CMTR_NPVAC
ID CMTR_NPVAC Reviewed; 262 AA.
AC P41469;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase;
DE EC=2.1.1.57 {ECO:0000269|PubMed:12610118};
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12610118; DOI=10.1128/jvi.77.6.3430-3440.2003;
RA Wu X., Guarino L.A.;
RT "Autographa californica nucleopolyhedrovirus orf69 encodes an RNA cap
RT (nucleoside-2'-O)-methyltransferase.";
RL J. Virol. 77:3430-3440(2003).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of
CC late viral transcripts. {ECO:0000269|PubMed:12610118}.
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:12610118};
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DR EMBL; L22858; AAA66699.1; -; Genomic_DNA.
DR PIR; F72858; F72858.
DR RefSeq; NP_054099.1; NC_001623.1.
DR SMR; P41469; -.
DR PRIDE; P41469; -.
DR GeneID; 1403902; -.
DR KEGG; vg:1403902; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..262
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase"
FT /id="PRO_0000133008"
FT DOMAIN 34..226
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
SQ SEQUENCE 262 AA; 30355 MW; 05C1B44B00406AEC CRC64;
MLQQKLNKLK DGLNTFSSKS VVCARSKLFD KRPTRRPRCW RKLSEIDKKF HVCRHVDTFL
DLCGGPGEFA NYTMSLNPLC KAYGVTLTNN SVCVYKPTVR KRKNFTTITG PDKSGDVFDK
NVVFEISIKC GNACDLVLAD GSVDVNGREN EQERLNFDLI MCETQLILIC LRPGGNCVLK
VFDAFEHETI QMLNKFVNHF EKWVLYKPPS SRPANSERYL ICFNKLVRPY CNNYVNELEK
QFEKYYRIQL KNLNKLINLL KI
