ID A0A132ACI7_SARSC Unreviewed; 498 AA.
AC A0A132ACI7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN ORFNames=QR98_0066740 {ECO:0000313|EMBL:KPM08160.1}, SSS_5058
GN {ECO:0000313|EMBL:KAF7492944.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM08160.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM08160.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM08160.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
RN [2] {ECO:0000313|Proteomes:UP000070412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33001992;
RA Korhonen P.K., Gasser R.B., Ma G., Wang T., Stroehlein A.J., Young N.D.,
RA Ang C.S., Fernando D.D., Lu H.C., Taylor S., Reynolds S.L., Mofiz E.,
RA Najaraj S.H., Gowda H., Madugundu A., Renuse S., Holt D., Pandey A.,
RA Papenfuss A.T., Fischer K.;
RT "High-quality nuclear genome for Sarcoptes scabiei-A critical resource for
RT a neglected parasite.";
RL PLoS Negl. Trop. Dis. 14:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF7492944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SSS_KF_BRIS2020 {ECO:0000313|EMBL:KAF7492944.1};
RA Korhonen P.K.K., Guangxu M.G., Wang T.W., Stroehlein A.J.S., Young N.D.,
RA Ang C.-S.A., Fernando D.W.F., Lu H.L., Taylor S.T., Ehtesham M.E.M.,
RA Najaraj S.H.N., Harsha G.H.G., Madugundu A.M., Renuse S.R., Holt D.H.,
RA Pandey A.P., Papenfuss A.P., Gasser R.B.G., Fischer K.F.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblMetazoa:KAF7492944.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
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}.
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DR EMBL; WVUK01000056; KAF7492944.1; -; Genomic_DNA.
DR EMBL; JXLN01012231; KPM08160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132ACI7; -.
DR EnsemblMetazoa; SSS_5058s_mrna; KAF7492944.1; SSS_5058.
DR VEuPathDB; VectorBase:SSCA000121; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 5479950at2759; -.
DR Proteomes; UP000070412; Unassembled WGS sequence.
DR Proteomes; UP000616769; 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:SF6; RUVB-LIKE 1; 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:UP000070412};
KW Transcription {ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 105..407
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 498 AA; 55369 MW; 56DBCFC25E9BEA5C CRC64;
MSYCALHNAS HALNYCGPVC DLDSKKRFLR ADLFKILIGS KMFKVDTIKT NDKHQRISAH
SHIKGLGLDP ELEISSTNSC GLIGQNDARK AAGVVVELIK MKKMSGRAIL FVGPTCTGKT
ALAMAISKEL GNQIPFCPMV AGEVYSAEVK KTEILMENFR KSIGLRIKEM KEVYEGEVTQ
IEPMEMENPI GYGKQIHHLS LTLKATKGTK KLKLDPSIYE ALQKQKVEVG DVIYIEVNSG
SLKRIGRSDA YATEFDLEAD EYVPIPKGDV FKKKTVIQDI TLHDLDQANA HPSGSQDVLS
LMEQLLKPKK TEITEKLRKE INNKVNKLIE SGVAELITGV LFIDEVHMLD IECFTFLSKA
LESNIAPIVI LASNKGNCLI RGTDNIFSPH GIPVDFLDRT IIIKTIPFTM EEMIQIIGIR
SIAEGLKIDD DVLLKLGQIG SATSLRYAIQ LLNPCHQLAK TYCQNSINLQ VLDEVTELFC
DSRKSAIELG KMRSKYLK
//
