ID   MCEL_CWPXB              Reviewed;         844 AA.
AC   Q8QMV9;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-NOV-2008, entry version 24.
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=CPXV118;
OS   Cowpox virus (strain Brighton Red) (CPV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus.
OX   NCBI_TaxID=265872;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis silvestris catus (Cat).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dietrich F.S., Ray C.A., Sharma D.A., Allen A., Pickup D.J.;
RL   Submitted (MAY-2003) 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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the viral GTase family.
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DR   EMBL; AF482758; AAM13560.1; -; Genomic_DNA.
DR   RefSeq; NP_619902.1; -.
DR   GeneID; 1485995; -.
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   Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN         1    844       mRNA-capping enzyme large subunit.
FT                                /FTId=PRO_0000210128.
FT   ACT_SITE    260    260       N6-GMP-lysine intermediate (Potential).
SQ   SEQUENCE   844 AA;  96703 MW;  C760E4B77B43A3E8 CRC64;
     MDANVVSSST IATYIDALAK NASELEQGST AYEINNELEL VFIKPPLITL TNVVNISTIQ
     ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID NIVWEKKSLV TENRLHKECL
     LRLSTEERHI FLDYKKYGSS IRLELVNLIQ AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI
     NHPKSRPNTS LEIEFTPRDN EKVPYDELIK ELTTLSRHIF MASPENVILS PPINPPIKTF
     MLPKQDIVGL DLENLYAVTK TDGIPITIRV TSKGLYCYFT HLGYIIRYPV KRIIDSEVVV
     FGEAVKDKNW TVYLIKLIEP VNAISDRLEE SKYVESKLVD ICDRIVFKSK KYEGPFTTTS
     EVVDMLSTYL PKQPEGVILF YSKGPKSNID FKIKKENTID QTANVVFRYM SSEPIIFGES
     SIFIEYKKFT NDKGFPKEYG SGKIVLYNGV NYLNNIYCLE YINTHNEVGI KSVVVPIKFI
     AEFLVNGEIL KPRIDKTMKY INSEDYYGNQ HNVIVEHLRD QSIKIGDVFN EDKLSDVGHQ
     YANNDKFRLN PEVSYFTNKR TRGPLGILSN YVKTLLISMY CSKTFLDDSN KRKVLAIDFG
     NGADLEKYFY GEIALLVATD PDADAIARGN ERYNKLNSGI KTKYYKFDYI QETIRSDTFV
     SSVREVFYFG KFNIIDWQFA IHYSFHPRHY ATVMNNLSEL TASGGKVLIT TMDGDKLSKL
     TDKKTFIIHK NLPSSENYMS VEKIADDRIL VYNPSTMSTP MTEYIIKKND IVRVFNEYGF
     VLVDNIDFAT IIERSKKFIN GASTMEDRPS TRNFFELNRG AIKCEGLDVE DLLSYYVVYV
     FSKR
//