MCE_MYXVL
ID MCE_MYXVL Reviewed; 338 AA.
AC P68544; P18628;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=m065R;
OS Myxoma virus (strain Lausanne) (MYXV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX NCBI_TaxID=31530;
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10562494; DOI=10.1006/viro.1999.0001;
RA Cameron C., Hota-Mitchell S., Chen L., Barrett J.W., Cao J.-X.,
RA Macaulay C., Willer D.O., Evans D.H., McFadden G.;
RT "The complete DNA sequence of myxoma virus.";
RL Virology 264:298-318(1999).
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; AF170726; AAF14953.1; -; Genomic_DNA.
DR RefSeq; NP_051779.1; NC_001132.2.
DR SMR; P68544; -.
DR GeneID; 932114; -.
DR KEGG; vg:932114; -.
DR Proteomes; UP000000867; 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..338
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase"
FT /id="PRO_0000099116"
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..338
FT /note="Disordered"
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 338 AA; 39722 MW; F57436067FD239CB CRC64;
MEPVSMDKPF MYFDEIDDEL EYEPESVNET PKKLPHQGQL KLLLGELFFL SKLQRHGILD
GSTIVYIGSA PGTHIKYLRD HFMSMGLVIK WMLIDGRTHD PILEGLRDVI LITKFVDEAY
IRQLKKQLYP SRVILISDVR SKRGQKEPTT QDLLSNYSLQ NIMVSVLKPA ASSLKWRCPF
PDQWIKDFYV PHGNEMLQPF APSYSAEMRL LSIYSGTPIR LKCITQQDSS KYEKKMYYLN
KIIRNRIIIN FDYSNQEYDF FHMYHMLKTV YSNKSFTSNK SKVLHFHQSI FRFLKIPITN
TEKIHHEPTQ RKVPSKNTML KSRNTKKSVR GNKQGRRT
