ID Q01C90_OSTTA Unreviewed; 812 AA.
AC Q01C90;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=OT_ostta03g04230 {ECO:0000313|EMBL:CAL53063.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CAL53063.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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:CAL53063.1}.
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DR EMBL; CAID01000003; CAL53063.1; -; Genomic_DNA.
DR RefSeq; XP_003078322.1; XM_003078274.1.
DR AlphaFoldDB; Q01C90; -.
DR STRING; 70448.Q01C90; -.
DR GeneID; 9833802; -.
DR KEGG; ota:OT_ostta03g04230; -.
DR InParanoid; Q01C90; -.
DR OMA; RCQEIDY; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000009170; Chromosome 3.
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 CDD; cd18789; SF2_C_XPB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 SMART; SM00490; HELICc; 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 ATP-binding {ECO:0000313|EMBL:CAL53063.1};
KW Helicase {ECO:0000313|EMBL:CAL53063.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000313|EMBL:CAL53063.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT DOMAIN 320..484
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 539..685
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 778..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 91008 MW; BAE60BE780535E79 CRC64;
MGGGRVKLSV KMRVKSERAP RVSFLNEDAE LNDYGPSESD SDLEDALWGG GDGFGDNDFS
ALELKPDHAN RPLWVCDDGR IFLESFSPVY KAAYDFLISV AEPVCRPANM HEYVLTPHSL
YAAVSVGLET STILSVLDRL SKTHLSEEIH DFVHQCTENY GKVKLVLQRN KFYLESNDPK
ILQELLQDDV IRAARVAGSG NASFHVSHAL KEKGAQKLVD ITEEGQDDDT AGVDVPADGL
DAKYQQEFLP EYDPDRQMHS FEIEARQVEH VKQRCLPGNL GYPTLEEYDF RNDTRNPDLN
IELKPMTRIR PYQEKSLSKM FGNGRARSGI IVLPCGAGKS LTGIAAAARI RKSCLCLCTS
SVSVDQWSAQ FKLWTNLTDL NIVRFTSQNK DEFPPPGEAC VCVTTYNMVS AGGKRSEGSE
RILEAIRSRE WGCMLLDEVH VVPAAMFRKV IGITKAHCKL GLTATLVRED DKVDHLNFLI
GPKLYEANWL DLQRDGHIAN VQCVEVWCPM TAEFFRKYCD SNYSNKKQVL YCMNPNKFMA
CQFLMQFHEQ QRKDKVIVFS DNIFALREYA TALRRPLIYG DTSHAERTRV LHAFKYSNEI
NTIFLSKVGD NSIDIPEANV IIQISSHAGS RRQEAQRLGR ILRPKAAQLS GKKTNADEHN
AFFYSLVSTD TAEMYYSTKR QQFLIQQGYA FKVVTDLIGP QDKQQLMYST QEKQLDLLAK
VLSAGEAEAG EEVLPDDEDA IRKAQKPAGA ARRTAGSMTA LSGADGAYME FDAQRGGVKK
KPSFQRASGA PKSVKPKNPI LRERDAMLRG KK
//
