MCE_ASFK5
ID MCE_ASFK5 Reviewed; 868 AA.
AC P0C995;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=mRNA-capping enzyme;
DE AltName: Full=VTF/CE;
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;
DE Includes:
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE EC=2.1.1.56;
GN OrderedLocusNames=Ken-113;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably catalyzes the second reaction in the mRNA cap
CC formation pathway. Forms a covalent complex with GTP.
CC {ECO:0000250|UniProtKB:P32094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a
CC 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33;
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:P32094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- PATHWAY: mRNA processing; mRNA capping.
CC -!- SUBUNIT: Part of the viral DNA-directed RNA polymerase that consists of
CC 8 polII-like subunits (RPB1, RPB2, RPB3, RPB5, RPB6, RPB7, RPB9,
CC RPB10), a capping enzyme and a termination factor.
CC {ECO:0000250|UniProtKB:P32094}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P32094}. Note=Found
CC in association with viral nucleoid. {ECO:0000250|UniProtKB:P32094}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- DOMAIN: The N-terminus contains the mRNA 5'-triphosphatase domain, the
CC central part contains the mRNA guanylyltransferase, and C-terminus
CC contains the methyltransferase domain. {ECO:0000250|UniProtKB:P32094}.
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PRIDE; P0C995; -.
DR UniPathway; UPA00922; -.
DR Proteomes; UP000000861; Genome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 3: Inferred from homology;
KW Early protein; GTP-binding; Hydrolase; Methyltransferase; mRNA capping;
KW mRNA processing; Nucleotide-binding; Nucleotidyltransferase; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Virion.
FT CHAIN 1..868
FT /note="mRNA-capping enzyme"
FT /id="PRO_0000373095"
FT DOMAIN 545..868
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT ACT_SITE 282
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P32094"
FT BINDING 607
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 624
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 646
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 710..712
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 627
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 658
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 713
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 806
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ SEQUENCE 868 AA; 99880 MW; 5FAD8401A9BB162B CRC64;
MASLENLVAR YQRCFNDQSL KNSTIELEIR FQHINFLLFK TVYEALVAQE IPSTISHSIR
CIKKVHHENH CREKILPSDN FYFKKQPLMF FKFSEPASLG CKVSLAIEQP IRKFILDSSV
LVRLKNRTTF QISDLWKIEL TVVKQLMGSE VSAKLTAFKT LLFDTPEQQT AKNMMTLINP
DDEYLYEIEI EYTGKPESLT AADVIKIKNT VLTLISPNHL MLTAYHQAIE FIASHILSSE
ILLARIKSGK WGLKRLLPQV KSMTKADYMK FYPPVGYYVT DKADGIRGIA VIQDTQMYVV
ADQLYSLGTT GIEPLKPTIL DGEFMPEKKE FYGFDVIMYE GNLLTQQGFE TRIEALNKGI
KVLQAFNIKA EMKPFISLTS ADPNVLLKNF ESVFKKKTRP YSIDGIILVE PGNSYLNTNT
FKWKPTWDNT LDFLVRKCPE SLNVPEYAPK KGFSLHLLFV GISGELFKKL ALNWCPGYTK
LFPVTQRNQN YFPVQFQPSD FPLAFLYYHP DTSSFSDIDG KVLEMRCLKR EVNYVSWEIV
KIREDRQQDL KTGGYFGNDF KTAELTWLNY MDPFSFEELA KGPSGMYFAG AKTGIYRAQT
ALISFIKQEI IQKISHQSWV IDLGIGKGQD LGRYLDAGIR HLVGIDKDQT ALAELIYRKF
SHATTRQHKH ATNIYVLHQD LAEPAKEISE KVHQIYGFPK EGASSIVSNL FIHYLMKSSQ
QVENLAVLCH KLLQPGGMVW FTTMLGERVL ELLHENRVEL NEVWEARENE VVKFAIKRLF
KEDVLQETGQ EIGVLLPFSN GDFYNEYLVN TAFLIKIFKH HGFSLVQMQS FKDWIPEFQT
FSKSLYKILT EADKTWTSLF GFICLRKN
