ID K5WFI8_PHACS Unreviewed; 835 AA.
AC K5WFI8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PHACADRAFT_252066 {ECO:0000313|EMBL:EKM58070.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM58070.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM58070.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM58070.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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; JH930470; EKM58070.1; -; Genomic_DNA.
DR RefSeq; XP_007393398.1; XM_007393336.1.
DR AlphaFoldDB; K5WFI8; -.
DR STRING; 650164.K5WFI8; -.
DR GeneID; 18915398; -.
DR KEGG; pco:PHACADRAFT_252066; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; K5WFI8; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000008370; 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:UP000008370}.
FT DOMAIN 348..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 564..718
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 94075 MW; 78BD346F0208DAA8 CRC64;
MENEDYVDVD DNDFAESDTD TSLVPRSATI NFSALTRKLE ASRKDGDNGD DSSGLPTHRR
QQDSLVSHIF QDHDFSWLHL KSDHASRPLW ISPEDGHIIL EAFSPIAEQA QDFLVAISEP
VSRPAFIHEY KLTSYSLYAA VSVGLQTEDI IEVLNRLSKV PVPESITTFI RERTLSYGKV
KLVLKHNKYY VESSHPETLQ ILLKDRVIRE ARVHSAPVDN SIKASTFTTA KAPVKGNLVI
SGTKEAEKKK DESASGKGTN GAPTSDKELF TSVVGVESDE IEEDDDTVHS FEIDDTKIDD
VKRRCNELEY PMLEEYDFRN DTVNANLDID LKPSTVIRPY QETSLSKMFG NGRARSGIIV
LPCGAGKTLV GITAACTIKK SCLVLCTSSV SVMQWRQQFM QWSNITDRQI AVFTADQKEK
FAGESGIVVS TYSMVANTHN RSHESKKMMD FLTSREWGFI LLDEVHVVPA AMFRRVVTTI
KAHSKLGLTA TLVREDDKIA DLNYMIGPKL YEANWMDLAA KGHIANVQCA EVWCPMTPEF
YREYLREQSR KRMLLYCMNP KKFQACQFLI KYHEDRGDKI IVFSDNVYAL EAYAKKLGKL
YIHGGTGQVE RMRILQHFQH SPEVNTIFLS KVGDTSIDLP EATCLIQISS HFGSRRQEAQ
RLGRILRAKR RNDEGFNAFF YSLVSKDTQE MFYSTKRQQF LIDQGYAFKV ITHLDGMEDM
SDLVYKTRDE QIELLSSVLM ANESEADLGT DVRANEGDLA GTITSKDFGM PGKFPAVQRT
TGSLAALSGG QHMSYVEQNK SANKKLAREA APRHKLFAKR DKDKAAARKE ARAQV
//
