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Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase (EC 2.1.1.57)

 Q91MU2_LSDVN            Unreviewed;       333 AA.
Q91MU2; Q77GM0;
01-DEC-2001, integrated into UniProtKB/TrEMBL.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 59.
RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000256|PIRNR:PIRNR003726};
EC=2.1.1.57 {ECO:0000256|PIRNR:PIRNR003726};
Name=LSDV068 {ECO:0000313|EMBL:AAK85029.1};
Synonyms=LD068 {ECO:0000313|EMBL:AAN02636.1};
Lumpy skin disease virus (isolate Bovine/Kenya/Neethling 2490/1958)
(LSDV) (Lumpy skin disease virus (isolate NI-2490)).
Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
Capripoxvirus.
NCBI_TaxID=376849 {ECO:0000313|EMBL:AAK85029.1, ECO:0000313|Proteomes:UP000127252};
NCBI_TaxID=9913; Bos taurus (Bovine).
[1] {ECO:0000313|EMBL:AAK85029.1, ECO:0000313|Proteomes:UP000127252}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Neethling 2490 {ECO:0000313|EMBL:AAK85029.1};
PubMed=11435593; DOI=10.1128/JVI.75.15.7122-7130.2001;
Tulman E.R., Afonso C.L., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
"Genome of lumpy skin disease virus.";
J. Virol. 75:7122-7130(2001).
[2] {ECO:0000313|EMBL:AAN02636.1, ECO:0000313|Proteomes:UP000126568}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Neethling Warmbaths LW {ECO:0000313|EMBL:AAN02636.1};
PubMed=12827464; DOI=10.1007/s00705-003-0102-0;
Kara P.D., Afonso C.L., Wallace D.B., Kutish G.F., Abolnik C., Lu Z.,
Vreede F.T., Taljaard L.C.F., Zsak A., Viljoen G.J., Rock D.L.;
"Comparative sequence analysis of the South African vaccine strain and
two virulent field isolates of Lumpy skin disease virus.";
Arch. Virol. 148:1335-1356(2003).
-!- FUNCTION: Displays methyltransferase, positive regulation of the
poly(A) polymerase and transcription elongation activities.
Involved in the modification of both mRNA ends and in intermediate
and late gene positive transcription elongation. At the mRNAs 5'
end, methylates the ribose 2' OH group of the first transcribed
nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3'
end, functions as a processivity factor which stimulates the
activity of the viral poly(A) polymerase VP55 that creates mRNA's
poly(A) tail. In the presence of VP39, VP55 does not dissociate
from the RNA allowing tail elongation to around 250 adenylates.
{ECO:0000256|PIRNR:PIRNR003726}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000256|PIRNR:PIRNR003726}.
-!- SUBUNIT: Methyltransferase activity: Monomer, poly(A) polymerase
activity: Heterodimer composed of a catalytic component, VP55, and
a processivity factor, VP39. {ECO:0000256|PIRNR:PIRNR003726}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase
family. {ECO:0000256|PROSITE-ProRule:PRU00944}.
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EMBL; AF325528; AAK85029.1; -; Genomic_DNA.
EMBL; AF409137; AAN02636.1; -; Genomic_DNA.
RefSeq; NP_150502.1; NC_003027.1.
ProteinModelPortal; Q91MU2; -.
GeneID; 921599; -.
KEGG; vg:921599; -.
Proteomes; UP000126568; Genome.
Proteomes; UP000127252; Genome.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:InterPro.
InterPro; IPR000176; mRNA_MeTrfase-like.
InterPro; IPR025804; Pox/kineto_cap_MeTfrase.
InterPro; IPR030375; Poxvir_cap_MeTfrase.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01358; PARP_regulatory; 1.
PIRSF; PIRSF003726; PolA_polym_reg_poxV; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51612; SAM_MT_2O_PK; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000126568,
ECO:0000313|Proteomes:UP000127252};
Methyltransferase {ECO:0000256|PIRNR:PIRNR003726, ECO:0000256|PROSITE-
ProRule:PRU00944};
mRNA capping {ECO:0000256|PIRNR:PIRNR003726, ECO:0000256|PROSITE-
ProRule:PRU00944};
mRNA processing {ECO:0000256|PIRNR:PIRNR003726, ECO:0000256|PROSITE-
ProRule:PRU00944};
S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR003726,
ECO:0000256|PROSITE-ProRule:PRU00944};
Transferase {ECO:0000256|PIRNR:PIRNR003726, ECO:0000256|PROSITE-
ProRule:PRU00944}.
REGION 177 180 mRNA cap binding.
{ECO:0000256|PIRSR:PIRSR003726-3,
ECO:0000256|PROSITE-ProRule:PRU00944}.
REGION 205 207 mRNA cap binding.
{ECO:0000256|PIRSR:PIRSR003726-3,
ECO:0000256|PROSITE-ProRule:PRU00944}.
ACT_SITE 175 175 For methyltransferase activity.
{ECO:0000256|PIRSR:PIRSR003726-1,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 22 22 mRNA cap. {ECO:0000256|PIRSR:PIRSR003726-
3, ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 39 39 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 66 66 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 68 68 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 72 72 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000256|PIRSR:PIRSR003726-
2, ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 95 95 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 97 97 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 116 116 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 138 138 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003726-2,
ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 182 182 mRNA cap. {ECO:0000256|PIRSR:PIRSR003726-
3, ECO:0000256|PROSITE-ProRule:PRU00944}.
BINDING 233 233 mRNA cap. {ECO:0000256|PIRSR:PIRSR003726-
3, ECO:0000256|PROSITE-ProRule:PRU00944}.
SEQUENCE 333 AA; 39440 MW; 45BE5DF86A66F05C CRC64;
MEAVSMDKPF MYFDEIDNEL EYDPKTSEEK PKKLPYQGQL KLLLCELFFL SKLQRHGILD
GCTIVYVGSA PGTHIKYLRD HFLSMGLVIR WILIDGRQHD TILNGLRDVT LITKFVDESY
IRVLKKQLYQ SKIVLISDVR SKRGGNEPST FDLLSNYALQ NIMVSILKPA ASSLKWRCPF
PDQWVKDFYI PHGNEMLQPF APKYSAEMRL ISIYSGNPIK LRCITKDDSI KYEKKMFYFN
KIIRNRIIIN FDYSNQEYDF YHMYNMLKTV YSNKDFSSIK SKVLFFHHSI FKFLKIPIFN
TEKINYEPAQ RKILSKNIMF KNRNIKKSIR YNK


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