ID Q6FKV9_CANGA Unreviewed; 862 AA.
AC Q6FKV9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN OrderedLocusNames=CAGL0L08250g {ECO:0000313|CGD:CAL0135812,
GN ECO:0000313|EMBL:CAG62105.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG62105.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG62105.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR380958; CAG62105.1; -; Genomic_DNA.
DR RefSeq; XP_449135.1; XM_449135.1.
DR AlphaFoldDB; Q6FKV9; -.
DR STRING; 284593.Q6FKV9; -.
DR EnsemblFungi; CAGL0L08250g-T; CAGL0L08250g-T-p1; CAGL0L08250g.
DR GeneID; 2890562; -.
DR KEGG; cgr:CAGL0L08250g; -.
DR CGD; CAL0135812; CAGL0L08250g.
DR VEuPathDB; FungiDB:CAGL0L08250g; -.
DR eggNOG; KOG1123; Eukaryota.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; Q6FKV9; -.
DR OMA; RCQEIDY; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IEA:EnsemblFungi.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:EnsemblFungi.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:EnsemblFungi.
DR GO; GO:0097550; C:transcription preinitiation complex; IEA:EnsemblFungi.
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:EnsemblFungi.
DR GO; GO:0015616; F:DNA translocase activity; IEA:EnsemblFungi.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:EnsemblFungi.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0000019; P:regulation of mitotic recombination; IEA:EnsemblFungi.
DR GO; GO:0001111; P:RNA polymerase II promoter clearance; IEA:EnsemblFungi.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IEA:EnsemblFungi.
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:0000256|ARBA:ARBA00022806};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT DOMAIN 393..555
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 609..763
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97438 MW; A2146AEA68834D97 CRC64;
MTDTEKHVHR PDEEDDEEQV VAKPRRVVPM MEGFFSSDDE SAATDENEPD EDYDLNEDDK
LTKDMTSKGN DEPEEKVMST VRLTEKPRGR KKGAAAKSKI GTASYDKMKD RDLMADADND
IPADFVPDSV SAMFRTHDFS YLKLKPDHAS RPIWISPSDG RIILESFSPL AEQAQDFLVT
IAEPISRPSH IHEYKITAYS LYAAVSVGLE TDDIISVLDR LSKVPVAQSI INFIKGATIS
YGKVKLVIKH NRYFVETTQA DILKMLLRDP IIGPLRIDGE HQAQVDGNKG TGTSSVDKSS
INPNDVEAMF SAVVGEGANG EEDEENEDDI DAVHSFEIAN SSVEIVKRRC QEIDYPVLEE
YDFRNDNRNP DLEIDLKPST QIRPYQEKSL SKMFGNGRAR SGIIVLPCGA GKTLVGITAA
CTIKKSVIVL CTSSVSVMQW RQQFLQWCTL QPENCAVFTS DNKEMFQTES GLVVSTYSMV
ANTRNRSHDS QKVMDFLTGR EWGFIILDEV HVVPAAMFRR VVSTIAAHAK LGLTATLVRE
DDKISDLNFL IGPKLYEANW MELSQKGHIA NVQCAEVWCP MTAEFYQEYL RETARKRMLL
YIMNPTKFQA CQFLIQYHER RGDKIIVFSD NVYALQEYAL KLGKPFIFGS TPQQERMNIL
QNFQYNDQIN TIFLSKVGDT SIDLPEATCL IQISSHYGSR RQEAQRLGRI LRAKRRNDEG
FNAFFYSLVS KDTQEMYYST KRQAFLVDQG YAFKVITHLH GMENLPNLAY ASARERRELL
QEVLLKNEEA AGIEIGDDAD NSIGRGGSLY KKARSKAMRG EGSLAGLAGG EDMAYMEYST
KAKDLKEHHP LIRKMYYKNL KR
//
