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Database: UniProt
Entry: A0A3P9NSA8_POERE
LinkDB: A0A3P9NSA8_POERE
Original site: A0A3P9NSA8_POERE 
ID   A0A3P9NSA8_POERE        Unreviewed;       629 AA.
AC   A0A3P9NSA8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000012432.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000012432.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000012432.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC       maintenance of both mitochondrial and nuclear genome stability.
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. {ECO:0000256|HAMAP-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   RefSeq; XP_008431609.1; XM_008433387.2.
DR   AlphaFoldDB; A0A3P9NSA8; -.
DR   STRING; 8081.ENSPREP00000012432; -.
DR   Ensembl; ENSPRET00000012565.1; ENSPREP00000012432.1; ENSPREG00000008426.1.
DR   GeneID; 103479137; -.
DR   KEGG; pret:103479137; -.
DR   CTD; 80119; -.
DR   GeneTree; ENSGT00530000063561; -.
DR   OMA; SSAWESC; -.
DR   OrthoDB; 5474774at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000008426; Expressed in caudal fin.
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:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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; 2.
DR   HAMAP; MF_03176; PIF1; 1.
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   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:UP000242638}.
FT   DOMAIN          453..499
FT                   /note="DNA helicase Pif1-like 2B"
FT                   /evidence="ECO:0000259|Pfam:PF21530"
FT   DNA_BIND        572..591
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT   REGION          160..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ   SEQUENCE   629 AA;  69409 MW;  2ED4DE1899F893F2 CRC64;
     MLAGEDGAQL QCCVAVEKLN SCGQATRRQL IRKASVILGR NEFQELILRV HDGKLSHSYL
     LKEFRLFTKF ASDGKCTVKL LPENTQVLLS NCPPDRLKLF LKTLSIKHQV WQSGKTLTDR
     EKLKADLPRS FEAISPLQQK DIQRVNELLS RAAPSGLTAR INKGSAAGTG QQVKRSRSDA
     SSSPVKGNPS KRAILSFPIR KLSKEQAAVL SAVLSGKNVF FTGSAGTGKS FLLKRILGSL
     PPKSTFATAS TGVAACHIGG TTLHSFAGIG SGSAPLEQCV ELAQRPAVLQ HWTSCHHLII
     DEVSMVEAQF FDKLESVARS VRRSTQPFGG IQLIVCGDFL QLPPVPKGKE KASFCFQARS
     WRKVIQVNME LTEVRRQTDQ NFISLLQAVR VGRVSEEVTA TLLKSAYHQI ERDGILATRL
     CTHKDDVELT NQNKLQQLPG SSRAFEALDS DPELVRTIDA HSPVSRLIQL KVGAQVMLTK
     NLDVARGLVN GARGVVVSFD SGKQGFPCMR FLCGVTEVLK PERWVFKSTG GIHLSRQQLP
     LKLAWAISIH KSQGMTLDCV EISLARVFES GQAYVALSRA RSLEGLRVMD FDPHVVRADP
     DVLLFYKKLR KERLLMQASM DDFYNKENS
//
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