PIF1_YEAST
ID PIF1_YEAST Reviewed; 859 AA.
AC P07271; D6VZB2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 196.
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};
DE AltName: Full=Petite integration frequency protein 1;
DE AltName: Full=Telomere stability protein 1;
DE Flags: Precursor;
GN Name=PIF1 {ECO:0000255|HAMAP-Rule:MF_03176}; Synonyms=TST1;
GN OrderedLocusNames=YML061C; ORFNames=YM9958.01C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN MITOCHONDRIAL DNA
RP REPAIR.
RX PubMed=3038524; DOI=10.1002/j.1460-2075.1987.tb02385.x;
RA Foury F., Lahaye A.;
RT "Cloning and sequencing of the PIF gene involved in repair and
RT recombination of yeast mitochondrial DNA.";
RL EMBO J. 6:1441-1449(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP COFACTOR.
RX PubMed=8253734; DOI=10.1016/s0021-9258(19)74294-x;
RA Lahaye A., Leterme S., Foury F.;
RT "PIF1 DNA helicase from Saccharomyces cerevisiae. Biochemical
RT characterization of the enzyme.";
RL J. Biol. Chem. 268:26155-26161(1993).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1849081; DOI=10.1002/j.1460-2075.1991.tb08034.x;
RA Lahaye A., Stahl H., Thines-Sempoux D., Foury F.;
RT "PIF1: a DNA helicase in yeast mitochondria.";
RL EMBO J. 10:997-1007(1991).
RN [6]
RP FUNCTION IN TELOMERE LENGTH REGULATION, MUTAGENESIS OF MET-1 AND MET-40,
RP AND ALTERNATIVE PRODUCT.
RX PubMed=8287473; DOI=10.1016/0092-8674(94)90179-1;
RA Schulz V.P., Zakian V.A.;
RT "The Saccharomyces PIF1 DNA helicase inhibits telomere elongation and de
RT novo telomere formation.";
RL Cell 76:145-155(1994).
RN [7]
RP FUNCTION IN RIBOSOMAL DNA MAINTENANCE.
RX PubMed=10693764; DOI=10.1016/s0092-8674(00)80683-2;
RA Ivessa A.S., Zhou J.-Q., Zakian V.A.;
RT "The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p have
RT opposite effects on replication fork progression in ribosomal DNA.";
RL Cell 100:479-489(2000).
RN [8]
RP FUNCTION IN TELOMERE LENGTH REGULATION, AND MUTAGENESIS OF LYS-264.
RX PubMed=10926538; DOI=10.1126/science.289.5480.771;
RA Zhou J.-Q., Monson E.K., Teng S.-C., Schulz V.P., Zakian V.A.;
RT "Pif1p helicase, a catalytic inhibitor of telomerase in yeast.";
RL Science 289:771-774(2000).
RN [9]
RP FUNCTION IN GENOMIC DNA MAINTENANCE.
RX PubMed=11429610; DOI=10.1038/35082608;
RA Myung K., Chen C., Kolodner R.D.;
RT "Multiple pathways cooperate in the suppression of genome instability in
RT Saccharomyces cerevisiae.";
RL Nature 411:1073-1076(2001).
RN [10]
RP FUNCTION IN MITOCHONDRIAL DNA REPAIR.
RX PubMed=12024022; DOI=10.1128/mcb.22.12.4086-4093.2002;
RA O'Rourke T.W., Doudican N.A., Mackereth M.D., Doetsch P.W., Shadel G.S.;
RT "Mitochondrial dysfunction due to oxidative mitochondrial DNA damage is
RT reduced through cooperative actions of diverse proteins.";
RL Mol. Cell. Biol. 22:4086-4093(2002).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [14]
RP FUNCTION IN MITOCHONDRIAL DNA REPAIR.
RX PubMed=15907372; DOI=10.1016/j.gene.2005.03.031;
RA O'Rourke T.W., Doudican N.A., Zhang H., Eaton J.S., Doetsch P.W.,
RA Shadel G.S.;
RT "Differential involvement of the related DNA helicases Pif1p and Rrm3p in
RT mtDNA point mutagenesis and stability.";
RL Gene 354:86-92(2005).
RN [15]
RP FUNCTION IN MITOCHONDRIAL DNA REPAIR.
RX PubMed=15923634; DOI=10.1128/mcb.25.12.5196-5204.2005;
RA Doudican N.A., Song B., Shadel G.S., Doetsch P.W.;
RT "Oxidative DNA damage causes mitochondrial genomic instability in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 25:5196-5204(2005).
RN [16]
RP FUNCTION IN TELOMERE LENGTH REGULATION, AND MUTAGENESIS OF LYS-264.
RX PubMed=16121131; DOI=10.1038/nature04091;
RA Boule J.-B., Vega L.R., Zakian V.A.;
RT "The yeast Pif1p helicase removes telomerase from telomeric DNA.";
RL Nature 438:57-61(2005).
RN [17]
RP FUNCTION, MUTAGENESIS OF LYS-264, AND SUBCELLULAR LOCATION.
RX PubMed=16816432; DOI=10.1534/genetics.104.036905;
RA Wagner M., Price G., Rothstein R.;
RT "The absence of Top3 reveals an interaction between the Sgs1 and Pif1 DNA
RT helicases in Saccharomyces cerevisiae.";
RL Genetics 174:555-573(2006).
RN [18]
RP FUNCTION IN DNA REPLICATION.
RX PubMed=16537895; DOI=10.1128/mcb.26.7.2490-2500.2006;
RA Budd M.E., Reis C.C., Smith S., Myung K., Campbell J.L.;
RT "Evidence suggesting that Pif1 helicase functions in DNA replication with
RT the Dna2 helicase/nuclease and DNA polymerase delta.";
RL Mol. Cell. Biol. 26:2490-2500(2006).
RN [19]
RP FUNCTION IN TELOMERE LENGTH REGULATION, AND INTERACTION WITH TELOMERASE
RP RNA.
RX PubMed=16878131; DOI=10.1038/nsmb1126;
RA Eugster A., Lanzuolo C., Bonneton M., Luciano P., Pollice A.,
RA Pulitzer J.F., Stegberg E., Berthiau A.-S., Foerstemann K., Corda Y.,
RA Lingner J., Geli V., Gilson E.;
RT "The finger subdomain of yeast telomerase cooperates with Pif1p to limit
RT telomere elongation.";
RL Nat. Struct. Mol. Biol. 13:734-739(2006).
RN [20]
RP FUNCTION IN MITOCHONDRIAL DNA MAINTENANCE, AND DNA-BINDING.
RX PubMed=17257907; DOI=10.1016/j.mito.2006.11.023;
RA Cheng X., Dunaway S., Ivessa A.S.;
RT "The role of Pif1p, a DNA helicase in Saccharomyces cerevisiae, in
RT maintaining mitochondrial DNA.";
RL Mitochondrion 7:211-222(2007).
RN [21]
RP FUNCTION.
RX PubMed=17720711; DOI=10.1093/nar/gkm613;
RA Boule J.-B., Zakian V.A.;
RT "The yeast Pif1p DNA helicase preferentially unwinds RNA-DNA substrates.";
RL Nucleic Acids Res. 35:5809-5818(2007).
RN [22]
RP FUNCTION IN TELOMERE LENGTH REGULATION, AND INDUCTION.
RX PubMed=17590086; DOI=10.1371/journal.pgen.0030105;
RA Vega L.R., Phillips J.A., Thornton B.R., Benanti J.A., Onigbanjo M.T.,
RA Toczyski D.P., Zakian V.A.;
RT "Sensitivity of yeast strains with long G-tails to levels of telomere-bound
RT telomerase.";
RL PLoS Genet. 3:1065-1075(2007).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [24]
RP FUNCTION IN G4-UNWINDING.
RX PubMed=19424434; DOI=10.1371/journal.pgen.1000475;
RA Ribeyre C., Lopes J., Boule J.B., Piazza A., Guedin A., Zakian V.A.,
RA Mergny J.L., Nicolas A.;
RT "The yeast Pif1 helicase prevents genomic instability caused by G-
RT quadruplex-forming CEB1 sequences in vivo.";
RL PLoS Genet. 5:E1000475-E1000475(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-72 AND SER-169, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [26]
RP SUBUNIT.
RX PubMed=20795654; DOI=10.1021/bi100984j;
RA Barranco-Medina S., Galletto R.;
RT "DNA binding induces dimerization of Saccharomyces cerevisiae Pif1.";
RL Biochemistry 49:8445-8454(2010).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=20655619; DOI=10.1016/j.ejcb.2010.06.008;
RA Cheng X., Ivessa A.S.;
RT "Association of the yeast DNA helicase Pif1p with mitochondrial membranes
RT and mitochondrial DNA.";
RL Eur. J. Cell Biol. 89:742-747(2010).
RN [28]
RP FUNCTION IN TELOMERE LENGTH REGULATION.
RX PubMed=20225162; DOI=10.1007/978-1-60327-355-8_25;
RA Boule J.B., Zakian V.A.;
RT "Characterization of the helicase activity and anti-telomerase properties
RT of yeast Pif1p in vitro.";
RL Methods Mol. Biol. 587:359-376(2010).
RN [29]
RP FUNCTION IN G4-UNWINDING.
RX PubMed=21620135; DOI=10.1016/j.cell.2011.04.015;
RA Paeschke K., Capra J.A., Zakian V.A.;
RT "DNA replication through G-quadruplex motifs is promoted by the
RT Saccharomyces cerevisiae Pif1 DNA helicase.";
RL Cell 145:678-691(2011).
RN [30]
RP PHOSPHORYLATION.
RX PubMed=22927468; DOI=10.1083/jcb.201205193;
RA Crider D.G., Garcia-Rodriguez L.J., Srivastava P., Peraza-Reyes L.,
RA Upadhyaya K., Boldogh I.R., Pon L.A.;
RT "Rad53 is essential for a mitochondrial DNA inheritance checkpoint
RT regulating G1 to S progression.";
RL J. Cell Biol. 198:793-798(2012).
RN [31]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23596008; DOI=10.1074/jbc.m113.470013;
RA Ramanagoudr-Bhojappa R., Chib S., Byrd A.K., Aarattuthodiyil S., Pandey M.,
RA Patel S.S., Raney K.D.;
RT "Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for
RT unwinding duplex DNA.";
RL J. Biol. Chem. 288:16185-16195(2013).
RN [32]
RP FUNCTION IN G4-UNWINDING.
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).
RN [33]
RP FUNCTION, AND INTERACTION WITH RIM1.
RX PubMed=23175612; DOI=10.1093/nar/gks1088;
RA Ramanagoudr-Bhojappa R., Blair L.P., Tackett A.J., Raney K.D.;
RT "Physical and functional interaction between yeast Pif1 helicase and Rim1
RT single-stranded DNA binding protein.";
RL Nucleic Acids Res. 41:1029-1046(2013).
RN [34]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23446274; DOI=10.1093/nar/gkt117;
RA Galletto R., Tomko E.J.;
RT "Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on
RT single-stranded DNA.";
RL Nucleic Acids Res. 41:4613-4627(2013).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of both mitochondrial and nuclear genome stability.
CC Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA
CC hybrids. Appears to move along DNA in single nucleotide or base pair
CC steps, powered by hydrolysis of 1 molecule of ATP. Processes at an
CC unwinding rate of about 75 bp/s. Resolves G4 structures, preventing
CC replication pausing and double-strand breaks (DSBs) at G4 motifs.
CC Involved in the maintenance of telomeric DNA. Inhibits telomere
CC elongation, de novo telomere formation and telomere addition to DSBs
CC via catalytic inhibition of telomerase. Reduces the processivity of
CC telomerase by displacing active telomerase from DNA ends. Releases
CC telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid
CC that is the intermediate in the telomerase reaction. Involved in the
CC maintenance of ribosomal (rDNA). Required for efficient fork arrest at
CC the replication fork barrier within rDNA. Involved in the maintenance
CC of mitochondrial (mtDNA). Required to maintain mtDNA under conditions
CC that introduce dsDNA breaks in mtDNA, either preventing or repairing
CC dsDNA breaks. May inhibit replication progression to allow time for
CC repair. May have a general role in chromosomal replication by affecting
CC Okazaki fragment maturation. May have a role in conjunction with DNA2
CC helicase/nuclease in 5'-flap extension during Okazaki fragment
CC processing. {ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:10693764, ECO:0000269|PubMed:10926538,
CC ECO:0000269|PubMed:11429610, ECO:0000269|PubMed:12024022,
CC ECO:0000269|PubMed:15907372, ECO:0000269|PubMed:15923634,
CC ECO:0000269|PubMed:16121131, ECO:0000269|PubMed:16537895,
CC ECO:0000269|PubMed:16816432, ECO:0000269|PubMed:16878131,
CC ECO:0000269|PubMed:17257907, ECO:0000269|PubMed:17590086,
CC ECO:0000269|PubMed:17720711, ECO:0000269|PubMed:1849081,
CC ECO:0000269|PubMed:19424434, ECO:0000269|PubMed:20225162,
CC ECO:0000269|PubMed:21620135, ECO:0000269|PubMed:23175612,
CC ECO:0000269|PubMed:23446274, ECO:0000269|PubMed:23596008,
CC ECO:0000269|PubMed:23657261, ECO:0000269|PubMed:3038524,
CC ECO:0000269|PubMed:8287473}.
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 ECO:0000269|PubMed:1849081, ECO:0000269|PubMed:23446274,
CC ECO:0000269|PubMed:23596008};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:8253734};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:8253734};
CC Note=Mg(2+). To a lesser extent, can also use Mn(2+).
CC {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for ATP {ECO:0000269|PubMed:8253734};
CC KM=0.4 mM for dATP {ECO:0000269|PubMed:8253734};
CC pH dependence:
CC Optimum pH is 7.5-9.5. {ECO:0000269|PubMed:8253734};
CC -!- SUBUNIT: Monomer in solution. DNA binding induces dimerization.
CC Associates with mitochondrial and telomeric DNA. Binding to mtDNA is
CC non-specific and the protein seems to coat the entire mtDNA molecule.
CC Binds to the telomerase RNA TLC1. Interacts with the mitochondrial
CC single-strand DNA-binding protein RIM1. {ECO:0000255|HAMAP-
CC Rule:MF_03176, ECO:0000269|PubMed:16878131,
CC ECO:0000269|PubMed:20795654, ECO:0000269|PubMed:23175612,
CC ECO:0000269|PubMed:8253734}.
CC -!- INTERACTION:
CC P07271; Q12306: SMT3; NbExp=2; IntAct=EBI-13404, EBI-17490;
CC -!- SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16816432}. Note=Mainly
CC concentrated in the nucleolus, and occasionally redistributes to single
CC nuclear foci outside the nucleolus, probably sites of DNA repair.
CC {ECO:0000269|PubMed:16816432}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion inner
CC membrane {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16816432,
CC ECO:0000269|PubMed:1849081, ECO:0000269|PubMed:20655619}; Peripheral
CC membrane protein {ECO:0000269|PubMed:20655619}; Matrix side
CC {ECO:0000269|PubMed:20655619}. Note=Bound to the mitochondrial inner
CC membrane either directly or indirectly via a protein complex.
CC {ECO:0000269|PubMed:20655619}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P07271-1; Sequence=Displayed;
CC Name=Nuclear;
CC IsoId=P07271-2; Sequence=VSP_034601;
CC -!- INDUCTION: Cell cycle-regulated. The nuclear isoform is present in very
CC low amounts in G1 phase cells, but increases as cells progress through
CC S phase, with a peak in late S/G2. The mitochondrial isoform follows a
CC similar, but less pronounced induction pattern. The nuclear isoform is
CC prone to APC/C-dependent degradation in G1, whereas the mitochondrial
CC isoform is not. {ECO:0000269|PubMed:17590086}.
CC -!- PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in
CC response to loss of mtDNA. {ECO:0000269|PubMed:22927468}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform Nuclear]: Produced by alternative initiation at
CC Met-40 of isoform Mitochondrial. {ECO:0000305|PubMed:8287473}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR EMBL; X05342; CAA28953.1; -; Genomic_DNA.
DR EMBL; Z46729; CAA86714.1; -; Genomic_DNA.
DR EMBL; Z38114; CAA86260.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09836.1; -; Genomic_DNA.
DR PIR; A29457; A29457.
DR RefSeq; NP_013650.1; NM_001182420.1. [P07271-1]
DR PDB; 5O6B; X-ray; 2.03 A; A/B=237-780.
DR PDB; 5O6D; X-ray; 3.28 A; A/B=237-780.
DR PDB; 5O6E; X-ray; 3.35 A; A/B=237-780.
DR PDB; 6E49; X-ray; 2.90 A; D/E/F=815-831.
DR PDBsum; 5O6B; -.
DR PDBsum; 5O6D; -.
DR PDBsum; 5O6E; -.
DR PDBsum; 6E49; -.
DR AlphaFoldDB; P07271; -.
DR SMR; P07271; -.
DR BioGRID; 35105; 196.
DR DIP; DIP-4448N; -.
DR IntAct; P07271; 3.
DR MINT; P07271; -.
DR STRING; 4932.YML061C; -.
DR iPTMnet; P07271; -.
DR MaxQB; P07271; -.
DR PaxDb; P07271; -.
DR PRIDE; P07271; -.
DR EnsemblFungi; YML061C_mRNA; YML061C; YML061C. [P07271-1]
DR GeneID; 854941; -.
DR KEGG; sce:YML061C; -.
DR SGD; S000004526; PIF1.
DR VEuPathDB; FungiDB:YML061C; -.
DR eggNOG; KOG0987; Eukaryota.
DR GeneTree; ENSGT00530000063561; -.
DR HOGENOM; CLU_001613_0_0_1; -.
DR InParanoid; P07271; -.
DR OMA; VEPEQWT; -.
DR BioCyc; YEAST:G3O-32656-MON; -.
DR BRENDA; 3.6.4.12; 984.
DR PRO; PR:P07271; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P07271; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
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:0003678; F:DNA helicase activity; IDA:SGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0010521; F:telomerase inhibitor activity; IDA:SGD.
DR GO; GO:0051276; P:chromosome organization; IMP:SGD.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0098781; P:ncRNA transcription; IMP:SGD.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:SGD.
DR GO; GO:0071932; P:replication fork reversal; IGI:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03176; PIF1; 1.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05970; PIF1; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; ATP-binding;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8253734"
FT CHAIN 46..859
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000013269"
FT DNA_BIND 727..746
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 142..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform Nuclear)"
FT /evidence="ECO:0000305"
FT /id="VSP_034601"
FT MUTAGEN 1
FT /note="M->A: In PIF1-m1; loss of mitochondrial function."
FT /evidence="ECO:0000269|PubMed:8287473"
FT MUTAGEN 40
FT /note="M->A: In PIF1-m2; loss of nuclear function."
FT /evidence="ECO:0000269|PubMed:8287473"
FT MUTAGEN 264
FT /note="K->A,R: Abolishes helicase activity resulting in
FT elongated telomeres; binds normally to DNA substrates."
FT /evidence="ECO:0000269|PubMed:10926538,
FT ECO:0000269|PubMed:16121131, ECO:0000269|PubMed:16816432"
FT CONFLICT 309
FT /note="Missing (in Ref. 1; CAA28953)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="V -> VG (in Ref. 1; CAA28953)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="D -> E (in Ref. 1; CAA28953)"
FT /evidence="ECO:0000305"
FT CONFLICT 800..801
FT /note="Missing (in Ref. 1; CAA28953)"
FT /evidence="ECO:0000305"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:5O6E"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:5O6B"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:5O6B"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:5O6B"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 422..432
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5O6D"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 497..505
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:5O6D"
FT STRAND 536..543
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 545..555
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 563..570
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 572..582
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 593..600
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:5O6B"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 639..648
FT /evidence="ECO:0007829|PDB:5O6B"
FT TURN 649..652
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 656..662
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 687..693
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 712..718
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 727..733
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:5O6B"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 755..761
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 767..777
FT /evidence="ECO:0007829|PDB:5O6B"
FT HELIX 817..821
FT /evidence="ECO:0007829|PDB:6E49"
FT TURN 822..827
FT /evidence="ECO:0007829|PDB:6E49"
SQ SEQUENCE 859 AA; 97682 MW; D7E4CAE499822C2C CRC64;
MPKWIRSTLN HIIPRRPFIC SFNSFLLLKN VSHAKLSFSM SSRGFRSNNF IQAQLKHPSI
LSKEDLDLLS DSDDWEEPDC IQLETEKQEK KIITDIHKED PVDKKPMRDK NVMNFINKDS
PLSWNDMFKP SIIQPPQLIS ENSFDQSSQK KSRSTGFKNP LRPALKKESS FDELQNNSIS
QERSLEMINE NEKKKMQFGE KIAVLTQRPS FTELQNDQDD SNLNPHNGVK VKIPICLSKE
QESIIKLAEN GHNIFYTGSA GTGKSILLRE MIKVLKGIYG RENVAVTAST GLAACNIGGI
TIHSFAGIGL GKGDADKLYK KVRRSRKHLR RWENIGALVV DEISMLDAEL LDKLDFIARK
IRKNHQPFGG IQLIFCGDFF QLPPVSKDPN RPTKFAFESK AWKEGVKMTI MLQKVFRQRG
DVKFIDMLNR MRLGNIDDET EREFKKLSRP LPDDEIIPAE LYSTRMEVER ANNSRLSKLP
GQVHIFNAID GGALEDEELK ERLLQNFLAP KELHLKVGAQ VMMVKNLDAT LVNGSLGKVI
EFMDPETYFC YEALTNDPSM PPEKLETWAE NPSKLKAAME REQSDGEESA VASRKSSVKE
GFAKSDIGEP VSPLDSSVFD FMKRVKTDDE VVLENIKRKE QLMQTIHQNS AGKRRLPLVR
FKASDMSTRM VLVEPEDWAI EDENEKPLVS RVQLPLMLAW SLSIHKSQGQ TLPKVKVDLR
RVFEKGQAYV ALSRAVSREG LQVLNFDRTR IKAHQKVIDF YLTLSSAESA YKQLEADEQV
KKRKLDYAPG PKYKAKSKSK SNSPAPISAT TQSNNGIAAM LQRHSRKRFQ LKKESNSNQV
HSLVSDEPRG QDTEDHILE
