Q6BT58 (MCE1_DEBHA) 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:	DEHA2D03322g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	458 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 – 458	458	mRNA-capping enzyme subunit alpha		PRO_0000210101
Sites
	Active site	67	1	N6-GMP-lysine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BT58 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: CC0BB8061AF0739A	FASTA	458	53,123
	10 20 30 40 50 60 MIQLEERDMP EIPGTILDRN ETQELRLMVA DLLGRRNPSF PGAQPISFER YHLNDTLMNK 70 80 90 100 110 120 DYYVCEKSDG LRCLLFIINH PERGEGVFLI TRENDYYYIP NIHFPLTNNE EKGKTYHHGT 130 140 150 160 170 180 LLDGELVLET KNVPEPVLRF CIFDALAING KDITKRHLPK RLGYITEQVM KPFDNFKRKN 190 200 210 220 230 240 PEIVNAPDFP FKVSFKLMTS SYHADDVLSK MDQLFHESDG LIFTCAETPY VFGTDSTLLK 250 260 270 280 290 300 WKPAHENTVD YKMEMIFKKF QDPDLDPRDP DSTYTDYDSK PELIKLRVWK GGADYEDFTK 310 320 330 340 350 360 LSLENEDWEK LKNLRQPLQG RIVECRKKLS DPGFWEMLRF RNDKSNGNHI SVVDKILHSI 370 380 390 400 410 420 QDGVSEEELI EACPKIGKAW KKRIYEKSQG SRSSYSETGR SHPEPNREDE PASKRTKIDM 430 440 450 EEPEPNGFGG STTNHQNASK QNSGEFQDIP TYEDSDDE

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 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382136 Genomic DNA. Translation: CAG86747.2.
RefSeq	XP_458612.2. XM_458612.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BT58.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2901066.
GenomeReviews	Gene locus DEHA2D03322g in contig CR382136_GR.
KEGG	dha:DEHA2D03322g.
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_DEBHA

Accession

Primary (citable) accession number: Q6BT58

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	December 16, 2008
Last modified:	November 16, 2011
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program