Q84424 (MCE_PBCV1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-capping enzyme

Alternative name(s):
GTP--RNA guanylyltransferase
mRNA guanylyltransferase
EC=2.7.7.50

Gene names

Ordered Locus Names:

A103R

Organism

Paramecium bursaria Chlorella virus 1 (PBCV-1)

Taxonomic identifier

10506 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Phycodnaviridae › Chlorovirus

Virus host

Chlorella [TaxID: 114049]

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	mRNA capping. Transfers a GMP cap onto the end of mRNA that terminates with a 5'-diphosphate tail.
Catalytic activity	GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
Cofactor	Magnesium or manganese.
Subunit structure	Monomer.
Sequence similarities	Belongs to the eukaryotic GTase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Ligand	GTP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW
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 – 330

330

mRNA-capping enzyme

PRO_0000210107

Sites

Active site

82

1

N6-GMP-lysine intermediate

Secondary structure

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330

Helix Strand Turn

Details...

Beta strand

14 – 21

8

Beta strand

24 – 31

8

Helix

33 – 46

14

Beta strand

57 – 63

7

Helix

66 – 68

3

Helix

69 – 74

6

Beta strand

77 – 83

7

Beta strand

85 – 95

11

Beta strand

98 – 104

7

Beta strand

110 – 112

3

Helix

122 – 124

3

Beta strand

126 – 135

10

Turn

136 – 139

4

Beta strand

140 – 151

12

Helix

161 – 172

12

Beta strand

181 – 187

7

Helix

196 – 209

14

Beta strand

212 – 222

11

Beta strand

227 – 235

9

Beta strand

243 – 247

5

Beta strand

254 – 257

4

Turn

259 – 261

3

Beta strand

264 – 266

3

Beta strand

279 – 285

7

Beta strand

288 – 294

7

Helix

304 – 316

13

Helix

320 – 323

4

Sequences

	Sequence		Length	Mass (Da)
	Q84424 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6AF8A404710812D9	FASTA	330	37,832
	10 20 30 40 50 60 MVPPTINTGK NITTERAVLT LNGLQIKLHK VVGESRDDIV AKMKDLAMDD HKFPRLPGPN 70 80 90 100 110 120 PVSIERKDFE KLKQNKYVVS EKTDGIRFMM FFTRVFGFKV CTIIDRAMTV YLLPFKNIPR 130 140 150 160 170 180 VLFQGSIFDG ELCVDIVEKK FAFVLFDAVV VSGVTVSQMD LASRFFAMKR SLKEFKNVPE 190 200 210 220 230 240 DPAILRYKEW IPLEHPTIIK DHLKKANAIY HTDGLIIMSV DEPVIYGRNF NLFKLKPGTH 250 260 270 280 290 300 HTIDFIIMSE DGTIGIFDPN LRKNVPVGKL DGYYNKGSIV ECGFADGTWK YIQGRSDKNQ 310 320 330 ANDRLTYEKT LLNIEENITI DELLDLFKWE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of 43 kb of the Chlorella virus PBCV-1 330-kb genome: map positions 45 to 88." Li Y., Lu Z., Burbank D.E., Kutish G.F., Rock D.L., Etten J.L. Virology 212:134-150(1995) [PubMed: 7676624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes." Haakansson K., Doherty A.J., Shuman S., Wigley D.B. Cell 89:545-553(1997) [PubMed: 9160746] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[3]	"Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping." Haakansson K., Wigley D.B. Proc. Natl. Acad. Sci. U.S.A. 95:1505-1510(1998) [PubMed: 9465045] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 11-327.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

JF411744 Genomic DNA. Translation: AAC96471.1.

PIR

T17593.

RefSeq

NP_048451.1. NC_000852.5.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CKM	X-ray	2.50	A/B	1-330	[»]
1CKN	X-ray	2.50	A/B	1-330	[»]
1CKO	X-ray	3.10	A	1-330	[»]

ProteinModelPortal

Q84424.

SMR

Q84424. Positions 11-327.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

918242.

Phylogenomic databases

ProtClustDB

CLSP2510470.

Family and domain databases

InterPro

IPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
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]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MCE_PBCV1

Accession

Primary (citable) accession number: Q84424

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	October 19, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program