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PIF7_TRYB2
ID   PIF7_TRYB2              Reviewed;         992 AA.
AC   Q57YG0; D6XMN8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=ATP-dependent DNA helicase PIF7;
DE            EC=3.6.4.12;
DE   AltName: Full=DNA repair and recombination helicase PIF7;
DE   Flags: Precursor;
GN   Name=PIF7; ORFNames=Tb927.8.700;
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).
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC       maintenance of mitochondrial (kinetoplast) genome stability.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast
CC       {ECO:0000269|PubMed:19646907}. Note=Localizes predominantly to the kDNA
CC       disk.
CC   -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC159407; AAX69358.1; -; Genomic_DNA.
DR   EMBL; CP000071; AAZ12841.1; -; Genomic_DNA.
DR   RefSeq; XP_846907.1; XM_841814.1.
DR   AlphaFoldDB; Q57YG0; -.
DR   SMR; Q57YG0; -.
DR   STRING; 5691.AAZ12841; -.
DR   PaxDb; Q57YG0; -.
DR   PRIDE; Q57YG0; -.
DR   GeneID; 3659043; -.
DR   KEGG; tbr:Tb927.8.700; -.
DR   VEuPathDB; TriTrypDB:Tb927.8.700; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   InParanoid; Q57YG0; -.
DR   OMA; MEDAKND; -.
DR   Proteomes; UP000008524; Chromosome 8.
DR   GO; GO:0020023; C:kinetoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISM: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; IC: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; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003840; DNA_helicase.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02689; Herpes_Helicase; 1.
DR   Pfam; PF05970; PIF1; 1.
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; Kinetoplast; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..992
FT                   /note="ATP-dependent DNA helicase PIF7"
FT                   /id="PRO_0000423753"
FT   DNA_BIND        651..670
FT                   /evidence="ECO:0000255"
FT   REGION          20..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         237..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   992 AA;  108863 MW;  B293A11FE489A0BA CRC64;
     MWDGPLRSRQ NLRTVAKLRS SGCPLTQSAI HPTTTSPSEG ETASEILQGQ ASAGYIEEQQ
     LPATSSQLEM SGDSNAASDN NVVIMTKRQR DDLSQASQAE VLSRLRTEDA QGPAENNGAQ
     SDLALHSCDM EERVDSSKLN LNHVTVNKHS PPASKSAGIS QQNDDGGCGA SENVDNTTTA
     ASKQRGKLLL DSSSSNCTPK QQAQQAVTQV PEWELSHEQE RIFDIVVNHR RSVFLTGGAG
     TGKSHLLRAI IAALPLSTTF VTATTGLAAL NLGGTTLHSF SGCGFVDQHT STHQMVYRNV
     LGRKKARANW RKCRVLVVDE VSMLDAWFFD MLEYVARHIR GCRKPFGGIQ LVLSGDFLQL
     PPVNKHSPKQ ETRLCFEAKS WPRVNPLVCT LSHQFRQKDK EFFSLLNEVR VGALTAPSLG
     LLSSLSVITT VSFVDEEKLK LKREVGAEAV DIITDSKGRT RRQRQDGFTI LRARRSEVDA
     INTEKFGELD TEIYSYKGAH RGEGHFPSDL PSTVSVRAGC RVMLLANLDL SAGLANGSIG
     TVESFVSSKL HQTANPSTKD DLQHLADHMM LPVVRFDHKG KQGPGDGGGA AAGRLVVIEP
     HRWTMRQGDS DVSCSIQIPL QLAYAITIHK SQGMSLSHVN VDFAGIFEEG QAYVALSRCT
     DVANLVIENF DAQRVNPNIK ALAYYRALEF VGTEHREAEK KLIDNGNKMN PWGPYDVEDF
     EASDDDNGGA VKKEVVENLT YDAENISCMV EQFRQRYMPQ YIMFSTLRRR VLSNTEDAAR
     VKGALLVMDT TSLLALTNMT GPTSLYQTIF TERGNMMRVP RVVKEELLFL ASTDVKEVSS
     VTTPTLHSFC STCSSTPCST GFSYDFVEVV SCALSIMENA KCDFLLDEQR EGEANSLPPV
     IQEWRSLSPL LMLNSSPDTG EKDAPSVIGF GERSREQHHS TLMFASFLVS RYSGNGAVYV
     CTETVELAAR ALAIGLRVCS IAYLCNRARR VN
 
 
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