MCE_PBCV1
ID MCE_PBCV1 Reviewed; 330 AA.
AC Q84424;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=mRNA-capping enzyme;
DE AltName: Full=GTP--RNA guanylyltransferase;
DE AltName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50;
GN OrderedLocusNames=A103R;
OS Paramecium bursaria Chlorella virus 1 (PBCV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=10506;
OH NCBI_TaxID=114055; Chlorella.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7676624; DOI=10.1006/viro.1995.1462;
RA Li Y., Lu Z., Burbank D.E., Kutish G.F., Rock D.L., Etten J.L.;
RT "Analysis of 43 kb of the Chlorella virus PBCV-1 330-kb genome: map
RT positions 45 to 88.";
RL Virology 212:134-150(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9160746; DOI=10.1016/s0092-8674(00)80236-6;
RA Haakansson K., Doherty A.J., Shuman S., Wigley D.B.;
RT "X-ray crystallography reveals a large conformational change during guanyl
RT transfer by mRNA capping enzymes.";
RL Cell 89:545-553(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 11-327.
RX PubMed=9465045; DOI=10.1073/pnas.95.4.1505;
RA Haakansson K., Wigley D.B.;
RT "Structure of a complex between a cap analogue and mRNA guanylyl
RT transferase demonstrates the structural chemistry of RNA capping.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1505-1510(1998).
CC -!- FUNCTION: mRNA capping. Transfers a GMP cap onto the end of mRNA that
CC terminates with a 5'-diphosphate tail.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the eukaryotic GTase family. {ECO:0000305}.
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DR EMBL; JF411744; AAC96471.1; -; Genomic_DNA.
DR PIR; T17593; T17593.
DR RefSeq; NP_048451.1; NC_000852.5.
DR PDB; 1CKM; X-ray; 2.50 A; A/B=1-330.
DR PDB; 1CKN; X-ray; 2.50 A; A/B=1-330.
DR PDB; 1CKO; X-ray; 3.10 A; A=1-330.
DR PDBsum; 1CKM; -.
DR PDBsum; 1CKN; -.
DR PDBsum; 1CKO; -.
DR SMR; Q84424; -.
DR DrugBank; DB03931; Diguanosine-5'-Triphosphate.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR PRIDE; Q84424; -.
DR GeneID; 918242; -.
DR KEGG; vg:918242; -.
DR BRENDA; 2.7.7.50; 4540.
DR EvolutionaryTrace; Q84424; -.
DR Proteomes; UP000000862; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; mRNA capping; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..330
FT /note="mRNA-capping enzyme"
FT /id="PRO_0000210107"
FT ACT_SITE 82
FT /note="N6-GMP-lysine intermediate"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 85..95
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1CKM"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1CKM"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1CKN"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:1CKM"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:1CKM"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:1CKM"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1CKM"
SQ SEQUENCE 330 AA; 37832 MW; 6AF8A404710812D9 CRC64;
MVPPTINTGK NITTERAVLT LNGLQIKLHK VVGESRDDIV AKMKDLAMDD HKFPRLPGPN
PVSIERKDFE KLKQNKYVVS EKTDGIRFMM FFTRVFGFKV CTIIDRAMTV YLLPFKNIPR
VLFQGSIFDG ELCVDIVEKK FAFVLFDAVV VSGVTVSQMD LASRFFAMKR SLKEFKNVPE
DPAILRYKEW IPLEHPTIIK DHLKKANAIY HTDGLIIMSV DEPVIYGRNF NLFKLKPGTH
HTIDFIIMSE DGTIGIFDPN LRKNVPVGKL DGYYNKGSIV ECGFADGTWK YIQGRSDKNQ
ANDRLTYEKT LLNIEENITI DELLDLFKWE
