ID A0A081CCF7_PSEA2 Unreviewed; 793 AA.
AC A0A081CCF7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=PAN0_005c2566 {ECO:0000313|EMBL:GAK64353.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK64353.1};
RN [1] {ECO:0000313|EMBL:GAK64353.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK64353.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; DF830072; GAK64353.1; -; Genomic_DNA.
DR RefSeq; XP_014657293.1; XM_014801807.1.
DR AlphaFoldDB; A0A081CCF7; -.
DR GeneID; 26303346; -.
DR HOGENOM; CLU_001613_0_2_1; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
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: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; 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};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_03176, ECO:0000313|EMBL:GAK64353.1};
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:UP000053758}.
FT DOMAIN 355..506
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 751..770
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 128..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 793 AA; 85623 MW; B46674451503A85F CRC64;
MLLASDSTWT CDASGQNRIG LHTPKTTPQR RAVLQNVASS YPVAGDNLKP LLAQLGHALQ
EHTRTCGPRL STTPPTSYIH SSVTNTIDQC SLAVPSARHS VMYAKGSASN NAGERPQVRS
ALGSLKRTWS GNQHDLGSTA QTSQTRTGFK SGAPPSSQEI FYEWSPSPSP PPTASRSAVR
NSDSDKENGF GATAAKRTKV ATASSDKSSA FGQRPIHNGF VAASTIHRSA SHGSAVASSS
ASNSAYGRSG AGASYQSQPN RSDSRSSSIT PTAQQSTASA RNLPWTKSAS QLKSEKRNDP
EAYRASSLVS SVGGPSGSRA STPSTVASGP DGKKSVNKIF LSQEQRKVLS MVVDEGKNVF
FTGSAGTGKS VLLREIIREL RRKHSKSPDA VAVTASTGIA ACNIGGVTIH SFAGIGLGKE
PVAQLVSKIR KNRKATGRWS RTQVLIIDEI SMVDPALLDK LEEIARVLRK KPKPFGGIQI
VITGDFFQLP PVNPGGSVTF AFDAQCWEHV VQHKVNLTQV FRQKDSSFVT MLNEMRFGKL
SQKTIEAFKK LERVPQYDGD IVPTELFPMR NEVDAANAQR LNALQAESQT YRAQDGGSLQ
AEARERVLQN SIALPVLHVK KGAQVMLIKN IDETLVNGSI GKVVDFVDEM EHARLAGDLE
SHDQMNAERE KMTRMPGRKW PLVRFHVPGG GTRDYLAMPE TWKTELPDGE IQASRSQVPL
ILAWAMSIHK SQGQTLPCCK INLNRVFEKG QAYVALSRAT SIEGLQVLGF QASKVMAHPR
VIEWSKSLIA LGE
//
