ID PIF1_TRYB2 Reviewed; 929 AA.
AC Q384Y1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=ATP-dependent DNA helicase PIF1;
DE EC=3.6.4.12;
DE AltName: Full=DNA repair and recombination helicase PIF1;
DE Flags: Precursor;
GN Name=PIF1; ORFNames=Tb11.02.4730;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=19646907; DOI=10.1016/j.molcel.2009.07.004;
RA Liu B., Wang J., Yaffe N., Lindsay M.E., Zhao Z., Zick A., Shlomai J.,
RA Englund P.T.;
RT "Trypanosomes have six mitochondrial DNA helicases with one controlling
RT kinetoplast maxicircle replication.";
RL Mol. Cell 35:490-501(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=20042610; DOI=10.1074/jbc.m109.084038;
RA Liu B., Yildirir G., Wang J., Tolun G., Griffith J.D., Englund P.T.;
RT "TbPIF1, a Trypanosoma brucei mitochondrial DNA helicase, is essential for
RT kinetoplast minicircle replication.";
RL J. Biol. Chem. 285:7056-7066(2010).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of mitochondrial (kinetoplast) genome stability. Essential
CC for replication of kinetoplast minicircles. Involved in the segregation
CC of minicircle progeny. {ECO:0000269|PubMed:20042610}.
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:0000269|PubMed:20042610};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20042610};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19646907,
CC ECO:0000269|PubMed:20042610}. Note=Localizes to the antipodal sites
CC flanking the kDNA disk.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CH464491; EAN79650.1; -; Genomic_DNA.
DR RefSeq; XP_828762.1; XM_823669.1.
DR AlphaFoldDB; Q384Y1; -.
DR SMR; Q384Y1; -.
DR STRING; 185431.Q384Y1; -.
DR PaxDb; 5691-EAN79650; -.
DR GeneID; 3665289; -.
DR KEGG; tbr:Tb11.02.4730; -.
DR VEuPathDB; TriTrypDB:Tb927.11.6890; -.
DR eggNOG; KOG0987; Eukaryota.
DR InParanoid; Q384Y1; -.
DR OrthoDB; 169314at2759; -.
DR BRENDA; 3.6.4.12; 6519.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0031981; C:nuclear lumen; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISA:GeneDB.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:GeneDB.
DR GO; GO:0051276; P:chromosome organization; ISA:GeneDB.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; ISA:GeneDB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; ISA:GeneDB.
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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23274:SF19; ATP-DEPENDENT DNA HELICASE PIF1; 1.
DR PANTHER; PTHR23274; DNA HELICASE-RELATED; 1.
DR Pfam; PF05970; PIF1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..929
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000423747"
FT DNA_BIND 776..796
FT /evidence="ECO:0000255"
FT REGION 55..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 929 AA; 102508 MW; 38D1CED7ACCE921F CRC64;
MLRRLLQPAY NVALSGTSAS TLPRKSASVG LVRTALMPVD YNAGALFCAM RFTSGTEKER
KREPKRGSKR RSKATTTLST PTDAQTSVTG AREGVALPQE NMPDAIQPPA TLEVRAAEVK
EEPLAATPPQ IQPQEETMGP IDGEPQLPLH STLVYNALTG RMTSETSPSF LCLKSIGFGV
NNKRQLYVEK PDVLRDLAQR MRKGTATLPS NWPVTIIRAL GVILRNRRVE DPAEAIQQMM
QVKINNLTHS RYAAVVNAVG DTDLQNILDG GLADEFVAVD LNEEQEKVIN LALKGHLMYI
GGSAGTGKTV LLRALCRRMQ AEGLRVAMTA TTGVAGCHIG GSTFHHAMGV SAQGDFVRKN
HLLSYDAIII DEVSMLPKKM FEEFDRVLRE EAGAPDVPFG GVQIILCGDF LQLGVINEPP
IIHSTTFREK FVKIRLETQV RQAKSSLFAD ALQQMRVGLV PESLTASVEQ LPPGTMVPAA
VNLLPTNKEV NTANEEELKR LPGDAVTLTP ETGITALRCD TTATLLMRTT KDFKVEEFTK
HLRGLLQATV DIPRASMVSA YRIYEDGHAV RVYLPQSESV AWRDAIRERF LEVAGLINDL
DIGATVTEII PSGDGLHTPE HEECLQRLMA KHPIAQPLTL KKGCRVLLRT NLTSRLVNGS
IGTVVDFVEC SMENIPVALR CERVNRCVDR YRIYCTMECG MPVPLLPVVK FHSGETIVVP
PWEFLVGGNP ITQYYSLSSV SLPLSLAYAF TVHKVQGLTL VGRVHLELSR MWPCEHLLYV
AMSRVRNPEQ LSMSSFDPKM VLANEACVKF DRELNTVDNL PSLAEYPVSS WKRCNDMVYH
LRRQGTSLDR YLQNGAAKEG GSVPVQQLGL SGPVKGSLEH SMVVSRRLRK LIKQTERTIR
MHERRQKKMA VEGAKQTDTT KASSGESLE
//
