ID   MCEL_VACCC              Reviewed;         844 AA.
AC   P20979;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-NOV-2008, entry version 48.
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   ORFNames=D1R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=91021027; PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   COMPLETE GENOME.
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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; M35027; AAA48095.1; -; Genomic_DNA.
DR   PIR; I42514; QQVZVC.
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:InterPro.
DR   InterPro; IPR004971; Pox_MCEL.
DR   Pfam; PF03291; Pox_MCEL; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    844       mRNA-capping enzyme large subunit.
FT                                /FTId=PRO_0000210122.
FT   ACT_SITE    260    260       N6-GMP-lysine intermediate (Potential).
SQ   SEQUENCE   844 AA;  96733 MW;  9982FDC819867277 CRC64;
     MDANVVSSST 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 TSNGLYCYFT 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
//