MCE_MIMIV
ID MCE_MIMIV Reviewed; 1170 AA.
AC Q5UQX1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable mRNA-capping enzyme;
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=MIMI_R382;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP LOCATION.
RX PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT "Mimivirus giant particles incorporate a large fraction of anonymous and
RT unique gene products.";
RL J. Virol. 80:11678-11685(2006).
CC -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs.
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 -!- 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 -!- 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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
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}.
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DR EMBL; AY653733; AAV50651.1; -; Genomic_DNA.
DR RefSeq; YP_003986887.1; NC_014649.1.
DR PDB; 2QY2; X-ray; 2.00 A; A/B=1-237.
DR PDB; 2QZE; X-ray; 2.90 A; A/B=1-237.
DR PDB; 3BGY; X-ray; 1.65 A; A/B=1-237.
DR PDBsum; 2QY2; -.
DR PDBsum; 2QZE; -.
DR PDBsum; 3BGY; -.
DR SMR; Q5UQX1; -.
DR PRIDE; Q5UQX1; -.
DR GeneID; 9925004; -.
DR KEGG; vg:9925004; -.
DR BRENDA; 2.7.7.50; 9231.
DR UniPathway; UPA00922; -.
DR EvolutionaryTrace; Q5UQX1; -.
DR Proteomes; UP000001134; 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 CDD; cd07470; CYTH-like_mRNA_RTPase; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.20.100.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR004206; mRNA_triPase_Cet1.
DR InterPro; IPR037009; mRNA_triPase_Cet1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Virion.
FT CHAIN 1..1170
FT /note="Probable mRNA-capping enzyme"
FT /id="PRO_0000210133"
FT DOMAIN 645..1017
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT ACT_SITE 292
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000255"
FT BINDING 693..694
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 697
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 715
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 737
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 813..815
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 724
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 753
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 817
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 912
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:3BGY"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:3BGY"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3BGY"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:3BGY"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 122..136
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 140..152
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 169..183
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 186..199
FT /evidence="ECO:0007829|PDB:3BGY"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3BGY"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:3BGY"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:3BGY"
SQ SEQUENCE 1170 AA; 136508 MW; 320D8F4137C55AD6 CRC64;
MGTKLKKSNN DITIFSENEY NEIVEMLRDY SNGDNLEFEV SFKNINYPNF MRITEHYINI
TPENKIESNN YLDISLIFPD KNVYRVSLFN QEQIGEFITK FSKASSNDIS RYIVSLDPSD
DIEIVYKNRG SGKLIGIDNW AITIKSTEEI PLVAGKSKIS KPKITGSERI MYRYKTRYSF
TINKNSRIDI TDVKSSPIIW KLMTVPSNYE LELELINKID INTLESELLN VFMIIQDTKI
PISKAESDTV VEEYRNLLNV RQTNNLDSRN VISVNSNHII NFIPNRYAVT DKADGERYFL
FSLNSGIYLL SINLTVKKLN IPVLEKRYQN MLIDGEYIKT TGHDLFMVFD VIFAEGTDYR
YDNTYSLPKR IIIINNIIDK CFGNLIPFND YTDKHNNLEL DSIKTYYKSE LSNYWKNFKN
RLNKSTDLFI TRKLYLVPYG IDSSEIFMYA DMIWKLYVYN ELTPYQLDGI IYTPINSPYL
IRGGIDAYDT IPMEYKWKPP SQNSIDFYIR FKKDVSGADA VYYDNSVERA EGKPYKICLL
YVGLNKQGQE IPIQFKVNGV EQTANIYTKD GEATDINGNA INDNTVVEFV FDTLKIDMDD
SYKWIPIRTR YDKTESVQKY HKRYGNNLQI ANRIWKTITN PITEDIISSL GDPTTFNKEI
TLLSDFRDTK YNKQALTYYQ KNTSNAAGMR AFNNWIKSNM ITTYCRDGSK VLDIGCGRGG
DLIKFINAGV EFYVGIDIDN NGLYVINDSA NNRYKNLKKT IQNIPPMYFI NADARGLFTL
EAQEKILPGM PDFNKSLINK YLVGNKYDTI NCQFTIHYYL SDELSWNNFC KNINNQLKDN
GYLLITSFDG NLIHNKLKGK QKLSSSYTDN RGNKNIFFEI NKIYSDTDKV GLGMAIDLYN
SLISNPGTYI REYLVFPEFL EKSLKEKCGL ELVESDLFYN IFNTYKNYFK KTYNEYGMTD
VSSKKHSEIR EFYLSLEGNA NNDIEIDIAR ASFKLAMLNR YYVFRKTSTI NITEPSRIVN
ELNNRIDLGK FIMPYFRTNN MFIDLDNVDT DINRVYRNIR NKYRTTRPHV YLIKHNINEN
RLEDIYLSNN KLDFSKIKNG SDPKVLLIYK SPDKQFYPLY YQNYQSMPFD LDQIYLPDKK
KYLLDSDRII NDLNILINLT EKIKNIPQLS
