6HD5

Cryo-EM structure of the ribosome-NatA complex

Functional Information from GO Data

Chain	GOid	namespace	contents
t	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
t	0005515	molecular_function	protein binding
t	0005737	cellular_component	cytoplasm
t	0005739	cellular_component	mitochondrion
t	0006474	biological_process	N-terminal protein amino acid acetylation
t	0010698	molecular_function	acetyltransferase activator activity
t	0031415	cellular_component	NatA complex
t	0043022	molecular_function	ribosome binding
u	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
u	0005515	molecular_function	protein binding
u	0005737	cellular_component	cytoplasm
u	0006474	biological_process	N-terminal protein amino acid acetylation
u	0008999	molecular_function	protein-N-terminal-alanine acetyltransferase activity
u	0016740	molecular_function	transferase activity
u	0016746	molecular_function	acyltransferase activity
u	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
u	0031415	cellular_component	NatA complex
u	0042802	molecular_function	identical protein binding
u	0061606	biological_process	N-terminal protein amino acid propionylation
u	1990189	molecular_function	protein N-terminal-serine acetyltransferase activity
u	1990190	molecular_function	protein-N-terminal-glutamate acetyltransferase activity
v	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
v	0005515	molecular_function	protein binding
v	0005737	cellular_component	cytoplasm
v	0006474	biological_process	N-terminal protein amino acid acetylation
v	0007064	biological_process	mitotic sister chromatid cohesion
v	0016740	molecular_function	transferase activity
v	0016746	molecular_function	acyltransferase activity
v	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
v	0031415	cellular_component	NatA complex
v	0061733	molecular_function	protein-lysine-acetyltransferase activity
v	0120518	molecular_function	protein N-terminal-methionine acetyltransferase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	33
Details	Repeat: {"description":"TPR 1"}

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site_id	SWS_FT_FI2
Number of Residues	33
Details	Repeat: {"description":"TPR 2"}

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site_id	SWS_FT_FI3
Number of Residues	33
Details	Repeat: {"description":"TPR 3"}

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site_id	SWS_FT_FI4
Number of Residues	36
Details	Repeat: {"description":"TPR 4"}

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site_id	SWS_FT_FI5
Number of Residues	33
Details	Repeat: {"description":"TPR 5"}

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site_id	SWS_FT_FI6
Number of Residues	33
Details	Repeat: {"description":"TPR 6"}

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site_id	SWS_FT_FI7
Number of Residues	33
Details	Repeat: {"description":"TPR 7"}

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site_id	SWS_FT_FI8
Number of Residues	33
Details	Repeat: {"description":"TPR 8"}

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site_id	SWS_FT_FI9
Number of Residues	42
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

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Residue

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site_id	SWS_FT_FI10
Number of Residues	44
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

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site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

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site_id	SWS_FT_FI12
Number of Residues	160
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

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