UniProt: A0A232FD79

Database: UniProt
Entry: A0A232FD79_9HYME

LinkDB:  A0A232FD79_9HYME 
Original site:  A0A232FD79_9HYME

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   A0A232FD79_9HYME        Unreviewed;       462 AA.
AC   A0A232FD79;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-NOV-2023, entry version 26.
DE   RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN   ORFNames=TSAR_016743 {ECO:0000313|EMBL:OXU28453.1};
OS   Trichomalopsis sarcophagae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC   Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX   NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU28453.1, ECO:0000313|Proteomes:UP000215335};
RN   [1] {ECO:0000313|EMBL:OXU28453.1, ECO:0000313|Proteomes:UP000215335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alberta {ECO:0000313|EMBL:OXU28453.1,
RC   ECO:0000313|Proteomes:UP000215335};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXU28453.1};
RX   PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA   Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT   "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL   Curr. Biol. 27:2007-2013(2017).
CC   -!- FUNCTION: Proposed core component of the chromatin remodeling Ino80
CC       complex which is involved in transcriptional regulation, DNA
CC       replication and probably DNA repair. {ECO:0000256|ARBA:ARBA00002300,
CC       ECO:0000256|RuleBase:RU363048}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU363048};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU363048}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC       ECO:0000256|RuleBase:RU363048}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXU28453.1}.
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DR   EMBL; NNAY01000430; OXU28453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A232FD79; -.
DR   STRING; 543379.A0A232FD79; -.
DR   Proteomes; UP000215335; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.50.360; RuvB-like helicase, domain II; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
DR   InterPro; IPR041048; RuvB-like_C.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093:SF2; RUVB-LIKE 2; 1.
DR   PANTHER; PTHR11093; RUVB-RELATED REPTIN AND PONTIN; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363048};
KW   Chromatin regulator {ECO:0000256|RuleBase:RU363048};
KW   DNA damage {ECO:0000256|RuleBase:RU363048};
KW   DNA repair {ECO:0000256|RuleBase:RU363048};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363048};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363048};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363048};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW   Transcription {ECO:0000256|RuleBase:RU363048};
KW   Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT   DOMAIN          67..359
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   462 AA;  51492 MW;  CE51E98235B39E7A CRC64;
     MAIAASKVHE VREITRIERI GAHSHIRGLG LDDSLEPRNV SQGMVGQFQA RRATGIILEM
     IKEGKIAGRS VLLAGQPGTG KTAVALGLAQ SLGADTPFTL MAGSEIYSLE MSKTEALTQA
     IRKSIGIRIK EESEIIEGEV VEIQVDRPVS GVGAKVGKLT LKTTEMETIY DLGNKMIECL
     MKEKVQAGDV ITIDKATGKI SKLGRSFTRA RDYDATGPQT RFIQCPEGEL QKRKEVVHTV
     TLHEIDVINS RTHGFLALFS GDTGEIKSEV REQINQKVAE WREEGKAEIV PGVLFIDEVH
     MLDIECFSFL NRALENEMAP VVIMATNRGI TRIRGTNYKS PHGIPIDLLD RMIIVPTIPY
     QESELKEILK IRCEEEDCEM SNDALLVLTR IALETSLRYA IQLITTSSLI SRKSKNIEVG
     VDDVKRAYTL FMDENRSSQF LKEYQEDFMF YEAEEPAEME VA
//

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