Reviewed, UniProtKB/Swiss-Prot P78587 (MCE1_CANAL)

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:

CGT1

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	449 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.
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	3D-structure
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_0000210099

Regions

Compositional bias

427 – 435

9

Poly-Gln

Sites

Active site

67

1

N6-GMP-lysine intermediate Potential

Secondary structure

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449

Helix Strand Turn

Details...

Beta strand

13 – 16

4

Helix

19 – 33

15

Beta strand

43 – 47

5

Helix

50 – 54

5

Helix

56 – 59

4

Beta strand

62 – 68

7

Beta strand

70 – 80

11

Turn

81 – 83

3

Beta strand

84 – 91

8

Beta strand

96 – 98

3

Beta strand

112 – 114

3

Beta strand

119 – 130

12

Beta strand

133 – 135

3

Beta strand

138 – 149

12

Helix

159 – 169

11

Helix

171 – 180

10

Helix

182 – 185

4

Beta strand

193 – 196

4

Helix

202 – 205

4

Helix

206 – 209

4

Helix

212 – 214

3

Beta strand

219 – 229

11

Beta strand

233 – 242

10

Helix

245 – 247

3

Beta strand

250 – 257

8

Beta strand

259 – 262

4

Beta strand

274 – 277

4

Beta strand

283 – 290

8

Beta strand

296 – 302

7

Helix

306 – 314

9

Beta strand

315 – 317

3

Beta strand

323 – 328

6

Beta strand

330 – 332

3

Beta strand

335 – 341

7

Helix

351 – 363

13

Helix

367 – 389

23

Sequences

	Sequence		Length	Mass (Da)
	P78587-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: D93F44BF112305BB	FASTA	449	52,253
	10 20 30 40 50 60 MIQLEEREIP VIPGNKLDEE ETKELRLMVA ELLGRRNTGF PGSQPVSFER RHLEETLMQK 70 80 90 100 110 120 DYFVCEKTDG LRCLLFLIND PDKGEGVFLV TRENDYYFIP NIHFPLSVNE TREKPTYHHG 130 140 150 160 170 180 TLLDGELVLE NRNVSEPVLR YVIFDALAIH GKCIIDRPLP KRLGYITENV MKPFDNFKKH 190 200 210 220 230 240 NPDIVNSPEF PFKVGFKTML TSYHADDVLS KMDKLFHASD GLIYTCAETP YVFGTDQTLL 250 260 270 280 290 300 KWKPAEENTV DFQLEFVFNE VQDPDLDERD PTSTYLDYDA KPNLIKLRVW QGSNVHTDFA 310 320 330 340 350 360 KLDLSDDDWE RLKALEQPLQ GRIAECRQST TKKGYWEMLR FRNDKSNGNH ISVVEKILVS 370 380 390 400 410 420 IKDGVKEKEV IEWCPKISRA WKKRENDRRQ KHFNGVARPA SVSHEEPLRK KIKTESNGNG 430 440 HQTPPRQEQQ QQSQQILNDI PTYEDSDDE

References

[1]	"Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans." Yamada-Okabe T., Shimmi O., Doi R., Mizumoto K., Arisawa M., Yamada-Okabe H. Microbiology 142:2515-2523(1996) [PubMed: 8828219] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10259 / CBS 5796 / IFO 1060 / JCM 2078.
[2]	"Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II." Fabrega C., Shen V., Shuman S., Lima C.D. Mol. Cell 11:1549-1561(2003) [PubMed: 12820968] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D83180 Genomic DNA. Translation: BAA11833.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P16	X-ray	2.70	A/B	3-395	[»]

ModBase

Search...

Phylogenomic databases

OMA

DGLIFTC.

Enzyme and pathway databases

BRENDA

2.7.7.50. 1124.

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_CANAL

Accession

Primary (citable) accession number: P78587

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	November 24, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)