ID A0A1E4T623_9ASCO Unreviewed; 869 AA.
AC A0A1E4T623;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CANARDRAFT_26553 {ECO:0000313|EMBL:ODV87128.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV87128.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) 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; KV453848; ODV87128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4T623; -.
DR STRING; 983967.A0A1E4T623; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000094801; 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:UP000094801}.
FT DOMAIN 394..556
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 610..764
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 13..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 98367 MW; 3AFC8390632F6EDF CRC64;
MSSKVDYAKL ANGNVNDDDF LSSGESGSSS ENDSDFELAK QTSHATKLRK QNLTKQTKNS
IKTIKDTTDD KEFEEDELIK VSLDRPSDFI PDSVSTIFGN SDFSYLKLKP DHSSRPIWIS
PLDGKIFLES FSPLSEQAQD FLVTIAEPVS RPSFMHEYRI TTHSLYAAVS VGLETDDIIS
VLSRLSKVPV ATSVINFIKQ ATVSYGKVKL VLKHNRYFVE SPQADILQML LKDEVIGKLR
IQSSETTVTT SDGLVLTKAP SQGDLIIPGT EQNRKEKEEK EKQRKEVVNR KKNRIIDDED
EDGNDDEIKE DVEDIFANVI GEANDDDDDD FDTVHSFEIA SGSVEIVKKR CQEIDYPMLE
EYDFRNDTRN PDLEIDLKPS TQIRPYQEKS LSKMFGNGRA RSGIIVLPCG AGKTLVGITA
ACTIRKSVIV LCTSSVSVMQ WRQQFLQWCT IQPENVAVFT SENKEMFRGD AGLVVSTYSM
VANTRNRSHD SQKVMDFLTG REWGFIILDE VHVVPAAMFR RVVTTIAAHA KLGLTATLVR
EDEKISDLNF LIGPKLYEAN WMELSQKGHI ANVQCAEVWC PMTSEFYQEY LRESARKRML
LYIMNPTKFQ ACQFLIHYHE KRGDKIIVFS DNVYALQEYA LKLGKPFIYG ATPQQERMNI
LQNFQYNDQV NTIFLSKVGD TSIDLPEATC LIQISSHYGS RRQEAQRLGR ILRAKRRNDE
GFNAFFYSLV SKDTQEMYYS TKRQAFLVDQ GYAFKIITHL HGMESLPGLA YSTAKERREL
LQEVLLKNED LAGVEIGEDS DNLIGHGVSK RLKNGGSGGS NSRVQKNQGS LAGLAGGEDM
AYVEYSKNKN KELAHHPFFQ KNYYKKKKK
//
