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 02-SEP-2026, entry version 113. DE RecName: Full=mRNA-capping enzyme catalytic subunit; DE AltName: Full=Virus termination factor large subunit; DE Short=VTF large subunit; DE AltName: Full=mRNA-capping enzyme 97 kDa subunit; DE AltName: Full=mRNA-capping enzyme D1 subunit; DE AltName: Full=mRNA-capping enzyme large subunit; DE Includes: DE RecName: Full=Polynucleotide 5'-triphosphatase; DE EC=3.6.1.74; 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; DE Includes: DE RecName: Full=mRNA (guanine-N(7))-methyltransferase; DE EC=2.1.1.56; DE AltName: Full=mRNA cap methyltransferase; GN Name=OPG113; ORFNames=D1R; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10249; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: Catalytic subunit of the mRNA capping enzyme which catalyzes CC three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is CC hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate CC RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap CC is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA CC capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to CC the first transcribed nucleotide (cap 0 structure), whereas the CC methyltransferase OPG102 is responsible for a second methylation at the CC 2'-O position of the ribose (cap 1 structure). Also involved in early CC viral gene transcription termination and intermediate viral gene CC transcription initiation. Early gene transcription termination requires CC the termination factor VTF, the DNA-dependent ATPase NPH-I/OPG123 and CC the RAP94/OPG109 subunit of the viral RNA polymerase, as well as the CC presence of a specific termination motif. Binds, together with CC RAP94/OPG109, to the termination motif 5'-UUUUUNU-3' in the nascent CC early mRNA. {ECO:0000250|UniProtKB:P04298}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end CC diphospho-ribonucleoside in mRNA + phosphate + H(+); CC Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; CC Evidence={ECO:0000250|UniProtKB:P04298}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; CC Evidence={ECO:0000250|UniProtKB:P04298}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- CC end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; CC Evidence={ECO:0000250|UniProtKB:P04298}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; CC Evidence={ECO:0000250|UniProtKB:P04298}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P04298}; CC -!- SUBUNIT: Forms a heterodimer with the regulatory subunit OPG124. CC {ECO:0000250|UniProtKB:P04298}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P04298}. Note=All CC the enzymes and other proteins required to synthesize early mRNAs are CC packaged within the virion core along with the DNA genome. CC {ECO:0000250|UniProtKB:P04298}. CC -!- DOMAIN: The N-terminus contains the triphosphatase and CC guanylyltransferase domains, whereas the C-terminus contains the CC methyltransferase domain. The N-terminus is involved in binding to the CC termination motif 5'-UUUUUNU-3' in the nascent mRNA. CC {ECO:0000250|UniProtKB:P04298}. CC -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA CC guanylyltransferase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the class I-like SAM- CC binding methyltransferase superfamily. mRNA cap 0 methyltransferase CC family. {ECO:0000255|PROSITE-ProRule:PRU00895}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35027; AAA48095.1; -; Genomic_DNA. DR PIR; I42514; QQVZVC. DR PDB; 8P0J; EM; 2.39 A; O=1-844. DR PDB; 8P0K; EM; 2.64 A; O=1-844. DR PDB; 8P0N; EM; 2.58 A; O=1-844. DR PDB; 8RQK; EM; 2.65 A; O=1-844. DR PDB; 9FQ6; EM; 2.50 A; O=1-844. DR EMDB; EMD-17334; -. DR EMDB; EMD-17335; -. DR EMDB; EMD-17336; -. DR EMDB; EMD-19442; -. DR EMDB; EMD-50644; -. DR SMR; P20979; -. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0050355; F:inorganic triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0140818; F:mRNA 5'-triphosphate monophosphatase activity; ISS:UniProtKB. DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR FunFam; 3.30.470.140:FF:000001; mRNA-capping enzyme catalytic subunit; 1. DR FunFam; 3.40.50.150:FF:000307; mRNA-capping enzyme catalytic subunit; 1. DR Gene3D; 2.40.50.830; -; 1. DR Gene3D; 3.20.100.20; -; 1. DR Gene3D; 3.30.470.140; -; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR048425; MCEL_GT_NTPase. DR InterPro; IPR048426; MCEL_GT_OB. DR InterPro; IPR046429; MCEL_NTPase_sf. DR InterPro; IPR046428; MCEL_OB_dom_sf. DR InterPro; IPR019602; MCEL_TPase. DR InterPro; IPR046430; MCEL_TPase_sf. DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom. DR InterPro; IPR039753; RG7MT1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1. DR PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1. DR Pfam; PF21004; MCEL_GT_NTPase; 1. DR Pfam; PF10640; MCEL_TPase; 1. DR Pfam; PF03291; mRNA_G-N7_MeTrfase; 1. DR Pfam; PF21005; OB_MCEL_GT; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51562; RNA_CAP0_MT; 1. DR PDBsum; 8P0J; -. DR PDBsum; 8P0K; -. DR PDBsum; 8P0N; -. DR PDBsum; 8RQK; -. DR PDBsum; 9FQ6; -. PE 1: Evidence at protein level; KW 3D-structure; GTP-binding; Hydrolase; Magnesium; Metal-binding; KW Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme; KW Nucleotide-binding; Nucleotidyltransferase; RNA-binding; KW S-adenosyl-L-methionine; Transferase; Virion. FT CHAIN 1..844 FT /note="mRNA-capping enzyme catalytic subunit" FT /id="PRO_0000210122" FT DOMAIN 516..844 FT /note="mRNA cap 0 methyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT REGION 1..539 FT /note="Triphosphatase-guanylyltransferase" FT /evidence="ECO:0000250|UniProtKB:P04298" FT ACT_SITE 260 FT /note="N6-GMP-lysine intermediate" FT /evidence="ECO:0000250" FT BINDING 37 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT BINDING 549..550 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 569..570 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 573 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 598 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 620 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT BINDING 678..680 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 77 FT /note="Essential for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT SITE 107 FT /note="Essential for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT SITE 126 FT /note="Essential for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT SITE 159 FT /note="Essential for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT SITE 161 FT /note="Essential for RNA triphosphatase activity" FT /evidence="ECO:0000250|UniProtKB:P04298" FT SITE 607 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 632 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 682 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 763 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT SITE 836 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895" FT HELIX 3..7 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 32..44 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 58..69 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 92..97 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 102..116 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 119..130 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 142..152 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 154..168 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 175..181 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 188..195 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 205..220 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 264..270 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 280..282 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 299..317 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 327..337 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 343..349 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:9FQ6" FT HELIX 359..369 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 370..372 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 377..384 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 385..388 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 389..393 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 398..405 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 422..432 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 435..445 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 447..453 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 454..457 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 458..465 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 470..484 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 489..492 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 494..502 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 511..522 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 525..527 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 533..543 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 548..551 FT /evidence="ECO:0007829|PDB:9FQ6" FT HELIX 564..580 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 583..587 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 605..610 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 614..619 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 623..637 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 642..645 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 646..650 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 654..656 FT /evidence="ECO:0007829|PDB:8RQK" FT TURN 657..659 FT /evidence="ECO:0007829|PDB:9FQ6" FT HELIX 660..664 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 672..679 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 681..683 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 687..689 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 690..699 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 701..712 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 714..719 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 724..727 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 729..732 FT /evidence="ECO:0007829|PDB:9FQ6" FT HELIX 734..736 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 737..745 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 748..752 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 754..756 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 761..764 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 768..777 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 780..787 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 788..801 FT /evidence="ECO:0007829|PDB:8P0J" FT TURN 803..805 FT /evidence="ECO:0007829|PDB:9FQ6" FT HELIX 809..822 FT /evidence="ECO:0007829|PDB:8P0J" FT HELIX 829..833 FT /evidence="ECO:0007829|PDB:8P0J" FT STRAND 836..843 FT /evidence="ECO:0007829|PDB:8P0J" 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 //