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7WHG

Lokiarchaeota gelsolin (2DGel) bound to two molecules of rabbit actin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
B0000287molecular_functionmagnesium ion binding
B0001725cellular_componentstress fiber
B0003785molecular_functionactin monomer binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0010628biological_processpositive regulation of gene expression
B0016787molecular_functionhydrolase activity
B0019904molecular_functionprotein domain specific binding
B0030027cellular_componentlamellipodium
B0030041biological_processactin filament polymerization
B0030175cellular_componentfilopodium
B0030240biological_processskeletal muscle thin filament assembly
B0031013molecular_functiontroponin I binding
B0031432molecular_functiontitin binding
B0031941cellular_componentfilamentous actin
B0032036molecular_functionmyosin heavy chain binding
B0032432cellular_componentactin filament bundle
B0042802molecular_functionidentical protein binding
B0044297cellular_componentcell body
B0048306molecular_functioncalcium-dependent protein binding
B0048741biological_processskeletal muscle fiber development
B0051017biological_processactin filament bundle assembly
B0090131biological_processmesenchyme migration
B0098723cellular_componentskeletal muscle myofibril
B0140660molecular_functioncytoskeletal motor activator activity
G0003779molecular_functionactin binding
G0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
G0005737cellular_componentcytoplasm
G0008154biological_processactin polymerization or depolymerization
G0015629cellular_componentactin cytoskeleton
G0046872molecular_functionmetal ion binding
G0051014biological_processactin filament severing
G0051015molecular_functionactin filament binding
G0051016biological_processbarbed-end actin filament capping
G0051693biological_processactin filament capping
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737
ChainResidueDetails
ACYS0
BCYS0

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
AASP1
BASP1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47
BMET44
BMET47

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61
BLYS61

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK
ChainResidueDetails
AHIC73
BHIC73

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
BLYS84

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177
BARG177

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PDB entries from 2024-11-06

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