ID A0A194SFK0_RHOGW Unreviewed; 976 AA.
AC A0A194SFK0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=RHOBADRAFT_47882 {ECO:0000313|EMBL:KPV78366.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV78366.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV78366.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV78366.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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; KQ474073; KPV78366.1; -; Genomic_DNA.
DR RefSeq; XP_018274415.1; XM_018415062.1.
DR AlphaFoldDB; A0A194SFK0; -.
DR STRING; 578459.A0A194SFK0; -.
DR GeneID; 28975510; -.
DR OMA; GKQKDPI; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000053890; 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};
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:UP000053890}.
FT DOMAIN 484..646
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 700..854
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 107053 MW; D5CE8C208F512617 CRC64;
MASHTLSDSD STASGPATKR ARRAAATAAP VDLTGAASSD SDQSDDGKNP DRSYKLTRQE
RAAEYESDYD LDDVDHDADA QLDDDADEDE DDFVPDRSSA AAAAAKGKGK AKPKPKAKAG
AKGGKGKGKA AAASASGSGT TRFKLSSASA AAYGADSAAS SSSSRLPILQ SAGVSAHEAV
GALLNANIRQ DRDYGYLPLR PDQASRPFYI VPSTGHIILE NFHPLAKYAT DFLVAIAEPV
SRPRFIHEYK LTPHSLYAAV SVGLETENII EVLNRMSKVP VPDELCDFIR DCTHSYGKVK
MVLKKNKHFV ESSDPETLRI LLRDDVIAKA RVPPDEQLAR DGAAAQANGT ATATFGLEKD
KAPSRAGLVI PGTSKGDGAG VAGAAAGQEA GKDGAAQMSR EEEDLFTAVV GLDKEDQMDD
DDEVHSFEVR EAEIEAVKRR CLDLDYRMME EYDFRHDEVN PTLEIDLKPT AALRPYQEKS
LGKMFGNGRA RSGIIVLPCG AGKTLVGITA ATTIRKSCIV LCTSSVSVMQ WRQQFLQWST
IKESAISVFT ADQKEKFTGD AGIVVSTYSM VANRQKRSHD SQKMMDFLTS REWGFILLDE
VHVVPAAMFR RVVTKIKAHT KLGLTATLVR EDDKIDDLNF LIGPKLYEAN WMDLAENGHI
AKVQCAEVWC DMTPEFYREY LRENVRRKML LYCMNPRKFQ ACQFLIQYHE NRGDKIIVFS
DNVYALEAYA KKLGKLYIHG GTPQVERMRI LQNFQHNPIV NTIFLSKVGD TSIDLPEATC
LIQISSHFGS RRQEAQRLGR ILRAKRRNDE GFNAFFYSLV SKDTQEMFYS SKRQGFLVDQ
GYAFKVITSL DGLEQLDNLV YPTRAEQIEL LQSVLLASET DADRAAAAGE DDGMGAKDVG
GFGGTPAPFG RRDGAPQATR IAGNLQALSG GQSMAYSERQ KSANKQLAKD SKSQRNALFR
KRDEEKKRRA KEKAAG
//
