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Database: UniProt
Entry: A0A284RAN9_ARMOS
LinkDB: A0A284RAN9_ARMOS
Original site: A0A284RAN9_ARMOS 
ID   A0A284RAN9_ARMOS        Unreviewed;       630 AA.
AC   A0A284RAN9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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   ORFNames=ARMOST_09171 {ECO:0000313|EMBL:SJL05835.1};
OS   Armillaria ostoyae (Armillaria root rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47428 {ECO:0000313|EMBL:SJL05835.1, ECO:0000313|Proteomes:UP000219338};
RN   [1] {ECO:0000313|Proteomes:UP000219338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C18/9 {ECO:0000313|Proteomes:UP000219338};
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
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; FUEG01000006; SJL05835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A284RAN9; -.
DR   STRING; 47428.A0A284RAN9; -.
DR   OMA; HICATTH; -.
DR   OrthoDB; 5474774at2759; -.
DR   Proteomes; UP000219338; 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   Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 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   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_sf.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF01693; Cauli_VI; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   Pfam; PF21530; Pif1_2B_dom; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 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:UP000219338}.
FT   DOMAIN          167..319
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DNA_BIND        579..598
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT   REGION          85..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ   SEQUENCE   630 AA;  70598 MW;  60F35D8A0E9CFC87 CRC64;
     MVVKPKFWAV RIGREGPKIY TSWEECKKNV DKYPSAKQKG FPTRVLAQEY IAPFLRASSS
     QSTSKTPMAK PEIIYIDSDS DSDVQIIEKP KPSSSTKKSA PKRKPLRVET YLDDDDSDLE
     IQLLKGPFSD KVSKAPSEPK AGPSTPDGSS AIRLSPEQQH VLNLVKEGRS VFFTGSAGTG
     KSVLLREIIK SLREKPGHVT AITASTGIAS VNIGGTTLHS WAGIGLGQDE AKKYADKFIF
     QKIFKPTLKR WRTTDTLIID EISMLDGKLF DKLEYIGRRV CNAMDVPFGG IQLVLSGDFC
     QLPPVPDRRD GKIMPVTFAF DSESWKKCVG PPVTLTRVFR QKDQAFVDIL NDMRFGELSE
     TAIETFRILT RRVTYNDGIE PTELFALRGE VDGANSARLK NLNGFAHTYQ SRDRPGVDVD
     GRAVSSQQMD RLLERLVAPK LIQLKVGAQV MLIKNLEQGH LVNGSVGNVV DFETQRQALA
     SEDTEIGEVE RKDETDEERA ARLEKLPAQQ VWPVVRFTNG RRILCIPQEF TVENSNGDVE
     AKRDQVPLIL AWALSVHKSQ GQTIERVRVD LKRIFEKGQA YVALSRATTM EHLQVLNFDP
     SKVLAHPRVI EWHHGQCTHE IDEPLDEMEY
//
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