6RAP

Cryo-EM structure of the anti-feeding prophage cap (AFP tube terminating cap)

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth B]	UNK_F_TYPE	e6rapB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel	F: UNK_F_TYPE	ECOD (1.6)
B [auth A]	UNK_F_TYPE	e6rapA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel	F: UNK_F_TYPE	ECOD (1.6)
C	Phage_sheath_1C	e6rapC1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: gpW/gp25-like (From Topology)	T: gpW/gp25-like	F: Phage_sheath_1C	ECOD (1.6)
C	Phage_sheath_1	e6rapC2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Domain III of tail sheath protein Gp18 (From Topology)	T: Domain III of tail sheath protein Gp18	F: Phage_sheath_1	ECOD (1.6)
D	Phage_sheath_1C	e6rapD1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: gpW/gp25-like (From Topology)	T: gpW/gp25-like	F: Phage_sheath_1C	ECOD (1.6)
D	Phage_sheath_1	e6rapD2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Domain III of tail sheath protein Gp18 (From Topology)	T: Domain III of tail sheath protein Gp18	F: Phage_sheath_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF06841	T4-like virus tail tube protein gp19 (Phage_T4_gp19)	T4-like virus tail tube protein gp19	-	Family
C	PF17482	Phage tail sheath C-terminal domain (Phage_sheath_1C)	Phage tail sheath C-terminal domain	This entry represents the C-terminal domain in a variety of phage tail sheath proteins [4].	Domain
C	PF04984	Phage tail sheath protein subtilisin-like domain (Phage_sheath_1)	Phage tail sheath protein subtilisin-like domain	This entry represents the second domain in a variety of phage tail sheath proteins. According to ECOD this domain has a subtilisin-like structure.	Domain
D	PF17482	Phage tail sheath C-terminal domain (Phage_sheath_1C)	Phage tail sheath C-terminal domain	This entry represents the C-terminal domain in a variety of phage tail sheath proteins [4].	Domain
E	PF14065	Pvc16 N-terminal domain (Pvc16_N)	Pvc16 N-terminal domain	This protein forms part of a contractile injection system [1]. Photorhabdus virulence cassette (PVC) represents one group of extracellular CISs that are present in both bacteria and archaea [1]. This entry include Pvc16. This family of proteins is f ...	This protein forms part of a contractile injection system [1]. Photorhabdus virulence cassette (PVC) represents one group of extracellular CISs that are present in both bacteria and archaea [1]. This entry include Pvc16. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 190 and 320 amino acids in length. This domain alone in Pvc16 is able to produce PVC particles with normal length but without the outer sheath, indicating the main function of this N-terminal domain in terminating the tube growth [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Afp1	structural molecule activity	-	-
C	Afp2	-	-	-
D	Afp3	-	-	-
E	Afp16	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR011747	Conserved hypothetical protein CHP02241	Family
A [auth B], B [auth A]	IPR010667	Bacteriophage T4, Gp19, tail tube	Family
C	IPR020287	Tail sheath protein, C-terminal domain	Domain
C	IPR035089	Tail sheath protein, subtilisin-like domain	Domain
D	IPR020287	Tail sheath protein, C-terminal domain	Domain
D	IPR035089	Tail sheath protein, subtilisin-like domain	Domain
E	IPR025351	Pvc16, N-terminal	Domain

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.