ID   MCEL_VACCV              Reviewed;         844 AA.
AC   P04298; Q76ZS6;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   04-NOV-2008, entry version 52.
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=VACWR106; ORFNames=D1R;
OS   Vaccinia virus (strain Western Reserve / WR) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86291159; 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
RT   HindIII D fragment.";
RL   Virology 153:96-112(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M.,
RA   Osborne J., 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   [3]
RP   INTERACTION WITH SMALL SUBUNIT, AND PROTEIN SEQUENCE OF 1-20 AND
RP   498-517.
RX   MEDLINE=90272646; PubMed=2161527;
RA   Guo P., Moss B.;
RT   "Interaction and mutual stabilization of the two subunits of vaccinia
RT   virus mRNA capping enzyme coexpressed in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4023-4027(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; M15058; AAA48253.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89385.1; -; Genomic_DNA.
DR   PIR; A03872; QQVZ1.
DR   RefSeq; YP_232988.1; -.
DR   PDB; 2VDW; X-ray; 2.70 A; A/C/E/G=545-844.
DR   PDBsum; 2VDW; -.
DR   GeneID; 3707562; -.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:EC.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:EC.
DR   InterPro; IPR004971; Pox_MCEL.
DR   Pfam; PF03291; Pox_MCEL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN         1    844       mRNA-capping enzyme large subunit.
FT                                /FTId=PRO_0000210124.
FT   ACT_SITE    260    260       N6-GMP-lysine intermediate (Potential).
FT   HELIX       563    580
FT   TURN        583    585
FT   STRAND      593    596
FT   TURN        600    604
FT   HELIX       605    610
FT   STRAND      614    621
FT   HELIX       623    636
FT   STRAND      646    651
FT   STRAND      656    658
FT   HELIX       659    664
FT   STRAND      672    679
FT   HELIX       681    683
FT   TURN        687    689
FT   HELIX       690    700
FT   STRAND      701    712
FT   HELIX       714    717
FT   STRAND      724    727
FT   STRAND      730    732
FT   TURN        734    736
FT   STRAND      737    741
FT   STRAND      743    745
FT   STRAND      748    752
FT   TURN        754    756
FT   STRAND      757    759
FT   STRAND      761    764
FT   HELIX       768    777
FT   STRAND      780    787
FT   HELIX       788    793
FT   HELIX       796    800
FT   HELIX       802    805
FT   HELIX       809    823
FT   HELIX       829    833
FT   STRAND      836    843
SQ   SEQUENCE   844 AA;  96734 MW;  8B9FD3DE836FA6E7 CRC64;
     MDANVVSSST IATYIDALAK NASELEQRST AYEINNELEL VFIKPPLITL TNVVNISTIQ
     ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID NIVWEKKSLV TENRLHKECL
     LRLSTEERHI FLDYKKYGSS IRLELVNLIQ AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI
     NHPKSRPNTS LEIEFTPRDN ETVPYDELIK 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 TRNFFELNRG AIKCEGLDVE DLLSYYVVYV
     FSKR
//