MCES_VACCW
ID MCES_VACCW Reviewed; 287 AA.
AC P04318; Q76ZR5;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 29-SEP-2021, entry version 104.
DE RecName: Full=mRNA-capping enzyme regulatory subunit;
DE AltName: Full=Virus termination factor small subunit;
DE Short=VTF small subunit;
DE AltName: Full=mRNA-capping enzyme 33 kDa subunit;
DE AltName: Full=mRNA-capping enzyme D12 subunit;
DE AltName: Full=mRNA-capping enzyme small subunit;
GN OrderedLocusNames=VACWR117; ORFNames=D12L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT fragment.";
RL Virology 153:96-112(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008103; DOI=10.1093/nar/14.7.3003;
RA Weinrich S.L., Hruby D.E.;
RT "A tandemly-oriented late gene cluster within the vaccinia virus genome.";
RL Nucleic Acids Res. 14:3003-3016(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=2552660; DOI=10.1016/0042-6822(89)90194-3;
RA Niles E.G., Lee-Chen G.-J., Shuman S., Moss B., Broyles S.S.;
RT "Vaccinia virus gene D12L encodes the small subunit of the viral mRNA
RT capping enzyme.";
RL Virology 172:513-522(1989).
RN [5]
RP INTERACTION WITH LARGE SUBUNIT.
RX PubMed=2161527; DOI=10.1073/pnas.87.11.4023;
RA Guo P., Moss B.;
RT "Interaction and mutual stabilization of the two subunits of vaccinia virus
RT mRNA capping enzyme coexpressed in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4023-4027(1990).
RN [6]
RP MUTAGENESIS OF PRO-23.
RX PubMed=1649315; DOI=10.1128/jvi.65.8.4042-4050.1991;
RA Carpenter M.S., DeLange A.M.;
RT "A temperature-sensitive lesion in the small subunit of the vaccinia virus-
RT encoded mRNA-capping enzyme causes a defect in viral telomere resolution.";
RL J. Virol. 65:4042-4050(1991).
RN [7]
RP FUNCTION.
RC STRAIN=IHDW, and mutant Dts36;
RX PubMed=18295814; DOI=10.1016/j.virol.2008.01.028;
RA Shatzer A.N., Kato S.E., Condit R.C.;
RT "Phenotypic analysis of a temperature sensitive mutant in the large subunit
RT of the vaccinia virus mRNA capping enzyme.";
RL Virology 375:236-252(2008).
RN [8]
RP FUNCTION.
RX PubMed=18455214; DOI=10.1016/j.virol.2008.03.031;
RA Christen L.A., Piacente S., Mohamed M.R., Niles E.G.;
RT "Vaccinia virus early gene transcription termination factors VTF and Rap94
RT interact with the U9 termination motif in the nascent RNA in a
RT transcription ternary complex.";
RL Virology 376:225-235(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ADOHCY AND THE
RP CATALYTIC SUBUNIT.
RX PubMed=17989694; DOI=10.1038/sj.emboj.7601912;
RA De la Pena M., Kyrieleis O.J., Cusack S.;
RT "Structural insights into the mechanism and evolution of the vaccinia virus
RT mRNA cap N7 methyl-transferase.";
RL EMBO J. 26:4913-4925(2007).
CC -!- FUNCTION: Regulatory subunit of the mRNA cap enzyme which stabilizes
CC the catalytic subunit and enhances its methyltransferase activity
CC through an allosteric mechanism. Heterodimeric mRNA capping enzyme
CC catalyzes the linkage of a N7-methyl-guanosine moiety to the first
CC transcribed nucleotide (cap 0 structure), whereas the polymerase
CC associated VP39 is responsible for a second methylation at the 2'-O
CC position of the ribose (cap 1 structure).
CC -!- FUNCTION: The heterodimeric enzyme is also involved in early viral gene
CC transcription termination and intermediate viral gene transcription
CC initiation. Early gene transcription termination requires the
CC termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94
CC subunit of the viral RNA polymerase, as well as the presence of a
CC specific termination motif. Binds, together with RAP94, to the
CC termination motif 5'-UUUUUNU-3' in the nascent early mRNA.
CC -!- SUBUNIT: Heterodimer of a catalytic and a regulatory subunit. Intrinsic
CC methyltransferase activity of the catalytic subunit is weak and needs
CC to be stimulated 30- to 50-fold by the regulatory subunit, which is
CC itself catalytically inert. {ECO:0000269|PubMed:17989694}.
CC -!- INTERACTION:
CC P04318; P04298: VACWR106; NbExp=3; IntAct=EBI-16095776, EBI-16095746;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and
CC other proteins required to synthesize early mRNAs are packaged within
CC the virion core along with the DNA genome.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae mRNA-capping enzyme
CC regulatory subunit family. {ECO:0000305}.
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DR EMBL; M15058; AAA48270.1; -; Genomic_DNA.
DR EMBL; X03729; CAA27369.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89396.1; -; Genomic_DNA.
DR PIR; A03892; QQVZ22.
DR RefSeq; YP_232999.1; NC_006998.1.
DR PDB; 2VDW; X-ray; 2.70 A; B/D/F/H=1-287.
DR PDB; 4CKB; X-ray; 2.80 A; B/E=1-287.
DR PDB; 4CKC; X-ray; 2.90 A; B/E=1-287.
DR PDB; 4CKE; X-ray; 2.90 A; B/E=1-287.
DR PDB; 6RIE; EM; 3.10 A; L=1-287.
DR PDBsum; 2VDW; -.
DR PDBsum; 4CKB; -.
DR PDBsum; 4CKC; -.
DR PDBsum; 4CKE; -.
DR PDBsum; 6RIE; -.
DR SMR; P04318; -.
DR DIP; DIP-60665N; -.
DR IntAct; P04318; 1.
DR DNASU; 3707515; -.
DR GeneID; 3707515; -.
DR KEGG; vg:3707515; -.
DR EvolutionaryTrace; P04318; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11680; -; 1.
DR InterPro; IPR005009; Poxvirus_mRNA-cap_ssu.
DR InterPro; IPR043096; Poxvirus_mRNA-cap_ssu_sf.
DR Pfam; PF03341; Pox_mRNA-cap; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA capping; mRNA processing; Reference proteome;
KW Transcription; Transcription regulation; Transcription termination; Virion.
FT CHAIN 1..287
FT /note="mRNA-capping enzyme regulatory subunit"
FT /id="PRO_0000210137"
FT MUTAGEN 23
FT /note="P->S: In ts9383; conditional lethal mutant defective
FT in the ability to convert the replicated form of the viral
FT telomere to hairpin termini."
FT /evidence="ECO:0000269|PubMed:1649315"
FT CONFLICT 134
FT /note="K -> N (in Ref. 2; CAA27369)"
FT /evidence="ECO:0000305"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2VDW"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6RIE"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6RIE"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 239..268
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:2VDW"
SQ SEQUENCE 287 AA; 33352 MW; EA9CE30A7661A7ED CRC64;
MDEIVKNIRE GTHVLLPFYE TLPELNLSLG KSPLPSLEYG ANYFLQISRV NDLNRMPTDM
LKLFTHDIML PESDLDKVYE ILKINSVKYY GRSTKADAVV ADLSARNKLF KRERDAIKSN
NHLTENNLYI SDYKMLTFDV FRPLFDFVNE KYCIIKLPTL FGRGVIDTMR IYCSLFKNVR
LLKCVSDSWL KDSAIMVASD VCKKNLDLFM SHVKSVTKSS SWKDVNSVQF SILNNPVDTE
FINKFLEFSN RVYEALYYVH SLLYSSMTSD SKSIENKHQR RLVKLLL
