PIF5_TRYB2
ID PIF5_TRYB2 Reviewed; 928 AA.
AC Q580X6; D6XL91;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent DNA helicase PIF5;
DE EC=3.6.4.12;
DE AltName: Full=DNA repair and recombination helicase PIF5;
DE Flags: Precursor;
GN Name=PIF5; ORFNames=Tb927.8.3560;
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=19779567; DOI=10.1371/journal.ppat.1000589;
RA Liu B., Wang J., Yildirir G., Englund P.T.;
RT "TbPIF5 is a Trypanosoma brucei mitochondrial DNA helicase involved in
RT processing of minicircle Okazaki fragments.";
RL PLoS Pathog. 5:E1000589-E1000589(2009).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of mitochondrial (kinetoplast) genome stability. Involved
CC in processing of minicircle Okazaki fragments.
CC {ECO:0000269|PubMed:19779567}.
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:19779567};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19779567};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19646907,
CC ECO:0000269|PubMed:19779567}. Note=Enriched in 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; AC092212; AAX78977.1; -; Genomic_DNA.
DR EMBL; CP000071; AAZ13121.1; -; Genomic_DNA.
DR RefSeq; XP_847187.1; XM_842094.1.
DR AlphaFoldDB; Q580X6; -.
DR SMR; Q580X6; -.
DR STRING; 5691.AAZ13121; -.
DR PaxDb; Q580X6; -.
DR GeneID; 3659361; -.
DR KEGG; tbr:Tb927.8.3560; -.
DR VEuPathDB; TriTrypDB:Tb927.8.3560; -.
DR eggNOG; KOG0987; Eukaryota.
DR InParanoid; Q580X6; -.
DR OMA; AYSTHET; -.
DR Proteomes; UP000008524; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0005730; C:nucleolus; IDA:GeneDB.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:GeneDB.
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:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IDA:GeneDB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; TAS:GeneDB.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..928
FT /note="ATP-dependent DNA helicase PIF5"
FT /id="PRO_0000423751"
FT DNA_BIND 858..877
FT /evidence="ECO:0000255"
FT REGION 29..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 264..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 928 AA; 102457 MW; 750FB43EA0472F8D CRC64;
MLSRLSAVWR PSRVALRIQR VDFTTCGNRL NRSTQPNEPP LVSGIAARSR TAKAEPVEKR
GRAAIKIDSP PPPLEPPRIS EEHMTRRRKV GGGKTKAAAV TKSKQRRSGR TVGASAFNTA
RRANGIEGSA PGKGGASDVA IDDDDDEKLV DEESKQLMQL LKEEALRREE EKKKRLRAKA
AAEPTEVTDD KEYLSKLGVA ERTQPVGTEA KISAQGKAEG ASEGQTHFSD ADADSQLPIL
TSLSPEQQRA LRLALKGRNL FITGGAGSGK SLLIREIVYQ LRHNKRRCVY VTATTGVAAL
NVRGSTVNSF AGVKFGDGDA RQLLKWVRRS RRAAGRWRYC QTLIIDEISM MDPLLLDKLD
VIARAIRRRN EPFGGIQVIL CGDFLQLPPI PPRNKPQQKT EENAEAQEGG DPTDGTPAPS
KLQYCFETST WTSLNLITVI LHKKFRQHDD LAFQQVLDEL RVGSLSPESY ELLLSRTVAS
KSSAKSRKKK DEDAGNDGVL PLTDAETTPA AAEKDRHVRL CATNKEVEMR NAKYFAALEP
KGLPIYPSPN DGSSQQTGSS NGANSVTEED TMRPLQVYRA YDAYSTHETE PETTEETTTG
TQPSQPWVRF EDSTLPTDLA LKVGTRVMVL QNISLRLGLV NGSVGEVVGF LHPLELVELV
LRAPRERHFP SARGQELLER AGLPTLQDAF RCVDTALGQS LFYYLRERGI RRPEDASYGC
VYGNTHCRDI LRLVGLGKTE SANAVHPLEM YLGGIAPQHV RLTRLPIVRL DLREGNHTSS
DSGAVEDGGF ANGSKRLPKH VYAFISPSSH QWYMGDQPVA TRTQLPLRQA WAMTVHKAQG
LTISHVEVAI HRFFSPGQAY VALSRSTRLD NIRLLDFNNA SVHACPRAKE FYTVLEEEEL
DNEIEDDGTE GDEEALEGDG EYEGEVEE
