ID   MCEL_VACCA              Reviewed;         844 AA.
AC   O57209;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=mRNA-capping enzyme large subunit;
DE   Includes:
DE     RecName: Full=Polynucleotide 5'-triphosphatase;
DE              EC=3.1.3.33;
DE     AltName: Full=mRNA 5'-triphosphatase;
DE              Short=TPase;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.50;
DE     AltName: Full=GTP--RNA guanylyltransferase;
DE              Short=GTase;
GN   OrderedLocusNames=MVA098R, ACAM3000_MVA_098;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=98263813; PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S.,
RA   Osborne J., Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first two reactions in the mRNA cap
CC       formation pathway.
CC   -!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
CC       polynucleotide + phosphate.
CC   -!- CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate +
CC       G(5')ppp-Pur-mRNA.
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SIMILARITY: Belongs to the viral GTase family.
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DR   EMBL; U94848; AAB96511.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10496.1; -; Genomic_DNA.
DR   PIR; T37374; T37374.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:EC.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:EC.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   InterPro; IPR019602; mRNA_cap_ATPase/GuylTrfase_vir.
DR   InterPro; IPR004971; Pox_MCEL.
DR   Pfam; PF10640; Pox_ATPase-GT; 1.
DR   Pfam; PF03291; Pox_MCEL; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN         1    844       mRNA-capping enzyme large subunit.
FT                                /FTId=PRO_0000210121.
FT   ACT_SITE    260    260       N6-GMP-lysine intermediate (Potential).
SQ   SEQUENCE   844 AA;  96761 MW;  BC7052355070FE2C CRC64;
     MDANIVSSST IATYIDALAK NASELEQRST AYEINNELEL VFIKPPLITL TNVVNISTIQ
     ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID NIVWEKKSLV TENRLHKECL
     LRLSTEERHI FLDYKKYGSS IRLELVNLIQ AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI
     NHPKSRPNTS LEIEFTPRDN EKVPYDELIK ELTTLSRHIF MASPENVILS PPINAPIKTF
     MLPKQDIVGL DLENLYAVTK TDGIPITIRV TSKGLYCYFT HLGYIIRYPV KRIIDSEVVV
     FGEAVKDKNW TVYLIKLIEP VNAINDRLEE SKYVESKLVD ICDRIVFKSK KYEGPFTTTS
     EVVDMLSTYL PKQPEGVILF YSKGPKSNID FKIKKENTID QTANVVFRYM SSEPIIFGES
     SIFVEYKKFS NDKGFPKEYG SGKIVLYNGV NYLNNIYCLE YINTHNEVGI KSVVVPIKFI
     AEFLVNGEIL KPRIDKTMKY INSEDYYGNQ HNIIVEHLRD QSIKIGDIFN EDKLSDVGHQ
     YANNDKFRLN PEVSYFTNKR TRGPLGILSN YVKTLLISMY CSKTFLDDSN KRKVLAIDFG
     NGADLEKYFY GEIALLVATD PDADAIARGN ERYNKLNSGI KTKYYKFDYI QETIRSDTFV
     SSVREVFYFG KFNIIDWQFA IHYSFHPRHY ATVMNNLSEL TASGGKVLIT TMDGDKLSKL
     TDKKTFIIHK NLPSSENYMS VEKIADDRIV VYNPSTMSTP MTEYIIKKND IVRVFNEYGF
     VLVDNVDFAT IIERSKKFIN GASTMEDRPS TKNFFELNRG AIKCEGLDVE DLLSYYVVYV
     FSKR
//