Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8VFM

Salmonella effector protein SipA decorated actin filament

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003779	molecular_function	actin binding
A	0005576	cellular_component	extracellular region
B	0003779	molecular_function	actin binding
B	0005576	cellular_component	extracellular region
C	0003779	molecular_function	actin binding
C	0005576	cellular_component	extracellular region
I	0003779	molecular_function	actin binding
I	0005576	cellular_component	extracellular region
J	0000166	molecular_function	nucleotide binding
J	0001725	cellular_component	stress fiber
J	0005200	molecular_function	structural constituent of cytoskeleton
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005856	cellular_component	cytoskeleton
J	0005865	cellular_component	striated muscle thin filament
J	0005884	cellular_component	actin filament
J	0015629	cellular_component	actin cytoskeleton
J	0016787	molecular_function	hydrolase activity
J	0030240	biological_process	skeletal muscle thin filament assembly
J	0048741	biological_process	skeletal muscle fiber development
L	0000166	molecular_function	nucleotide binding
L	0001725	cellular_component	stress fiber
L	0005200	molecular_function	structural constituent of cytoskeleton
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005856	cellular_component	cytoskeleton
L	0005865	cellular_component	striated muscle thin filament
L	0005884	cellular_component	actin filament
L	0015629	cellular_component	actin cytoskeleton
L	0016787	molecular_function	hydrolase activity
L	0030240	biological_process	skeletal muscle thin filament assembly
L	0048741	biological_process	skeletal muscle fiber development
M	0000166	molecular_function	nucleotide binding
M	0001725	cellular_component	stress fiber
M	0005200	molecular_function	structural constituent of cytoskeleton
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005856	cellular_component	cytoskeleton
M	0005865	cellular_component	striated muscle thin filament
M	0005884	cellular_component	actin filament
M	0015629	cellular_component	actin cytoskeleton
M	0016787	molecular_function	hydrolase activity
M	0030240	biological_process	skeletal muscle thin filament assembly
M	0048741	biological_process	skeletal muscle fiber development
N	0000166	molecular_function	nucleotide binding
N	0001725	cellular_component	stress fiber
N	0005200	molecular_function	structural constituent of cytoskeleton
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005856	cellular_component	cytoskeleton
N	0005865	cellular_component	striated muscle thin filament
N	0005884	cellular_component	actin filament
N	0015629	cellular_component	actin cytoskeleton
N	0016787	molecular_function	hydrolase activity
N	0030240	biological_process	skeletal muscle thin filament assembly
N	0048741	biological_process	skeletal muscle fiber development
R	0000166	molecular_function	nucleotide binding
R	0001725	cellular_component	stress fiber
R	0005200	molecular_function	structural constituent of cytoskeleton
R	0005515	molecular_function	protein binding
R	0005524	molecular_function	ATP binding
R	0005856	cellular_component	cytoskeleton
R	0005865	cellular_component	striated muscle thin filament
R	0005884	cellular_component	actin filament
R	0015629	cellular_component	actin cytoskeleton
R	0016787	molecular_function	hydrolase activity
R	0030240	biological_process	skeletal muscle thin filament assembly
R	0048741	biological_process	skeletal muscle fiber development
S	0000166	molecular_function	nucleotide binding
S	0001725	cellular_component	stress fiber
S	0005200	molecular_function	structural constituent of cytoskeleton
S	0005515	molecular_function	protein binding
S	0005524	molecular_function	ATP binding
S	0005856	cellular_component	cytoskeleton
S	0005865	cellular_component	striated muscle thin filament
S	0005884	cellular_component	actin filament
S	0015629	cellular_component	actin cytoskeleton
S	0016787	molecular_function	hydrolase activity
S	0030240	biological_process	skeletal muscle thin filament assembly
S	0048741	biological_process	skeletal muscle fiber development
U	0000166	molecular_function	nucleotide binding
U	0001725	cellular_component	stress fiber
U	0005200	molecular_function	structural constituent of cytoskeleton
U	0005515	molecular_function	protein binding
U	0005524	molecular_function	ATP binding
U	0005856	cellular_component	cytoskeleton
U	0005865	cellular_component	striated muscle thin filament
U	0005884	cellular_component	actin filament
U	0015629	cellular_component	actin cytoskeleton
U	0016787	molecular_function	hydrolase activity
U	0030240	biological_process	skeletal muscle thin filament assembly
U	0048741	biological_process	skeletal muscle fiber development
W	0000166	molecular_function	nucleotide binding
W	0001725	cellular_component	stress fiber
W	0005200	molecular_function	structural constituent of cytoskeleton
W	0005515	molecular_function	protein binding
W	0005524	molecular_function	ATP binding
W	0005856	cellular_component	cytoskeleton
W	0005865	cellular_component	striated muscle thin filament
W	0005884	cellular_component	actin filament
W	0015629	cellular_component	actin cytoskeleton
W	0016787	molecular_function	hydrolase activity
W	0030240	biological_process	skeletal muscle thin filament assembly
W	0048741	biological_process	skeletal muscle fiber development

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
J	TYR53-GLY63

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

Chain	Residue	Details
J	TRP356-GLU364

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

Chain	Residue	Details
J	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)