7QIO

Homology model of myosin neck domain in skeletal sarcomere

Functional Information from GO Data

Chain	GOid	namespace	contents
L	0003774	molecular_function	cytoskeletal motor activity
L	0005524	molecular_function	ATP binding
L	0016459	cellular_component	myosin complex
L	0051015	molecular_function	actin filament binding
M	0003774	molecular_function	cytoskeletal motor activity
M	0005524	molecular_function	ATP binding
M	0016459	cellular_component	myosin complex
M	0051015	molecular_function	actin filament binding
N	0005509	molecular_function	calcium ion binding
N	0006936	biological_process	muscle contraction
N	0008307	molecular_function	structural constituent of muscle
N	0016459	cellular_component	myosin complex
N	0030016	cellular_component	myofibril
O	0005509	molecular_function	calcium ion binding
O	0006936	biological_process	muscle contraction
O	0008307	molecular_function	structural constituent of muscle
O	0016459	cellular_component	myosin complex
O	0030016	cellular_component	myofibril
P	0005509	molecular_function	calcium ion binding
P	0006936	biological_process	muscle contraction
P	0006955	biological_process	immune response
P	0007519	biological_process	skeletal muscle tissue development
P	0008307	molecular_function	structural constituent of muscle
P	0016459	cellular_component	myosin complex
P	0046872	molecular_function	metal ion binding
Q	0005509	molecular_function	calcium ion binding
Q	0006936	biological_process	muscle contraction
Q	0006955	biological_process	immune response
Q	0007519	biological_process	skeletal muscle tissue development
Q	0008307	molecular_function	structural constituent of muscle
Q	0016459	cellular_component	myosin complex
Q	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DQNRDGIIDkeDL

Chain	Residue	Details
P	ASP38-LEU50

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
P	ASP38
P	ASN40
P	ASP42
P	ASP49
Q	ASP38
Q	ASN40
Q	ASP42
Q	ASP49

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N,N,N-trimethylalanine => ECO:0000250|UniProtKB:P02608

Chain	Residue	Details
P	ALA2
Q	ALA2
O	THR65
O	THR81
M	SER36
M	SER79
M	SER392
M	SER625

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
P	SER15
M	THR776
P	SER16
Q	SER15
Q	SER16
L	THR776
M	THR64
M	THR69
M	THR391
M	THR419

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04466

Chain	Residue	Details
P	THR25
P	THR35
P	THR101
Q	THR25
Q	THR35
Q	THR101

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04466

Chain	Residue	Details
P	SER75
Q	SER75
M	TYR389
M	TYR424

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Pros-methylhistidine => ECO:0000250|UniProtKB:Q28641

Chain	Residue	Details
L	HIS757
M	HIS757

---