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Database: UniProt
Entry: W9HBG0_FUSOX
LinkDB: W9HBG0_FUSOX
Original site: W9HBG0_FUSOX 
ID   W9HBG0_FUSOX            Unreviewed;      2093 AA.
AC   W9HBG0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=FOYG_17266 {ECO:0000313|EMBL:EWY79572.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY79572.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY79572.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-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|RuleBase:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363044};
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|RuleBase:RU363044}.
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DR   EMBL; JH717860; EWY79572.1; -; Genomic_DNA.
DR   HOGENOM; CLU_001248_5_0_1; -.
DR   OrthoDB; 2672428at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR046700; DUF6570.
DR   InterPro; IPR025476; Helitron_helicase-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF20209; DUF6570; 1.
DR   Pfam; PF14214; Helitron_like_N; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
KW   DNA damage {ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|RuleBase:RU363044};
KW   Hydrolase {ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753}.
FT   DOMAIN          346..489
FT                   /note="DUF6570"
FT                   /evidence="ECO:0000259|Pfam:PF20209"
FT   DOMAIN          708..925
FT                   /note="Helitron helicase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14214"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2093 AA;  237063 MW;  DE3D1E00C002389C CRC64;
     MESDLRNGKL RVPLEEVNRT IDGLDRRHTE RTAHRRDGGR QQEASKPQTQ GEKVMGPLEE
     ITCTLADLDR QHTEESIHRR QGERPQEAVE SQLRDGRLGL PVEEITRTSK NLDRQHAEET
     LHRTQGTVRQ GKILLPPEEI ARTLDELNRR YSGGTARPRT CDDLDRQRAR DTELVQGPST
     PEPTFRPPQT PPSRKRHRTQ QEGLLTPPPS GPSRSRKRPR LLDETVQLQQ QPLDEFLQYR
     ESCFHAKRDA SLSRSWCKEV PLALQVETSK SFYEAFTDER TLPISHCTFC YRKCPPANIT
     TIHWRTYLTP ALLQATTALQ KCKKCLPQGG DMGVDICLEC RGVFENGKLP KACSVNNMDI
     GCEHRYPREL DGLSPVEERL IALQAPFGYI TKFTVDNKTP SGVSYRKHVK GHIVVFPNNV
     DDLVATVLPH PLLQTIENIH VSWSGANRPS PAEVGTLLQV RKSRVTAALL WLQRNNPLYR
     DIEINLDEIQ GWQYAEGSTV PTALMERMQR EEPSAVEKTH TDPIVPNTDR GLEENRFTSI
     EDLLTSLQPD PSDDTPISVA NASMEQPHPP PEDAHMSAPD PESLDRDGDI LYETSTSGMF
     PLDGPAAFAE ADKLSFLAEA IQPSHTGHGN DVEPSAMAVH AAGDQPFIRV ERGADFADNL
     HEDFFPRTFP KLFPWGRGGP KALSEPDGNL HDASEPARRS GNHSLNYWAK YVLQRHGGRF
     ATHPVFCFLV FNLLLRSTNR RISMVRMTRG SFDRLERVYG SLTADRLKIA EEEMRETRTT
     TDPDISFLLR ELSIFGHAQP LSNETRLLMR RKIQAVNIWT GMPAIWITVN PNDINNPVKM
     WLSIHRLHDY DTAKELLADL RGRYDRIALS TMDPVSAAIF FHREISLFFE KYVRAGQESI
     FGKISHYYAT VETNDRGSLH LHGLLWLEGN MRLPSLIDEM ANPEEEEYRG QVVRYLDSVF
     HECLDEEAGK AIRKERKPID PVEEIMHDTE ALAAAFDNES NYIAYCCQVH SHTYTCIKYS
     LKRLVGEGAD KHKKRTACRF KAPWRIVEDT GFTEDGLLKI RRNHPLVNRY NKAMAVGLRH
     NHDISMILTR TKGLAMVFYI TNYATKLDTP MWKRLVFAAD VLRQLRESEG HPRPNLAEQD
     SRRQAVVNES RQFLMRSANR IFSERQLSAV EVCYFLLGYQ TDFTNVPQWS YINLTALYWT
     IFRRWTHLRR QASTQTDAEE PSETVQFRES GRTLLYLDAY AYRGPVLREV CLYDYMSMIT
     LERRHGRDED EAYIALEGPP ECYGWIQKLR EPPEYAVPIF QGFISDDHMD EHPVYFKRNS
     VLHLALFVPW ENFLSETQGD ITGIWSNYAA TLCPRLRSHV SNISLLRKSA EDARKDAKLW
     ASRSEGDDTV DVDFPLDEGD YSDEPTMAEH HQTYTALLQT LRSAVRDSDA TRDSPVLQSL
     IQDLCYENPV EEDRPFVQRH DNFYQQIRYN QNSPLSQCPI PSAQDLQAAA KAQDMLHLRM
     LDEMEGGIQG GTTSIGGADV DDLLVRQCDT EIPIPRQHGY PVTQNPRMFV EVGPARGFVE
     LGLLAASSYT LNDLQSMALQ LVCRFLDNYI ANPDSAGQHL QYVGGPGGTG KSRIVDALRD
     VFTARDQPHH LHITGTSGSA AAQIGGTTLH SALGLDTHRS HDKQKPPIFS EAKKWMWKQK
     LVLVIDEVSM LGGATLFHAN CHLQALRDCP DKPFGGIPVV LLMGDFYQFA PVLETSLLVD
     RMVDLAYTAS LGQATIAHHR GHSLWLLFKT VILLEEQVRA RDDPQLGALL DRVRAGTQTT
     EDLDLLNTKL VDRSQVTFKD GLRAITPLNR NRWSLNMEAV VGWARFHRRH ISVFVSSHTW
     RSRALSQQEV AQTIEQGDNS NCKIPGVFFY AQGMPVVVNK NTYTGLKVVN GAEFTAADVI
     PDPKSPGYHL ADDVTIHFGP PLGILLESQE TKDLAIPALP TGTVLIRPTT HTLDPANSHY
     RFLSGKCARR GLPVVPAFVL TDYKAQSKTF VEVLLELRGN RMTNGQPSKC DFTSLYVQLS
     RCRTLQGIKL LSPVRPQDFI GNKLDQNIID AMQRLTDLAA ETRRLFESQQ GFA
//
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