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8Y2O

The Cryo-EM structure of human tRNA methyltransferase FTSJ1-THADA with substrate tRNA and S-adenosyl homocysteine (SAH)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002128biological_processtRNA nucleoside ribose methylation
A0005515molecular_functionprotein binding
A0008033biological_processtRNA processing
A0030234molecular_functionenzyme regulator activity
A0030488biological_processtRNA methylation
A0032471biological_processnegative regulation of endoplasmic reticulum calcium ion concentration
A0055088biological_processlipid homeostasis
A0098554cellular_componentcytoplasmic side of endoplasmic reticulum membrane
A1990845biological_processadaptive thermogenesis
B0001510biological_processRNA methylation
B0002128biological_processtRNA nucleoside ribose methylation
B0002130biological_processwobble position ribose methylation
B0002181biological_processcytoplasmic translation
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008168molecular_functionmethyltransferase activity
B0008175molecular_functiontRNA methyltransferase activity
B0016423molecular_functiontRNA (guanine) methyltransferase activity
B0016740molecular_functiontransferase activity
B0022008biological_processneurogenesis
B0030488biological_processtRNA methylation
B0032259biological_processmethylation
B0106050molecular_functiontRNA 2'-O-methyltransferase activity
B0106339molecular_functiontRNA (cytidine(32)-2'-O)-methyltransferase activity
B0106340molecular_functiontRNA (guanosine(34)-2'-O)-methyltransferase activity
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PROSITE/UniProt
site_idPS01005
Number of Residues10
DetailsFORMATE_NITRITE_TP_1 Formate and nitrite transporters signature 1. IIsGSELITG
ChainResidueDetails
AILE1493-GLY1502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03162","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03162","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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