3MN6

Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000281	biological_process	mitotic cytokinesis
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005856	cellular_component	cytoskeleton
A	0006338	biological_process	chromatin remodeling
A	0007010	biological_process	cytoskeleton organization
A	0007291	biological_process	sperm individualization
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0030723	biological_process	ovarian fusome organization
A	0031011	cellular_component	Ino80 complex
A	0032507	biological_process	maintenance of protein location in cell
A	0035060	cellular_component	brahma complex
A	0035148	biological_process	tube formation
A	0048468	biological_process	cell development
A	0048646	biological_process	anatomical structure formation involved in morphogenesis
F	0000166	molecular_function	nucleotide binding
F	0000281	biological_process	mitotic cytokinesis
F	0005200	molecular_function	structural constituent of cytoskeleton
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005856	cellular_component	cytoskeleton
F	0006338	biological_process	chromatin remodeling
F	0007010	biological_process	cytoskeleton organization
F	0007291	biological_process	sperm individualization
F	0015629	cellular_component	actin cytoskeleton
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0030723	biological_process	ovarian fusome organization
F	0031011	cellular_component	Ino80 complex
F	0032507	biological_process	maintenance of protein location in cell
F	0035060	cellular_component	brahma complex
F	0035148	biological_process	tube formation
F	0048468	biological_process	cell development
F	0048646	biological_process	anatomical structure formation involved in morphogenesis
K	0000166	molecular_function	nucleotide binding
K	0000281	biological_process	mitotic cytokinesis
K	0005200	molecular_function	structural constituent of cytoskeleton
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005634	cellular_component	nucleus
K	0005856	cellular_component	cytoskeleton
K	0006338	biological_process	chromatin remodeling
K	0007010	biological_process	cytoskeleton organization
K	0007291	biological_process	sperm individualization
K	0015629	cellular_component	actin cytoskeleton
K	0016787	molecular_function	hydrolase activity
K	0016887	molecular_function	ATP hydrolysis activity
K	0030723	biological_process	ovarian fusome organization
K	0031011	cellular_component	Ino80 complex
K	0032507	biological_process	maintenance of protein location in cell
K	0035060	cellular_component	brahma complex
K	0035148	biological_process	tube formation
K	0048468	biological_process	cell development
K	0048646	biological_process	anatomical structure formation involved in morphogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 901

Chain	Residue
A	HOH381
A	HOH405
A	HOH421
A	HOH428
A	HOH449
A	ATP800

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP A 800

Chain	Residue
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159
A	GLY182
A	LYS213
A	GLU214
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336
A	HOH421
A	HOH429
A	HOH436
A	HOH449
A	HOH464
A	HOH521
A	CA901
A	HOH1
A	GLY13
A	SER14

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 901

Chain	Residue
F	HOH390
F	HOH413
F	HOH419
F	HOH424
F	HOH427
F	ATP800

---

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP F 800

Chain	Residue
F	GLY13
F	SER14
F	GLY15
F	MET16
F	LYS18
F	GLY156
F	ASP157
F	GLY158
F	VAL159
F	GLY182
F	LYS213
F	GLU214
F	GLY302
F	THR303
F	MET305
F	TYR306
F	LYS336
F	HOH378
F	HOH419
F	HOH427
F	HOH468
F	HOH495
F	HOH509
F	HOH590
F	CA901

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA K 901

Chain	Residue
K	HOH388
K	HOH398
K	HOH416
K	HOH426
K	HOH462
K	ATP800

---

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP K 800

Chain	Residue
K	GLY13
K	SER14
K	GLY15
K	MET16
K	LYS18
K	GLY156
K	ASP157
K	GLY158
K	VAL159
K	GLY182
K	ARG210
K	LYS213
K	GLU214
K	GLY301
K	GLY302
K	THR303
K	MET305
K	TYR306
K	HOH377
K	HOH398
K	HOH426
K	HOH465
K	HOH496
K	HOH498
K	CA901

---

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
A	TYR53-GLY63

---

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WISKqEYDE

Chain	Residue	Details
A	TRP356-GLU364

---

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
A	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P02572","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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