MCE1_CAEEL
ID MCE1_CAEEL Reviewed; 623 AA.
AC Q17607; O02558;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=mRNA-capping enzyme;
DE Includes:
DE RecName: Full=mRNA 5'-triphosphate monophosphatase;
DE EC=3.6.1.74 {ECO:0000269|PubMed:9200605};
DE AltName: Full=mRNA 5'-phosphatase;
DE Includes:
DE RecName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50 {ECO:0000269|PubMed:9200605};
DE AltName: Full=GTP--RNA guanylyltransferase;
DE Short=GTase;
GN Name=cel-1; ORFNames=C03D6.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-585.
RC STRAIN=Bristol N2;
RA Shuman S., Ho C.K.;
RT "Identification of mRNA capping enzyme from C.elegans.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP ACTIVE SITE, MUTAGENESIS OF CYS-136, FUNCTION, ACTIVITY REGULATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9200605; DOI=10.1016/s0092-8674(00)80272-x;
RA Takagi T., Moore C.R., Diehn F., Buratowski S.;
RT "An RNA 5'-triphosphatase related to the protein tyrosine phosphatases.";
RL Cell 89:867-873(1997).
CC -!- FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-
CC triphosphate monophosphatase activity in the N-terminal part and mRNA
CC guanylyltransferase activity in the C-terminal part. Catalyzes the
CC first two steps of cap formation: by removing the gamma-phosphate from
CC the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and
CC by transferring the GMP moiety of GTP to the 5'-diphosphate terminus
CC via a covalent enzyme-GMP reaction intermediate.
CC {ECO:0000269|PubMed:9200605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC diphospho-ribonucleoside in mRNA + H(+) + phosphate;
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:0000269|PubMed:9200605};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005;
CC Evidence={ECO:0000305|PubMed:9200605};
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:0000269|PubMed:9200605};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000305|PubMed:9200605};
CC -!- ACTIVITY REGULATION: RNA triphosphatase activity is inhibited by
CC magnesium. {ECO:0000269|PubMed:9200605}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the non-receptor
CC class of the protein-tyrosine phosphatase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase
CC family. {ECO:0000305}.
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DR EMBL; Z75525; CAA99765.2; -; Genomic_DNA.
DR EMBL; AF003925; AAB61344.1; -; mRNA.
DR PIR; T18885; T18885.
DR RefSeq; NP_001020979.1; NM_001025808.4.
DR RefSeq; NP_001020980.1; NM_001025809.1.
DR AlphaFoldDB; Q17607; -.
DR SMR; Q17607; -.
DR STRING; 6239.C03D6.3a; -.
DR EPD; Q17607; -.
DR PaxDb; Q17607; -.
DR PeptideAtlas; Q17607; -.
DR EnsemblMetazoa; C03D6.3a.1; C03D6.3a.1; WBGene00000466.
DR GeneID; 172814; -.
DR KEGG; cel:CELE_C03D6.3; -.
DR UCSC; C03D6.3a; c. elegans.
DR CTD; 172814; -.
DR WormBase; C03D6.3a; CE32300; WBGene00000466; cel-1.
DR eggNOG; KOG2386; Eukaryota.
DR InParanoid; Q17607; -.
DR OMA; PAWENGP; -.
DR OrthoDB; 1544021at2759; -.
DR PhylomeDB; Q17607; -.
DR Reactome; R-CEL-72086; mRNA Capping.
DR Reactome; R-CEL-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:Q17607; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000466; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q17607; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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; IBA:GO_Central.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IDA:WormBase.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:WormBase.
DR GO; GO:0098507; P:polynucleotide 5' dephosphorylation; IDA:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR017074; mRNA_cap_enz_bifunc.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR PIRSF; PIRSF036958; mRNA_capping_HCE; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Protein phosphatase; Reference proteome; Transferase.
FT CHAIN 1..623
FT /note="mRNA-capping enzyme"
FT /id="PRO_0000210110"
FT DOMAIN 44..196
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 13..224
FT /note="TPase"
FT REGION 213..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..585
FT /note="GTase"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:9200605"
FT ACT_SITE 311
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 357..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 477..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 553..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MUTAGEN 136
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9200605"
SQ SEQUENCE 623 AA; 72129 MW; F1C78AB66465355B CRC64;
MATRGPTPDK ARMGLPDRWL HCPKTGTLIN NLFFPFKTPL CKMYDNQIAE RRYQFHPAEV
FSHPHLHGKK IGLWIDLTNT DRYYFREEVT EHECIYHKMK MAGRGVSPTQ EDTDNFIKLV
QEFHKKYPDR VVGVHCTHGF NRTGFLIAAY LFQVEEYGLD AAIGEFAENR QKGIYKQDYI
DDLFARYDPT EDDKILAPEK PDWEREMSIG MSTQIDNGRP STSQQIPATN GNNNQNGNQL
SGGGDNSKLF MDGLIRGVKV CEDEGKKSML QAKIKNLCKY NKQGFPGLQP VSLSRGNINL
LEQESYMVSW KADGMRYIIY INDGDVYAFD RDNEVFEIEN LDFVTKNGAP LMETLVDTEV
IIDKVEINGA MCDQPRMLIY DIMRFNSVNV MKEPFYKRFE IIKTEIIDMR TAAFKTGRLK
HENQIMSVRR KDFYDLEATA KLFGPKFVQH VGHEIDGLIF QPKKTKYETG RCDKVLKWKP
PSHNSVDFLL KVEKKCKEGM LPEWIGYLFV QNLSDPFGTM KATATLKKYH NKIIECTLLV
DNQGRPKEWK FMRERTDKSL PNGLRTAENV VETMVNPVTE TYLIEYVNHA LRVLKRAAAA
HRHHQIHQQQ LHEGEPEARR QKL
