4K25

Crystal Structure of yeast Qri7 homodimer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0008252	molecular_function	nucleotidase activity
A	0008270	molecular_function	zinc ion binding
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0046872	molecular_function	metal ion binding
A	0061711	molecular_function	N(6)-L-threonylcarbamoyladenine synthase activity
A	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process
A	0072670	biological_process	mitochondrial tRNA threonylcarbamoyladenosine modification

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 601

Chain	Residue
A	HIS145
A	HIS149
A	HIS175
A	ASP361

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 602

Chain	Residue
A	ASP227
A	ASP384
A	ASP400

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Functional Information from PROSITE/UniProt

site_id	PS01016
Number of Residues	21
Details	GLYCOPROTEASE Glycoprotease family signature. KGlavaWNkPlIgvhHmlGHL

Chain	Residue	Details
A	LYS130-LEU150

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:23620299

Chain	Residue	Details
A	HIS145
A	HIS149
A	ASP361

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:25084372

Chain	Residue	Details
A	LEU170
A	ASP203
A	ALA217
A	GLU221
A	SER328
A	SER360

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