A5HZ44 (TRMB_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA (guanine-N(7)-)-methyltransferase
EC=2.1.1.33

Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase

Gene names

Name:	trmB
Ordered Locus Names:	CBO0499, CLC_0573

Organism

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]

Taxonomic identifier

441771 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium botulinum › Clostridium botulinum A

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_01057
Catalytic activity	S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_01057
Pathway	tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057
Sequence similarities	Belongs to the methyltransferase superfamily. TrmB family.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC
Molecular_function	tRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 217	217	tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057		PRO_1000136346
Regions
	Region	129 – 134	6	Interaction with RNA Potential
	Region	196 – 199	4	Substrate binding Potential
Sites
	Binding site	43	1	S-adenosyl-L-methionine By similarity
	Binding site	68	1	S-adenosyl-L-methionine By similarity
	Binding site	101	1	S-adenosyl-L-methionine By similarity
	Binding site	123	1	S-adenosyl-L-methionine By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	159	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	A5HZ44 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: C9CEDFA575906AD2	FASTA	217	26,259
	10 20 30 40 50 60 MRLRKKWWAR PEIEASDKFA EEPKELRGKW NKEFNNNNDI HLELGCGRGG FISQLVEKNK 70 80 90 100 110 120 DINYVGIDLK DEVIVYAIRK VKEKEEEVKR EFKNIKFVTM NIMGIAEVFD KNEISKIYIN 130 140 150 160 170 180 FCNPWPKERH NKRRLTHTKL LTEYKKFLKP NTEIWFKTDD KELFEDSQEY FKESGFNIEY 190 200 210 ITYDLHNSDF KENIKTEYET KFETMGMKIM FLKARLL

References

[1]

"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes." Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J. Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

[2]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000727 Genomic DNA. Translation: ABS38078.1. AM412317 Genomic DNA. Translation: CAL82053.1.
RefSeq	YP_001253043.1. NC_009495.1. YP_001386456.1. NC_009698.1.
3D structure databases
ProteinModelPortal	A5HZ44.
ModBase	Search...
Protein-protein interaction databases
STRING	413999.CBO0499.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS38078; ABS38078; CLC_0573.
GeneID	5184754. 5399680.
KEGG	cbh:CLC_0573. cbo:CBO0499.
PATRIC	19363117. VBICloBot22612_0502.
Phylogenomic databases
eggNOG	COG0220.
HOGENOM	HOG000251689.
KO	K03439.
OMA	RLRNKPW.
ProtClustDB	PRK00121.
Enzyme and pathway databases
BioCyc	CBOT413999:GJ72-562-MONOMER. CBOT441771:GIWX-545-MONOMER.
UniPathway	UPA00989.
Family and domain databases
HAMAP	MF_01057. tRNA_methyltr_TrmB.
InterPro	IPR003358. tRNA_(Gua-N-7)_MeTrfase. [Graphical view]
Pfam	PF02390. Methyltransf_4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00091. TIGR00091. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TRMB_CLOBH

Accession

Primary (citable) accession number: A5HZ44
Secondary accession number(s): A7G137

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	June 26, 2007
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program