7WHF

Heimdallarchaeota gelsolin (2DGel) bound to rabbit actin

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Actin-like ATPases	8040506	3000092	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Actin-like ATPases	8040509	3000092	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Actin-like ATPases	8040506	3000092	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Actin-like ATPases	8040509	3000092	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Actin_1st	e7whfA1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Actin_1st	ECOD (1.6)
A	Actin_2nd	e7whfA2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Actin_2nd	ECOD (1.6)
C [auth B]	Actin_1st	e7whfB1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Actin_1st	ECOD (1.6)
C [auth B]	Actin_2nd	e7whfB2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Actin_2nd	ECOD (1.6)
B [auth G]	Gelsolin	e7whfG1	A: a+b three layers	X: Gelsolin-like (From Topology)	H: Gelsolin-like (From Topology)	T: Gelsolin-like	F: Gelsolin	ECOD (1.6)
B [auth G]	Gelsolin_1	e7whfG2	A: a+b three layers	X: Gelsolin-like (From Topology)	H: Gelsolin-like (From Topology)	T: Gelsolin-like	F: Gelsolin_1	ECOD (1.6)
D [auth C]	Gelsolin	e7whfC1	A: a+b three layers	X: Gelsolin-like (From Topology)	H: Gelsolin-like (From Topology)	T: Gelsolin-like	F: Gelsolin	ECOD (1.6)
D [auth C]	Gelsolin_1	e7whfC2	A: a+b three layers	X: Gelsolin-like (From Topology)	H: Gelsolin-like (From Topology)	T: Gelsolin-like	F: Gelsolin_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B [auth G], D [auth C]	PF00626	Gelsolin repeat (Gelsolin)	Gelsolin repeat	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth B]	Actin, alpha skeletal muscle	cytoskeletal protein binding titin binding protein binding binding cation binding ion binding calcium ion binding metal ion binding small molecule binding protein domain specific binding hydrolase activity catalytic activity troponin I binding cytoskeletal motor activator activity cytoskeletal protein binding titin binding protein binding binding cation binding ion binding calcium ion binding metal ion binding small molecule binding protein domain specific binding hydrolase activity catalytic activity troponin I binding cytoskeletal motor activator activity cytoskeletal motor regulator activity molecular function activator activity molecular function regulator activity magnesium ion binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding myosin heavy chain binding myosin binding tropomyosin binding calcium-dependent protein binding identical protein binding actin monomer binding actin binding	developmental process mesenchyme migration multicellular organismal process mesenchyme morphogenesis animal organ development mesenchyme development tissue development tissue morphogenesis anatomical structure morphogenesis tissue migration anatomical structure development animal organ morphogenesis myotube cell development skeletal muscle fiber development developmental process mesenchyme migration multicellular organismal process mesenchyme morphogenesis animal organ development mesenchyme development tissue development tissue morphogenesis anatomical structure morphogenesis tissue migration anatomical structure development animal organ morphogenesis myotube cell development skeletal muscle fiber development cellular developmental process skeletal muscle tissue development cell development muscle cell differentiation myotube differentiation muscle structure development skeletal muscle organ development muscle cell development cell differentiation cellular process muscle tissue development muscle organ development striated muscle cell differentiation regulation of cellular process cellular biosynthetic process positive regulation of biological process positive regulation of cellular metabolic process positive regulation of macromolecule biosynthetic process positive regulation of metabolic process positive regulation of biosynthetic process positive regulation of macromolecule metabolic process positive regulation of cellular process regulation of biosynthetic process regulation of biological process cellular metabolic process biological regulation regulation of cellular metabolic process regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process regulation of cellular biosynthetic process regulation of gene expression biosynthetic process positive regulation of gene expression regulation of macromolecule biosynthetic process metabolic process macromolecule metabolic process regulation of metabolic process positive regulation of cellular biosynthetic process cellular component assembly involved in morphogenesis non-membrane-bounded organelle assembly skeletal myofibril assembly cellular component organization cellular component biogenesis striated muscle cell development cellular anatomical entity morphogenesis cellular component assembly actin filament-based process cellular component organization or biogenesis skeletal muscle thin filament assembly actin cytoskeleton organization actomyosin structure organization organelle assembly actin filament organization organelle organization myofibril assembly anatomical structure formation involved in morphogenesis supramolecular fiber organization cytoskeleton organization protein polymerization actin polymerization or depolymerization actin filament polymerization protein-containing complex organization protein-containing complex assembly actin filament bundle organization actin filament bundle assembly	intracellular anatomical structure skeletal muscle myofibril cellular anatomical entity intracellular organelle organelle intracellular non-membrane-bounded organelle contractile muscle fiber cytoplasm supramolecular fiber myofibril supramolecular polymer supramolecular complex non-membrane-bounded organelle cell projection intracellular anatomical structure skeletal muscle myofibril cellular anatomical entity intracellular organelle organelle intracellular non-membrane-bounded organelle contractile muscle fiber cytoplasm supramolecular fiber myofibril supramolecular polymer supramolecular complex non-membrane-bounded organelle cell projection cell leading edge plasma membrane bounded cell projection lamellipodium cytoskeleton actin filament bundle actin cytoskeleton actomyosin stress fiber contractile actin filament bundle polymeric cytoskeletal fiber actin filament protein-containing complex filamentous actin cell body striated muscle thin filament myofilament sarcomere actin-based cell projection filopodium
B [auth G], D [auth C]	Heimdallarchaeota Gelsolin domain-containing protein 2DGel	binding ion binding phosphatidylinositol-4,5-bisphosphate binding anion binding phosphatidylinositol bisphosphate binding phospholipid binding lipid binding phosphatidylinositol phosphate binding phosphatidylinositol binding small molecule binding cytoskeletal protein binding actin binding protein-containing complex binding protein binding binding ion binding phosphatidylinositol-4,5-bisphosphate binding anion binding phosphatidylinositol bisphosphate binding phospholipid binding lipid binding phosphatidylinositol phosphate binding phosphatidylinositol binding small molecule binding cytoskeletal protein binding actin binding protein-containing complex binding protein binding actin filament binding cation binding metal ion binding	actin filament severing actin filament-based process cellular process regulation of cellular process regulation of cellular component size negative regulation of biological process protein-containing complex disassembly regulation of protein-containing complex disassembly actin filament depolymerization regulation of actin filament depolymerization cellular component biogenesis actin filament capping cellular component assembly negative regulation of supramolecular fiber organization actin filament severing actin filament-based process cellular process regulation of cellular process regulation of cellular component size negative regulation of biological process protein-containing complex disassembly regulation of protein-containing complex disassembly actin filament depolymerization regulation of actin filament depolymerization cellular component biogenesis actin filament capping cellular component assembly negative regulation of supramolecular fiber organization regulation of biological quality negative regulation of actin filament polymerization cellular component disassembly regulation of biological process barbed-end actin filament capping negative regulation of cellular component organization actin filament organization regulation of organelle organization negative regulation of protein depolymerization negative regulation of protein-containing complex assembly regulation of protein polymerization regulation of supramolecular fiber organization supramolecular fiber organization regulation of cytoskeleton organization regulation of cellular component organization regulation of actin filament-based process cellular component organization regulation of protein-containing complex assembly negative regulation of protein-containing complex disassembly negative regulation of cellular process protein-containing complex assembly negative regulation of protein polymerization cellular component organization or biogenesis regulation of actin filament polymerization actin polymerization or depolymerization protein polymerization regulation of actin filament organization actin cytoskeleton organization actin filament polymerization protein-containing complex organization regulation of protein depolymerization negative regulation of cytoskeleton organization biological regulation regulation of actin polymerization or depolymerization regulation of cellular component biogenesis organelle organization negative regulation of organelle organization regulation of actin filament length regulation of actin cytoskeleton organization negative regulation of actin filament depolymerization protein depolymerization cytoskeleton organization regulation of anatomical structure size	intracellular anatomical structure cytoplasm cellular anatomical entity intracellular organelle cytoskeleton organelle intracellular non-membrane-bounded organelle actin cytoskeleton non-membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth B]	IPR020902	Actin/actin-like conserved site	Conserved Site
A, C [auth B]	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
A, C [auth B]	IPR004001	Actin, conserved site	Conserved Site
A, C [auth B]	IPR004000	Actin family	Family
B [auth G], D [auth C]	IPR007123	Gelsolin-like domain	Domain
B [auth G], D [auth C]	IPR007122	Villin/Gelsolin	Family
B [auth G], D [auth C]	IPR029006	ADF-H/Gelsolin-like domain superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, C [auth B]	HIC	Parent Component: HIS RESID: AA0317 PSI-MOD : 1'-methyl-L-histidine MOD:00322

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.