ID   PIF1_XENLA              Reviewed;         635 AA.
AC   Q0R4F1; Q4V7N6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03176};
DE   AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
GN   Name=pif1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nakaoka H., Nishiyama A., Ishikawa F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-635.
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC       maintenance of both mitochondrial and nuclear genome stability.
CC       {ECO:0000255|HAMAP-Rule:MF_03176}.
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:0000255|HAMAP-Rule:MF_03176};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03176};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03176}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03176}.
CC       Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03176}.
CC   -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR   EMBL; DQ119644; AAZ41379.1; -; mRNA.
DR   EMBL; BC097805; AAH97805.2; -; mRNA.
DR   RefSeq; NP_001089530.1; NM_001096061.1.
DR   AlphaFoldDB; Q0R4F1; -.
DR   SMR; Q0R4F1; -.
DR   PRIDE; Q0R4F1; -.
DR   DNASU; 734585; -.
DR   GeneID; 734585; -.
DR   KEGG; xla:734585; -.
DR   CTD; 734585; -.
DR   Xenbase; XB-GENE-5924693; pif1.L.
DR   OrthoDB; 931726at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 734585; Expressed in egg cell and 11 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_03176; PIF1; 1.
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   2: Evidence at transcript level;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..635
FT                   /note="ATP-dependent DNA helicase PIF1"
FT                   /id="PRO_0000295094"
FT   DNA_BIND        578..597
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT   REGION          150..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         229..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT   CONFLICT        5
FT                   /note="E -> K (in Ref. 2; AAH97805)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   635 AA;  70954 MW;  B410F4761F3AE829 CRC64;
     MMLAEQLSPE IQSSITIEYL NSSGQALKRK VIRNSFISLG RNEFRDLVLK VSDGKLQQNF
     VIKQIQLFTR FIRDGKASVV LLPENIQLLI SNCPADKLKH FMKTLLIKHE AGKKEKPVNE
     RTRLLSGLPR MFETISPVQK KDVEQANEMR AKANSETPVK GKGLSHKGVN GGNRCQQKRT
     RTESSNSLIA DLRPSKKPTL SMPKQIRLST EQSLVLNTVL SGRNVFFTGS AGTGKSYLLK
     RIVGALPPKS TYATASTGVA ACHIGGTTLH AFAGIGSGKA SLEQCIELAK RPGVRQHWTS
     CKHLIIDEIS MVEGEFFDKL EAVARAVRGK DEPFGGIQLI VCGDFLQLPP VTQASSQTKF
     CFQGKSWRKC IHLTMELTEV RRQTDKNFIS LLQAIRLGRC TDDVARQLLQ TTNHKVERDG
     ILATRLCTHK DDVEITNERR LQQLPGESHS YEALDSDPML VKTINAQCPV NQQIQLKKGA
     QVMLAKNLDV SRGLVNGARG VVIKFEEGNK NLPVVRFLCG VTEVIKPDRW VFKGHGGIYL
     SRQQLPLKLA WAISIHKSQG MSLDCVEISL SRVFESGQAY VALSRARNLE GLRVMDFDPK
     VVRANPYVLQ FYHQMQKERA LRQTSLDDFL DKENC