ID A0A1E3I3G1_9TREE Unreviewed; 656 AA.
AC A0A1E3I3G1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=L202_01327 {ECO:0000313|EMBL:ODN83122.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN83122.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN83122.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN83122.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN83122.1}.
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DR EMBL; AWGJ01000002; ODN83122.1; -; Genomic_DNA.
DR RefSeq; XP_018997122.1; XM_019134695.1.
DR AlphaFoldDB; A0A1E3I3G1; -.
DR STRING; 1295533.A0A1E3I3G1; -.
DR GeneID; 30152636; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000094065; 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; 2.
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:UP000094065}.
FT DOMAIN 202..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 613..632
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 656 AA; 71901 MW; 2E3268FB6600A8EC CRC64;
MPIVTPAARS GKGSSFSRVN SFKRDWGDDQ AASDAIPWSS SPDVRKHDTT ATTTATATET
AASANAAVAE TASQRRRRAI LAALNADNTY APSEISMGLS KAIASQPGHL APPHSSANLD
ATSRALPGPF DGKAGADRFY QPKRPLPWEE ESSSSKKAMT TITQPTLVSK VQPKLKGSSS
MTIKQQVVLS DEQKKVLMLV KEGKNIFYTG SAGTGKSVLL REIITTLRSK YVRTPEAVAV
TASTGIAACN IGGVTLHSFG GVGLATDPAE VLVRRLRKNP KATARWMKTK VLIVDEVSMV
DGDMFDKFCK LGQLMRKNTK PWGGIQIIVT GDFFQLPPVT NGGQPKFAFE AEMWNETIPI
SVNLSQVFRQ KDPRFVDMLN EMRFGRLTSA SIDTFKSLAR PVKYSDGIEP TSLFPRREEV
ERANLYRLNQ LHTEGHTYIS VDGGKLEGAQ RDKLLSNFMA PKTIELKVDA QVMLIKNLDE
TLANGSMGRI IGFCYRPFFL EEAGRWAPDA EFRHMDESER KRAIALRDGS LEKYKASGSP
PLPVVRFKVP GGGTRDVLIE HDVFKSDLPN GETQAQRTQL PIILSWAMSI HKSQGQTLDR
VKVDLGKVFE KGQAYVALSR ATSLEGLEVR GFSADKVMAH KKVAIWSSTL KDLNVL
//
