A6SMI7 (A6SMI7_BOTFB) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
mRNA-capping enzyme subunit alpha PIRNR PIRNR036959
EC=2.7.7.50 PIRNR PIRNR036959

Alternative name(s):
GTP--RNA guanylyltransferase PIRNR PIRNR036959
mRNA guanylyltransferase PIRNR PIRNR036959

Gene names

ORF Names:

BC1G_14137 EMBL EDN20267.1

Organism

Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) [Complete proteome]

Taxonomic identifier

332648 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. PIRNR PIRNR036959
Catalytic activity	GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. PIRNR PIRNR036959
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. PIRNR PIRNR036959
Subcellular location	Nucleus By similarity PIRNR PIRNR036959.
Sequence similarities	Belongs to the eukaryotic GTase family. PIRNR PIRNR036959

Ontologies

Keywords
Biological process	mRNA capping PIRNR PIRNR036959 mRNA processing
Cellular component	Nucleus PIRNR PIRNR036959
Ligand	GTP-binding PIRNR PIRNR036959 Nucleotide-binding
Molecular function	Nucleotidyltransferase PIRNR PIRNR036959 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
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A6SMI7 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: EE53C25B8C1930A6	FASTA	389	45,426
	10 20 30 40 50 60 MSGPVHDIQA PGIQAQGEIL FHMRREVAQL LNRSNPSFPG AQPVSFTRRH LDELTRQDYY 70 80 90 100 110 120 VCEKSDGFRY LLYLTDDEAH EECHYLIDRR NDYWYVPKGS LHFPIPRDIE GFHRKTLIDG 130 140 150 160 170 180 ELVMDKTPNG MQPKFLVFDC MVLDGNSLMN RTLDKRLAYF SERIFSPYQD LLRNFPQEIP 190 200 210 220 230 240 YFHFLMELKR MEFGYAMEMM FRQTLPNLPH GNDGLIFTCR SSEYKHGTDQ NILKWKPENE 250 260 270 280 290 300 NSIDFKLGLD FPTVEPDAMD LAEGNTEPYI DYDAIPVCNL SVNAGNGKDE WYGTMHLEPE 310 320 330 340 350 360 EWEKLKELNE PLNDRIVECY MDDKKRWRYM KFRDDKEVAN HTSTVESVIE SIRDRVTEKD 370 380 LIAAAPRIRD AWKRRDAEKK AAAAAAAAA

References

[1]

"Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea." Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E. , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M. PLoS Genet. 7:E1002230-E1002230(2011) [PubMed: 21876677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B05.10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476972 Genomic DNA. Translation: EDN20267.1.
RefSeq	XP_001547510.1. XM_001547460.1.
3D structure databases
ProteinModelPortal	A6SMI7.
ModBase	Search...
Protein-protein interaction databases
STRING	A6SMI7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5427988.
KEGG	bfu:BC1G_14137.
Phylogenomic databases
OMA	GSQPVSF.
OrthoDB	EOG4RV611.
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

A6SMI7_BOTFB

Accession

Primary (citable) accession number: A6SMI7

Entry history

Integrated into UniProtKB/TrEMBL:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)