ID A0A024U8R2_9STRA Unreviewed; 598 AA.
AC A0A024U8R2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, 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=H310_05291 {ECO:0000313|EMBL:ETW02806.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW02806.1};
RN [1] {ECO:0000313|EMBL:ETW02806.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW02806.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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DR EMBL; KI913960; ETW02806.1; -; Genomic_DNA.
DR RefSeq; XP_008868190.1; XM_008869968.1.
DR AlphaFoldDB; A0A024U8R2; -.
DR EnsemblFungi; H310_05291-t26_2; H310_05291-t26_2-p1; H310_05291.
DR EnsemblProtists; ETW02806; ETW02806; H310_05291.
DR GeneID; 20082341; -.
DR VEuPathDB; FungiDB:H310_05291; -.
DR OrthoDB; 124793at2759; -.
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 CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
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}.
FT DOMAIN 1..187
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 598 AA; 66710 MW; 215E2201298549D8 CRC64;
MHEIKKTEFG KTIRTLTLGA RKSLCIHPDV RKLSSDTAMS DKCLDMIQST KSKTPGCPYN
KRNTQVYFRN HALAQVQDIE ELHDLGEQMS SCSYYGTRSA IPLAQVIAMP YSMLLSKSTR
ESMGINIKGS IVIFDEAHNI ADAVNNTYSV TVSGQHLIKT RRQVWSYFQR YEKRLQGRNV
YYIKQLLAVL QNCHKFLTSK SALNAIFTIT DFLFEAKVDN INLFKIQQYL ERSKLAQKLL
GFVASEDGSE GVVTHVSPLR TIGAFFMALT TATANGRILV TQQEKEEGGK EHCLKFMLLN
PALHFSDIIA EAKSVILAGG TMQPVSQVLH SLLLGVDSQR VDMFSCGHII PPTNLTSVAL
AVGPTNTELD FTFSKRNRTE VMDEVGRIVL NLVRVVPGGL VVFFPSYSYE NQVVQHWQST
GVLAAIEAKK VAFREPKCTA EVDSVLTSFA AQCQASGAIL FSVVGGKMSE GINFSDDLAR
CVVMVGLPYP NPHDPELTQQ MEYMTQSVSG LSAHDFYTNL CMKAVNQSIG RSIRHRNDFA
SIVLLDRRYN TIAIRSRLPR WINDRTVSYP TFGPTIPHLV QFFKHHRANE TNAGGRTS
//
