PIF1_YEAS7
ID PIF1_YEAS7 Reviewed; 859 AA.
AC A6ZM04;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 ORFNames=SCY_4116;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity). {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 Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176};
CC Note=Mg(2+). To a lesser extent, can also use Mn(2+).
CC {ECO:0000255|HAMAP-Rule:MF_03176};
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 (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
CC -!- SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus
CC {ECO:0000250}. Note=Mainly concentrated in the nucleolus, and
CC occasionally redistributes to single nuclear foci outside the
CC nucleolus, probably sites of DNA repair. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion inner
CC membrane {ECO:0000255|HAMAP-Rule:MF_03176}; Peripheral membrane protein
CC {ECO:0000250}; Matrix side {ECO:0000250}. Note=Bound to the
CC mitochondrial inner membrane either directly or indirectly via a
CC protein complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=A6ZM04-1; Sequence=Displayed;
CC Name=Nuclear;
CC IsoId=A6ZM04-2; Sequence=VSP_034602;
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 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in
CC response to loss of mtDNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR EMBL; AAFW02000020; EDN64334.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZM04; -.
DR SMR; A6ZM04; -.
DR PRIDE; A6ZM04; -.
DR EnsemblFungi; EDN64334; EDN64334; SCY_4116. [A6ZM04-1]
DR HOGENOM; CLU_001613_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; 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:0051880; F:G-quadruplex DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010521; F:telomerase inhibitor activity; IEA:UniProtKB-UniRule.
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:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:UniProtKB-UniRule.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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 3: Inferred from homology;
KW Alternative initiation; ATP-binding; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 46..859
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000343448"
FT DNA_BIND 727..746
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 142..183
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:0000250|UniProtKB:P07271"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07271"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07271"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07271"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform Nuclear)"
FT /evidence="ECO:0000305"
FT /id="VSP_034602"
SQ SEQUENCE 859 AA; 97628 MW; 7D40E00665852D44 CRC64;
MPKWIRSTLN HIIPRRPFIC SFNSFLLLKN VSHAKLSFSM SSRGFRSNNF IQAQLKHPSI
LSKEDLDLLS DSDDWEEPDC IQLETEKQEK KIITDIHKED PVDKKPMRDK NVMNFINKDS
PLSWNDMFKP SIIQPPQLIS ENSFDQSSQK KSRSTGFKNP LRPALKKESS FDELQNSSIS
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 TQSNSGIAAM LQRHSRKRFQ LKKESNSNQV
HSLVSDEPRG QDTEDHILE
