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Database: UniProt
Entry: A0A4Z1JMP0_9HELO
LinkDB: A0A4Z1JMP0_9HELO
Original site: A0A4Z1JMP0_9HELO 
ID   A0A4Z1JMP0_9HELO        Unreviewed;       755 AA.
AC   A0A4Z1JMP0;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=BELL_0253g00010 {ECO:0000313|EMBL:TGO74828.1};
OS   Botrytis elliptica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=278938 {ECO:0000313|EMBL:TGO74828.1, ECO:0000313|Proteomes:UP000297229};
RN   [1] {ECO:0000313|EMBL:TGO74828.1, ECO:0000313|Proteomes:UP000297229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Be9601 {ECO:0000313|EMBL:TGO74828.1,
RC   ECO:0000313|Proteomes:UP000297229};
RA   Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA   Valdes J.H., Van Kan J.A.L.;
RT   "Comparative genomics of Botrytis spp.";
RL   Submitted (DEC-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TGO74828.1}.
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DR   EMBL; PQXM01000252; TGO74828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z1JMP0; -.
DR   STRING; 278938.A0A4Z1JMP0; -.
DR   Proteomes; UP000297229; 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; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 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   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_sf.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF01693; Cauli_VI; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   Pfam; PF21530; Pif1_2B_dom; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 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:UP000297229}.
FT   DOMAIN          260..420
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          190..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  85488 MW;  9049800E6EEAB7B2 CRC64;
     MPKLRLPVFL SLFANKLSTK YPRPNQTDVC QTRALVMGKR GPKKNYFVVC RGRTTGILDG
     WAQCQASTSG FSGAKFKGYE THDEAQKAWN EWLQTQGFAP TEGVPHDTLE NDLTDLSRVV
     NQTAIDNHLN ARVGLKRKYE DEDSSMNIKD SVVITSARPI EAEISAMSTE KTFIDLTKSP
     ERAISPVKLL DSEGGKTPSF KKAKSGESTP TLNPDVEIPD SEFELSDEEI FDNITSTCED
     IPKPVELTTE QKLVVKMAMG RDNIFLTGAA GSGKTVTLLQ IIEKLKKTLQ DNNSNIPKVQ
     VAAPTGLAAL PLNGRTTYSV AGWKPDSFKM PLDRLLDDNN IKKKTIKALR RLEVLILEEI
     SMVESQFLER FNLLLQTVKQ TKKPFGGIQV IFLGDFYQLP PVKPFEHCMI CGVEMAGVFD
     RVCKSNLCKD RSDNNPFKPG DKWAFNAPVW KQLKFRHVKL EQIHRQKDEK FKDLLNKVRN
     GVELSDAEWH DLIRPKVLPP NAFPIRLMAK RFDVDRFNDS QLDLIKSEAK VWEALDDSCQ
     LYRNELDYLR QHEINKKMEE YKIAISEYHR FPKRLTLKVG AKVVLLHNQE QKGGLVNGSQ
     GTIVGFVNAQ KWPAAVIQGD HADWRQVQMN HFIEKNPWRP VVKFTDGKTT AIAPVSSETL
     MGTVEDRYLA CRTQIPLILA WALSIHKSQG MTMEHVEVSR KDIFESGQLY VALSRATTLE
     GLTVTGYSRE QIAMDEDVVD FYQKTQWENL QPPSK
//
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