A2YB34 (TRMB_ORYSI) 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

ORF Names:

OsI_22311

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine tRNA-binding
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological_process	RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	tRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 259	259	tRNA (guanine-N(7)-)-methyltransferase		PRO_0000370581
Regions
	Region	103 – 104	2	S-adenosyl-L-methionine binding By similarity
	Region	136 – 137	2	S-adenosyl-L-methionine binding By similarity
	Region	234 – 236	3	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	159	1	By similarity
	Binding site	80	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	156	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2YB34 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 378AC5DAA0F9AAF9	FASTA	259	29,078
	10 20 30 40 50 60 MASGDGANGG GGGGQGKLPR KRFYRARAHS NPLSDSHFPI PISPDEVDLS QHYPRYFPSG 70 80 90 100 110 120 EGEARQGDAA VPRIRFADVG CGFGGLLVGL STLFPDTLMI GMELRDKVTE YVKERILALR 130 140 150 160 170 180 ASNPGKYDNI SVVRTNSMKY IPNYFRKAQL SKMFFLFPDP HFKEKNHRRR VISMQLLDEY 190 200 210 220 230 240 AYVMEVGGII YTITDVEELG EWMRSCLEKH PLFEAIPEEE TKADPVVKLL STATEEGQKV 250 ARNGGQTFQA IFRRISLQE

References

[1]

"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000131 Genomic DNA. Translation: EAZ00295.1.
3D structure databases
ProteinModelPortal	A2YB34.
ModBase	Search...
Protein-protein interaction databases
STRING	39947.LOC_Os06g12990.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
KEGG	dosa:Os06t0236900-01.
Organism-specific databases
Gramene	A2YB34.
Phylogenomic databases
eggNOG	COG0220.
HOGENOM	HOG000260965.
Enzyme and pathway databases
UniPathway	UPA00989.
Gene expression databases
ArrayExpress	A2YB34.
Family and domain databases
InterPro	IPR003358. tRNA_(Gua-N-7)_MeTrfase. IPR025763. tRNA_(Gua-N-7)_MeTrfase_euk. [Graphical view]
Pfam	PF02390. Methyltransf_4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00091. TIGR00091. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TRMB_ORYSI

Accession

Primary (citable) accession number: A2YB34

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	March 20, 2007
Last modified:	April 3, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program