PIF1_EMENI
ID PIF1_EMENI Reviewed; 745 AA.
AC Q5AXT5; C8V2X2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03176};
DE AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
GN Name=pif1; ORFNames=AN6895;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of both mitochondrial and nuclear genome stability.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_03176};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03176}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03176}.
CC Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03176}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF71681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA58294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BN001301; CBF71681.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000113; EAA58294.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_664499.1; XM_659407.1.
DR AlphaFoldDB; Q5AXT5; -.
DR SMR; Q5AXT5; -.
DR STRING; 227321.Q5AXT5; -.
DR EnsemblFungi; EAA58294; EAA58294; AN6895.2.
DR GeneID; 2870605; -.
DR KEGG; ani:AN6895.2; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001613_0_1_1; -.
DR InParanoid; Q5AXT5; -.
DR OrthoDB; 931726at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
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:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF05970; PIF1; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..745
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000423709"
FT DNA_BIND 670..689
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
SQ SEQUENCE 745 AA; 83072 MW; C0848F8A31F483D8 CRC64;
MFKKAVKDHS AAAARPLQST IPNSSGVAST KLPPPQSIGV KRKIELTSTK STLGSLHSAV
YFDENDFDDD DDLDFESPDP YIPPARIEKD SFREESFHAA KSNSTLSHKA DSQSAVTVSK
TNYESDIKYP DLPPVPPDDN PGPSSSALPW SSSPPSHFQK PAAPRTVPWR KQENNIITID
DEAKPETPAR PAATAPWNKT ASAIKEEQKE LRRQNKKAQA QKTQSSTKHH MPRAQVAPIF
LSQKHVLKAV VEKGQSIFFT GSAGTGKSVL MREIIKKLRD KYRKEPDRIA VTASTGLAAC
NIEGVTLHSF AGIGLGKEPV PELVKKIKKN QKARNRWLRT KVLVIDEVSM VDGDLFDKLE
EIARLIRNNG RPFGGIQLVV TGDFFQLPPV PEGHNREAKF SFAAASWNTS IQHTILLTHV
FRQRDPEFAD MLNEMRLGKL SPRTIQAFKE LSRPLDFHDA LEATELFPTR AEVDNANSAR
MARLSGETMT FNAVDSGTIQ DIQFREKLLS NCMAPQTIHL KKGSQVMLIK NMEDTLVNGS
IGRVVAFMDE ATFDFYVENE NDFASGKFDE GDEDRAARAR KKIKGMGHRD GGVTVTRKWP
LVCFIQPDGT ERHLLCQPES WKIELPNGEV QAQRQQVPLI LAWALSIHKA QGQTLQRVKV
DLGKVFEKGQ AYVALSRATS KAGLQVLRFD PRKVMVHPKV IEFYRNLVHA SDLIKSKQPP
KPQRTISNGD EDVYIDELIA EAEAY
