Reviewed, UniProtKB/Swiss-Prot Q6FQ31 (MCE1_CANGA)

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:	CAGL0I09570g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 – 449	449	mRNA-capping enzyme subunit alpha		PRO_0000210100
Sites
	Active site	66	1	N6-GMP-lysine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FQ31-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 5537EF3CF6F56E7D	FASTA	449	51,664
	10 20 30 40 50 60 MDARISPEIP GIIQPGNVTQ DLKMLVCKLL NSPKPSKTFP GSQPVSFQHS DIRDKLVAQD 70 80 90 100 110 120 YYVCEKTDGL RVLMLVVVNP ITGEQGCFMI DRENNYYLVN GFHFPRLPQK KKEELLETSQ 130 140 150 160 170 180 NGTLIDGELV IQKNPMTKLQ ELRYLMFDCL AINGRSLVQS PTSSRLAHLG KEFYKPYYDL 190 200 210 220 230 240 RSIYPDKCAT FPFKLSMKHM DFSYSLVKVA NSLDKLPHLS DGLIFTPVRT PYAVGGKDSL 250 260 270 280 290 300 LLKWKPEQEN SVDFKLILEI PMTEDNSVAK KDPRRWYYNY DAKPTFALYV WQGGSDVNTK 310 320 330 340 350 360 LQNFEQPFDK REMQVLEKTY KRFAELSISD EQWQELKNLE EPLNGRIVEC TKDPETGSWT 370 380 390 400 410 420 MLRFRDDKLN GNHTSVVQKV LESISDSVTI DDLAESVPEI KSAWDERKNG AYQHHSSSFS 430 440 ESRQQPKAEP VAEKKQTEPK YVDDDDWSD

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 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380955 Genomic DNA. Translation: CAG60600.1.
RefSeq	XP_447663.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FQ31.
Genome annotation databases
GeneID	2888936.
GenomeReviews	Gene locus CAGL0I09570g in contig CR380955_GR.
KEGG	cgr:CAGL0I09570g.
Phylogenomic databases
HOGENOM	Q6FQ31.
OMA	DGLIFTC.
Enzyme and pathway databases
BRENDA	2.7.7.50. 189220.
Family and domain databases
InterPro	IPR001339. mRNA_cap_enzyme. IPR013846. mRNA_cap_enzyme_C. IPR017075. mRNA_capping_enz_asu. IPR012340. NA-bd_OB-fold. [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_CANGA

Accession

Primary (citable) accession number: Q6FQ31

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)