8JON

Structure of a synthetic circadian clock protein KaiC mutant of cyanobacteria Synechococcus elongatus PCC 7942

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0007623	biological_process	circadian rhythm
A	0009649	biological_process	entrainment of circadian clock
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0042754	biological_process	negative regulation of circadian rhythm
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048511	biological_process	rhythmic process
A	0070297	biological_process	regulation of phosphorelay signal transduction system
A	0106310	molecular_function	protein serine kinase activity
B	0000287	molecular_function	magnesium ion binding
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0007623	biological_process	circadian rhythm
B	0009649	biological_process	entrainment of circadian clock
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0042754	biological_process	negative regulation of circadian rhythm
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048511	biological_process	rhythmic process
B	0070297	biological_process	regulation of phosphorelay signal transduction system
B	0106310	molecular_function	protein serine kinase activity
C	0000287	molecular_function	magnesium ion binding
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0007623	biological_process	circadian rhythm
C	0009649	biological_process	entrainment of circadian clock
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0042754	biological_process	negative regulation of circadian rhythm
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048511	biological_process	rhythmic process
C	0070297	biological_process	regulation of phosphorelay signal transduction system
C	0106310	molecular_function	protein serine kinase activity
D	0000287	molecular_function	magnesium ion binding
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0007623	biological_process	circadian rhythm
D	0009649	biological_process	entrainment of circadian clock
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0042754	biological_process	negative regulation of circadian rhythm
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0048511	biological_process	rhythmic process
D	0070297	biological_process	regulation of phosphorelay signal transduction system
D	0106310	molecular_function	protein serine kinase activity
E	0000287	molecular_function	magnesium ion binding
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0007623	biological_process	circadian rhythm
E	0009649	biological_process	entrainment of circadian clock
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0042754	biological_process	negative regulation of circadian rhythm
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0048511	biological_process	rhythmic process
E	0070297	biological_process	regulation of phosphorelay signal transduction system
E	0106310	molecular_function	protein serine kinase activity
F	0000287	molecular_function	magnesium ion binding
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0007623	biological_process	circadian rhythm
F	0009649	biological_process	entrainment of circadian clock
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0042754	biological_process	negative regulation of circadian rhythm
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0048511	biological_process	rhythmic process
F	0070297	biological_process	regulation of phosphorelay signal transduction system
F	0106310	molecular_function	protein serine kinase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor in CI (KaiC 1) => ECO:0000305|PubMed:22304631

Chain	Residue	Details
A	GLU81
B	GLU81
C	GLU81
D	GLU81
E	GLU81
F	GLU81

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Proton acceptor in CII (KaiC 2) => ECO:0000305|PubMed:22304631

Chain	Residue	Details
A	GLU322
B	GLU322
C	GLU322
D	GLU322
E	GLU322
F	GLU322

---

site_id	SWS_FT_FI3
Number of Residues	150
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225, ECO:0000269|PubMed:22304631, ECO:0007744|PDB:1TF7, ECO:0007744|PDB:2GBL, ECO:0007744|PDB:4DUG

Chain	Residue	Details
A	GLY53
A	HIS234
D	LYS469
E	GLY53
E	THR54
E	GLY55
E	LYS56
E	LEU58
E	SER93
E	LYS228
E	ARG230
E	THR232
A	ASN244
E	HIS234
E	ASN244
E	ASP245
E	THR294
E	GLY295
E	THR296
E	GLY297
E	LYS298
E	LEU300
E	TRP335
A	ASP245
E	ARG455
E	LYS461
E	ARG463
E	SER465
E	HIS467
E	LYS469
F	GLY53
F	THR54
F	GLY55
F	LYS56
A	THR294
F	LEU58
F	SER93
F	LYS228
F	ARG230
F	THR232
F	HIS234
F	ASN244
F	ASP245
F	THR294
F	GLY295
A	GLY295
F	THR296
F	GLY297
F	LYS298
F	LEU300
F	TRP335
F	ARG455
F	LYS461
F	ARG463
F	SER465
F	HIS467
A	THR296
F	LYS469
A	GLY297
A	LYS298
A	LEU300
A	TRP335
A	THR54
A	ARG455
A	LYS461
A	ARG463
A	SER465
A	HIS467
A	LYS469
B	GLY53
B	THR54
B	GLY55
B	LYS56
A	GLY55
B	LEU58
B	SER93
B	LYS228
B	ARG230
B	THR232
B	HIS234
B	ASN244
B	ASP245
B	THR294
B	GLY295
A	LYS56
B	THR296
B	GLY297
B	LYS298
B	LEU300
B	TRP335
B	ARG455
B	LYS461
B	ARG463
B	SER465
B	HIS467
A	LEU58
B	LYS469
C	GLY53
C	THR54
C	GLY55
C	LYS56
C	LEU58
C	SER93
C	LYS228
C	ARG230
C	THR232
A	SER93
C	HIS234
C	ASN244
C	ASP245
C	THR294
C	GLY295
C	THR296
C	GLY297
C	LYS298
C	LEU300
C	TRP335
A	LYS228
C	ARG455
C	LYS461
C	ARG463
C	SER465
C	HIS467
C	LYS469
D	GLY53
D	THR54
D	GLY55
D	LYS56
A	ARG230
D	LEU58
D	SER93
D	LYS228
D	ARG230
D	THR232
D	HIS234
D	ASN244
D	ASP245
D	THR294
D	GLY295
A	THR232
D	THR296
D	GLY297
D	LYS298
D	LEU300
D	TRP335
D	ARG455
D	LYS461
D	ARG463
D	SER465
D	HIS467

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0007744|PDB:4DUG, ECO:0007744|PDB:4TL6, ECO:0007744|PDB:7DXQ

Chain	Residue	Details
A	THR57
B	THR57
C	THR57
D	THR57
E	THR57
F	THR57

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225, ECO:0007744|PDB:1TF7, ECO:0007744|PDB:2GBL

Chain	Residue	Details
A	LEU229
E	MET462
F	LEU229
F	MET462
A	MET462
B	LEU229
B	MET462
C	LEU229
C	MET462
D	LEU229
D	MET462
E	LEU229

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225, ECO:0007744|PDB:1U9I, ECO:0007744|PDB:2GBL, ECO:0007744|PDB:4DUG, ECO:0007744|PDB:7DXQ

Chain	Residue	Details
A	THR299
B	THR299
C	THR299
D	THR299
E	THR299
F	THR299

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225

Chain	Residue	Details
A	GLU322
B	GLU322
C	GLU322
D	GLU322
E	GLU322
F	GLU322

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15347809, ECO:0000269|PubMed:15347812, ECO:0000269|PubMed:17717528, ECO:0000269|PubMed:17916691, ECO:0007744|PDB:1U9I, ECO:0007744|PDB:2GBL

Chain	Residue	Details
A	SER435
B	SER435
C	SER435
D	SER435
E	SER435
F	SER435

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:15347809, ECO:0000269|PubMed:15347812, ECO:0000269|PubMed:17717528, ECO:0000269|PubMed:17916691, ECO:0007744|PDB:1U9I, ECO:0007744|PDB:2GBL

Chain	Residue	Details
A	THR436
B	THR436
C	THR436
D	THR436
E	THR436
F	THR436

---