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Database: UniProt
Entry: A0A151GWK7_9HYPO
LinkDB: A0A151GWK7_9HYPO
Original site: A0A151GWK7_9HYPO 
ID   A0A151GWK7_9HYPO        Unreviewed;       878 AA.
AC   A0A151GWK7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=DCS_02554 {ECO:0000313|EMBL:KYK61412.1};
OS   Drechmeria coniospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX   NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK61412.1, ECO:0000313|Proteomes:UP000076580};
RN   [1] {ECO:0000313|EMBL:KYK61412.1, ECO:0000313|Proteomes:UP000076580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK61412.1,
RC   ECO:0000313|Proteomes:UP000076580};
RX   PubMed=26975455; DOI=10.1038/srep23122;
RA   Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA   Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA   Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA   Molnar I., Lin M.;
RT   "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT   Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL   Sci. Rep. 6:23122-23122(2016).
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:KYK61412.1}.
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DR   EMBL; LAYC01000001; KYK61412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151GWK7; -.
DR   STRING; 98403.A0A151GWK7; -.
DR   InParanoid; A0A151GWK7; -.
DR   OrthoDB; 5474774at2759; -.
DR   Proteomes; UP000076580; Chromosome 01.
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; 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   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:KYK61412.1};
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:UP000076580}.
FT   DOMAIN          362..523
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DNA_BIND        772..791
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT   REGION          15..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         370..377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ   SEQUENCE   878 AA;  95872 MW;  74C3DCA5EE609864 CRC64;
     MTTGIVTLPI RSSPTLRSIH RGGSGHPIHA AVRHRSTSSA ASIMFRRAAE RPPPPPPPRS
     TLEKTLFPSS SPSPSTHGDI RDQLRTPGRP VAASVSVSTS ARMAPSRPTT LTSWSANSTL
     PPNRASLHSL YTNSDSFKQE IDCVDLAAPA PLAQKKAEEV VYFAEDDFSD DDNLDLDYEA
     PKALPTPRVL VQEAPVKQQM PPPPTPSQAD SAIPWSSSPA SHFVAPTLPN PPPSRPDPSA
     STRSSVKRES SGETDVCEAP VPKKPKKRVL PAGFRSQDAP EPDEGYCVST ATPDTKSHYW
     DPTGSIVQEQ KRQLKNQRNS RQPEHDAPPD DASNAGPALV PKAVPLSLSA EQNQVLDLVV
     HKNASVFFTG PAGTGKSVLM RAIISELKKK FAREPDRVAV TASTGLAACN IGGITLHSFS
     GIGLGKEDAP ALIKKVRRNP KAKARWLKVK CLIIDEVSMV DGELFDKLSQ IGRVIRNNGR
     PWGGIQLIIT GDFFQLPPVP DFDKKREGIK FAFDAATWGT SIDHTIGLTQ VFRQRDPEFA
     RMLNEMRLGK ISQGTVEAFK ALSRPLSFDD GVDSAELYPT RAQVDSSNEK RLRELPGRSY
     RYDALDSGEP AIRDKLLTNM MAPRSLELKL NAQVMLIKNL DETLVNGTLG KVIAFSDEKT
     FDMTSVSAYD TDMDDPMSMA RRKLKGFSRD ANISDSNKKK YPVVQFVSSG GSPRVILCQP
     EEWKVELPNG DIQAKRNQLP LILAWALSIH KAQGQTLERV TVNLGRVFEK GQAYVALSRA
     TTQQGLRVLG FDQSKVMAHH RVVDFYSKLY SADQAQGQPT PTGIMDFVAN RRGVREPKAA
     APVVAVAAPS KPTQTTPSMR VEVIDLDEDE EAMASYGY
//
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