ID F0XUE7_GROCL Unreviewed; 850 AA.
AC F0XUE7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CMQ_4705 {ECO:0000313|EMBL:EFW98853.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFW98853.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL630006; EFW98853.1; -; Genomic_DNA.
DR RefSeq; XP_014168336.1; XM_014312861.1.
DR AlphaFoldDB; F0XUE7; -.
DR STRING; 655863.F0XUE7; -.
DR GeneID; 25977946; -.
DR eggNOG; KOG1123; Eukaryota.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; F0XUE7; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000007796; 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:UniProtKB-KW.
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:EFW98853.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EFW98853.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:EFW98853.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 368..530
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 584..738
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95546 MW; D915AC34663529DE CRC64;
MAPKRKAPPG SAKVVASKSG KLSDTATPGP GTPRSVASSG QYSDDDPLSE TEEENLDKAV
HKFSLDNIPT SRPSHLDAAS RFFGNRDFSF LQLKPDHHNR PLWMDPELGF IILESFHPLA
PPAQDFLITI AEPISRPTFL HEYRLTMHSL YAAVSVGLNP LDIINTLNRF LKTPVPDGVR
DFIIRTTDSY GKVKLVLKNT KYFVESNDPA ILQKLLKDPV IGPLRVHETE EISTTMAPKM
NGLVIPGTKN AAGVRQAKDL QKGAPEKSTG GVEETPGDSA PRAGAIGDDM FAVLNEEEDA
DDDDKDAVHA FEVKDQGIEV VQKRCLDLGY PVLEEYDFRN DEVNANLDID LKPNTQIRPY
QEKSLSKMFG NGRAKSGIIV LPCGAGKTLV GITAACTIKK GVIVLCTSSM SVVQWRQEFL
KWSNINPDDI AVFTSDNKSM FTGNTGIIVT TYSMVTQTRE RSHDAKKMMD FLEGREWGMM
LLDEVHVVPA NIFRKVTSNL KTHSKLGLTA TLLREDDKIS DLNFLIGPKL YEANWMELSQ
QGHIARVQCA EVWCPMTTEF YEEYLKSSSR TKQALYVMNP RKFQACQYLI NYHESRGDKI
IVFSDDVFAL TKYATKLGKA CIYGATSQSE RLRILENFQH NASINTLFLS KIGDTSLDLP
EATCLIQISS HYGSRRQEAQ RLGRILRAKR RNDEGFNAFF YSLVSKDTQE MFYSSKRQAF
LVDQGYAFKV ITQLQDIEKT PGLAFATARE RRELLQEVLV EREKLMEDKV DDDDLWEKTK
GRSMKRMPVA RRTAGTLGEL SGGQDMAYIE QNKSVNKMLK KAGKKGESNA FFKKLQREKD
RRKHQDDEPQ
//
