1S2E

BACTERIOPHAGE T4 GENE PRODUCT 9 (GP9), THE TRIGGER OF TAIL CONTRACTION AND THE LONG TAIL FIBERS CONNECTOR, ALTERNATIVE FIT OF THE FIRST 19 RESIDUES

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1s2ea_	All beta proteins	gp9	gp9	gp9	gp9	(Tequatrovirus T4 ) [TaxId: 10665 ],	SCOPe (2.08)
B	d1s2eb_	All beta proteins	gp9	gp9	gp9	gp9	(Tequatrovirus T4 ) [TaxId: 10665 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	gp9	8028872	4001664	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	gp9	8041251	3000227	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	gp9	8041251	3000227	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	T4_gp9_10_C	e1s2eA2	A: beta sandwiches	X: gp9 C-terminal domain-like	H: gp9 C-terminal domain-related (From Topology)	T: gp9 C-terminal domain-related	F: T4_gp9_10_C	ECOD (1.6)
A	T4_gp9_10_N	e1s2eA1	A: beta sandwiches	X: gp9 N-terminal domain-like	H: gp9 N-terminal domain-related (From Topology)	T: gp9 N-terminal domain-related	F: T4_gp9_10_N	ECOD (1.6)
B	T4_gp9_10_C	e1s2eB2	A: beta sandwiches	X: gp9 C-terminal domain-like	H: gp9 C-terminal domain-related (From Topology)	T: gp9 C-terminal domain-related	F: T4_gp9_10_C	ECOD (1.6)
B	T4_gp9_10_N	e1s2eB1	A: beta sandwiches	X: gp9 N-terminal domain-like	H: gp9 N-terminal domain-related (From Topology)	T: gp9 N-terminal domain-related	F: T4_gp9_10_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.5.960	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Bacteriophage t4 gene product 9 (gp9)	CATH (4.3.0)
A	2.60.120.640	Mainly Beta	Sandwich	Jelly Rolls	gp9	CATH (4.3.0)
A	2.60.40.1680	Mainly Beta	Sandwich	Immunoglobulin-like	4-oxalocrotonate tautomerase-like	CATH (4.3.0)
B	1.20.5.960	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Bacteriophage t4 gene product 9 (gp9)	CATH (4.3.0)
B	2.60.120.640	Mainly Beta	Sandwich	Jelly Rolls	gp9	CATH (4.3.0)
B	2.60.40.1680	Mainly Beta	Sandwich	Immunoglobulin-like	4-oxalocrotonate tautomerase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07880	Bacteriophage T4 gp9/10-like protein, N-terminal (T4_gp9_10_N)	Bacteriophage T4 gp9/10-like protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Baseplate structural protein Gp9	-	exit from host cell biological process involved in interspecies interaction between organisms viral process viral release from host cell viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction virion assembly viral tail assembly	virus tail virion component virus tail, baseplate

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036240	Gp9-like superfamily	Homologous Superfamily
A, B	IPR027412	Baseplate structural protein Gp9 C-terminal domain superfamily	Homologous Superfamily
A, B	IPR008987	Baseplate structural protein Gp9/Gp10	Domain
A, B	IPR027411	Baseplate structural protein Gp9/Gp10 middle 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.