Annotations: 6TIY

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6tiya1	Alpha and beta proteins (a/b)	Tubulin nucleotide-binding domain-like	Tubulin nucleotide-binding domain-like	Tubulin, GTPase domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
A	d6tiya2	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	Tubulin C-terminal domain-like	Tubulin, C-terminal domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
C	d6tiyc1	Alpha and beta proteins (a/b)	Tubulin nucleotide-binding domain-like	Tubulin nucleotide-binding domain-like	Tubulin, GTPase domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
C	d6tiyc2	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	Tubulin C-terminal domain-like	Tubulin, C-terminal domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
B	d6tiyb1	Alpha and beta proteins (a/b)	Tubulin nucleotide-binding domain-like	Tubulin nucleotide-binding domain-like	Tubulin, GTPase domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
B	d6tiyb2	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	Tubulin C-terminal domain-like	Tubulin, C-terminal domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
D	d6tiyd1	Alpha and beta proteins (a/b)	Tubulin nucleotide-binding domain-like	Tubulin nucleotide-binding domain-like	Tubulin, GTPase domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
D	d6tiyd2	Alpha and beta proteins (a+b)	Bacillus chorismate mutase-like	Tubulin C-terminal domain-like	Tubulin, C-terminal domain	automated matches	Fruit fly (Drosophila melanogaster ) [TaxId: 7227 ],	SCOPe (2.08)
E	d6tiye_	All alpha proteins	Non-globular all-alpha subunits of globular proteins	Stathmin	Stathmin	Stathmin 4	Rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
E	SCOP2B Superfamily	Stathmin	8041515	3001374	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	Tubulin_C	e6tiyA1	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	e6tiyA2	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	e6tiyC1	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	e6tiyC2	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	e6tiyB1	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	e6tiyB2	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	e6tiyD2	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	e6tiyD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
E	Stathmin	e6tiyE1	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	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	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	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	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
E	PF00836	Stathmin family (Stathmin)	Stathmin family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	Tubulin alpha-1 chain	structural constituent of cytoskeleton structural molecule activity hydrolase activity catalytic 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 structural constituent of cytoskeleton structural molecule activity hydrolase activity catalytic 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	cellular process cell cycle mitotic cell cycle localization organelle localization lysosome localization vacuolar localization cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization	intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton organelle intracellular non-membrane-bounded organelle cellular anatomical entity microtubule cytoskeleton non-membrane-bounded organelle perinuclear region of cytoplasm cytoplasm spindle polymeric cytoskeletal fiber intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton organelle intracellular non-membrane-bounded organelle cellular anatomical entity microtubule cytoskeleton non-membrane-bounded organelle perinuclear region of cytoplasm cytoplasm spindle polymeric cytoskeletal fiber aster astral microtubule spindle microtubule cytoplasmic microtubule supramolecular fiber microtubule supramolecular polymer supramolecular complex membrane-bounded organelle nucleus intracellular membrane-bounded organelle
B, D	Tubulin beta-1 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
E	Stathmin-4	cytoskeletal protein binding protein binding binding tubulin binding	regulation of cytoskeleton organization regulation of microtubule polymerization or depolymerization regulation of biological process regulation of cellular component organization regulation of cellular process microtubule cytoskeleton organization biological regulation regulation of microtubule-based process regulation of organelle organization cellular component organization organelle organization microtubule polymerization or depolymerization cellular process microtubule-based process regulation of cytoskeleton organization regulation of microtubule polymerization or depolymerization regulation of biological process regulation of cellular component organization regulation of cellular process microtubule cytoskeleton organization biological regulation regulation of microtubule-based process regulation of organelle organization cellular component organization organelle organization microtubule polymerization or depolymerization cellular process microtubule-based process cellular component organization or biogenesis cytoskeleton organization regulation of microtubule cytoskeleton organization cellular component disassembly protein-containing complex organization protein-containing complex disassembly microtubule depolymerization supramolecular fiber organization protein depolymerization developmental process multicellular organismal process plasma membrane bounded cell projection organization cellular developmental process cell projection organization cell development neuron projection development nervous system development generation of neurons neurogenesis multicellular organism development neuron differentiation cell differentiation neuron development anatomical structure development system development	membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system growth cone axon cell projection distal axon neuron projection membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system growth cone axon cell projection distal axon neuron projection plasma membrane bounded cell projection site of polarized growth

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
A, C	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
A, C	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
A, C	IPR017975	Tubulin, conserved site	Conserved Site
A, C	IPR002452	Alpha tubulin	Family
A, C	IPR000217	Tubulin	Family
A, C	IPR023123	Tubulin, C-terminal	Homologous Superfamily
A, C	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
A, C	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
B, D	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
B, D	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
B, D	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
B, D	IPR017975	Tubulin, conserved site	Conserved Site
B, D	IPR000217	Tubulin	Family
B, D	IPR023123	Tubulin, C-terminal	Homologous Superfamily
B, D	IPR002453	Beta tubulin	Family
B, D	IPR013838	Beta tubulin, autoregulation binding site	Binding Site
B, D	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
B, D	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
E	IPR000956	Stathmin family	Family
E	IPR030514	Stathmin, conserved site	Conserved Site
E	IPR036002	Stathmin superfamily	Homologous Superfamily