
"PWY-6122",
"PWY-6277"
] | [
"EC:6.3.1.21",
"METACYC:PWY-6122",
"METACYC:PWY-6277"
] | 3 | [
"1b6r",
"1b6s",
"1eyz",
"1ez1",
"1kj8",
"1kj9",
"1kji",
"1kjj",
"1kjq",
"2czg",
"2dwc",
"2z04",
"3aw8",
"3ax6",
"3eth",
"3etj",
"3k5h",
"3k5i",
"3orq",
"3orr",
"3q2o",
"3qff",
"3r5h",
"3v4s",
"4dlk",
"4e4t",
"4izo",
"4m9u",
"4ma0",
"4ma5",
"4mam",
"5jqw"... | 32 | [
"PUB00007904",
"PUB00014229",
"PUB00024709",
"PUB00051793",
"PUB00054788"
] | [
"10569930",
"11953435",
"10913290",
"19053251",
"20050602"
] | [
"Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily.",
"PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site.",
"Molecular structure of Escherichia coli PurT-enco... | [
1999,
2002,
2000,
2008,
2010
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
663,
28178,
2802,
380
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
2,
1,
3,
1,
1,
17
] | 7 | true | Domain | PurT/PurK-like, preATP-grasp domain | PurT/PurK-like, preATP-grasp domain | PurT/PurK_preATP-grasp | 5 |
IPR054351 | 54,351 | NADH-ubiquinone oxidoreductase, ferredoxin-like domain | NADH_UbQ_OxRdtase_ferredoxin | Domain | 22,835 | false | false | This entry represents the second ferredoxin-like domain found in proteins from the complex I 75 kDa subunit family, including human NADH-ubiquinone oxidoreductase 75 kDa subunit , mitochondrial [ , ], NADH-quinone oxidoreductase subunit G from Escherichia coli [ ] and NADH dehydrogenase [ubiquinone] iron-sulfur protein... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22117"
] | [
"Fer4_Nqo3"
] | [
22835
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1",
"R-BTA-611105",
"R-BTA-6799198",
"R-BTA-9837999",
"R-DDI-6799198",
"R-DDI-9837999",
"R-DME-611105",
"R-DME-6799198",
"R-DME-9837999",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-9837999",
"R-MMU-611105",
"R-MMU-6799198",
"R-MMU-9837999",
"R-RNO-611105",
"R-RNO-6799198",
"R-RNO... | [
"EC:7.1.1",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-BTA-9837999",
"REACTOME:R-DDI-6799198",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-6799198",
"REACTOME:R-HSA-9837999",... | 18 | [
"2fug",
"2ybb",
"3i9v",
"3iam",
"3ias",
"3m9s",
"4hea",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtb",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6gcs",
"6i0d",
"6i1p",
"6q8o",
"6q8w",
"6q8x",
"6q9d",
"6qa9",
"6qbx",
"6qc2",
"6qc3",
"6qc4"... | 327 | [
"PUB00002104",
"PUB00005074",
"PUB00040815",
"PUB00043561",
"PUB00045437",
"PUB00097662",
"PUB00098488",
"PUB00098489",
"PUB00103528",
"PUB00103529",
"PUB00149919",
"PUB00149920",
"PUB00154449",
"PUB00154450",
"PUB00155460"
] | [
"2188945",
"1470679",
"16469879",
"10940377",
"18394423",
"33060577",
"28844695",
"27595392",
"31557978",
"30879903",
"29395787",
"27509854",
"33768254",
"34562374",
"6822536"
] | [
"Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16.",
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.",
"The respiratory compl... | [
1990,
1992,
2006,
2000,
2008,
2020,
2017,
2016,
2019,
2019,
2018,
2016,
2021,
2022,
1983
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
48,
17281,
5007,
499
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
7,
1,
1,
4,
1,
4,
4,
1,
2,
4,
8
] | 11 | true | Domain | NADH-ubiquinone oxidoreductase, ferredoxin-like domain | NADH-ubiquinone oxidoreductase, ferredoxin-like domain | NADH_UbQ_OxRdtase_ferredoxin | 8 |
IPR054352 | 54,352 | Aspartokinase, ACT domain | ACT_Aspartokinase | Domain | 37,155 | false | false | This entry represents the ACT domain, found in Aspartate kinases from bacteria, archaea, plants and fungi. Aspartate kinase catalyses the phosphorylation of aspartic acid [ , , , , ]. Some members of this entry are bifunctional aspartokinase/homoserine dehydrogenases. This domain folds as a four-stranded antiparallel s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22468"
] | [
"ACT_9"
] | [
37155
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.2.4",
"PWY-2941",
"PWY-2942",
"PWY-5097",
"PWY-6160",
"PWY-6559",
"PWY-6562",
"PWY-7153",
"PWY-7977",
"PWY-8088",
"PWY-8179",
"PWY-8296"
] | [
"EC:2.7.2.4",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097",
"METACYC:PWY-6160",
"METACYC:PWY-6559",
"METACYC:PWY-6562",
"METACYC:PWY-7153",
"METACYC:PWY-7977",
"METACYC:PWY-8088",
"METACYC:PWY-8179",
"METACYC:PWY-8296"
] | 12 | [
"2cdq",
"2dt9",
"2dtj",
"2hmf",
"2j0w",
"2j0x",
"2re1",
"2zho",
"3aaw",
"3ab2",
"3ab4",
"3c1m",
"3c1n",
"3c20",
"3l76",
"3mah",
"3s1t",
"3tvi",
"4go5",
"4go7",
"5yei",
"6mx1"
] | 22 | [
"PUB00039980",
"PUB00040310",
"PUB00041449",
"PUB00041839",
"PUB00047275",
"PUB00050859"
] | [
"16731588",
"17350037",
"17012784",
"16905770",
"19490113",
"18334478"
] | [
"A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase.",
"Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum.",
"The initial step in the archaeal aspartate biosynthetic pathwa... | [
2006,
2007,
2006,
2006,
2009,
2008
] | 6 | [
"IPR002912"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
713,
30865,
4975,
2,
600
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
20,
2,
1,
24,
1,
1,
46
] | 7 | true | Domain | Aspartokinase, ACT domain | Aspartokinase, ACT domain | ACT_Aspartokinase | 5 |
IPR054353 | 54,353 | Transposase for insertion sequence element IS21-like, C-terminal domain | IstA-like_C | Domain | 14,063 | false | false | This entry represents a domain found towards the C-terminal end of Transposase for insertion sequence element IS21 from Pseudomonas aeruginosa (IstA) and similar prokaryotic integrases and transposases. This region adopts a β-barrel structure with Greek-key topology [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22483"
] | [
"Mu-transpos_C_2"
] | [
14063
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007414"
] | [
"7628012"
] | [
"Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Stenosarchaea group",
"plasmids",
"unclassified sequences"
] | [
13620,
4,
27,
90,
7,
315
] | 6 | [] | [] | 0 | true | Domain | Transposase for insertion sequence element IS21-like, C-terminal domain | Transposase for insertion sequence element IS21-like, C-terminal domain | IstA-like_C | 7 |
IPR054354 | 54,354 | Dynein 2 heavy chain 1, cytoplasmic, ATPase lid domain | DYNC2H1-like_lid | Domain | 8,332 | false | false | Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport and comprise cytoplasmic and axonemal isoforms. They consist of a motor domain that contains a ring-shaped head with six AAA-domains, a coiled-coil stalk with a microtubule binding ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22597"
] | [
"DYN_lid"
] | [
8332
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-5620924",
"R-CEL-6798695",
"R-CEL-6807878",
"R-CEL-6811436",
"R-CEL-9646399",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9646399",
"R-DME-3371497",
"R-DME-6798695",
"R-DME-6807878",
"R-DME-6811436",
"R-DME-9646399",
"R-HSA-141444",
"R-HSA-2132295",
"R-HSA-2467813",
"R-HSA-250025... | [
"REACTOME:R-CEL-5620924",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811436",
"REACTOME:R-CEL-9646399",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-9646399",
"REACTOME:R-DME-3371497",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-6807878",
"REACTOM... | 82 | [
"3j67",
"3j68",
"3qmz",
"3vkg",
"3vkh",
"4ai6",
"4akg",
"4akh",
"4aki",
"4rh7",
"4w8f",
"5nug",
"5vh9",
"5vlj",
"6rla",
"6rlb",
"6sc2",
"7mgm",
"7mi1",
"7mi3",
"7mi6",
"7mi8",
"7moq",
"7z8f",
"7z8g",
"7z8h",
"7z8i",
"7z8j",
"7z8k",
"7z8l",
"8dyu",
"8dyv"... | 137 | [
"PUB00055821",
"PUB00059369",
"PUB00062447",
"PUB00085943",
"PUB00152713"
] | [
"21330489",
"22426545",
"22398446",
"25470043",
"24727830"
] | [
"Crystal structure of the dynein motor domain.",
"Insights into dynein motor domain function from a 3.3-A crystal structure.",
"The 2.8 A crystal structure of the dynein motor domain.",
"Structure of human cytoplasmic dynein-2 primed for its power stroke.",
"Structural mechanism of the dynein power stroke."... | [
2011,
2012,
2012,
2015,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8332
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
3,
6,
10,
26,
6,
1,
13,
1,
1
] | 9 | true | Domain | Dynein 2 heavy chain 1, cytoplasmic, ATPase lid domain | Dynein 2 heavy chain 1, cytoplasmic, ATPase lid domain | DYNC2H1-like_lid | 6 |
IPR054355 | 54,355 | Decaheme cytochrome c component MtrF-like, domain III | MtrF-like_dom_III | Domain | 62 | false | false | This entry represents domain III of the decaheme cytochrome c component MtrF and similar proteins. MtrF is part of the MtrFDE complex and is a homologue of MtrC. In Shewanella oneidensis, these proteins are located at bacterial cell surface at the termini of trans-outer-membrane electron transfer conduits and allow the... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22118"
] | [
"MtrF-like_dom-III"
] | [
62
] | 1 | [] | [] | [] | 0 | [
"3pmq"
] | 1 | [
"PUB00065514",
"PUB00151187",
"PUB00151188",
"PUB00154087"
] | [
"21606337",
"34556577",
"32289252",
"26126857"
] | [
"Structure of a bacterial cell surface decaheme electron conduit.",
"Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme.",
"The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire.",
"Redox Linked Flavin ... | [
2011,
2021,
2020,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
62
] | 1 | [] | [] | 0 | true | Domain | Decaheme cytochrome c component MtrF-like, domain III | Decaheme cytochrome c component MtrF-like, domain III | MtrF-like_dom_III | 1 |
IPR054356 | 54,356 | Peptidoglycan muramidase Tse3, N-terminal domain | Tse3_N | Domain | 20 | false | false | This entry represents the catalytic domain found in Peptidoglycan muramidase Tse3. Tse3 is a toxin secreted by the H1 type VI (H1-T6SS) secretion system into the periplasm of recipient cells. This protein degrades peptidoglycan via muramidase activity. Tse3 is composed of a small N-terminal domain, which contains seven... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22120"
] | [
"T6SS_Tse3_N"
] | [
20
] | 1 | [] | [] | [] | 0 | [
"3wa5",
"4luq",
"4m5e",
"4m5f",
"4n7s",
"4n80",
"4n88"
] | 7 | [
"PUB00105729",
"PUB00105730",
"PUB00154253"
] | [
"24100309",
"24724564",
"24025333"
] | [
"Complex structure of type VI peptidoglycan muramidase effector and a cognate immunity protein.",
"Structural insights into the T6SS effector protein Tse3 and the Tse3-Tsi3 complex from Pseudomonas aeruginosa reveal a calcium-dependent membrane-binding mechanism.",
"Structural Insights on the bacteriolytic and ... | [
2013,
2014,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
20
] | 1 | [] | [] | 0 | true | Domain | Peptidoglycan muramidase Tse3, N-terminal domain | Peptidoglycan muramidase Tse3, N-terminal domain | Tse3_N | 6 |
IPR054357 | 54,357 | Peroxisomal multifunctional enzyme type 2-like, N-terminal domain | MFE-2_N | Domain | 11,079 | false | false | This entry represents a domain found at the N-terminal of Peroxisomal multifunctional enzyme type 2 (also known as MFE-2 hydratase 2) and related enzymes [ , , , , ]. This domain is housing the cavity for the aliphatic acyl part of the substrate molecule. The flexibility of region within this domain plays a role in sub... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22622"
] | [
"MFE-2_hydrat-2_N"
] | [
11079
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",... | [
"4.2.1.119",
"PWY-5138",
"PWY-5972",
"PWY-6657",
"PWY-6920",
"PWY-6944",
"PWY-7288",
"PWY-7337",
"PWY-7338",
"PWY-7339",
"PWY-7340",
"PWY-8152",
"R-DDI-193368",
"R-DDI-2046106",
"R-DDI-389887",
"R-DDI-390247",
"R-DDI-9033241",
"R-DME-193368",
"R-DME-2046106",
"R-DME-389887",
... | [
"EC:4.2.1.119",
"METACYC:PWY-5138",
"METACYC:PWY-5972",
"METACYC:PWY-6657",
"METACYC:PWY-6920",
"METACYC:PWY-6944",
"METACYC:PWY-7288",
"METACYC:PWY-7337",
"METACYC:PWY-7338",
"METACYC:PWY-7339",
"METACYC:PWY-7340",
"METACYC:PWY-8152",
"REACTOME:R-DDI-193368",
"REACTOME:R-DDI-2046106",
"... | 38 | [
"1pn2",
"1pn4",
"1s9c",
"2cdh",
"3kh8",
"3khp",
"3oml",
"7mku"
] | 8 | [
"PUB00029917",
"PUB00030962",
"PUB00039859",
"PUB00049478",
"PUB00154062"
] | [
"15051722",
"15644212",
"16963641",
"17431182",
"16513976"
] | [
"A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2.",
"Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2.",
"Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.",
"Structural ... | [
2004,
2005,
2006,
2007,
2006
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanoliparales",
"Eukaryota",
"unclassified sequences"
] | [
4212,
2,
6779,
86
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
1,
1,
2,
17,
3,
2,
2,
6,
1,
16
] | 11 | true | Domain | Peroxisomal multifunctional enzyme type 2-like, N-terminal domain | Peroxisomal multifunctional enzyme type 2-like, N-terminal domain | MFE-2_N | 9 |
IPR054358 | 54,358 | Magnetotaxis protein MtxA, C-terminal domain | MtxA_C | Domain | 41 | false | false | This domain is found at the C-terminal end of Magnetotaxis protein MtxA from Magnetospirillum gryphiswaldense ( ) and similar sequences from magnetotactic aquatic proteobacteria. Magnetotaxis is believed to direct the swimming of cells toward growth-favoring microoxic zones in natural waters. This domain contains five ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22121"
] | [
"MtxA_C"
] | [
41
] | 1 | [] | [] | [] | 0 | [
"4z29"
] | 1 | [
"PUB00154088"
] | [
"26052516"
] | [
"Crystal structure of the magnetobacterial protein MtxA C-terminal domain reveals a new sequence-structure relationship."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine metagenome"
] | [
36,
5
] | 2 | [] | [] | 0 | true | Domain | Magnetotaxis protein MtxA, C-terminal domain | Magnetotaxis protein MtxA, C-terminal domain | MtxA_C | 1 |
IPR054360 | 54,360 | Internalin K, domain D2 | InlK_D2 | Domain | 330 | false | false | This entry represents domain D2 of the surface-associated internalin InlK from Listeria monocytogenes ( ), also present in similar proteins mainly found in Bacilli. InlK interacts with the highly conserved major vault protein (MVP), the main component of cytoplasmic ribonucleoproteic particules named vaults that are wi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22122"
] | [
"InlK_D2"
] | [
330
] | 1 | [] | [] | [] | 0 | [
"4l3a",
"4l3f"
] | 2 | [
"PUB00094686",
"PUB00105020"
] | [
"23958637",
"21829365"
] | [
"Structure of internalin InlK from the human pathogen Listeria monocytogenes.",
"Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy."
] | [
2013,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Ecdysozoa"
] | [
328,
2
] | 2 | [] | [] | 0 | true | Domain | Internalin K, domain D2 | Internalin K, domain D2 | InlK_D2 | 4 |
IPR054361 | 54,361 | Zinc finger CCCH domain-containing protein 4/6/8, CCCH zinc finger | Znf-CCCH_ZC3H4/6/8 | Domain | 2,303 | false | false | This domain is found in human KIAA1064 (also known as Zinc finger CCCH domain-containing protein 4), Zinc finger CCCH domain-containing protein 6 and 8. ZC3H4 is a RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) [ , ]. ZC3H8 is a component of the little elongation complex (LEC), a co... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22623"
] | [
"zf-CCCH_9"
] | [
2303
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6807505",
"R-HSA-9930044",
"R-MMU-6807505",
"R-MMU-9930044"
] | [
"REACTOME:R-HSA-6807505",
"REACTOME:R-HSA-9930044",
"REACTOME:R-MMU-6807505",
"REACTOME:R-MMU-9930044"
] | 4 | [
"2cqe"
] | 1 | [
"PUB00072917",
"PUB00154337",
"PUB00154338"
] | [
"23932780",
"33913806",
"33767452"
] | [
"The little elongation complex functions at initiation and elongation phases of snRNA gene transcription.",
"ZC3H4 restricts non-coding transcription in human cells.",
"A first exon termination checkpoint preferentially suppresses extragenic transcription."
] | [
2013,
2021,
2021
] | 3 | [
"IPR000571"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2303
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
6,
6,
7
] | 5 | true | Domain | Zinc finger CCCH domain-containing protein 4/6/8, CCCH zinc finger | Zinc finger CCCH domain-containing protein 4/6/8, CCCH zinc finger | Znf-CCCH_ZC3H4/6/8 | 4 |
IPR054362 | 54,362 | Exuperantia RNAse H-like domain | Exu_RNase_H-like | Domain | 700 | false | false | This entry represents the RNAse H-like domain found at the N-terminal of exuperantia (Exu) from Drosophila and similar sequences from insects. Exu is a RNA-binding pseudonuclease associated with bicoid mRNA and required for its localisation [ ]. The catalytic site is degenerate and inactive, and as such, this domain me... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22123"
] | [
"Exu_RNase_H_like"
] | [
700
] | 1 | [] | [] | [] | 0 | [
"5l7z",
"5l80"
] | 2 | [
"PUB00088023"
] | [
"27376588"
] | [
"The bicoid mRNA localization factor Exuperantia is an RNA-binding pseudonuclease."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
700
] | 1 | [
"Drosophila melanogaster"
] | [
2
] | 1 | true | Domain | Exuperantia RNAse H-like domain | Exuperantia RNAse H-like domain | Exu_RNase_H-like | 2 |
IPR054363 | 54,363 | Glycosyl hydrolase family 95, catalytic domain | GH95_cat | Domain | 15,198 | false | false | This entry represents the central catalytic domain of proteins from the GH95 family of glycosyl hydrolases, including Alpha-1,2-fucosidase 2 from Arabidopsis thaliana, which catalyses the hydrolysis of an alpha-1,2-linked fucose [ ]. A member of this family, FucOB from A. muciniphila was shown to hydrolyse all three ty... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22124"
] | [
"Glyco_hydro_95_cat"
] | [
15198
] | 1 | [
"EC",
"METACYC"
] | [
"3.2.1.51",
"PWY-6807"
] | [
"EC:3.2.1.51",
"METACYC:PWY-6807"
] | 2 | [
"2eab",
"2eac",
"2ead",
"2eae",
"2rdy",
"4ufc",
"7kmq",
"7znz",
"7zo0",
"8zbv"
] | 10 | [
"PUB00008368",
"PUB00040386",
"PUB00084310",
"PUB00151755",
"PUB00153980",
"PUB00153981",
"PUB00153982"
] | [
"11587643",
"17459873",
"18495185",
"26112186",
"36997505",
"24255995",
"34728215"
] | [
"Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases.",
"Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum.",
"Identification of an Arabidopsis gene encoding a GH95 alpha1,2-... | [
2001,
2007,
2008,
2015,
2023,
2014,
2021
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Pyramimonas orientalis virus",
"unclassified sequences"
] | [
11752,
3283,
23,
1,
139
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
7,
9
] | 3 | true | Domain | Glycosyl hydrolase family 95, catalytic domain | Glycosyl hydrolase family 95, catalytic domain | GH95_cat | 6 |
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