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   03-AUG-2022, entry version 108.
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; 5691.EAN79650; -.
DR   PaxDb; Q384Y1; -.
DR   GeneID; 3665289; -.
DR   KEGG; tbr:Tb11.02.4730; -.
DR   VEuPathDB; TriTrypDB:Tb927.11.6890; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   InParanoid; Q384Y1; -.
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:0005634; C:nucleus; ISA:GeneDB.
DR   GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF05970; PIF1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 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