MTR1_LEIBR
ID MTR1_LEIBR Reviewed; 398 AA.
AC A4HQI9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=LbrM35_V2.7020, LbrM_35_7020;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA to produce m(7)GpppNmp (cap1). {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;
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DR EMBL; FR799010; CAM44455.1; -; Genomic_DNA.
DR RefSeq; XP_001569314.1; XM_001569264.1.
DR AlphaFoldDB; A4HQI9; -.
DR SMR; A4HQI9; -.
DR STRING; 5660.A4HQI9; -.
DR GeneID; 5420298; -.
DR KEGG; lbz:LBRM_35_7020; -.
DR VEuPathDB; TriTrypDB:LbrM.35.7020; -.
DR VEuPathDB; TriTrypDB:LBRM2903_350083300; -.
DR InParanoid; A4HQI9; -.
DR OMA; MESTGVW; -.
DR Proteomes; UP000007258; Chromosome 36.
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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..398
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399805"
FT DOMAIN 85..298
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT REGION 371..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
SQ SEQUENCE 398 AA; 45037 MW; 9F6AB34E995619C4 CRC64;
MRTVEDRSLE FLIRRDREAE LPPLASLCCN YFKQRHWRDA FDDEQASLRE ELWAVKTQLD
TIPMEAYTAT RNKLFPLALS GEQQQFSNRA GHKLLESMES TGVWMELSKL LCGKSRKRPR
DFAFADVCGG PGAFSQALFK AGRKQGWRHL HGYGMTLAGV SGLDWYNSLL NSPQFTCTYG
LDGTGDIFKL SNIDCLVSIT KAAPMFLVVA DGGFSVDFSV ANYQETISSR IMYGQWLAAL
KLLRKGGCCV LKLFDTFSPL SRAVVYLSCF LYSRVHVAKP RHSRVVNSER YLVCVDFLGY
PNEAWGRYLD CFYELGFVDN EHVPELMPRE WCLQDEIFMA DMRDMNMTVA TNQMTALQMI
LNAASAVEEE LKAKETTTRT SAESDDSPLS SRESCKDG
