MCE_FOWPN
ID MCE_FOWPN Reviewed; 308 AA.
AC P15916; Q85279; Q9J594;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=FPV134; ORFNames=FP9;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Salisbury;
RX PubMed=2820129; DOI=10.1016/0042-6822(87)90061-4;
RA Drillien R., Spehner D., Villeval D., Lecocq J.-P.;
RT "Similar genetic organization between a region of fowlpox virus DNA and the
RT vaccinia virus HindIII J fragment despite divergent location of the
RT thymidine kinase gene.";
RL Virology 160:203-209(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206.
RC STRAIN=FP-9 / Isolate HP-444;
RX PubMed=2838574; DOI=10.1099/0022-1317-69-6-1275;
RA Binns M.M., Tomley F.M., Campbell J., Boursnell M.E.G.;
RT "Comparison of a conserved region in fowlpox virus and vaccinia virus
RT genomes and the translocation of the fowlpox virus thymidine kinase gene.";
RL J. Gen. Virol. 69:1275-1283(1988).
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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Localizes to the
CC virion core. {ECO:0000305}.
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}.
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DR EMBL; M17418; AAA66422.1; -; Genomic_DNA.
DR EMBL; AF198100; AAF44478.1; -; Genomic_DNA.
DR EMBL; D00320; BAA00231.1; -; Genomic_DNA.
DR PIR; PS0044; WMVZP9.
DR RefSeq; NP_039097.1; NC_002188.1.
DR SMR; P15916; -.
DR GeneID; 1486682; -.
DR KEGG; vg:1486682; -.
DR Proteomes; UP000008597; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transcription; Transferase; Virion.
FT CHAIN 1..308
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase"
FT /id="PRO_0000099115"
FT REGION 177..257
FT /note="Binding to NPH-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT ACT_SITE 183
FT /note="For methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 30
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 185..188
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 190
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 213..215
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT BINDING 241
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00944"
FT CONFLICT 244
FT /note="M -> R (in Ref. 1; AAA66422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 36655 MW; 921B7C5A8E6361FF CRC64;
MHEGHQESFK ELEMTKPYMF FNELVGEEDY NKELENSNTK FQGQGQLKLL LGELYFLNTL
IKNKTLCSDT VIVYIGSAPG SHINFLYHYM DDLKIDLKWI LIDGRDHDRS LESLKNVSII
HRFVDEQYLF KLRNMIRKNH KIVLISDIRS LRGKEPTSED LLHDYALQNQ MVSILKPIAS
SLKWRCPFPD QWIRDFYIPC GDEFLQPFAP PFSAEMRLLS CYSRAPIRLI RIDKNAAIEY
EKKMFYLNTK IRPKIVLDFD YPNQKYDYFY MFYILKDIVL PTYKEFSTYK QKVIFLQEAI
FNALNIKP
