ID C5DS62_ZYGRC Unreviewed; 864 AA.
AC C5DS62;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03176};
DE AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
GN Name=PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
GN OrderedLocusNames=ZYRO0B14168g {ECO:0000313|EMBL:CAR26623.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR26623.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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 replicaion 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:0000256|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:0000256|HAMAP-Rule:MF_03176};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03176};
CC -!- SUBUNIT: Monomer. Interacts with telomerase. {ECO:0000256|HAMAP-
CC Rule:MF_03176}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03176}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03176}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03176}.
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DR EMBL; CU928174; CAR26623.1; -; Genomic_DNA.
DR RefSeq; XP_002495556.1; XM_002495511.1.
DR AlphaFoldDB; C5DS62; -.
DR STRING; 559307.C5DS62; -.
DR GeneID; 8202722; -.
DR KEGG; zro:ZYRO0B14168g; -.
DR HOGENOM; CLU_001613_0_0_1; -.
DR InParanoid; C5DS62; -.
DR Proteomes; UP000008536; Chromosome B.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:InterPro.
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 CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR048293; PIF1_RRM3_pfh1.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03176}; DNA damage {ECO:0000256|HAMAP-Rule:MF_03176};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_03176}; DNA repair {ECO:0000256|HAMAP-Rule:MF_03176};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03176}; Helicase {ECO:0000256|HAMAP-Rule:MF_03176};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03176};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03176};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03176};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03176};
KW Reference proteome {ECO:0000313|Proteomes:UP000008536}.
FT DOMAIN 258..555
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 733..752
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 107..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 864 AA; 97793 MW; A7922C6E952186AF CRC64;
MVLCRLRLFT KVCIIPQIPI ASRLTHFRPR FGMIYRSSSS LSQSSNSFKR LKLSHPEYDE
LDKLLSDSDG WEDIAEVKLK ESSNNNNSNN NDKDYDDDDD SLIELFERPL TKDPPKSLLG
ASSKSRSNLP FKSPVIPNGT KNLEPLGAST QKTVFPHQEQ YKEEHPKEEP NKDVKQEVKD
EQESVKQEDS KVDESSIHMV EEKKKVQYGE KFALLTQREG FSDTESLSAK LNLAPSTKVV
VPIRLSKEQE DVIHLAKAGH NIFYTGSAGT GKSVLLREMI KVLKSTFGSD GVAITASTGL
AACNIGGITV HSFAGVGLGN GEADKLCKKV RRSKKHVRRW QEVSALVIDE ISMLDGELLD
KLNYIAKKIR RSDLPFGGIQ LIFCGDFFQL PPVNKNDDKQ TKFAFESTIW KDGIDVTIML
EKVFRQQGDT KFVEMLNKMR LGQIDEDTEM EFKRLNRPLP EDEIIPAELY STRHEVERAN
NFRLKGLPGK IHLYHAIDGG SLEDQSLKDK LLQNFLAPKE LSLKVGAQVM MIKNIDASLV
NGSLGKVIDF MDPETYMFYD TIVKHPEIDS DSLEGLRDPE FRKRYFKEQK MYEDDEQQVR
NKGLKDAFSK NGLEEPSFEL GDTIFDFLKN SASDGEEERS NIERKMNLIQ EIHKSSKSGR
KLPLVRFKTT DAGSRTVLVE PEDWAIEDEN EKPLVSRVQL PLMLAWSLSI HKSQGQTLPK
VKVDLRRVFE RGQAYVALSR AVSRDGLQVL NFDKTRIKAH QKVIDFYSTL SSAEQAIKAI
ESSGAAKKKG RQRRLDFAPD RPVGHRRTKD SKSNSATPAP VVPDRIMSML KRKTEKQPSG
NESNGMPLFK SDVDVENLDD RNMF
//
