3IYG

Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005832	cellular_component	chaperonin-containing T-complex
A	0005856	cellular_component	cytoskeleton
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005832	cellular_component	chaperonin-containing T-complex
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005813	cellular_component	centrosome
D	0005832	cellular_component	chaperonin-containing T-complex
D	0005856	cellular_component	cytoskeleton
D	0005929	cellular_component	cilium
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0042470	cellular_component	melanosome
D	0042995	cellular_component	cell projection
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005832	cellular_component	chaperonin-containing T-complex
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0000166	molecular_function	nucleotide binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005832	cellular_component	chaperonin-containing T-complex
H	0006457	biological_process	protein folding
H	0016887	molecular_function	ATP hydrolysis activity
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
Q	0000166	molecular_function	nucleotide binding
Q	0005524	molecular_function	ATP binding
Q	0005737	cellular_component	cytoplasm
Q	0005813	cellular_component	centrosome
Q	0005832	cellular_component	chaperonin-containing T-complex
Q	0005856	cellular_component	cytoskeleton
Q	0005929	cellular_component	cilium
Q	0006457	biological_process	protein folding
Q	0016887	molecular_function	ATP hydrolysis activity
Q	0042995	cellular_component	cell projection
Q	0051082	molecular_function	unfolded protein binding
Q	0140662	molecular_function	ATP-dependent protein folding chaperone
Z	0005524	molecular_function	ATP binding
Z	0006457	biological_process	protein folding
Z	0016887	molecular_function	ATP hydrolysis activity
Z	0051082	molecular_function	unfolded protein binding
Z	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK

Chain	Residue	Details
B	VAL82-LYS107

---

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT

Chain	Residue	Details
Q	ALA266-THR277

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site_id	PS00751
Number of Residues	17
Details	TCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILknIgVdNP

Chain	Residue	Details
B	VAL50-PRO66
E	VAL48-GLN64
A	ILE48-PRO64
G	MET47-PRO63
D	ILE49-PRO65
Z	LEU48-PRO64
H	ILE49-PRO65
Q	VAL49-PRO65

---

site_id	PS00995
Number of Residues	9
Details	TCP1_3 Chaperonins TCP-1 signature 3. QDdeVGDGT

Chain	Residue	Details
B	GLN78-THR86
E	GLN76-THR84
A	GLN76-THR84
G	GLN75-THR83
D	GLN77-THR85
Z	GLN76-THR84
H	GLN77-THR85
Q	GLN77-THR85

---

site_id	PS00750
Number of Residues	13
Details	TCP1_1 Chaperonins TCP-1 signature 1. KStLGPkGmdKIL

Chain	Residue	Details
B	LYS27-LEU39
E	LYS27-MET39
A	LYS27-LEU39
G	ARG26-LEU38
D	ARG28-ILE40
Z	ARG27-LEU39
H	ARG28-ILE40
Q	ARG28-VAL40

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99832

Chain	Residue	Details
H	LYS58
H	LYS311
D	SER181
D	SER423

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P80313

Chain	Residue	Details
H	LYS241
A	LYS394
D	LYS298
D	LYS305

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q99832

Chain	Residue	Details
H	LYS421
G	SER232
G	SER240

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P78371

Chain	Residue	Details
B	LYS235
Q	LYS238
Q	LYS244

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P49368

Chain	Residue	Details
G	THR418
G	THR447

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P49368

Chain	Residue	Details
G	LYS3
G	LYS236
G	LYS237
G	LYS369

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