MTR1_TRYCC
ID MTR1_TRYCC Reviewed; 362 AA.
AC Q4E123;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
GN ORFNames=Tc00.1047053506247.320;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AAHK01000054; EAN98495.1; -; Genomic_DNA.
DR RefSeq; XP_820346.1; XM_815253.1.
DR AlphaFoldDB; Q4E123; -.
DR SMR; Q4E123; -.
DR STRING; 5693.XP_820346.1; -.
DR PaxDb; Q4E123; -.
DR EnsemblProtists; EAN98495; EAN98495; Tc00.1047053506247.320.
DR GeneID; 3552959; -.
DR KEGG; tcr:506247.320; -.
DR eggNOG; KOG3673; Eukaryota.
DR OMA; MESTGVW; -.
DR OrthoDB; 1336442at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..362
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399803"
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:0000255|PROSITE-ProRule:PRU00945"
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:0000255|PROSITE-ProRule:PRU00945"
SQ SEQUENCE 362 AA; 40886 MW; 05C98798787F4E18 CRC64;
MSEVTDKTVE FLLRHSASRR PPDIGSLKEK AFERVNWRDA FDRFQETERL TLWETKSELD
GVDEGAYRVA RDALFPFAVS GSQGAVSFGN RAGHKLREVM EATGVWEHLQ RETSGQKGAV
VFADVCGGPG AFSQALFEMS RQYKLRMRGF GMTLRNVRGL DWYSSLPLGK FLPTYGIDGT
GDIFNLANIE ALLSLTIRER LKLVVADGGF NVPFNIANYQ ETLSGRILFG QWLAALKLLR
PGGCFILKLF DTFSPLSRAL LYLSTYLYDR VHVVKPRHSR VVNSERYLVC LGFLGTPGPW
MEYFEHCYQV GFSDNDSIPK IMPTSWVMED KTFMKDLKQM NSTIASNQTL ALKMVLAKLQ
PS
