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Database: UniProt
Entry: A0A074S981_9AGAM
LinkDB: A0A074S981_9AGAM
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ID   A0A074S981_9AGAM        Unreviewed;       634 AA.
AC   A0A074S981;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=V565_020980 {ECO:0000313|EMBL:KEP54155.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP54155.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP54155.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP54155.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA   Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA   Zafar N., Nierman W.;
RL   Submitted (DEC-2013) 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:KEP54155.1}.
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DR   EMBL; AZST01000036; KEP54155.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074S981; -.
DR   STRING; 1423351.A0A074S981; -.
DR   HOGENOM; CLU_001613_0_3_1; -.
DR   OrthoDB; 5474774at2759; -.
DR   Proteomes; UP000027456; 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};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_03176, ECO:0000313|EMBL:KEP54155.1};
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:UP000027456}.
FT   DOMAIN          188..358
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DNA_BIND        589..608
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT   REGION          1..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         196..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ   SEQUENCE   634 AA;  69349 MW;  3509DE1A9CBD82A6 CRC64;
     MSRISSFRRD WDGEPPAAVE ETTVQRTKVT STTVVAASSQ ASASGAAPRP GGKSRLATIM
     AALQASENNK ASGKMNPSST APSTMSMSQE STATWVDSVS GFGSPSTQTS MSTTQNSLSG
     TSKRSRDSTE EIEEMAKKQR PSREKSSAAM QTNLTVMEKA VVGSATGSEK LVITLSYEQS
     QILDIVKKGS NIFFTGSAGT GKSVLLREII KALRKKHGKA QDAVAITAST GIAACNIGGV
     TLHSFGGIGI GEGSPESLAM KVRKNKNALA RWLRCKVLII DEVSMLDGDL FDRLARVACI
     VRKSPKPFGG IQLIVTGDFF QLPPVVKGGQ PKFAFEAEKW SECVERTFNL SKVFRQKDPR
     FVDMLNEMRF GRLTPASTRT FYELSRPIPD DGIQATELFP RREDVDRSNS LRMAALPGKE
     QVFSARDAGT ITDPVQRDKM LQNFMAPKEI SLKINAQVML LKNIDETLVN GSVGRVIGFY
     DATEVDVGEK GELIHIYAPE ERKKLAKKQK DLPHGLAKYP LVEFRVPRGT RKLLVMPDAF
     KVELPNGEVQ VSRTQIPLIL SWAMSIHKSQ GQTLDRVKVD CGRIFEKGQA YVALSRATSL
     EGLQVLNFDP KKVQAHDKVK TWSQTLECIT HEGE
//
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