ID G8B8R9_CANPC Unreviewed; 794 AA.
AC G8B8R9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD {ECO:0000256|ARBA:ARBA00014344};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN OrderedLocusNames=CPAR2_300070 {ECO:0000313|CGD:CAL0000144509,
GN ECO:0000313|EMBL:CCE41018.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE41018.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC transmission and normal cell cycle progression in G(2)/M (By
CC similarity). May have a role in changing DNA topology to allow the
CC loading of proteins involved in maintaining sister chromatid cohesion
CC in the vicinity of the centromeres (By similarity). Has a specific role
CC in chromosome segregation during meiosis II.
CC {ECO:0000256|ARBA:ARBA00025396}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000256|ARBA:ARBA00009146}.
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DR EMBL; HE605204; CCE41018.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B8R9; -.
DR STRING; 578454.G8B8R9; -.
DR EnsemblFungi; CPAR2_300070-T; CPAR2_300070-T-p1; CPAR2_300070.
DR CGD; CAL0000144509; CPAR2_300070.
DR VEuPathDB; FungiDB:CPAR2_300070; -.
DR eggNOG; KOG1131; Eukaryota.
DR Proteomes; UP000005221; Chromosome 3.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 1.10.275.40; -; 1.
DR Gene3D; 1.10.30.20; Bacterial XPD DNA helicase, FeS cluster domain; 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; IPR010643; HBB.
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 InterPro; IPR001945; RAD3/XPD.
DR InterPro; IPR042493; XPD_DNA_FeS.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF1; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF06777; HBB; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR PRINTS; PR00852; XRODRMPGMNTD.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000005221}.
FT DOMAIN 7..295
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT COILED 266..308
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 794 AA; 91137 MW; B856E040D3893231 CRC64;
MKFYIDDLPV LFPYPRIYPE QYAYMSDIKK TLDVGGNCIL EMPSGTGKTI SLLSLTVAYQ
MHYPEHRKIV YCSRTMSEIE KALIELHKLM EFRASELGYV EDFRGLGLTS RKNLCLNPLI
SREKKGNVVD EMCRRVTNGQ LKEKIEKGVV TEEDQIQDPA KYSLCSFHEK LYDLDPHDLI
PQGVYSFDAL IRYCKEMGTC PYFTARRMIP FCNIIIYSYH YLLDPKIADR VSRELSKDSI
IIFDEAHNID NVCIESLSLD LTEDVLKRAT RGANKLADAV EDMKAQDSEK LQNEYEQLVE
GLRQAEVERE QEMFMSNPIL PQDLLDEAIP GNIRKGEHFV AFLKRFIEYL KTRMKVLHVI
SETPTSFLQH LKELTYIDKK PLKFCSERLS LLVKTLELTE IEDFNALKDI ATFATLVSTY
DTGFQLILEP FETEGSTVPN PMLHFTCLDA SIAIKPVFER FSSVIITSGT ISPLDMYPKM
LNFQTVIQES YAMTLARRSF LPMIVTKGSD QVSISSRFEI RNDPSVVRNY GSLLIEFAKI
TPDGMVVFFP SYLYMESIIS MWQTMGVLDE VWKHKLILVE TPDAQETSLA LETYRKACSN
GRGAVLLSVA RGKVSEGIDF DHHYGRTVLM IGIPFQYTES RILKARLEFM RDHFQIKEND
FLSFDAMRHA AQCLGRVLRG KDDYGIMVLA DRRFARKKAQ LPKWIAQALN DSDTNLSTDM
ALATAKKFLR SLAQPTNPKD QEGVSVWDID QLEAYQKQYN QGCVKDKEET EKNGKIEEMG
EEFMDIDDED IDLL
//
