3Q5I

Crystal Structure of PBANKA_031420

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005509	molecular_function	calcium ion binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006468	biological_process	protein phosphorylation
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0020002	cellular_component	host cell plasma membrane
A	0020005	cellular_component	symbiont-containing vacuole membrane
A	0031514	cellular_component	motile cilium
A	0045727	biological_process	positive regulation of translation
A	0046872	molecular_function	metal ion binding
A	2000147	biological_process	positive regulation of cell motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	ASP384
A	ASN386
A	ASP388
A	GLN390
A	GLU395
A	HOH530

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 524

Chain	Residue
A	TYR434
A	GLU436
A	GLU439
A	ASP428
A	ASP430
A	ASN432

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 525

Chain	Residue
A	HOH2
A	ASP464
A	ASP466
A	SER468
A	LYS470
A	GLU475

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 526

Chain	Residue
A	HOH3
A	ASP498
A	ASN500
A	ASP502
A	MET504
A	GLU509

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 528

Chain	Residue
A	ASN195
A	ASP211
A	HOH531
A	HOH532
A	ANP1634

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ANP A 1634

Chain	Residue
A	VAL71
A	ALA84
A	LYS86
A	ILE128
A	THR144
A	GLU145
A	PHE146
A	TYR147
A	GLU151
A	ASN195
A	LEU197
A	ASP211
A	CA528
A	MG529
A	HOH532
A	HOH591
A	HOH622

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 529

Chain	Residue
A	ASP211
A	GLU412
A	HOH553
A	ANP1634

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 527

Chain	Residue
A	HOH12
A	GLU31
A	TYR34
A	PHE35
A	GLN36
A	HOH610
A	HOH660

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP384-LEU396
A	ASP428-PHE440
A	ASP464-LEU476
A	ASP498-PHE510

---

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAYGEVLlCkeknghsekaik......VIKK

Chain	Residue	Details
A	LEU63-LYS90

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpeNILL

Chain	Residue	Details
A	ILE186-LEU198

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	35
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	35
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	18
Details	Region: {"description":"J domain","evidences":[{"source":"UniProtKB","id":"P62344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	Motif: {"description":"J domain autoinhibitory motif","evidences":[{"source":"UniProtKB","id":"P62344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	Motif: {"description":"J domain interacts with the EF-hand domains","evidences":[{"source":"UniProtKB","id":"P62344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10141","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---