ID MCEL_RFVKA Reviewed; 836 AA. AC P25950; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 25-NOV-2008, entry version 46. 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=D3R; OS Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain OS Kasza)). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Leporipoxvirus. OX NCBI_TaxID=10272; OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91306463; PubMed=1649507; DOI=10.1016/0042-6822(91)91009-6; RA Upton C., Stuart D., McFadden G.; RT "Identification and DNA sequence of the large subunit of the capping RT enzyme from Shope fibroma virus."; RL Virology 183:773-777(1991). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M63902; AAA47224.1; -; Genomic_DNA. DR PIR; A40478; QQVZRA. 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 InterPro; IPR002035; VWF_A. DR Pfam; PF03291; Pox_MCEL; 1. DR PRINTS; PR00453; VWFADOMAIN. PE 3: Inferred from homology; KW Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; KW Nucleotidyltransferase; Transferase. FT CHAIN 1 836 mRNA-capping enzyme large subunit. FT /FTId=PRO_0000210131. FT ACT_SITE 256 256 N6-GMP-lysine intermediate (Potential). SQ SEQUENCE 836 AA; 97018 MW; 7375FDA548AE1730 CRC64; MDDSKKKRGT DYIEELILLY EDVPNPVQTD DMNHEVELTF IQPPVITLST LLPFATSQES YILFTVTNKG VKIRNRINLS KIHGLDLKNI QLVDSIDNII WEKKTLVKEH KIDSVALVKY STEEKYIFLD YKKYLSAIKL ELVNVVQVKV KHVTVDFKFK YFLGSGAQAK SSLLHVLNHP KSKPNPSLEF EIITTDEKID SASLRKELIA LFKLVFMASP SNIILDVVFK NPVQTILLKK NELPGIDLTN LYVTTKTDGV GVLITVTNKG IYCFFTHLQY TIRYDTTFES NESVTLYGEA VKQNNVWQIY LIKLITPKVS DRFKEKEYVE ERLQNICDRM TFKVKKYEGP FESHSEIIDL LTTYLPSQPE GVVLFYSDQR NQPDYKIKLD NTTDHMINII YRYMSSEPVI FGENSTFLEY KKFSDDKGFP KDYGTGKLML TDNVRYLNNI YCIAFTNVYE DVGIKNVVVP IKFISEFSAT GELIKPRIDK TFKYLYKEYY GNQYQIVVAH IRDQNIKIGD VLDEDKLSDV GQHYANDKYR LNPDVSYFTN KRTRGPLGIL SNYVKTLLIS LYCSKTFLDN SNKRKVLAID FGNGADLEKY FYGEISSLVA TDPDKEAIGR CIERYNSLNS GIKSKYYKFD YIQETIRSVT YVSSVREVFF FGKFDLVDWQ FAIHYSFHPK HYATVMNNLT ELTASGGKVL ITTMDGDLLS QLTDKKTFVI HKNLPSSENY MSVEKIHEDQ ILVYNPSSMS RPMQEYIVKR VNLTKIFSEY GFELIDCVHF DTIIERSKRF INSVSKMEER KSTKNFFELN REALKHEGTD IDDLLRYYIV YVFSKR //