ID A0A0J0XUY5_9TREE Unreviewed; 822 AA.
AC A0A0J0XUY5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CC85DRAFT_290675 {ECO:0000313|EMBL:KLT44872.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT44872.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT44872.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT44872.1,
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 -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000256|ARBA:ARBA00006637}.
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DR EMBL; KQ087184; KLT44872.1; -; Genomic_DNA.
DR RefSeq; XP_018281363.1; XM_018424750.1.
DR AlphaFoldDB; A0A0J0XUY5; -.
DR STRING; 879819.A0A0J0XUY5; -.
DR GeneID; 28985353; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
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:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KLT44872.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KLT44872.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:KLT44872.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT DOMAIN 351..513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 567..738
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 92305 MW; 0EA56B67D11408F6 CRC64;
MSRSPSPASS LDFMHSDGSE DEYAELRRSV QKRKPKKAAA RAVPKINLTA LQRAAAAHPA
EGQFDSDAES DDAGFLDRLG GTIDLSKQDL KPDHAARPLW IDQTGNIILE AFSPLAGAAQ
DFLVAIAEPV SRPDLMHEYR ITKSSLHAAM SVGLETNDII EVLRRLSKIP LPHKLVAHVR
EWTASYGKIK LVLKHNRYWL ESSVPEYLQR LLKDDVIKTC RVHRDEEQSD MTFGVEQGSK
PKRDYMIPGT TEARRAAGET TENGNNANGD DVIGAVIGIN ETDELDEEDA VQAFEVAGDR
IEEVRRRCKD IDLPALEEYD FRNDSVNPNL DMQLKPMTVI RPYQETSLSK MFGNGRARSG
IIVLPCGAGK TLVGITAACT IRKSTLVLCT SAVSVAQWKQ QFLQFSNISE RQICAFTRDE
KEMFQGPAGV VVSTYSMIAK TGKRAHDAQK VMDWLKTLEW GFLLLDEVHV VPAEMFRKCV
SNFKVHAKLG LTATLVREDD KIGDLGYLIG PKLYEANWKD LTRNGHIAAV QCSEVWCPMT
PEFYREYLRN PSRKRILLHA MNPNKMQAAQ FLINFHENRG DKIIVFSDNV FALEQYAQKL
GKAFIHGGTP ENERLRILSR FQHDPNLNTI FLSKVGDTSI DLPEASVLIQ ISSHFGSRRQ
EAQRLGRILR AKRRNEEGFN AFFYSLVSKD TQEMYYSTKR QGFLVDQGYE FRVITELHGI
EKMEGLVHRT KASQIELLEQ VLNASADASE TADHYGRQHG GKHQKRAAGA QPKNLASAKG
TAPAQRYTAP LEHLSGGQHM SYREQNKSVK CVQLLEGWRV QS
//
