MTR1_TRYB2
ID MTR1_TRYB2 Reviewed; 370 AA.
AC Q38AH0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57 {ECO:0000269|PubMed:17606627};
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
DE Short=TbMTr1;
GN Name=MTR1; ORFNames=Tb10.6k15.2610;
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, AND SUBCELLULAR LOCATION.
RX PubMed=17606627; DOI=10.1128/mcb.00647-07;
RA Zamudio J.R., Mittra B., Foldynova-Trantirkova S., Zeiner G.M., Lukes J.,
RA Bujnicki J.M., Sturm N.R., Campbell D.A.;
RT "The 2'-O-ribose methyltransferase for cap 1 of spliced leader RNA and U1
RT small nuclear RNA in Trypanosoma brucei.";
RL Mol. Cell. Biol. 27:6084-6092(2007).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-95;
RP ASP-207; LYS-248 AND GLU-285.
RC STRAIN=YTAT;
RX PubMed=18048356; DOI=10.1074/jbc.m707367200;
RA Mittra B., Zamudio J.R., Bujnicki J.M., Stepinski J., Darzynkiewicz E.,
RA Campbell D.A., Sturm N.R.;
RT "The TbMTr1 spliced leader RNA cap 1 2'-O-ribose methyltransferase from
RT Trypanosoma brucei acts with substrate specificity.";
RL J. Biol. Chem. 283:3161-3172(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=YTAT;
RX PubMed=19103757; DOI=10.1128/mcb.01496-08;
RA Zamudio J.R., Mittra B., Chattopadhyay A., Wohlschlegel J.A., Sturm N.R.,
RA Campbell D.A.;
RT "Trypanosoma brucei spliced leader RNA maturation by the cap 1 2'-O-ribose
RT methyltransferase and SLA1 H/ACA snoRNA pseudouridine synthase complex.";
RL Mol. Cell. Biol. 29:1202-1211(2009).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC spliced leader and U1 small nuclear RNAs. Methylates the ribose of the
CC first nucleotide of a m(7)GpppG-capped RNA to produce m(7)GpppNmp
CC (cap1). Cap1 modification is linked to higher levels of translation.
CC Recognizes a guanosine cap on RNA independent of its N(7) methylation
CC status. {ECO:0000269|PubMed:17606627, ECO:0000269|PubMed:18048356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000269|PubMed:17606627};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18048356};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:18048356};
CC -!- SUBUNIT: Component of a complex composed of CBF5, GAR1, NHP2, MTR1,
CC NOP10 and Tb11.01.8210. {ECO:0000269|PubMed:19103757}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17606627}.
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DR EMBL; CM000208; EAN78200.1; -; Genomic_DNA.
DR RefSeq; XP_823028.1; XM_817935.1.
DR AlphaFoldDB; Q38AH0; -.
DR SMR; Q38AH0; -.
DR STRING; 5691.EAN78200; -.
DR PaxDb; Q38AH0; -.
DR GeneID; 3662615; -.
DR KEGG; tbr:Tb10.6k15.2610; -.
DR VEuPathDB; TriTrypDB:Tb927.10.7940; -.
DR eggNOG; KOG3673; Eukaryota.
DR OMA; MESTGVW; -.
DR Proteomes; UP000008524; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008649; F:rRNA methyltransferase activity; ISM:GeneDB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IMP:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; ISM:GeneDB.
DR InterPro; IPR030376; Cap_mRNA_MeTrfase_1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16121:SF0; PTHR16121:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..370
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399802"
FT DOMAIN 87..294
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305"
FT MUTAGEN 95
FT /note="K->A: 98% reduction of activity."
FT /evidence="ECO:0000269|PubMed:18048356"
FT MUTAGEN 207
FT /note="D->A: 96% reduction of activity."
FT /evidence="ECO:0000269|PubMed:18048356"
FT MUTAGEN 248
FT /note="K->A: 98% reduction of activity."
FT /evidence="ECO:0000269|PubMed:18048356"
FT MUTAGEN 285
FT /note="E->A: 93% reduction of activity."
FT /evidence="ECO:0000269|PubMed:18048356"
SQ SEQUENCE 370 AA; 40896 MW; 1BC008132428795F CRC64;
MPAVADCTVV FPLRHDPAST HPDVSGLVGK AFERVNWRDA FDTFLAEERS ALWAAKTAFD
NTDTSAYIAA RDALFPQAVS GVHGAVAFRN RAGHKLHETM EAVGLWEYLK GGATRAKGTF
TFVDVCGGPG AFSQALFAMG KEHKLRLRGF GLTLRNVKGL DWYTDLPSRS FFPCYGIDGT
GDVFKLENIE SLCSLTCKEN VRLVVADGGF DVPTEVVNFQ ETISCRIVYG QWLSAVKLLR
PGGCFVLKLF DCFSPFTRAI LFLTTHLYES VQVVKPRHSR VVNSERYLVC IGFIGAPKQW
LEHFERCYQE GFVDNDNIPT VLPTSLFSGD KIFGADVERM SATIASNQVS GLHAILEKLQ
SKPAMEEVKS
