ID N1J746_BLUG1 Unreviewed; 830 AA.
AC N1J746;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=BGHDH14_bgh00472 {ECO:0000313|EMBL:CCU75089.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU75089.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU75089.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU75089.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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:CCU75089.1}.
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DR EMBL; CAUH01000956; CCU75089.1; -; Genomic_DNA.
DR AlphaFoldDB; N1J746; -.
DR STRING; 546991.N1J746; -.
DR EnsemblFungi; BLGH_02798-mRNA-1; BLGH_02798-mRNA-1; BLGH_02798.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_0_1_1; -.
DR InParanoid; N1J746; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
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:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0061995; F:ATP-dependent protein-DNA complex displacement activity; IEA:EnsemblFungi.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IEA:EnsemblFungi.
DR GO; GO:0070336; F:flap-structured DNA binding; IEA:EnsemblFungi.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IEA:EnsemblFungi.
DR GO; GO:0043504; P:mitochondrial DNA repair; IEA:EnsemblFungi.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:EnsemblFungi.
DR GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
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:CCU75089.1};
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:UP000015441}.
FT DOMAIN 368..529
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 781..800
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 830 AA; 91719 MW; 44D4D3C7D32D1EEC CRC64;
MLGRAVKEFN PPNPKRDVCK EQFPSNGLVK DRDIGVELQK AREPALLNSS LPSYHKSSSS
HSNYISNGNL ITNQKRPFAQ SNSLTKPSSS TSKGLYSVLC KPDPFEEAQE NIDANHMSSI
SASSNKHLVE FNEEDFDDDA DLDLDCSPLR STSQLQPNVT NELPTSTYGT LNMDKAMSFS
SNHQPSSAIS WPSSSPSHKL TPPGAKHGQK RAAHSTIENS SHRASRSTKR RTLPWIPEDT
IGEFSSISDN PEILSSSGSL RNTSFTKQPN SNQISPDSGD FAASEEVSEK EQDIQPQKKS
SRIMPWNTTE SMVKETKTIF KNARKASKRV GRKSLDNKDE QSITTKPVVA PFSLSEEQKR
VLNLVVNKSK SVFFTGSAGT GKSILMRAII TELKKKYCRE NDRVAVTAST GLAACNIGGV
TLHSFGGIGL GKEDVAALVR RIKKNPKARS RWIRTKILII DEISMVDGEL FDKLESVARA
MRNNGRPFGG IQLVITGDFF QLPPVPERDD NSRAVKFAFD ASTWSTTIDH TIGLTQVFRQ
KDPMFANMLN EMRIGKITDE TVTAFQKLNR PVSDQGLEAT ELFPTRHEVD RANASRIGNL
SGTSYKYVSQ DGGAIKDPKS LERLLSNMMA PKILELKKGA QVMLIKNMDE SLVNGTLGKV
QSFMSEKDFK HLEDIEGGLD ALEYESENDV GGKSRISTNG VSTTGSGRLY PYVSFKLADG
TKRMMLILPE EWKVELPNGE VQAQRSQVPL ILAWALSIHK AQGQTLERVK IDLKKIFEKG
QAYVALSRAT SQAGLQVLNF DKVKVNAHPR VAQFYNSLYE SSQALKDSTN
//
