PIF1_SCHPO
ID PIF1_SCHPO Reviewed; 805 AA.
AC Q9UUA2; O74239;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ATP-dependent DNA helicase pfh1;
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03176};
DE AltName: Full=DNA repair and recombination helicase pfh1;
DE AltName: Full=PIF1 helicase homolog;
DE AltName: Full=RRM3/PIF1 homolog 1;
DE Flags: Precursor;
GN Name=pfh1; Synonyms=pif1, rph1; ORFNames=SPBC887.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND COFACTOR.
RX PubMed=12058079; DOI=10.1091/mbc.02-02-0021;
RA Zhou J.-Q., Qi H., Schulz V.P., Mateyak M.K., Monson E.K., Zakian V.A.;
RT "Schizosaccharomyces pombe pfh1(+) encodes an essential 5' to 3' DNA
RT helicase that is a member of the PIF1 subfamily of DNA helicases.";
RL Mol. Biol. Cell 13:2180-2191(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-338; LEU-458 AND GLY-508.
RX PubMed=12409464; DOI=10.1093/nar/gkf590;
RA Tanaka H., Ryu G.H., Seo Y.S., Tanaka K., Okayama H., MacNeill S.A.,
RA Yuasa Y.;
RT "The fission yeast pfh1(+) gene encodes an essential 5' to 3' DNA helicase
RT required for the completion of S-phase.";
RL Nucleic Acids Res. 30:4728-4739(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=15302919; DOI=10.1093/nar/gkh720;
RA Ryu G.H., Tanaka H., Kim D.H., Kim J.H., Bae S.H., Kwon Y.N., Rhee J.S.,
RA MacNeill S.A., Seo Y.S.;
RT "Genetic and biochemical analyses of Pfh1 DNA helicase function in fission
RT yeast.";
RL Nucleic Acids Res. 32:4205-4216(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-1 AND MET-21, AND
RP ALTERNATIVE INITIATION (ISOFORM MITOCHONDRIAL AND NUCLEAR).
RX PubMed=18725402; DOI=10.1128/mcb.00191-08;
RA Pinter S.F., Aubert S.D., Zakian V.A.;
RT "The Schizosaccharomyces pombe Pfh1p DNA helicase is essential for the
RT maintenance of nuclear and mitochondrial DNA.";
RL Mol. Cell. Biol. 28:6594-6608(2008).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of both mitochondrial and nuclear genome stability.
CC Involved in the maintenance of mitochondrial (mtDNA). Required for both
CC repair of mitochondrial DNA and recognition of a recombinogenic signal
CC characterized by a 26-bp palindromic at sequence in the ery region of
CC mitochondrial DNA. May have a general role in chromosomal replication
CC by affecting Okazaki fragment maturation. Required for the completion
CC of S-phase. {ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:12058079, ECO:0000269|PubMed:12409464,
CC ECO:0000269|PubMed:15302919, ECO:0000269|PubMed:18725402}.
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:12409464, ECO:0000269|PubMed:15302919};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:12058079};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:15302919}.
CC -!- SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:12409464, ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:18725402}. Note=Mainly concentrated in the
CC nucleolus, and occasionally redistributes to single nuclear foci
CC outside the nucleolus, probably sites of DNA repair.
CC {ECO:0000269|PubMed:18725402}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18725402}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=Q9UUA2-1; Sequence=Displayed;
CC Name=Nuclear;
CC IsoId=Q9UUA2-2; Sequence=VSP_053259;
CC -!- MISCELLANEOUS: [Isoform Nuclear]: Produced by alternative initiation at
CC Met-40 of isoform Mitochondrial. {ECO:0000305|PubMed:18725402}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR EMBL; AF074944; AAC26139.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21899.1; -; Genomic_DNA.
DR PIR; T40739; T40739.
DR PIR; T47241; T47241.
DR RefSeq; NP_596488.1; NM_001022408.2.
DR AlphaFoldDB; Q9UUA2; -.
DR SMR; Q9UUA2; -.
DR BioGRID; 277727; 61.
DR STRING; 4896.SPBC887.14c.1; -.
DR iPTMnet; Q9UUA2; -.
DR MaxQB; Q9UUA2; -.
DR PaxDb; Q9UUA2; -.
DR PRIDE; Q9UUA2; -.
DR EnsemblFungi; SPBC887.14c.1; SPBC887.14c.1:pep; SPBC887.14c. [Q9UUA2-1]
DR GeneID; 2541213; -.
DR KEGG; spo:SPBC887.14c; -.
DR PomBase; SPBC887.14c; pfh1.
DR VEuPathDB; FungiDB:SPBC887.14c; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_0_1_1; -.
DR InParanoid; Q9UUA2; -.
DR OMA; QRETWNI; -.
DR PhylomeDB; Q9UUA2; -.
DR BRENDA; 3.6.4.12; 5613.
DR PRO; PR:Q9UUA2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0043601; C:nuclear replisome; EXP:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:PomBase.
DR GO; GO:0033678; F:5'-3' DNA/RNA helicase activity; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR GO; GO:0061995; F:ATP-dependent protein-DNA complex displacement activity; IDA:PomBase.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:PomBase.
DR GO; GO:0070336; F:flap-structured DNA binding; IDA:PomBase.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:PomBase.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; ISO:PomBase.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IMP:PomBase.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:PomBase.
DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IGI:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:CACAO.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
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; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative initiation; ATP-binding; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..805
FT /note="ATP-dependent DNA helicase pfh1"
FT /id="PRO_0000013268"
FT DNA_BIND 744..763
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 58..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform Nuclear)"
FT /evidence="ECO:0000305"
FT /id="VSP_053259"
FT MUTAGEN 1
FT /note="M->A: In pfh1-m1; localizes exclusively to nucleus,
FT loss of mitochondrial function."
FT /evidence="ECO:0000269|PubMed:18725402"
FT MUTAGEN 21
FT /note="M->A: In pfh1-m21; localizes exclusively to
FT mitochondria, loss of nuclear function."
FT /evidence="ECO:0000269|PubMed:18725402"
FT MUTAGEN 338
FT /note="K->E: Abolishes ATPase and DNA unwinding
FT activities."
FT /evidence="ECO:0000269|PubMed:12409464"
FT MUTAGEN 458
FT /note="L->S: In pfh1-R20; cold sensitive for growth,
FT suppresses a temperature-sensitive allele of cdc24."
FT /evidence="ECO:0000269|PubMed:12409464"
FT MUTAGEN 508
FT /note="G->E: In pfh1-R23; cold sensitive for growth,
FT suppresses a temperature-sensitive allele of cdc24."
FT /evidence="ECO:0000269|PubMed:12409464"
FT CONFLICT 203
FT /note="T -> A (in Ref. 1; AAC26139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 90050 MW; AD6DA44B47C8CABF CRC64;
MFSCQSLYKF SHSFRKRIPV MFQRAQQKSS LLHTQNESSH QPSLNKLGGF SSASLNFNSS
RSSTNDDQQT FSSQSDNLPS SPITLPAKRG RSAASLKQLD NTVGFDVSKP SLPVFENSGL
GSKYSTEIAN GVYIDENDFD DDLLLENDID QKPIPWSSSP IEHTKLTKSM LSSEKRSKNH
LSKIYEDHTS EKGASSVISS NITRQGIKRS RTLPWAVDPY RYGDPDPKRT STSADISQHT
VSNDSSNKLS NGRSSSLDSL AKKRMSKSKS TPQISKKFSV PLNSASKSPI GSSLFKTSDS
RKKSVPSIFL SDEQKRILDM VVEQQHSIFF TGSAGTGKSV LLRKIIEVLK SKYRKQSDRV
AVTASTGLAA CNIGGVTLHS FAGVGLARES VDLLVSKIKK NKKCVNRWLR TRVLIIDEVS
MVDAELMDKL EEVARVIRKD SKPFGGIQLV LTGDFFQLPP VPENGKESKF CFESQTWKSA
LDFTIGLTHV FRQKDEEFVK MLNELRLGKL SDESVRKFKV LNRTIEYEDG LLPTELFPTR
YEVERSNDMR MQQINQNPVT FTAIDSGTVR DKEFRDRLLQ GCMAPATLVL KVNAQVMLIK
NIDDQLVNGS LGKVIGFIDD ETYQMEKKDA EMQGRNAFEY DSLDISPFDL PDVKQKKYKL
IAMRKASSTA IKWPLVRFKL PNGGERTIVV QRETWNIELP NGEVQASRSQ IPLILAYAIS
IHKAQGQTLD RVKVDLGRVF EKGQAYVALS RATTQEGLQV LNFSPAKVMA HPKVVQFYKQ
LASVNGLPIR NENKAPVQMR GVKNK
