Q9J584 (MCEL_FOWPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-capping enzyme catalytic subunit

Alternative name(s):
Virus termination factor large subunit
Short name=VTF large subunit
mRNA-capping enzyme 97 kDa subunit
mRNA-capping enzyme large subunit

Including the following 3 domains:

1. Polynucleotide 5'-triphosphatase
   EC=3.1.3.33
   Alternative name(s):
   mRNA 5'-triphosphatase
   Short name=TPase
2. mRNA guanylyltransferase
   EC=2.7.7.50
   Alternative name(s):
   GTP--RNA guanylyltransferase
   Short name=GTase
3. mRNA (guanine-N(7)-)-methyltransferase
   EC=2.1.1.56
   Alternative name(s):
   mRNA cap methyltransferase

Gene names

Ordered Locus Names:

FPV146

Organism

Fowlpox virus (strain NVSL) (FPV)

Taxonomic identifier

928301 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Avipoxvirus

Virus host

Vertebrata [TaxID: 7742]

Protein attributes

Sequence length	851 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the polymerase associated VP39 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure) By similarity. The heterodimeric enzyme is also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA By similarity.
Catalytic activity	A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
Subunit structure	Heterodimer of a catalytic and a regulatory subunit. Intrinsic methyltransferase activity of the catalytic subunit is weak and needs to be stimulated 30- to 50-fold by the regulatory subunit, which is itself catalytically inert By similarity.
Subcellular location	Virion Probable. Note: All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome.
Domain	The N-terminus contains the triphosphatase and guanylyltransferase domains, whereas the C-terminus contains the methyltransferase domain. The N-terminus is involved in binding to the temination motif 5'-UUUUUNU-3' in the nascent mRNA By similarity.
Sequence similarities	Belongs to the viral GTase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Virion
Ligand	Metal-binding S-adenosyl-L-methionine
Molecular function	Hydrolase Methyltransferase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	mRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC mRNA guanylyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide 5'-phosphatase 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 – 851	851	mRNA-capping enzyme catalytic subunit		PRO_0000210130
Regions
	Region	1 – 544	544	Triphosphatase-guanylyltransferase By similarity
	Region	545 – 850	306	Methyltransferase By similarity
Sites
	Active site	266	1	N6-GMP-lysine intermediate By similarity
	Metal binding	38	1	Catalytic; for RNA triphosphatase activity Potential
	Metal binding	40	1	Catalytic; for RNA triphosphatase activity Potential
	Metal binding	199	1	Catalytic; for RNA triphosphatase activity Potential
	Metal binding	201	1	Catalytic; for RNA triphosphatase activity Potential
	Site	80	1	Essential for RNA triphosphatase activity By similarity
	Site	110	1	Essential for RNA triphosphatase activity By similarity
	Site	131	1	Essential for RNA triphosphatase activity By similarity
	Site	164	1	Essential for RNA triphosphatase activity By similarity
	Site	166	1	Essential for RNA triphosphatase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9J584 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: DC3607ADD634BA7A	FASTA	851	98,888
	10 20 30 40 50 60 MDKYISKTPL SCYFEELVDT FISVVNSINK VDESKHHEVE LILFKPPIIT LTNLYNMATT 70 80 90 100 110 120 TESYIEFTML PVDKPNTKFR NRIPLSKIHG LDVKNNQLVE SLDGFIWEEK SLLLKKDISD 130 140 150 160 170 180 NSSAIIKYSI EEKTLFVDYK RRNASIKLEL VSVVRAKLRN IVIDFKMKYF LGSGAQSANS 190 200 210 220 230 240 SSLLCALNHP KNKPSLYIEF EIMMQDKNIS KKKLLEELNM SASALFLSHP KYIRLCPSIN 250 260 270 280 290 300 PILRTHLLKK QDIININTDD LYITSKTDGI FSHVYIEKKS IFCYFSHLGY IKEYTASREI 310 320 330 340 350 360 EETIYLYAEM RKEESILYLT VIKVLKPCME DRLSELAFVK NHLTGIHDRL VFVTKCYDGP 370 380 390 400 410 420 FESSSDLVVS IEEMLKTEQE GIILFYSKGE DSTTDYKVKK DNTIDQCVNV IYRYMSSEPI 430 440 450 460 470 480 VFNDKGSFLE YKRYSNDKGF PKEFSTGKLD LNGSVEYINN IYCIEIKHLN PCTGITNLVL 490 500 510 520 530 540 PIKFIAEFSH NDELIQPRID KTMKYLYESG YYGNQLSVIM DHLNDQKLRI GDVFEEEKLA 550 560 570 580 590 600 DIAAHMKLKD SMRLNPDGNY FLSNRVRGAL GILSNFVKTL LISLYCSKTY LDNHSKRKVL 610 620 630 640 650 660 AIDFGNGADL EKYFYGEIAL MVATDPDDNA IETGKKRYNE RNAGDKSKYY KFNYIKETIR 670 680 690 700 710 720 SETYVSSIRQ VLYFEKFSLV DWQFAIHYSF HPKHYSTIMT NLQELTESGC KVLITTMDGD 730 740 750 760 770 780 YLDTLKEKKK FIIRKLLPET ENYLSIEKID DDKVLVYNPS SMSKPMAEYI VRRDTLIRVF 790 800 810 820 830 840 REYKFKLIDS CNFKTIIDRN ISFINGVSRL ESRGSTKNFF ELNRKALEEC NDTDVLELLS 850 HYMVYVFSKE V

References

[1]	"The genome of fowlpox virus." Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L. J. Virol. 74:3815-3831(2000) [PubMed: 10729156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF198100 Genomic DNA. Translation: AAF44490.1.
RefSeq	NP_039109.1. NC_002188.1.
3D structure databases
ProteinModelPortal	Q9J584.
SMR	Q9J584. Positions 550-849.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1486694.
Phylogenomic databases
ProtClustDB	CLSP2509789.
Family and domain databases
InterPro	IPR019602. mRNA_cap_ATPase/GuylTrfase_vir. IPR004971. Pox_MCEL. [Graphical view]
Pfam	PF10640. Pox_ATPase-GT. 1 hit. PF03291. Pox_MCEL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MCEL_FOWPN

Accession

Primary (citable) accession number: Q9J584

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program