3BT7

Structure of E. coli 5-Methyluridine Methyltransferase TrmA in complex with 19 nucleotide T-arm analogue

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0005829	cellular_component	cytosol
A	0006396	biological_process	RNA processing
A	0008033	biological_process	tRNA processing
A	0008168	molecular_function	methyltransferase activity
A	0008173	molecular_function	RNA methyltransferase activity
A	0019843	molecular_function	rRNA binding
A	0030488	biological_process	tRNA methylation
A	0030697	molecular_function	tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent
A	0032259	biological_process	methylation
A	0061818	biological_process	tRNA folding
B	0000049	molecular_function	tRNA binding
B	0005829	cellular_component	cytosol
B	0006396	biological_process	RNA processing
B	0008033	biological_process	tRNA processing
B	0008168	molecular_function	methyltransferase activity
B	0008173	molecular_function	RNA methyltransferase activity
B	0019843	molecular_function	rRNA binding
B	0030488	biological_process	tRNA methylation
B	0030697	molecular_function	tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent
B	0032259	biological_process	methylation
B	0061818	biological_process	tRNA folding

Functional Information from PROSITE/UniProt

site_id	PS01230
Number of Residues	30
Details	TRMA_1 RNA methyltransferase trmA family signature 1. DPPRsGldsetekmvqaypr.....ILYiSCNpeT

Chain	Residue	Details
A	ASP299-THR328

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000255\|HAMAP-Rule:MF_01011, ECO:0000269\|PubMed:18451029

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_01011, ECO:0000269\|PubMed:18451029

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01011