PIF2_TRYB2
ID PIF2_TRYB2 Reviewed; 1048 AA.
AC Q384Y0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent DNA helicase PIF2;
DE EC=3.6.4.12;
DE AltName: Full=DNA repair and recombination helicase PIF2;
DE Flags: Precursor;
GN Name=PIF2; ORFNames=Tb11.02.4740;
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-462.
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. Essential
CC for replication of kinetoplast maxicircles, but not minicircles.
CC {ECO:0000269|PubMed:19646907}.
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:19646907};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19646907};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19646907}.
CC Note=Localizes throughout the tubular structure of the single
CC mitochondrion.
CC -!- INDUCTION: Protein level is regulated by mitochondrial proteasome-like
CC protease HslVU.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CH464491; EAN79651.1; -; Genomic_DNA.
DR RefSeq; XP_828763.1; XM_823670.1.
DR AlphaFoldDB; Q384Y0; -.
DR STRING; 5691.EAN79651; -.
DR PaxDb; Q384Y0; -.
DR GeneID; 3665290; -.
DR KEGG; tbr:Tb11.02.4740; -.
DR VEuPathDB; TriTrypDB:Tb927.11.6900; -.
DR eggNOG; KOG0987; Eukaryota.
DR InParanoid; Q384Y0; -.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0097014; C:ciliary plasm; IDA:GeneDB.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:GeneDB.
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:0006264; P:mitochondrial DNA replication; IDA:GeneDB.
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..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..1048
FT /note="ATP-dependent DNA helicase PIF2"
FT /id="PRO_0000423748"
FT DNA_BIND 951..971
FT /evidence="ECO:0000255"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 456..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 462
FT /note="K->A: Abolishes enzymatic activity, toxic for
FT trypanosome cell growth."
FT /evidence="ECO:0000269|PubMed:19646907"
SQ SEQUENCE 1048 AA; 115146 MW; 1055FCECF509C993 CRC64;
MSSKTVVWSS LGRFMRTSHH RLLDEKLFPA SHNRHVQSRL LSTPLSLIAV PSWMSKCRTS
AVRLSRHPPQ VSGQEPCAVT ASSSVGTWHG SSPAGLRRCQ HVRSLNGWTT PGDVPIRHGS
RSIATIATGC GGVGAGGINS SVDVAEVSGV STSGVAAAPT VALPPGPPVE KPPLICVVRR
ATRGGAAADS VGTGTPGKCD KPPDSSNTLV GTIARVLSSS GECGRHSNAN QEGYSLGSRP
ARKILVKLEA DTVAAPLADT KEKQIYVQQQ PVVVAQSPLA RSSSTVTWEE GDTLVYNIFT
QRVVKSSSAS IRALSVLGVG VRSSEKELSV VDPHALVEFR DKLREKEVSW PSAWRSSLFN
QLQHVLLKDQ PMEEMISRVH ELLQLHYQRV KRSCVANVTK GEPDTKTEEA NPAGDEVAIN
GEMTYHERLL GYPDLNEEQR RVVDFVLRGY NTYIGGGAGT GKSLLLRVIR QELVSRGLTV
ATTATTGIAA RRLNGATLHH CFGVNVYGEF TRRAELKEFD VIIIDEVSML SKELFESLEF
QLRRANGVDL PFGGVQVILS GDFLQLGAIC SVSLVHSSVF RRNFAMLKLQ RVVRQEGSSI
FAQQLQELRR GTVPHDLQDT VQFLSPPETA KWLEGEGKGA VKLLPTNKEV DEVNQAELDK
LPSDLVVYPA QMQAPSLVGR WTATYILEAV VKDTKMIDTH KLTRALEQYV LDFLQKTPYA
SDYTLPVVGQ RYIVLYKLFV DAFAFRVRIP QDMSEKDMRD LALHLRGLET WLPACGLGVF
LREILDSPDG LHTDADDYTL TRYAELHPMA SPLRLKKGAK VMLRTNLAPG LVNGSLGVVV
GFKELSAKHL PRFVNTPGRI AAVENYAEYL RYEHGFTTAF APEVDFGGGR VIVVPPVLFS
VGGLSNTNHY HVGIVSLPLS LAYAFTVHKV QGLTLAGRVH LELSRMWPCD HLLYVAMSRV
RNPEQLTVSS FHNSLVRCAS ECLLFDDSLP PVEQVRVLPH FFQASWQRTP SRRKAALQRK
REQAKQSKQK KAAKLKEAMI KQAKEATP
