PIF1_PSYWF
ID PIF1_PSYWF Reviewed; 659 AA.
AC A5WFR0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=ATP-dependent DNA helicase pif1;
DE EC=3.6.4.12;
GN Name=pif1; OrderedLocusNames=PsycPRwf_1560;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000713; ABQ94501.1; -; Genomic_DNA.
DR RefSeq; WP_011960782.1; NC_009524.1.
DR AlphaFoldDB; A5WFR0; -.
DR SMR; A5WFR0; -.
DR STRING; 349106.PsycPRwf_1560; -.
DR EnsemblBacteria; ABQ94501; ABQ94501; PsycPRwf_1560.
DR KEGG; prw:PsycPRwf_1560; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_001613_7_2_6; -.
DR OMA; ITLHQFA; -.
DR OrthoDB; 961809at2; -.
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; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR029491; Helicase_HTH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF14493; HTH_40; 1.
DR Pfam; PF05970; PIF1; 2.
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.
FT CHAIN 1..659
FT /note="ATP-dependent DNA helicase pif1"
FT /id="PRO_0000423712"
SQ SEQUENCE 659 AA; 72807 MW; AAF2EA6619C865FD CRC64;
MKQATALDIL KTGKNVFLTG SAGSGKTYTL NEYIHYLRAR RVPVATTAST GIAATHMNGI
TIHSWSGIGI KDELTERDLV NLSRKKVLKD RLQETAVLII DEISMLHAKQ LNLVNQVLKH
MRQNDKPFGG IQVVVAGDFF QLPPVGSRGE SNRDKFAFMS QAWLDAGFKI CYLSEQHRQQ
SGEGEDAQIT LDNILNQIRG ENGVSAAAIA ALQNTFYQDV DVNRTRLYTH NVNVNKINEH
ELALLEGETV TYNAIAHGDN KLVETLKKSV RTSDELTLKT GAKVMFIKNN SELGVSNGTM
GELIGFTTIK PLKLSIATID DGSADEDGSA EALDEALETL EDAEALAQNE SDKPLVSTDR
YPIVRLNSGR QVIAEGEEWI VEDESGEILA SYTQIPLTLA WAITIHKSQG MTLDAAEIDL
SKTFELGQGY VALSRLKSLE GLKLLGMNDL SLRLDPLARG ADSRFKDLSL EAQQAFEDIE
REVLQESHER FVIASGGTLN KANIAAFEKE YKNRKKKQAQ KLAQKDKLSN QLSDHSESTL
MATRILLEES LSIAEIAQSR GLAQSTIMGH VARLRRQDPS LNCEHLRPDE AILNKVSKAV
DAIIAAGDPN DFNAADDSTQ SVKGGDDFDK QRIKLRPIYE YLKQQIDYNT IRLALVFID