Annotations: 2XC1

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Pectin lyase-like	8042982	3001746	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Head-binding domain of phage P22 tailspike protein	8043159	3002008	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Pectin lyase-like	8042982	3001746	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Head-binding domain of phage P22 tailspike protein	8043159	3002008	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Pectin lyase-like	8042982	3001746	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Head-binding domain of phage P22 tailspike protein	8043159	3002008	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)
B	Head_binding	e2xc1B1	A: beta sandwiches	X: Head-binding domain of phage P22 tailspike protein (From Topology)	H: Head-binding domain of phage P22 tailspike protein (From Topology)	T: Head-binding domain of phage P22 tailspike protein	F: Head_binding	ECOD (1.6)
B	PhageP22-tail_N	e2xc1B2	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: PhageP22-tail_N	ECOD (1.6)
B	PhageP22-tail_C	e2xc1B3	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: PhageP22-tail_C	ECOD (1.6)
C	Head_binding	e2xc1C1	A: beta sandwiches	X: Head-binding domain of phage P22 tailspike protein (From Topology)	H: Head-binding domain of phage P22 tailspike protein (From Topology)	T: Head-binding domain of phage P22 tailspike protein	F: Head_binding	ECOD (1.6)
C	PhageP22-tail_N	e2xc1C2	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: PhageP22-tail_N	ECOD (1.6)
C	PhageP22-tail_C	e2xc1C3	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: PhageP22-tail_C	ECOD (1.6)
A	Head_binding	e2xc1A2	A: beta sandwiches	X: Head-binding domain of phage P22 tailspike protein (From Topology)	H: Head-binding domain of phage P22 tailspike protein (From Topology)	T: Head-binding domain of phage P22 tailspike protein	F: Head_binding	ECOD (1.6)
A	PhageP22-tail_N	e2xc1A3	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pectin lyase-like (From Topology)	T: Pectin lyase-like	F: PhageP22-tail_N	ECOD (1.6)
A	PhageP22-tail_C	e2xc1A4	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: PhageP22-tail_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.170.14.10	Mainly Beta	Beta Complex	Tailspike Protein	Chain	CATH (4.3.0)
B	2.160.20.20	Mainly Beta	3 Solenoid	Pectate Lyase C-like		CATH (4.3.0)
C	2.170.14.10	Mainly Beta	Beta Complex	Tailspike Protein	Chain	CATH (4.3.0)
C	2.160.20.20	Mainly Beta	3 Solenoid	Pectate Lyase C-like		CATH (4.3.0)
A	2.170.14.10	Mainly Beta	Beta Complex	Tailspike Protein	Chain	CATH (4.3.0)
A	2.160.20.20	Mainly Beta	3 Solenoid	Pectate Lyase C-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF09251	Salmonella phage P22 tail-spike (PhageP22-tail)	Salmonella phage P22 tail-spike	-	Repeat
A, B, C	PF09008	Head binding (Head_binding)	Head binding	The head binding domain found in the Phage P22 tailspike protein contains two regular beta-sheets, A and B, oriented nearly perpendicular to each other and composed of five and three strands respectively. The topology of the strands is exclusively an ...	The head binding domain found in the Phage P22 tailspike protein contains two regular beta-sheets, A and B, oriented nearly perpendicular to each other and composed of five and three strands respectively. The topology of the strands is exclusively antiparallel. The tailspike protein trimerises through this domain, and the direction of the strands with respect to the molecular triad is almost parallel for beta-sheet A, whereas beta-sheet B is perpendicular to the triad, forming a dome-like structure. This domain is dispensable for thermostability and SDS resistance of the intact protein, and its deletion has only minor effects on tailspike folding kinetics [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	BIFUNCTIONAL TAIL PROTEIN	hydrolase activity, acting on glycosyl bonds endo-1,3-alpha-L-rhamnosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	virion attachment to host cell biological process involved in interspecies interaction between organisms adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated disruption of host anatomical structure symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide disruption of cell wall in another organism symbiont-mediated disruption of host cell wall symbiont-mediated disruption of host cell envelope disruption of cellular anatomical structure in another organism virion attachment to host cell biological process involved in interspecies interaction between organisms adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated disruption of host anatomical structure symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide disruption of cell wall in another organism symbiont-mediated disruption of host cell wall symbiont-mediated disruption of host cell envelope disruption of cellular anatomical structure in another organism symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell symbiont entry into host disruption of anatomical structure in another organism metabolic process symbiont entry into host cell via disruption of host cell envelope receptor-mediated virion attachment to host cell adhesion receptor-mediated virion attachment to host cell	virus tail, fiber virus tail virion component

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR036730	Phage P22 tailspike-like, N-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR012332	Autotransporter, pectate lyase C-like domain superfamily	Homologous Superfamily
A, B, C	IPR015331	P22 tailspike C-terminal domain	Domain
A, B, C	IPR009093	Bacteriophage P22 tailspike, N-terminal	Domain
A, B, C	IPR011050	Pectin lyase fold/virulence factor	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.