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Database: UniProt
Entry: M7SFF7_EUTLA
LinkDB: M7SFF7_EUTLA
Original site: M7SFF7_EUTLA 
ID   M7SFF7_EUTLA            Unreviewed;       583 AA.
AC   M7SFF7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=UCREL1_10105 {ECO:0000313|EMBL:EMR62968.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62968.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
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; KB707329; EMR62968.1; -; Genomic_DNA.
DR   RefSeq; XP_007797952.1; XM_007799761.1.
DR   AlphaFoldDB; M7SFF7; -.
DR   STRING; 1287681.M7SFF7; -.
DR   KEGG; ela:UCREL1_10105; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   HOGENOM; CLU_001613_0_1_1; -.
DR   OMA; LCENTKH; -.
DR   OrthoDB; 5474774at2759; -.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd18037; DEXSc_Pif1_like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049163; Pif1-like_2B_dom.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   Pfam; PF21530; Pif1_2B_dom; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000012174}.
FT   DOMAIN          145..353
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  64320 MW;  4D3093B7FE29552B CRC64;
     MFPPLTKKTF HPSNLTGNTL KRQSSENSSS AVPLIAKKRT KLPPGFKSEK EPKRLDEDDT
     RGTWAGLESQ QPTSTPPPNS KKGQLWDMTP SAYKEKQGKL KAASKKSESE VGQATAETHP
     KSKANASAIS LSSEQQQVID LVIKNKQSVF FTGPAGTGKS VLMRAIIQEL KRKWVRDPER
     LSVTASTGLA ACNIGGMTLH SFAGIGLGKE DVPTLVRKIR RNPKAKNRWL RTNTLIIDEV
     SMVDGDLFDK LAQIARTIRN NGRPWGGIQL IITGDFFQLP PVPDGGGKKD IKFAFEAATW
     NTSIDHTIGL TQVFRQKDPV RRFESVDSGD PNIRDKLLQH MMSPKTIDLK KGAQVMLIKN
     LDETLVNGSL GKVIGFSSEA AFAFTTNRDG GEPGDDDAEV DPRSKRKLES YSRDLGGLKD
     LKEYPIVQFS ATDGTHRALL CIPEDWKVEL PNGEVQAQRK QLPLILAWAL SIHKAQGQTL
     ERVKVDLGKV FEKGQAYVAL SRATSQQGLQ VLRFDKNKVI AHPRVTNFYN KLYSAESAIK
     PKKPPTISDF AFQGSTDPLR QKGVPRQVVD LDDDEEAMAS AYA
//
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