PIF1_CAMJE
ID PIF1_CAMJE Reviewed; 447 AA.
AC Q0P9V4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=ATP-dependent DNA helicase pif1;
DE EC=3.6.4.12;
GN Name=pif1; OrderedLocusNames=Cj0945c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION.
RX PubMed=23657261; DOI=10.1038/nature12149;
RA Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L.,
RA Kowalczykowski S.C., Zakian V.A.;
RT "Pif1 family helicases suppress genome instability at G-quadruplex
RT motifs.";
RL Nature 497:458-462(2013).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase that efficiently
CC unwinds G-quadruplex (G4) DNA structures. May be involved in resolving
CC commom issues that arise during DNA replication, recombination, and
CC repair. {ECO:0000269|PubMed:23657261}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL111168; CAL35065.1; -; Genomic_DNA.
DR PIR; H81368; H81368.
DR RefSeq; WP_002853306.1; NC_002163.1.
DR RefSeq; YP_002344343.1; NC_002163.1.
DR AlphaFoldDB; Q0P9V4; -.
DR SMR; Q0P9V4; -.
DR STRING; 192222.Cj0945c; -.
DR PaxDb; Q0P9V4; -.
DR PRIDE; Q0P9V4; -.
DR EnsemblBacteria; CAL35065; CAL35065; Cj0945c.
DR GeneID; 905207; -.
DR KEGG; cje:Cj0945c; -.
DR PATRIC; fig|192222.6.peg.929; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_001613_7_2_7; -.
DR OMA; ITLHQFA; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003840; DNA_helicase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02689; Herpes_Helicase; 1.
DR Pfam; PF05970; PIF1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..447
FT /note="ATP-dependent DNA helicase pif1"
FT /id="PRO_0000423711"
SQ SEQUENCE 447 AA; 51967 MW; 8D36DF2802CE25B0 CRC64;
MFDKLEKILA YDNVFLSGGA GVGKSFLTNE LIKSYRKQKK LAIALGSSAL SAFNIGGVTL
HSFFCLGYCD DMMKLSVLDR NQKQKEKLTK LKELLKTIEL IIIDEISMVS ANVFEMIGFR
LKNSQFNGKI LVVGDFFQLP PVIKEKKETL FNHSYYAFSS FFWQDLNFKN IKLSQPKRTQ
NMEFYNHLSL IRQGFLDEKI LSFFESLRID YKELENLEDD YTLLCGINKK VNNINQEKLS
KLETPLVCFK AQVKKEDKRI KDEELDSWIR SLNILEELNI KIGARIIFCV NNWDKNYYNG
EQGIIEDILY EEEKIYISII KNNGMKILLE PYTFFMEELE QSGKDFVVNI LASVTQFPIK
LAYAITIHKS QGMSIEKLVC DIDHIFENGQ LYVALSRATN PNTLKIYSTK KINFGFYFAN
ILKIDSNVIE FYKKHNFLDL EIQEQII