ID A0A2S7R479_9HELO Unreviewed; 723 AA.
AC A0A2S7R479;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=CJF32_00003466 {ECO:0000313|EMBL:PQE33587.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE33587.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE33587.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE33587.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PQE33587.1}.
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DR EMBL; NJPR01000014; PQE33587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7R479; -.
DR STRING; 2070412.A0A2S7R479; -.
DR InParanoid; A0A2S7R479; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000238813; 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 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:UP000238813}.
FT DOMAIN 326..487
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79813 MW; 1B454F07B4FD2DAE CRC64;
MPFGGATSPA KYTFVQRFLA YRWRAHAPYS LRATNVQNQA GQYSSIAAAM LKRAANNFEP
PKPKNNPPKQ VSKSSNPPQN VDIQESFKKI RSSQTIGGFT GYTNSTNPPN TLSTNVKATP
RERLSSVRPT STASSNLTSV FSRQDAFQDT PSSSVDLTQD ERPTGRPFPS AHDVSLSEFD
DFPDDDQVDL DNDVSLPLNV SMPAPPKPSR STILSSPFAP RSALRTQLET PSSALTWSSS
PPSHKDTPPG ALKRRELAQS ATIQSAIVID DDEEPNPRPD KQKKKLDDAE MAGTGADAHS
SKKNVKLSPI QLTDEQNRVK ELVVNQGKSV FFTGSAGTGK SVLMRAIIAA LKKKYVREAD
RVAVTASTGL AACNIGGVTL HSFGGIGLGK EDIPTLLKKI KRNQKAKNRW LRTKVLIVDE
ISMVDGDLFD KLEAIARGMR NNGRPFGGIQ LVITGDFFQL PPVPDQSQKS RGVKFAFDAA
TWNTAIHHTI GLTEVFRQKD PVFANMLNEM RLGKVSQETI NAFAAMKRTI EYEDNLAATE
LFPTRQEVEN SNAFRMRNLH GKLYKYEAVD TGTITDLTIR DKLLSNMMAP KTIELKKGAQ
VMLIKNMDDG LVNGSLGKVV AFMSEKSFKI YDENPDILND EGFSDMSQEN QRQKDIQKFK
MIDRELPNTN NSGLYPLYPT VAKADPPVKP TKVTKTTKEV DISDDDYDVM GWEKQGEKAR
AYV
//
