NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).

Comments

FUNCTION: Specifically methylates guanosine-37 in various tRNAs (By similarity).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N¹-methylguanine.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the RNA methyltransferase trmD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE015928; AAO76000.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_809806.1; -.

3D structure databases

ModBase

Q8A9C2.

Enzyme and pathway databases

BioCyc

BTHE226186:BT_0893-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0009019;	Molecular function: tRNA (guanine-N1-)-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006400;	Biological process: tRNA modification (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00605; -; 1.
PBIL [Tree]

InterPro

IPR016009; tRNA_m1G_MeTrfase.
IPR002649; tRNA_m1G_MeTrfase_bac.
Graphical view of domain structure.

Pfam

PF01746; tRNA_m1G_MT; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000386; tRNA_mtase; 1.

ProDom

PD004978; tRNA_m1G_mtfrase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00088; trmD; 1.

Genome annotation databases

GeneID

1073262; -.

GenomeReviews

AE015928_GR; BT_0893.

KEGG

bth:BT_0893; -.

NMPDR

fig|226186.1.peg.893; -.

Phylogenomic databases

HOGENOM

Q8A9C2; -.

Genome annotation databases

CMR

Q8A9C2; BT_0893.

Other

ProtoNet

Q8A9C2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase; tRNA processing.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 225`	`225`	`tRNA (guanine-N(1)-)-methyltransferase.`	`PRO_0000060330`
`REGION`	`132 137`	`6`	`S-adenosyl-L-methionine binding (By similarity).`
`BINDING`	`112 112`		`S-adenosyl-L-methionine; via amide nitrogen (By similarity).`

Sequence information

Length: 225 AA [This is the length of the unprocessed precursor]

Molecular weight: 25558 Da [This is the MW of the unprocessed precursor]

CRC64: 0B49CF62E2AC9E71 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRIDIITVLP EMIEGFFNCS IMKRAQNKGL AEIHIHNLRD YTEDKYRRVD DYPFGGFAGM 

        70         80         90        100        110        120 
VMKIEPIERC INALKAERDY DEVIFTTPDG EQFNQPMANS LSLAQNLIIL CGHFKGIDYR 

       130        140        150        160        170        180 
IREHLITKEI SIGDYVLTGG ELAAAVMADA IVRIIPGVIS DEQSALSDSF QDNLLAAPVY 

       190        200        210        220 
TRPADYKGWK VPDILLSGHE AKIKEWELQQ SLERTKKLRP DLLED

Q8A9C2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools