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ATP-dependent DNA helicase PIF1 (EC 3.6.4.12) (DNA repair and recombination helicase PIF1) (Petite integration frequency protein 1) (Telomere stability protein 1)

 PIF1_YEAST              Reviewed;         859 AA.
P07271; D6VZB2;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
22-NOV-2017, entry version 164.
RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03176};
AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
AltName: Full=Petite integration frequency protein 1;
AltName: Full=Telomere stability protein 1;
Flags: Precursor;
Name=PIF1 {ECO:0000255|HAMAP-Rule:MF_03176}; Synonyms=TST1;
OrderedLocusNames=YML061C; ORFNames=YM9958.01C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN MITOCHONDRIAL DNA
REPAIR.
PubMed=3038524;
Foury F., Lahaye A.;
"Cloning and sequencing of the PIF gene involved in repair and
recombination of yeast mitochondrial DNA.";
EMBO J. 6:1441-1449(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, BIOPHYSICOCHEMICAL
PROPERTIES, AND COFACTOR.
PubMed=8253734;
Lahaye A., Leterme S., Foury F.;
"PIF1 DNA helicase from Saccharomyces cerevisiae. Biochemical
characterization of the enzyme.";
J. Biol. Chem. 268:26155-26161(1993).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1849081;
Lahaye A., Stahl H., Thines-Sempoux D., Foury F.;
"PIF1: a DNA helicase in yeast mitochondria.";
EMBO J. 10:997-1007(1991).
[6]
FUNCTION IN TELOMERE LENGTH REGULATION, MUTAGENESIS OF MET-1 AND
MET-40, AND ALTERNATIVE PRODUCT.
PubMed=8287473; DOI=10.1016/0092-8674(94)90179-1;
Schulz V.P., Zakian V.A.;
"The Saccharomyces PIF1 DNA helicase inhibits telomere elongation and
de novo telomere formation.";
Cell 76:145-155(1994).
[7]
FUNCTION IN RIBOSOMAL DNA MAINTENANCE.
PubMed=10693764; DOI=10.1016/S0092-8674(00)80683-2;
Ivessa A.S., Zhou J.-Q., Zakian V.A.;
"The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p
have opposite effects on replication fork progression in ribosomal
DNA.";
Cell 100:479-489(2000).
[8]
FUNCTION IN TELOMERE LENGTH REGULATION, AND MUTAGENESIS OF LYS-264.
PubMed=10926538; DOI=10.1126/science.289.5480.771;
Zhou J.-Q., Monson E.K., Teng S.-C., Schulz V.P., Zakian V.A.;
"Pif1p helicase, a catalytic inhibitor of telomerase in yeast.";
Science 289:771-774(2000).
[9]
FUNCTION IN GENOMIC DNA MAINTENANCE.
PubMed=11429610; DOI=10.1038/35082608;
Myung K., Chen C., Kolodner R.D.;
"Multiple pathways cooperate in the suppression of genome instability
in Saccharomyces cerevisiae.";
Nature 411:1073-1076(2001).
[10]
FUNCTION IN MITOCHONDRIAL DNA REPAIR.
PubMed=12024022; DOI=10.1128/MCB.22.12.4086-4093.2002;
O'Rourke T.W., Doudican N.A., Mackereth M.D., Doetsch P.W.,
Shadel G.S.;
"Mitochondrial dysfunction due to oxidative mitochondrial DNA damage
is reduced through cooperative actions of diverse proteins.";
Mol. Cell. Biol. 22:4086-4093(2002).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[14]
FUNCTION IN MITOCHONDRIAL DNA REPAIR.
PubMed=15907372; DOI=10.1016/j.gene.2005.03.031;
O'Rourke T.W., Doudican N.A., Zhang H., Eaton J.S., Doetsch P.W.,
Shadel G.S.;
"Differential involvement of the related DNA helicases Pif1p and Rrm3p
in mtDNA point mutagenesis and stability.";
Gene 354:86-92(2005).
[15]
FUNCTION IN MITOCHONDRIAL DNA REPAIR.
PubMed=15923634; DOI=10.1128/MCB.25.12.5196-5204.2005;
Doudican N.A., Song B., Shadel G.S., Doetsch P.W.;
"Oxidative DNA damage causes mitochondrial genomic instability in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 25:5196-5204(2005).
[16]
FUNCTION IN TELOMERE LENGTH REGULATION, AND MUTAGENESIS OF LYS-264.
PubMed=16121131; DOI=10.1038/nature04091;
Boule J.-B., Vega L.R., Zakian V.A.;
"The yeast Pif1p helicase removes telomerase from telomeric DNA.";
Nature 438:57-61(2005).
[17]
FUNCTION, MUTAGENESIS OF LYS-264, AND SUBCELLULAR LOCATION.
PubMed=16816432; DOI=10.1534/genetics.104.036905;
Wagner M., Price G., Rothstein R.;
"The absence of Top3 reveals an interaction between the Sgs1 and Pif1
DNA helicases in Saccharomyces cerevisiae.";
Genetics 174:555-573(2006).
[18]
FUNCTION IN DNA REPLICATION.
PubMed=16537895; DOI=10.1128/MCB.26.7.2490-2500.2006;
Budd M.E., Reis C.C., Smith S., Myung K., Campbell J.L.;
"Evidence suggesting that Pif1 helicase functions in DNA replication
with the Dna2 helicase/nuclease and DNA polymerase delta.";
Mol. Cell. Biol. 26:2490-2500(2006).
[19]
FUNCTION IN TELOMERE LENGTH REGULATION, AND INTERACTION WITH
TELOMERASE RNA.
PubMed=16878131; DOI=10.1038/nsmb1126;
Eugster A., Lanzuolo C., Bonneton M., Luciano P., Pollice A.,
Pulitzer J.F., Stegberg E., Berthiau A.-S., Foerstemann K., Corda Y.,
Lingner J., Geli V., Gilson E.;
"The finger subdomain of yeast telomerase cooperates with Pif1p to
limit telomere elongation.";
Nat. Struct. Mol. Biol. 13:734-739(2006).
[20]
FUNCTION IN MITOCHONDRIAL DNA MAINTENANCE, AND DNA-BINDING.
PubMed=17257907; DOI=10.1016/j.mito.2006.11.023;
Cheng X., Dunaway S., Ivessa A.S.;
"The role of Pif1p, a DNA helicase in Saccharomyces cerevisiae, in
maintaining mitochondrial DNA.";
Mitochondrion 7:211-222(2007).
[21]
FUNCTION.
PubMed=17720711; DOI=10.1093/nar/gkm613;
Boule J.-B., Zakian V.A.;
"The yeast Pif1p DNA helicase preferentially unwinds RNA-DNA
substrates.";
Nucleic Acids Res. 35:5809-5818(2007).
[22]
FUNCTION IN TELOMERE LENGTH REGULATION, AND INDUCTION.
PubMed=17590086; DOI=10.1371/journal.pgen.0030105;
Vega L.R., Phillips J.A., Thornton B.R., Benanti J.A., Onigbanjo M.T.,
Toczyski D.P., Zakian V.A.;
"Sensitivity of yeast strains with long G-tails to levels of telomere-
bound telomerase.";
PLoS Genet. 3:1065-1075(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[24]
FUNCTION IN G4-UNWINDING.
PubMed=19424434; DOI=10.1371/journal.pgen.1000475;
Ribeyre C., Lopes J., Boule J.B., Piazza A., Guedin A., Zakian V.A.,
Mergny J.L., Nicolas A.;
"The yeast Pif1 helicase prevents genomic instability caused by G-
quadruplex-forming CEB1 sequences in vivo.";
PLoS Genet. 5:E1000475-E1000475(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-72 AND SER-169,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[26]
SUBUNIT.
PubMed=20795654; DOI=10.1021/bi100984j;
Barranco-Medina S., Galletto R.;
"DNA binding induces dimerization of Saccharomyces cerevisiae Pif1.";
Biochemistry 49:8445-8454(2010).
[27]
SUBCELLULAR LOCATION.
PubMed=20655619; DOI=10.1016/j.ejcb.2010.06.008;
Cheng X., Ivessa A.S.;
"Association of the yeast DNA helicase Pif1p with mitochondrial
membranes and mitochondrial DNA.";
Eur. J. Cell Biol. 89:742-747(2010).
[28]
FUNCTION IN TELOMERE LENGTH REGULATION.
PubMed=20225162; DOI=10.1007/978-1-60327-355-8_25;
Boule J.B., Zakian V.A.;
"Characterization of the helicase activity and anti-telomerase
properties of yeast Pif1p in vitro.";
Methods Mol. Biol. 587:359-376(2010).
[29]
FUNCTION IN G4-UNWINDING.
PubMed=21620135; DOI=10.1016/j.cell.2011.04.015;
Paeschke K., Capra J.A., Zakian V.A.;
"DNA replication through G-quadruplex motifs is promoted by the
Saccharomyces cerevisiae Pif1 DNA helicase.";
Cell 145:678-691(2011).
[30]
PHOSPHORYLATION.
PubMed=22927468; DOI=10.1083/jcb.201205193;
Crider D.G., Garcia-Rodriguez L.J., Srivastava P., Peraza-Reyes L.,
Upadhyaya K., Boldogh I.R., Pon L.A.;
"Rad53 is essential for a mitochondrial DNA inheritance checkpoint
regulating G1 to S progression.";
J. Cell Biol. 198:793-798(2012).
[31]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=23596008; DOI=10.1074/jbc.M113.470013;
Ramanagoudr-Bhojappa R., Chib S., Byrd A.K., Aarattuthodiyil S.,
Pandey M., Patel S.S., Raney K.D.;
"Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for
unwinding duplex DNA.";
J. Biol. Chem. 288:16185-16195(2013).
[32]
FUNCTION IN G4-UNWINDING.
PubMed=23657261; DOI=10.1038/nature12149;
Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L.,
Kowalczykowski S.C., Zakian V.A.;
"Pif1 family helicases suppress genome instability at G-quadruplex
motifs.";
Nature 497:458-462(2013).
[33]
FUNCTION, AND INTERACTION WITH RIM1.
PubMed=23175612; DOI=10.1093/nar/gks1088;
Ramanagoudr-Bhojappa R., Blair L.P., Tackett A.J., Raney K.D.;
"Physical and functional interaction between yeast Pif1 helicase and
Rim1 single-stranded DNA binding protein.";
Nucleic Acids Res. 41:1029-1046(2013).
[34]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=23446274; DOI=10.1093/nar/gkt117;
Galletto R., Tomko E.J.;
"Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on
single-stranded DNA.";
Nucleic Acids Res. 41:4613-4627(2013).
-!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for
the maintenance of both mitochondrial and nuclear genome
stability. Efficiently unwinds G-quadruplex (G4) DNA structures
and forked RNA-DNA hybrids. Appears to move along DNA in single
nucleotide or base pair steps, powered by hydrolysis of 1 molecule
of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves
G4 structures, preventing replication pausing and double-strand
breaks (DSBs) at G4 motifs. Involved in the maintenance of
telomeric DNA. Inhibits telomere elongation, de novo telomere
formation and telomere addition to DSBs via catalytic inhibition
of telomerase. Reduces the processivity of telomerase by
displacing active telomerase from DNA ends. Releases telomerase by
unwinding the short telomerase RNA/telomeric DNA hybrid that is
the intermediate in the telomerase reaction. Involved in the
maintenance of ribosomal (rDNA). Required for efficient fork
arrest at the replication fork barrier within rDNA. Involved in
the maintenance of mitochondrial (mtDNA). Required to maintain
mtDNA under conditions that introduce dsDNA breaks in mtDNA,
either preventing or repairing dsDNA breaks. May inhibit
replication progression to allow time for repair. May have a
general role in chromosomal replication by affecting Okazaki
fragment maturation. May have a role in conjunction with DNA2
helicase/nuclease in 5'-flap extension during Okazaki fragment
processing. {ECO:0000255|HAMAP-Rule:MF_03176,
ECO:0000269|PubMed:10693764, ECO:0000269|PubMed:10926538,
ECO:0000269|PubMed:11429610, ECO:0000269|PubMed:12024022,
ECO:0000269|PubMed:15907372, ECO:0000269|PubMed:15923634,
ECO:0000269|PubMed:16121131, ECO:0000269|PubMed:16537895,
ECO:0000269|PubMed:16816432, ECO:0000269|PubMed:16878131,
ECO:0000269|PubMed:17257907, ECO:0000269|PubMed:17590086,
ECO:0000269|PubMed:17720711, ECO:0000269|PubMed:1849081,
ECO:0000269|PubMed:19424434, ECO:0000269|PubMed:20225162,
ECO:0000269|PubMed:21620135, ECO:0000269|PubMed:23175612,
ECO:0000269|PubMed:23446274, ECO:0000269|PubMed:23596008,
ECO:0000269|PubMed:23657261, ECO:0000269|PubMed:3038524,
ECO:0000269|PubMed:8287473}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:1849081,
ECO:0000269|PubMed:23446274, ECO:0000269|PubMed:23596008}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
ECO:0000269|PubMed:8253734};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
ECO:0000269|PubMed:8253734};
Note=Mg(2+). To a lesser extent, can also use Mn(2+).
{ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.3 mM for ATP {ECO:0000269|PubMed:8253734};
KM=0.4 mM for dATP {ECO:0000269|PubMed:8253734};
pH dependence:
Optimum pH is 7.5-9.5. {ECO:0000269|PubMed:8253734};
-!- SUBUNIT: Monomer in solution. DNA binding induces dimerization.
Associates with mitochondrial and telomeric DNA. Binding to mtDNA
is non-specific and the protein seems to coat the entire mtDNA
molecule. Binds to the telomerase RNA TLC1. Interacts with the
mitochondrial single-strand DNA-binding protein RIM1.
{ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:16878131,
ECO:0000269|PubMed:20795654, ECO:0000269|PubMed:23175612,
ECO:0000269|PubMed:8253734}.
-!- INTERACTION:
Q12306:SMT3; NbExp=2; IntAct=EBI-13404, EBI-17490;
-!- SUBCELLULAR LOCATION: Isoform Nuclear: Nucleus, nucleolus
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16816432}.
Note=Mainly concentrated in the nucleolus, and occasionally
redistributes to single nuclear foci outside the nucleolus,
probably sites of DNA repair. {ECO:0000269|PubMed:16816432}.
-!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion inner
membrane {ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:16816432, ECO:0000269|PubMed:1849081,
ECO:0000269|PubMed:20655619}; Peripheral membrane protein
{ECO:0000269|PubMed:20655619}; Matrix side
{ECO:0000269|PubMed:20655619}. Note=Bound to the mitochondrial
inner membrane either directly or indirectly via a protein
complex. {ECO:0000269|PubMed:20655619}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Mitochondrial;
IsoId=P07271-1; Sequence=Displayed;
Name=Nuclear;
IsoId=P07271-2; Sequence=VSP_034601;
Note=Produced by alternative initiation at Met-40 of isoform
Mitochondrial. {ECO:0000305|PubMed:8287473};
-!- INDUCTION: Cell cycle-regulated. The nuclear isoform is present in
very low amounts in G1 phase cells, but increases as cells
progress through S phase, with a peak in late S/G2. The
mitochondrial isoform follows a similar, but less pronounced
induction pattern. The nuclear isoform is prone to APC/C-dependent
degradation in G1, whereas the mitochondrial isoform is not.
{ECO:0000269|PubMed:17590086}.
-!- PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in
response to loss of mtDNA. {ECO:0000269|PubMed:22927468}.
-!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03176}.
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EMBL; X05342; CAA28953.1; -; Genomic_DNA.
EMBL; Z46729; CAA86714.1; -; Genomic_DNA.
EMBL; Z38114; CAA86260.1; -; Genomic_DNA.
EMBL; BK006946; DAA09836.1; -; Genomic_DNA.
PIR; A29457; A29457.
RefSeq; NP_013650.1; NM_001182420.1. [P07271-1]
ProteinModelPortal; P07271; -.
SMR; P07271; -.
BioGrid; 35105; 176.
DIP; DIP-4448N; -.
IntAct; P07271; 3.
MINT; MINT-496209; -.
STRING; 4932.YML061C; -.
iPTMnet; P07271; -.
PRIDE; P07271; -.
EnsemblFungi; YML061C; YML061C; YML061C. [P07271-1]
GeneID; 854941; -.
KEGG; sce:YML061C; -.
EuPathDB; FungiDB:YML061C; -.
SGD; S000004526; PIF1.
GeneTree; ENSGT00530000063561; -.
InParanoid; P07271; -.
KO; K15255; -.
OMA; RQQGDTK; -.
OrthoDB; EOG092C600K; -.
BioCyc; YEAST:G3O-32656-MONOMER; -.
BRENDA; 3.6.4.12; 984.
PRO; PR:P07271; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IC:SGD.
GO; GO:0005657; C:replication fork; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IBA:GO_Central.
GO; GO:0003678; F:DNA helicase activity; IDA:SGD.
GO; GO:0051880; F:G-quadruplex DNA binding; IDA:SGD.
GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
GO; GO:0010521; F:telomerase inhibitor activity; IDA:SGD.
GO; GO:0051276; P:chromosome organization; IMP:SGD.
GO; GO:0006310; P:DNA recombination; IMP:SGD.
GO; GO:0000733; P:DNA strand renaturation; IDA:SGD.
GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:SGD.
GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:SGD.
GO; GO:0071932; P:replication fork reversal; IGI:SGD.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
HAMAP; MF_03176; PIF1; 1.
InterPro; IPR010285; DNA_helicase_pif1-like.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF05970; PIF1; 2.
SUPFAM; SSF52540; SSF52540; 4.
1: Evidence at protein level;
Alternative initiation; ATP-binding; Complete proteome;
Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
DNA-binding; Helicase; Hydrolase; Membrane; Mitochondrion;
Mitochondrion inner membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Transit peptide.
TRANSIT 1 45 Mitochondrion.
{ECO:0000269|PubMed:8253734}.
CHAIN 46 859 ATP-dependent DNA helicase PIF1.
/FTId=PRO_0000013269.
NP_BIND 258 265 ATP. {ECO:0000255|HAMAP-Rule:MF_03176}.
DNA_BIND 727 746 {ECO:0000255|HAMAP-Rule:MF_03176}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 584 584 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
VAR_SEQ 1 39 Missing (in isoform Nuclear).
{ECO:0000305}.
/FTId=VSP_034601.
MUTAGEN 1 1 M->A: In PIF1-m1; loss of mitochondrial
function. {ECO:0000269|PubMed:8287473}.
MUTAGEN 40 40 M->A: In PIF1-m2; loss of nuclear
function. {ECO:0000269|PubMed:8287473}.
MUTAGEN 264 264 K->A,R: Abolishes helicase activity
resulting in elongated telomeres; binds
normally to DNA substrates.
{ECO:0000269|PubMed:10926538,
ECO:0000269|PubMed:16121131,
ECO:0000269|PubMed:16816432}.
CONFLICT 309 309 Missing (in Ref. 1; CAA28953).
{ECO:0000305}.
CONFLICT 322 322 V -> VG (in Ref. 1; CAA28953).
{ECO:0000305}.
CONFLICT 426 426 D -> E (in Ref. 1; CAA28953).
{ECO:0000305}.
CONFLICT 800 801 Missing (in Ref. 1; CAA28953).
{ECO:0000305}.
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


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