ID T0PXH8_SAPDV Unreviewed; 816 AA.
AC T0PXH8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=SDRG_16396 {ECO:0000313|EMBL:EQC25735.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC25735.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC25735.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC25735.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) 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; JH767257; EQC25735.1; -; Genomic_DNA.
DR RefSeq; XP_008620827.1; XM_008622605.1.
DR AlphaFoldDB; T0PXH8; -.
DR EnsemblProtists; EQC25735; EQC25735; SDRG_16396.
DR GeneID; 19957123; -.
DR VEuPathDB; FungiDB:SDRG_16396; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000030762; 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 CDD; cd18788; SF2_C_XPD; 1.
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; 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 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762}.
FT DOMAIN 12..399
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 160..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 91095 MW; 9191EFD943A5221C CRC64;
MSAPKRQKVE EDAHPFGFPF PPYSIQESLM KELYEAIDER KIGIFESPTG TGKSLSLICG
TLTWLEHNTD SRGVLLEKDA AATASDEPAW LRAYAAPSAG AAHQAELKAL CTKLDEIRAN
PAHARMKDLR LMHGGRDAPR GRKPPAAATL ETDENYIVPE YLSDKETGSR DDSDDEVDDE
DAGRGFDEPV DYGIVQIFYC SRTHSQLSQF MHEIKKTKFG ASLRTLTLGA RKSLCIHPDV
RKLKTDAAMN DKCLDLIQST SAKKKAPGCP YNKKSLQRYF RQHALAQVQD IEELYTLGDQ
LSACAYYGAR SALSAAQVIA MPYSMLLSKA TRESLGIRLK DSIVIFDEAH NIADAVNATY
AVLVSSQQWI QTRRQVWSYF KRYEGRLKGR NVYYIKQLLN VLQSCHKFLT AKAKAKEATT
TVWSITDFLF ETKLDNINLF KLHQYLERSQ LSQKLLGFLS SEFSEDGERL QEATTVGATS
THISPLRSIQ SFMLALTTAS TNGRLLLHYQ DKEGGDGKMP CLKFLLLNPA LHFADVLSEA
RSVILAGGTM QPIDQVLHQL LLGSSPDRLK VFSCGHIIPP SHLTGVALSV GPTNQELDFT
YQKRNLPQTM DEVGRILLNL VRIVPAGVVC FFPSYAYEQQ IVNHWTANGQ LAALEQKKRI
FREPKSAADV DGVLTAYAAA CHDTGGLLFS VVGGKMSEGI NFSDDLARCV VMVGLPYPNP
HDAELLQQMK YMEASGAKLT SHEFYSNMCM KAVNQSIGRS IRHQKDYASI VLLDRRYNTP
IIRSRLPQWI NDRTQAFPSF GPALPHLVRF FKHHET
//
