PIF1_CANAL
ID PIF1_CANAL Reviewed; 906 AA.
AC Q59RQ0; A0A1D8PTG7; Q59RT8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 {ECO:0000255|HAMAP-Rule:MF_03176};
GN OrderedLocusNames=CAALFM_CR07360WA; ORFNames=CaO19.13552, CaO19.6133;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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. Resolves G4 structures, preventing replication pausing and
CC double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance
CC of telomeric DNA. Inhibits telomere elongation, de novo telomere
CC formation and telomere addition to DSBs via catalytic inhibition of
CC telomerase. Reduces the processivity of telomerase by displacing active
CC telomerase from DNA ends. Releases telomerase by unwinding the short
CC telomerase RNA/telomeric DNA hybrid that is the intermediate in the
CC telomerase reaction. Involved in the maintenance of ribosomal (rDNA).
CC Required for efficient fork arrest at the replication fork barrier
CC within rDNA. Involved in the maintenance of mitochondrial (mtDNA).
CC Required to maintain mtDNA under conditions that introduce dsDNA breaks
CC in mtDNA, either preventing or repairing dsDNA breaks. May inhibit
CC replication progression to allow time for repair. May have a general
CC role in chromosomal replication by affecting Okazaki fragment
CC maturation. May have a role in conjunction with DNA2 helicase/nuclease
CC in 5'-flap extension during Okazaki fragment processing.
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. Interacts with telomerase. {ECO:0000255|HAMAP-
CC 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; CP017630; AOW31431.1; -; Genomic_DNA.
DR RefSeq; XP_712340.2; XM_707247.2.
DR PDB; 7OTJ; X-ray; 2.58 A; A/B=367-883.
DR PDBsum; 7OTJ; -.
DR AlphaFoldDB; Q59RQ0; -.
DR SMR; Q59RQ0; -.
DR STRING; 237561.Q59RQ0; -.
DR PRIDE; Q59RQ0; -.
DR GeneID; 3646054; -.
DR KEGG; cal:CAALFM_CR07360WA; -.
DR CGD; CAL0000185430; PIF1.
DR VEuPathDB; FungiDB:CR_07360W_A; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_0_2_1; -.
DR InParanoid; Q59RQ0; -.
DR OrthoDB; 931726at2759; -.
DR PRO; PR:Q59RQ0; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:EnsemblFungi.
DR GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0010521; F:telomerase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IEA:EnsemblFungi.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0098781; P:ncRNA transcription; IEA:EnsemblFungi.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:UniProtKB-UniRule.
DR GO; GO:0071932; P:replication fork reversal; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03176; PIF1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05970; PIF1; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..906
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000423708"
FT DNA_BIND 840..859
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 77..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 396..410
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:7OTJ"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 457..465
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 479..493
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:7OTJ"
FT TURN 556..559
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 561..569
FT /evidence="ECO:0007829|PDB:7OTJ"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 577..584
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 605..618
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 624..627
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 638..644
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 650..654
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 675..681
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 754..759
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 781..785
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 789..794
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 800..806
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 817..820
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 825..831
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 840..846
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 851..853
FT /evidence="ECO:0007829|PDB:7OTJ"
FT STRAND 854..858
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 861..863
FT /evidence="ECO:0007829|PDB:7OTJ"
FT HELIX 868..876
FT /evidence="ECO:0007829|PDB:7OTJ"
SQ SEQUENCE 906 AA; 101321 MW; E0D56B2B5C702998 CRC64;
MLNANKSIIR LATYSIRNRI HHLRTLHSLN YINSRINIQD TNHIRPTCPC GSKQFMLESE
LDSALIEFLD NDDPFSDSEI KESDDLSKGQ SHVYNGSPVT KNSILQIEKQ QIQKSPRPTE
TNKRMQIRKD PDQNDNVDDD SLSSTFEFSD MDDDFMEALK AAEEITGNNT NCIKRTASTP
LKKPIAKSMK NSSTPSKSAG KKYCKYIKTS SPSPSHYLIR ESGSGVDILE GSPNKVQADN
ASPFRITSSF SSPSQIQNQG VGANPGPKSK AEQNVSSASQ SSSPPMTVSQ VRNPFKVPTQ
FRRNYSTRPI TNQGSDTKKG NSHHTILLAT QKPGVPFSNP SDRSYHKLEK TEGINEAQSE
AKNVKPIILS NEQEYVLKQV LSGVSLFYTG SAGTGKSVLL RSIIKSLRDK YPKGVAVTAS
TGLAACNIGG ITLHSFAGFG LGQGKVENLI KKIKRNKKAF TRWRETRVLI IDEISMVDGH
LLNKLNEIAK NLRRNNRPFG GIQLVACGDF YQLPPVVKKT AHDGTELDDV EVFFAFESSA
WKETIQRTIT LKEIFRQKGD QRFINMLNNL RDGNVPDDTA RDFCRLSRPL KCPEGIVPSE
LYATRYEVDM ANSRKLNTIQ GDVVVYNSVD TGILPEPQKT QVLTNFLAPQ VLNLKVGAQV
MCIKNFDDQL VNGTLGKVID FVDRDTYMKS ESKENPSTET SDEVSGLNDY IFNDFQKPKK
VVKEDAPIAE QVLFTGQLSQ KVEEESESSK RKSKLKDDLM KDYKNKKYPL VKFLLPDGIT
FRTVVVEPEQ WTTEDEDGTV LVSRIQFPLI LAWSLSIHKS QGQTLSKVVV DMKKIFENGQ
AYVALSRAVS RAGLQVLNFN RSKVASHRKV IEFYKNLSSH EKESRSGQQR LNFMQTSVKS
VARAQI
