ID X0C6P9_FUSOX Unreviewed; 758 AA.
AC X0C6P9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=FOQG_09751 {ECO:0000313|EMBL:EXK86484.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK86484.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK86484.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK86484.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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; JH658385; EXK86484.1; -; Genomic_DNA.
DR AlphaFoldDB; X0C6P9; -.
DR eggNOG; KOG1123; Eukaryota.
DR HOGENOM; CLU_008213_0_0_1; -.
DR Proteomes; UP000030663; 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};
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:UP000030663}.
FT DOMAIN 281..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 497..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 729..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 85444 MW; 5A7A062CC1983C86 CRC64;
MPLKRKAQKA SIDISSIVKR DFSYLARNPD SDNRPLWIDP DKGYIILERF HPLADLATDF
LVTIAEPQSR PAFLHEYKIT SHSLYAAVSV GLNGEDIINT LDKFLKTELP QTIRDFIRSC
TKSFGKVKLV LKDNKYFVES GDADVLQTLL KDNIIGPLRV NGSGEDITTT RAPALGVLVI
PGTKNAAGVQ QADLPQTADK ESGQIEAVLD DYDKDDEKEA VHAFEIPDSA VETVQKRCLD
LSYPILEEYD FRYDNVNPDL DIDLRPNIQI RSYQEKSLSK MFGNGRAKSG IIVLPCGAGK
TLVGITAACT IRKGVIVLCT SSVSAVQWRN EFLKWSNINP GDITTFTSDS KERFSGRTGV
IVTTYSMVTN SRERAHGSKK MMDFLSGREW GLMLLDEVHV VPANMFRRVV SSIKTHSKLG
LTATLLREDD KIDHLNFLIG PKLYEANWME LSQQGHIAKV QCAEVWCSMP TVFYEQYLQV
SSRMKRTLAA INPSKFQACQ FLINYHEARG DKIIVFSDEL YSLKLYAYKL KRYLIYGGTS
QEERLRVLDH FRHSPKVNTL FLSKIGDTSL DLPEATCLIQ ISSQFGSRRQ EAQRLGRILR
AKRRNDEGFN AFFYSLVSKD TSEMHFASKR QAFLIDQGYA FKVITKLHGI EKTPDLAFCT
AVEQRELLQG TLVDNETAVD DDCEADDLWG GDGKKSNGSG TKGKVKRVAG YLDQLSGVQD
MAYIERDTSA NKGLKRKKGE KNEFFKKVDR ENKRRKNT
//
