Reviewed, UniProtKB/Swiss-Prot Q6C783 (MCE1_YARLI)

Names and origin

Protein names

Recommended name:
    mRNA-capping enzyme subunit alpha
Alternative name(s):
    mRNA guanylyltransferase
    EC=2.7.7.50
    GTP--RNA guanylyltransferase
      Short name=GTase

Gene names

Name:	CEG1
Ordered Locus Names:	YALI0E02904g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	391 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 protein binding 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 – 391	391	mRNA-capping enzyme subunit alpha		PRO_0000210105
Sites
	Active site	63	1	N6-GMP-lysine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6C783-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 69B7E0EA6957D9C3	FASTA	391	45,531
	10 20 30 40 50 60 MSGIVPEIPG EQAPPDAAHQ LKVDVARLLQ KPKLNFPGAQ PVSFARKHIE EELFKRDYYV 70 80 90 100 110 120 CEKSDGLRCL MYVTWENNPD TGPQQVTYLI TRNNEFFFIP MVHFPSNDGK PLQDTIVDGE 130 140 150 160 170 180 LVLTKAEPRS LHFLMFDCLA CNKILLTGRP LDKRLGYLNA AISHPLKEYL HKNPEVARDF 190 200 210 220 230 240 PFSVRVKDMQ FAYNVMNVFA SFPHLPHITD GLIFTCRDHP YVSGTDERIL KWKKQDENSV 250 260 270 280 290 300 DFLMTMKFPI FEDTNGESWT DYDAKPEITL LVWTGRDGSR PYGELYLTDE EWDNLKALEE 310 320 330 340 350 360 PLEERVVECI KDDKKRWRYL RFRDDKTNAN YITTVEKVID SIDDPVSEKN LLDAAPKIKE 370 380 390 LWKERNRRPR DEDRKRVGGD DHDHGAKRAR Q

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: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382131 Genomic DNA. Translation: CAG79058.1.
RefSeq	XP_503479.1.
3D structure databases
SMR	Q6C783. Positions 2-370.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6C783.
Genome annotation databases
GeneID	2912122.
GenomeReviews	Gene locus YALI0E02904g in contig CR382131_GR.
KEGG	yli:YALI0E02904g.
Phylogenomic databases
eggNOG	fuNOG04646.
HOGENOM	HBG330574.
OMA	DGLIFTC.
OrthoDB	EOG9MKPZT.
PhylomeDB	Q6C783.
Enzyme and pathway databases
BRENDA	2.7.7.50. 3602.
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.
Pfam	PF03919. mRNA_cap_C. 1 hit. PF01331. mRNA_cap_enzyme. 1 hit. [Graphical view]
PIRSF	PIRSF036959. mRNA_cap_alpha. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MCE1_YARLI

Accession

Primary (citable) accession number: Q6C783

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	August 16, 2004
Last modified:	January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)