MCE_SWPVK
ID MCE_SWPVK Reviewed; 69 AA.
AC P23334;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 89.
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;
DE Flags: Fragment;
GN Name=PAPS; ORFNames=SWF9;
OS Swinepox virus (strain Kasza) (SWPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus.
OX NCBI_TaxID=10277;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840707; DOI=10.1016/0042-6822(91)90907-s;
RA Schnitzlein W.M., Tripathy D.N.;
RT "Identification and nucleotide sequence of the thymidine kinase gene of
RT swinepox virus.";
RL Virology 181:727-732(1991).
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}.
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; M59931; AAA47893.1; -; Genomic_DNA.
DR PIR; D37949; D37949.
DR SMR; P23334; -.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000176; mRNA_MeTrfase-like.
DR InterPro; IPR025804; Pox/kineto_cap_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01358; PARP_regulatory; 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;
KW Virion.
FT CHAIN 1..>69
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase"
FT /id="PRO_0000099118"
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 NON_TER 69
SQ SEQUENCE 69 AA; 8069 MW; C6830F285030213E CRC64;
MEPLSIDKPF MYFDEINNEL EYDPDSANEK HKKFPYQGQL KLLLCELFFL SKLQRHGILD
GSTIVYIGS
