ID A0A0J0XLJ7_9TREE Unreviewed; 801 AA.
AC A0A0J0XLJ7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 13-SEP-2023, entry version 42.
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 ORFNames=CC85DRAFT_328664 {ECO:0000313|EMBL:KLT41955.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41955.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT41955.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41955.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) 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 -!- 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; KQ087211; KLT41955.1; -; Genomic_DNA.
DR RefSeq; XP_018278446.1; XM_018426720.1.
DR AlphaFoldDB; A0A0J0XLJ7; -.
DR STRING; 879819.A0A0J0XLJ7; -.
DR GeneID; 28987323; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000053611; 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: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:InterPro.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 1.10.275.40; -; 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; 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 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; 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:UP000053611}.
FT DOMAIN 7..285
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 91492 MW; AE5142C758423777 CRC64;
MKFMIDDLPV LFPYDRVYPE QYSYMCDLKK TLDAGGHCVL EMPSGTGKTV SLLSLIVSYM
QFYPQKRKLI YCSRTVPEIE KALAELKRLM EYREEQGANE REFRGLGLTS RKNLCLNPEV
NKQKKGKVVD SMCRDLTSSY ACERGRAEPG SVPLCSWHEE LNNYETGNLI PPGVWTLDDV
KKYGQDKGVC PYFTIRRMMP FVDVIIYSFH YLLDPKVAEQ VSAELSAESI VVFDEAHNID
NVCIESLSID LTRPMLESAA RSVAKIGDKV DEIKKTDAAK LQEEYDKLVE GLRSSNDRHD
PEDDMLANPV LTDDMIQGAI PGNIRKAEHF IAFLKRFIEY LKTRMRVLHV VAETPVSFLA
HLKEITFIEK RPLQFCAERL TNLIRTLELT NIEEHAALQK IASFGTLVST YEKGFLLILE
PYETEHATVP NPIFRFTCLD PSLAIAPIFE RFGSVIITSG TISPLDMYPK ILQFQPVIQE
SYPMTLTRNA FLPMVITRGS DQVPISSRFE VRNDPAVVRN FGSILIELSK TVPDGVVAFF
PSYLYMESIV SAWYDMGILS EVWKHKLLFV ETPDAMETSI ALKNYREACN NGRGAVLLSV
ARGKVSEGID FDHNYGRAVI MFGIPYQYTE SRILKARLEF LRDNHRVREN DYLTFDAMRH
AAQCVGRVLR GKTDWGLMVF ADKRFARQDK RSKLPRWINQ YITDAHSNLS TDMAVVLAKK
FIRQISQPFD HTQTGISLWT LEDIEERQRQ DKEEAERAGA EIDRAFGPQV NGRVDDADVE
MDQHFEIDDA VLAEVDWPED V
//