MCE_VACCA
ID MCE_VACCA Reviewed; 333 AA.
AC Q76ZT1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase;
DE EC=2.1.1.57;
DE AltName: Full=Poly(A) polymerase regulatory subunit;
DE AltName: Full=Poly(A) polymerase small subunit;
DE Short=PAP-S;
DE AltName: Full=VP39;
GN Name=PAPS; OrderedLocusNames=MVA087R, ACAM3000_MVA_087;
OS Vaccinia virus (strain Ankara) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=126794;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT "The complete genomic sequence of the modified vaccinia Ankara strain:
RT comparison with other orthopoxviruses.";
RL Virology 244:365-396(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Acambis 3000;
RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA Khristova M., Wohlhueter R.M.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Displays methyltransferase, positive regulation of the
CC poly(A) polymerase and transcription elongation activities. Involved in
CC the modification of both mRNA ends and in intermediate and late gene
CC positive transcription elongation. At the mRNAs 5' end, methylates the
CC ribose 2' OH group of the first transcribed nucleotide, thereby
CC producing a 2'-O-methylpurine cap. At the 3' end, functions as a
CC processivity factor which stimulates the activity of the viral poly(A)
CC polymerase VP55 that creates mRNA's poly(A) tail. In the presence of
CC VP39, VP55 does not dissociate from the RNA allowing tail elongation to
CC around 250 adenylates. {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 -!- SUBUNIT: Methyltransferase activity: Monomer, poly(A) polymerase
CC activity: Heterodimer composed of a catalytic component, VP55, and a
CC processivity factor, VP39. Interacts with Rap94 and NPH-I; these
CC interactions might help linking transcription to capping and
CC polyadenylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00944}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U94848; AAB96504.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10485.1; -; Genomic_DNA.
DR RefSeq; YP_232977.1; NC_006998.1.
DR SMR; Q76ZT1; -.
DR DNASU; 3707551; -.
DR GeneID; 3707551; -.
DR KEGG; vg:3707551; -.
DR Proteomes; UP000159908; Genome.
DR Proteomes; UP000172909; Genome.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:InterPro.
DR CDD; cd20756; capping_2-OMTase_Poxviridae; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000176; mRNA_MeTrfase-like.
DR InterPro; IPR025804; Pox/kineto_cap_MeTfrase.
DR InterPro; IPR030375; Poxvir_cap_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01358; PARP_regulatory; 1.
DR PIRSF; PIRSF003726; PolA_polym_reg_poxV; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51612; SAM_MT_2O_PK; 1.
PE 3: Inferred from homology;
KW Elongation factor; Methyltransferase; mRNA capping; mRNA processing;
KW Protein biosynthesis; S-adenosyl-L-methionine; Transcription; Transferase.
FT CHAIN 1..333
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase"
FT /id="PRO_0000099110"
FT REGION 169..333
FT /note="Binding to Rap94"
FT /evidence="ECO:0000250"
FT REGION 169..249
FT /note="Binding to NPH-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT REGION 305..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="For methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 22
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 177..180
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 182
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 205..207
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 233
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
SQ SEQUENCE 333 AA; 38888 MW; 55A299DA4AAE1AD4 CRC64;
MDVVSLDKPF MYFEEIDNEL DYEPESANEV AKKLPYQGQL KLLLGELFFL SKLQRHGILD
GATVVYIGSA PGTHIRYLRD HFYNLGVIIK WMLIDGRHHD PILNGLRDVT LVTRFVDEEY
LRSIKKQLHP SKIILISDVR SKRGGNEPST ADLLSNYALQ NVMISILNPV ASSLKWRCPF
PDQWIKDFYI PHGNKMLQPF APSYSAEMRL LSIYTGENMR LTRVTKSDAV NYEKKMYYLN
KIVRNKVVVN FDYPNQEYDY FHMYFMLRTV YCNKTFPTTK AKVLFLQQSI FRFLNIPTTS
TEKVSHEPIQ RKISSKNSMS KNRNSKRSVR SNK
