P40997 (MCE1_SCHPO) 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
Synonyms:	pce1
ORF Names:	SPBC2F12.08c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
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 Reference proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	mRNA cap methyltransferase complex Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA guanylyltransferase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe protein binding Inferred from physical interaction. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 402	402	mRNA-capping enzyme subunit alpha		PRO_0000210104
Sites
	Active site	67	1	N6-GMP-lysine intermediate By similarity
Experimental info
	Mutagenesis	67	1	K → A: Loss of function.

Sequences

	Sequence		Length	Mass (Da)
	P40997 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 76B1E2052DABB974	FASTA	402	46,875
	10 20 30 40 50 60 MAPSEKDIEE VSVPGVLAPR DDVRVLKTRI AKLLGTSPDT FPGSQPVSFS KKHLQALKEK 70 80 90 100 110 120 NYFVCEKSDG IRCLLYMTEH PRYENRPSVY LFDRKMNFYH VEKIFYPVEN DKSGKKYHVD 130 140 150 160 170 180 TLLDGELVLD IYPGGKKQLR YLVFDCLACD GIVYMSRLLD KRLGIFAKSI QKPLDEYTKT 190 200 210 220 230 240 HMRETAIFPF LTSLKKMELG HGILKLFNEV IPRLRHGNDG LIFTCTETPY VSGTDQSLLK 250 260 270 280 290 300 WKPKEMNTID FMLKLEFAQP EEGDIDYSAM PEFQLGVWEG RNMYSFFAFM YVDEKEWEKL 310 320 330 340 350 360 KSFNVPLSER IVECYLDDEN RWRFLRFRDD KRDANHISTV KSVLQSIEDG VSKEDLLKEM 370 380 390 400 PIIREAYYNR KKPSVTKRKL DETSNDDAPA IKKVAKESEK EI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases." Shuman S., Liu Y., Schwer B. Proc. Natl. Acad. Sci. U.S.A. 91:12046-12050(1994) [PubMed: 7991582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Fresco L.D., Woo S., Buratowski S. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U16143 Genomic DNA. Translation: AAA64996.1. U18811 Genomic DNA. Translation: AAA58715.1. CU329671 Genomic DNA. Translation: CAB10156.1.
PIR	T40133.
RefSeq	NP_595708.1. NM_001021605.1.
3D structure databases
ProteinModelPortal	P40997.
ModBase	Search...
Protein-protein interaction databases
STRING	P40997.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC2F12.08c.1; SPBC2F12.08c.1:pep; SPBC2F12.08c.
GeneID	2540362.
GenomeReviews	Gene locus ceg1 in contig CU329671_GR.
KEGG	spo:SPBC2F12.08c.
NMPDR	fig|4896.1.peg.1574.
Organism-specific databases
GeneDB_Spombe	SPBC2F12.08c.
Phylogenomic databases
eggNOG	fuNOG04646.
GeneTree	EFGT00050000001354.
HOGENOM	HBG330574.
OMA	GSQPVSF.
OrthoDB	EOG4RV611.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003793-MONOMER.
Gene expression databases
ArrayExpress	P40997.
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_SCHPO

Accession

Primary (citable) accession number: P40997

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program