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 16-JUN-2009, entry version 77. DE RecName: Full=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; GN Name=cel-1; ORFNames=C03D6.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; 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 RT investigating 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 CHARACTERIZATION, AND MUTAGENESIS OF CYS-136. RX MEDLINE=97344078; 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 RT phosphatases."; RL Cell 89:867-873(1997). CC -!- FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'- CC triphosphatase 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 CC from the 5'-triphosphate end of nascent mRNA to yield a CC diphosphate end, and by transferring the gmp moiety of GTP to the CC 5'-diphosphate terminus. CC -!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a CC polynucleotide + phosphate. CC -!- CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate + CC G(5')ppp-Pur-mRNA. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- INDUCTION: Inhibited by magnesium. CC -!- SIMILARITY: In the N-terminal section; belongs to the non-receptor CC class of the protein-tyrosine phosphatase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic CC GTase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z75525; CAA99765.2; -; Genomic_DNA. DR EMBL; AF003925; AAB61344.1; -; mRNA. DR PIR; T18885; T18885. DR RefSeq; NP_001020979.1; -. DR UniGene; Cel.8014; -. DR HSSP; O55236; 1I9S. DR PRIDE; Q17607; -. DR Ensembl; C03D6.3; Caenorhabditis elegans. DR GeneID; 172814; -. DR KEGG; cel:C03D6.3; -. DR WormBase; WBGene00000466; cel-1. DR WormPep; C03D6.3; CE32300. DR OMA; Q17607; FFDIHAS. DR BRENDA; 2.7.7.50; 672. DR BRENDA; 3.1.3.33; 672. DR NextBio; 877107; -. DR ArrayExpress; Q17607; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:EC. DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:EC. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphata...; IEA:InterPro. DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0040007; P:growth; IMP:WormBase. DR GO; GO:0040011; P:locomotion; IMP:WormBase. DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based...; IMP:WormBase. DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase. DR GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro. DR GO; GO:0000003; P:reproduction; IMP:WormBase. DR InterPro; IPR017074; mRNA_cap_enz_bifunc. DR InterPro; IPR001339; mRNA_cap_enzyme. DR InterPro; IPR013846; mRNA_cap_enzyme_C. DR InterPro; IPR000387; Tyr_Pase. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000340; Tyr_Pase_dual_specific. 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 PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. PE 1: Evidence at protein level; KW Complete proteome; GTP-binding; Hydrolase; mRNA capping; KW mRNA processing; Multifunctional enzyme; Nucleotide-binding; KW Nucleotidyltransferase; Nucleus; Transferase. FT CHAIN 1 623 mRNA-capping enzyme. FT /FTId=PRO_0000210110. FT REGION 13 224 TPase. FT REGION 241 585 GTase. FT ACT_SITE 136 136 For RNA 5'-triphosphatase activity. FT ACT_SITE 311 311 N6-GMP-lysine intermediate (By FT similarity). FT MUTAGEN 136 136 C->A: Loss of activity. FT MUTAGEN 136 136 C->S: Loss of activity. 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 //