ID J9J7J2_9SPIT Unreviewed; 808 AA.
AC J9J7J2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=OXYTRI_19624 {ECO:0000313|EMBL:EJY82760.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY82760.1};
RN [1] {ECO:0000313|EMBL:EJY82760.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY82760.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000256|ARBA:ARBA00006637}.
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:EJY82760.1}.
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DR EMBL; AMCR01005607; EJY82760.1; -; Genomic_DNA.
DR AlphaFoldDB; J9J7J2; -.
DR EnsemblProtists; EJY82760; EJY82760; OXYTRI_19624.
DR OrthoDB; 1360679at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd18029; DEXHc_XPB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR NCBIfam; TIGR00603; rad25; 1.
DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR PRINTS; PR00851; XRODRMPGMNTB.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 357..524
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 580..745
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 177..206
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 765..795
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 808 AA; 93800 MW; FB778E9C5D788C13 CRC64;
MDQRSSSYIG DQQEMTDRDL FDNQEDFEEG NFFHREFQDY TQQIKLKEDH EKRPIWIGPN
FKLYLESFSP LYKAATEFMI AIAEPVSRPT YIHEYVLTAY SLYAAMSVNL TKDDIFEVLD
RLSKNAEIPP DVKGFIEQYS SRYGKAKLVL KSNKYFIETN DKNVRRNLLN IQQVASAYQS
QIEKNRLEEQ RQKERAERNI NVVESSEARA LRDRLMGVNS YSTSSQLNRA STATGTTGGQ
QILTQNIEQQ DLTERFMNLK DEFQIFIDQE MEDVDTNEGG QDGNSVDAKA LQRRKEELIL
EIDAEKIEEV KEACIRLNYP LIEEYDFKRD QTIPDLKIEL KSTTQIRSYQ EQSLSKMFSN
GRARSGVIVL PCGAGKTLAG IIAACTVKKS TMILCTSDVS VQQWRQQFYQ WSNIAGKVCR
FTSRTKDPMF ESKGPDSEAG IVISSYNMIA YLGSRSGQTQ KIMDTIRNTD WGLLILDEVQ
VVPAEMFRKV LAICKSHCKL GLTATLVRED NKIQDLNFLI GPKLYEANWL DLQEQGFLAR
VQCIEVWCEM TTEFYREYLN HNLKPRMKQV LYVNNPNKFL ACQYLINLHE SRGDKIIVFS
DNLFALKMYA KKLKKPYISG DVSQSERMGI LHYFQKTNEI NTIFLSKVGD TSIDLPGANV
INSNIFPFSL LVVRKPSALE EFSDLNKAEK ASLLQLRRFN AYFYSLVSTN TQEMYYADKR
QQFLIDQGYY FEVIQELPFQ KDPLQLQKLQ MTTIREQVDF LTSILQNDET KFEREEEQED
RIEEDEDQLE LERWRRRERN IGALTGAD
//
