Reviewed, UniProtKB/Swiss-Prot P40997 (MCE1_SCHPO)

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
Synonyms:	pce1
ORF Names:	SPBC2F12.08c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [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
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 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)
	P40997-1 [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: ATCC 38366 / 972.

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.
3D structure databases
SMR	P40997. Positions 4-371.
ModBase	Search...
Protein-protein interaction databases
STRING	P40997.
Genome annotation databases
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.
HOGENOM	HBG330574.
OMA	DGLIFTC.
OrthoDB	EOG9MKPZT.
PhylomeDB	P40997.
Enzyme and pathway databases
BRENDA	2.7.7.50. 653.
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.
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_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:	January 19, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)