ID A0A1V9Y8C4_9STRA Unreviewed; 695 AA.
AC A0A1V9Y8C4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE Flags: Fragment;
GN ORFNames=THRCLA_11287 {ECO:0000313|EMBL:OQR81918.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR81918.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR81918.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR81918.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OQR81918.1}.
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DR EMBL; JNBS01004870; OQR81918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Y8C4; -.
DR STRING; 74557.A0A1V9Y8C4; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000243217; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217}.
FT DOMAIN 13..379
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT NON_TER 695
FT /evidence="ECO:0000313|EMBL:OQR81918.1"
SQ SEQUENCE 695 AA; 78381 MW; C1F34973197C626A CRC64;
MDVPPRGIMI MGHSVEFPEG TKPFPAQLAV MSKVILALKK RQNALLESPT GSGKTLALLC
SSLAWQQQHR IDMAEQERIA HNEILERQRA AAEAPVPVPE VQIHPPTQSV DDDFEAISFS
QARSEKKRTF PESLRQYAFN ADQLPLPVPT TQEPPHDKPA AAVNREKTPT IYFCSRTHSQ
ITQVVQELRR CPTASGVRMV VLGSKKHYCV HPKVRNLDGG KVNDECSALQ DDNGCRFRKK
LKTHNEMRAY VPSVWDIEDL VKLGEEHREC PYYYTHLTVE NASLVFCPYN YIMDPSIRSA
LKIDLKNSIV ILDEAHNIED VCRSSASMEL TWEQLEEARA SFAATIKSQI SPQQMYASLL
KLLNGWGRWL EHVQREKLLK TIGYEHETQQ WSGVDCVAIM NEFCGLNPGN IETYNEIYQT
VATAERESDD DNKNPEKQAA PQEKAVKLTS TALMSVLSVL NVATFMFRND LQYVHDYKLV
VIRSRPFGGK ILHFWYRFNF AQGGRKAQHL QLKLCLWCLH AGVAFSDITS NVRSVILTSG
TLSPMTSFAG ELGTTFPITL EANHVVDLKK QVFIGSLMTG PNRVDLSATY SNQQDLSYQD
ALGQLVLNGI IPGGLLVFLP SYRLMTQLHK RWEETGLLDE ISQLKQVFLE PRSAGKDFDA
LLEEYKEVIE STRSPLLVKN EVDVVDLTES DTSMI
//
