Q6CWR0 (MCE1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-capping enzyme subunit alpha

Alternative name(s):
GTP--RNA guanylyltransferase
Short name=GTase
mRNA guanylyltransferase
EC=2.7.7.50

Gene names

Name:	CEG1
Ordered Locus Names:	KLLA0B02200g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate By similarity.
Catalytic activity	GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
Subunit structure	The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the eukaryotic GTase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Ligand	GTP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mRNA cap methyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA guanylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 466	466	mRNA-capping enzyme subunit alpha		PRO_0000210102
Sites
	Active site	67	1	N6-GMP-lysine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CWR0 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 7320E55CA86AA7B9	FASTA	466	53,980
	10 20 30 40 50 60 MDNNRVAPEI PGLRQPGQIT NDIRMLMCKL LNSAKPANTF PGSQPVSFHL ADIEEKLLAQ 70 80 90 100 110 120 DYYVCEKTDG LRALMLIMVN PVTKEQGCFM IDRENNYYMV NGFRFPCLPR ANKKELLETL 130 140 150 160 170 180 QDGTLIDGEL VMQTNPVTKL KELRYLMFDC LAVNGRSLVQ SPTSSRLAHL GKEFFKPYYD 190 200 210 220 230 240 LRSYFPDRCS TFPFKISMKH MNFSYDLAKV AKTLDSLPHV SDGLIFTPVQ AAYHIGGKDS 250 260 270 280 290 300 YLLKWKPEVE NTVDFKLIIE PPVVEDKSLP KSDKNRFYYN YDVKPLFHLY VWQGGNDVNN 310 320 330 340 350 360 RIQDFEQPFT KSDLELLERT YRKFAEIEID DKQWNELKAM EEPLNGRIVE CSKDQESGAW 370 380 390 400 410 420 KLLRFRDDKL NGNHVSVVQK VLESIGDSVS LDDLEQVVDE MRSRWKEREQ GLKNAQKQFN 430 440 450 460 HQASARSSLS QQHSTEPEQS QDQPKYVDDD DDNWSDDEPD TKRQKI

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382122 Genomic DNA. Translation: CAH02022.1.
RefSeq	XP_451629.1. XM_451629.1.
3D structure databases
ProteinModelPortal	Q6CWR0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CWR0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2897021.
GenomeReviews	Gene locus KLLA0B02200g in contig CR382122_GR.
KEGG	kla:KLLA0B02200g.
Phylogenomic databases
eggNOG	fuNOG04646.
HOGENOM	HBG330574.
OMA	GSQPVSF.
OrthoDB	EOG4RV611.
Family and domain databases
InterPro	IPR001339. mRNA_cap_enzyme. IPR013846. mRNA_cap_enzyme_C. IPR017075. mRNA_capping_enz_asu. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K00987.
Pfam	PF03919. mRNA_cap_C. 1 hit. PF01331. mRNA_cap_enzyme. 1 hit. [Graphical view]
PIRSF	PIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MCE1_KLULA

Accession

Primary (citable) accession number: Q6CWR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program