Reviewed, UniProtKB/Swiss-Prot Q17607 (MCE1_CAEEL)

Names and origin

Protein names

Recommended name:
    mRNA-capping enzyme
Including the following 2 domains:
    1- Recommended name:
            Polynucleotide 5'-triphosphatase
              EC=3.1.3.33
        Alternative name(s):
            mRNA 5'-triphosphatase
              Short name=TPase
    2- Recommended name:
            mRNA guanylyltransferase
              EC=2.7.7.50
        Alternative name(s):
            GTP--RNA guanylyltransferase
              Short name=GTase

Gene names

Name:	cel-1
ORF Names:	C03D6.3

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.
Catalytic activity	A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
Subcellular location	NucleusBy similarity.
Induction	Inhibited by magnesium.
Sequence similarities	In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family. In the C-terminal section; belongs to the eukaryotic GTase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Molecular function	Hydrolase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	body morphogenesis Inferred from mutant phenotype. Source: WormBase embryonic development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase mRNA capping Inferred from electronic annotation. Source: InterPro molting cycle, collagen and cuticulin-based cuticle Inferred from mutant phenotype. Source: WormBase morphogenesis of an epithelium Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase positive regulation of growth rate Inferred from mutant phenotype. Source: WormBase positive regulation of locomotion Inferred from mutant phenotype. Source: WormBase protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro reproduction Inferred from mutant phenotype. Source: WormBase
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	mRNA guanylyltransferase activity Inferred from electronic annotation. Source: InterPro polynucleotide 5'-phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 623	623	mRNA-capping enzyme		PRO_0000210110
Regions
	Region	13 – 224	212	TPase
	Region	241 – 585	345	GTase
Sites
	Active site	136	1	For RNA 5'-triphosphatase activity
	Active site	311	1	N6-GMP-lysine intermediate By similarity
Experimental info
	Mutagenesis	136	1	C → A: Loss of activity
	Mutagenesis	136	1	C → S: Loss of activity

Sequences

	Sequence		Length	Mass (Da)
	Q17607-1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: F1C78AB66465355B	FASTA	623	72,129
	10 20 30 40 50 60 MATRGPTPDK ARMGLPDRWL HCPKTGTLIN NLFFPFKTPL CKMYDNQIAE RRYQFHPAEV 70 80 90 100 110 120 FSHPHLHGKK IGLWIDLTNT DRYYFREEVT EHECIYHKMK MAGRGVSPTQ EDTDNFIKLV 130 140 150 160 170 180 QEFHKKYPDR VVGVHCTHGF NRTGFLIAAY LFQVEEYGLD AAIGEFAENR QKGIYKQDYI 190 200 210 220 230 240 DDLFARYDPT EDDKILAPEK PDWEREMSIG MSTQIDNGRP STSQQIPATN GNNNQNGNQL 250 260 270 280 290 300 SGGGDNSKLF MDGLIRGVKV CEDEGKKSML QAKIKNLCKY NKQGFPGLQP VSLSRGNINL 310 320 330 340 350 360 LEQESYMVSW KADGMRYIIY INDGDVYAFD RDNEVFEIEN LDFVTKNGAP LMETLVDTEV 370 380 390 400 410 420 IIDKVEINGA MCDQPRMLIY DIMRFNSVNV MKEPFYKRFE IIKTEIIDMR TAAFKTGRLK 430 440 450 460 470 480 HENQIMSVRR KDFYDLEATA KLFGPKFVQH VGHEIDGLIF QPKKTKYETG RCDKVLKWKP 490 500 510 520 530 540 PSHNSVDFLL KVEKKCKEGM LPEWIGYLFV QNLSDPFGTM KATATLKKYH NKIIECTLLV 550 560 570 580 590 600 DNQGRPKEWK FMRERTDKSL PNGLRTAENV VETMVNPVTE TYLIEYVNHA LRVLKRAAAA 610 620 HRHHQIHQQQ LHEGEPEARR QKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"Identification of mRNA capping enzyme from C.elegans." Shuman S., Ho C.K. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-585. Strain: Bristol N2.
[3]	"An RNA 5'-triphosphatase related to the protein tyrosine phosphatases." Takagi T., Moore C.R., Diehn F., Buratowski S. Cell 89:867-873(1997) [PubMed: 9200605] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-136.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z75525 Genomic DNA. Translation: CAA99765.2. AF003925 mRNA. Translation: AAB61344.1.
PIR	T18885.
RefSeq	NP_001020979.1.
UniGene	Cel.8014
3D structure databases
HSSP	HSSP built from PDB template 1I9S based on UniProtKB O55236.
ModBase	Search...
Genome annotation databases
Ensembl	C03D6.3. Caenorhabditis elegans. [Contig view]
GeneID	172814.
KEGG	cel:C03D6.3.
Organism-specific databases
WormBase	WBGene00000466. cel-1.
WormPep	C03D6.3. CE32300. [WorfDB]
Gene expression databases
ArrayExpress	Q17607.
Family and domain databases
InterPro	IPR017074. mRNA_cap_enz_bifunc. IPR001339. mRNA_cap_enzyme. IPR013846. mRNA_cap_enzyme_C. IPR000387. Tyr_Pase. IPR016130. Tyr_Pase_AS. IPR000340. Tyr_Pase_dual_specific. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. PF03919. mRNA_cap_C. 1 hit. PF01331. mRNA_cap_enzyme. 1 hit. [Graphical view]
PIRSF	PIRSF036958. mRNA_capping_HCE. 1 hit.
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	877107.

Entry information

Entry name

MCE1_CAEEL

Accession

Primary (citable) accession number: Q17607
Secondary accession number(s): O02558

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 16, 2003
Last modified:	November 25, 2008
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project