ID A0A452EN04_CAPHI Unreviewed; 649 AA.
AC A0A452EN04;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ECO:0000313|Ensembl:ENSCHIP00000013436.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000013436.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000013436.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000013436.1}
RP IDENTIFICATION.
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 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. Possesses an intrinsic strand annealing activity.
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; LWLT01000010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452EN04; -.
DR STRING; 9925.ENSCHIP00000013436; -.
DR Ensembl; ENSCHIT00000021228.1; ENSCHIP00000013436.1; ENSCHIG00000014856.1.
DR GeneTree; ENSGT00530000063561; -.
DR OMA; SSAWESC; -.
DR Proteomes; UP000291000; Chromosome 10.
DR Bgee; ENSCHIG00000014856; Expressed in thymus and 15 other cell types or tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
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:0033678; F:5'-3' DNA/RNA helicase activity; IEA:Ensembl.
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:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:Ensembl.
DR GO; GO:0010521; F:telomerase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042162; F:telomeric DNA binding; IEA:Ensembl.
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; 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:UP000291000}.
FT DOMAIN 469..512
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT DNA_BIND 585..604
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 174..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 649 AA; 70669 MW; 506474FA85F482A9 CRC64;
LRSGVTKPAE AAAMLSGTQA AAAECEDGEL RCRVAVEELS PGGQPRRRQS LRTAELSLGR
NERGELMLRL QAPGPAGRPR CFPVRAARLF TRFAAAGRST LRFPADSTLP ARAVQLLLSD
CPPDRLRRFL HTLRLKLAVA PGPGPGSART QLLGPRPRDF ISISPVQPEE LRRAAATRVT
DTRPVKRPTE PPEGEVARWP LPVKRLRLPP TKPELSKEQA AVLRAVLKGQ SIFFTGSAGT
GKSYLLKRIL GSLPPTGTVA TASTGVAACH IGGTTLHAFA GIGSGQAPLA QCVALAQRPG
VRQGWLNCQR LVIDEISMVE ADLFDKLEAV ARAVRQQNKP FGGIQLIICG DFLQLPPVTK
GSQLPQFCFQ AKSWRRCVQV TLELTEVWRQ TDKTFISLLQ AVRLGRCSDE VTRQLRATAA
HKVGRDGIVA TRLCTHQDDV ALTNERQLQE LPGEVHSFEA MDSDPEQART LDAQCPVSQL
LQLKLGAQVM LVKNLAVSRG LVNGARGVVV GFEAEGRGLP QVRFLCGVTE VIRADRWTVQ
TTGGQLLSRQ QLPLQLAWAI SIHKSQGMSL DCVEMSLGRV FASGQAYVAL SRARSLEGLR
VLDFDPMVVR CDPRVLSFYA TLRRDRALSL ESPDDEEATS DQENVDPNL
//
