Polynucleotide 5'-triphosphatase
     (EC 3.1.3.33)
     (mRNA 5'-triphosphatase)
     (TPase)
mRNA guanylyltransferase
     (EC 2.7.7.50)
     (GTP--RNA guanylyltransferase)
     (GTase)

Gene name

	Name:	cel-1
	ORFNames:	C03D6.3

From

Caenorhabditis elegans

[TaxID: 6239]

Taxonomy

Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 13-585. STRAIN=Bristol N2; Shuman S., Ho C.K.; "Identification of mRNA capping enzyme from C.elegans."; Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	CHARACTERIZATION, AND MUTAGENESIS OF CYS-136. DOI=10.1016/S0092-8674(00)80272-X; PubMed=9200605 [NCBI, ExPASy, EBI, Israel, Japan] Takagi T., Moore C.R., Diehn F., Buratowski S.; "An RNA 5'-triphosphatase related to the protein tyrosine phosphatases."; Cell 89:867-873(1997).

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 + H₂O = a polynucleotide + phosphate.
CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
SUBCELLULAR LOCATION: Nucleus (By similarity).
INDUCTION: Inhibited by magnesium.
SIMILARITY: In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.
SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z75525; CAA99765.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF003925; AAB61344.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T18885; T18885.

NP_001020979.1; -.

3D structure databases

HSSP

O55236; 1I9S. [HSSP ENTRY / PDB]

ModBase

Q17607.

Organism-specific databases

WormBase

WBGene00000466; cel-1.

WormPep

C03D6.3; CE32300. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

Q17607; -.

Ontologies

GO:0005622;	Cellular component: intracellular (traceable author statement from WormBase).
GO:0010171;	Biological process: body morphogenesis (inferred from mutant phenotype from WormBase).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0018996;	Biological process: molting cycle, collagen and cuticulin-based cuticle (inferred from mutant phenotype from WormBase).
GO:0002009;	Biological process: morphogenesis of an epithelium (inferred from mutant phenotype from WormBase).
GO:0002119;	Biological process: nematode larval development (inferred from mutant phenotype from WormBase).
GO:0040010;	Biological process: positive regulation of growth rate (inferred from mutant phenotype from WormBase).
GO:0040017;	Biological process: positive regulation of locomotion (inferred from mutant phenotype from WormBase).
GO:0000003;	Biological process: reproduction (inferred from mutant phenotype from WormBase).
QuickGo view.

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 of domain structure.

Pfam

PF00782; DSPc; 1.
PF03919; mRNA_cap_C; 1.
PF01331; mRNA_cap_enzyme; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036958; mRNA_capping_HCE; 1.

PROSITE

PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

C03D6.3; Caenorhabditis elegans. [Contig view]

GeneID

172814; -.

KEGG

cel:C03D6.3; -.

Other

NextBio

877107; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotidyltransferase; Nucleus; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 623`	`623`	`mRNA-capping enzyme.`	`PRO_0000210110`
`REGION`	`13 224`	`212`	`TPase.`
`REGION`	`241 585`	`345`	`GTase.`
`ACT_SITE`	`136 136`		`For RNA 5'-triphosphatase activity.`
`ACT_SITE`	`311 311`		`N6-GMP-lysine intermediate (By similarity).`
`MUTAGEN`	`136 136`		`C->A: Loss of activity.`
`MUTAGEN`	`136 136`		`C->S: Loss of activity.`

Sequence information

Length: 623 AA [This is the length of the unprocessed precursor]

Molecular weight: 72129 Da [This is the MW of the unprocessed precursor]

CRC64: F1C78AB66465355B [This is a checksum on the sequence]

        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

Q17607 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools