Annotations: 4F61

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Tubulin_C	e4f61A3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
A	Tubulin	e4f61A4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
C	Tubulin_C	e4f61C3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
C	Tubulin	e4f61C4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
E	Tubulin_C	e4f61E3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
E	Tubulin	e4f61E4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
G	Tubulin_C	e4f61G3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
G	Tubulin	e4f61G4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
B	Tubulin_C	e4f61B3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
B	Tubulin	e4f61B4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
D	Tubulin_C	e4f61D3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
D	Tubulin	e4f61D4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
F	Tubulin_C	e4f61F3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
F	Tubulin	e4f61F4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
H	Tubulin_C	e4f61H3	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
H	Tubulin	e4f61H4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
I	Stathmin	e4f61I5	A: extended segments	X: Stathmin (From Topology)	H: Stathmin (From Topology)	T: Stathmin	F: Stathmin	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C, E, G	PF00091	Tubulin/FtsZ family, GTPase domain (Tubulin)	Tubulin/FtsZ family, GTPase domain	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ...	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.	Domain
A, C, E, G	PF03953	Tubulin C-terminal domain (Tubulin_C)	Tubulin C-terminal domain	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tub ...	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).	Domain
B, D, F, H	PF00091	Tubulin/FtsZ family, GTPase domain (Tubulin)	Tubulin/FtsZ family, GTPase domain	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ...	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.	Domain
B, D, F, H	PF03953	Tubulin C-terminal domain (Tubulin_C)	Tubulin C-terminal domain	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tub ...	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C, E, G	Tubulin alpha chain	hydrolase activity catalytic activity protein-containing complex binding binding cation binding ion binding metal ion binding small molecule binding identical protein binding protein binding protein heterodimerization activity protein dimerization activity guanyl nucleotide binding GTP binding hydrolase activity catalytic activity protein-containing complex binding binding cation binding ion binding metal ion binding small molecule binding identical protein binding protein binding protein heterodimerization activity protein dimerization activity guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding structural constituent of cytoskeleton structural molecule activity	multicellular organismal process multicellular organismal-level homeostasis homeostatic process homeostasis of number of cells within a tissue anatomical structure homeostasis tissue homeostasis homeostasis of number of cells developmental process cerebellum morphogenesis cerebellar cortex morphogenesis head development hindbrain morphogenesis animal organ development brain development multicellular organismal process multicellular organismal-level homeostasis homeostatic process homeostasis of number of cells within a tissue anatomical structure homeostasis tissue homeostasis homeostasis of number of cells developmental process cerebellum morphogenesis cerebellar cortex morphogenesis head development hindbrain morphogenesis animal organ development brain development nervous system development cerebellar cortex development anatomical structure morphogenesis multicellular organism development cerebellum development central nervous system development metencephalon development anatomical structure development hindbrain development system development behavior system process learning or memory nervous system process cognition memory protein polymerization protein-containing complex organization microtubule cytoskeleton organization microtubule polymerization cellular component organization cellular component biogenesis organelle organization microtubule polymerization or depolymerization cellular component assembly protein-containing complex assembly cellular process microtubule-based process cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization cellular response to stimulus cellular response to metal ion cellular response to chemical stimulus response to stimulus response to metal ion response to chemical cellular response to calcium ion response to calcium ion startle response neuromuscular process response to external stimulus forebrain development pallium development cerebral cortex development telencephalon development brain morphogenesis forebrain morphogenesis animal organ morphogenesis response to acid chemical response to oxygen-containing compound response to nitrogen compound response to L-glutamate response to amino acid cellular developmental process neurogenesis gliogenesis glial cell differentiation cell differentiation establishment of organelle localization cellular localization organelle transport along microtubule transport intracellular transport establishment of localization localization organelle localization establishment of localization in cell microtubule-based transport transport along microtubule cytoskeleton-dependent intracellular transport microtubule-based movement cell cycle mitotic cell cycle regulation of biological process regulation of cellular process cell surface receptor signaling pathway signaling biological regulation smoothened signaling pathway cell communication signal transduction adult locomotory behavior adult behavior locomotory behavior regulation of cellular component organization regulation of synapse organization cell junction organization regulation of synapse structure or activity synapse organization regulation of biological quality response to light stimulus learning visual learning visual behavior associative learning response to radiation response to abiotic stimulus exploration behavior locomotory exploration behavior protein localization establishment of protein localization nitrogen compound transport protein transport cellular macromolecule localization macromolecule localization intracellular protein transport response to mechanical stimulus biosynthetic process cellular biosynthetic process cellular metabolic process metabolic process macromolecule metabolic process gene expression macromolecule biosynthetic process neuron apoptotic process apoptotic process cell death programmed cell death microtubule organizing center organization centrosome cycle cell cycle process generation of neurons neuron differentiation pyramidal neuron differentiation dentate gyrus development hippocampus development limbic system development motor behavior neuron migration cell migration cell motility cell projection organization plasma membrane bounded cell projection morphogenesis cell development neuron projection development cell morphogenesis cell projection morphogenesis neuron projection morphogenesis plasma membrane bounded cell projection organization neuron projection arborization neuron development response to peptide response to cytokine response to tumor necrosis factor	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol neuromuscular junction synapse cell junction membrane-bounded organelle endosome intracellular vesicle intracellular membrane-bounded organelle recycling endosome endomembrane system intracellular organelle intracellular anatomical structure cytoplasm cellular anatomical entity cytosol neuromuscular junction synapse cell junction membrane-bounded organelle endosome intracellular vesicle intracellular membrane-bounded organelle recycling endosome endomembrane system intracellular organelle cytoplasmic vesicle organelle vesicle intracellular non-membrane-bounded organelle chromosome condensed chromosome non-membrane-bounded organelle polymeric cytoskeletal fiber axoneme axonemal microtubule cytoplasmic microtubule plasma membrane bounded cell projection cytoplasm cytoskeleton supramolecular polymer supramolecular complex microtubule cytoskeleton ciliary plasm cilium cytoplasmic region plasma membrane bounded cell projection cell projection supramolecular fiber microtubule cell periphery plasma membrane membrane cytoplasmic ribonucleoprotein granule ribonucleoprotein granule
B, D, F, H	Tubulin beta chain	structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization	intracellular anatomical structure cytoplasm cellular anatomical entity polymeric cytoskeletal fiber intracellular organelle cytoskeleton organelle intracellular non-membrane-bounded organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton non-membrane-bounded organelle
I	Stathmin-like domain R4	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C, E, G	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
A, C, E, G	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
A, C, E, G	IPR000217	Tubulin	Family
A, C, E, G	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
A, C, E, G	IPR017975	Tubulin, conserved site	Conserved Site
A, C, E, G	IPR023123	Tubulin, C-terminal	Homologous Superfamily
A, C, E, G	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
A, C, E, G	IPR002452	Alpha tubulin	Family
A, C, E, G	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
B, D, F, H	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
B, D, F, H	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
B, D, F, H	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
B, D, F, H	IPR017975	Tubulin, conserved site	Conserved Site
B, D, F, H	IPR000217	Tubulin	Family
B, D, F, H	IPR023123	Tubulin, C-terminal	Homologous Superfamily
B, D, F, H	IPR002453	Beta tubulin	Family
B, D, F, H	IPR013838	Beta tubulin, autoregulation binding site	Binding Site
B, D, F, H	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
B, D, F, H	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily

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 R01GM157729.