5I4R

Contact-dependent inhibition system from Escherichia coli NC101 - ternary CdiA/CdiI/EF-Tu complex (trypsin-modified)

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C [auth D]	SCOP2B Superfamily	EF-Tu post-G domain-like	8056352	3002024	SCOP2B (2022-06-29)
C [auth D]	SCOP2B Superfamily	EF-Tu post-G domain-like	8056350	3002024	SCOP2B (2022-06-29)
G [auth H]	SCOP2B Superfamily	EF-Tu post-G domain-like	8056352	3002024	SCOP2B (2022-06-29)
G [auth H]	SCOP2B Superfamily	EF-Tu post-G domain-like	8056350	3002024	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	UNK_F_TYPE	e5i4rA1	A: a+b two layers	X: RelE-like	H: RelE-like (From Topology)	T: RelE-like	F: UNK_F_TYPE	ECOD (1.6)
E	UNK_F_TYPE	e5i4rE1	A: a+b two layers	X: RelE-like	H: RelE-like (From Topology)	T: RelE-like	F: UNK_F_TYPE	ECOD (1.6)
C [auth D]	GTP_EFTU_D2_1	e5i4rD2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2_1	ECOD (1.6)
C [auth D]	GTP_EFTU_D3	e5i4rD1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Aminomethyltransferase beta-barrel domain	F: GTP_EFTU_D3	ECOD (1.6)
C [auth D]	MnmE_helical_2nd	e5i4rD3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)
G [auth H]	GTP_EFTU_D2_1	e5i4rH2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2_1	ECOD (1.6)
G [auth H]	GTP_EFTU_D3	e5i4rH1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Aminomethyltransferase beta-barrel domain	F: GTP_EFTU_D3	ECOD (1.6)
G [auth H]	MnmE_helical_2nd	e5i4rH3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)
D [auth B]	UNK_F_TYPE	e5i4rB1	A: alpha bundles	X: Four-helical up-and-down bundle	H: Flagellar cap protein FliD helical bundle domain (From Topology)	T: Flagellar cap protein FliD helical bundle domain	F: UNK_F_TYPE	ECOD (1.6)
H [auth F]	UNK_F_TYPE	e5i4rF1	A: alpha bundles	X: Four-helical up-and-down bundle	H: Flagellar cap protein FliD helical bundle domain (From Topology)	T: Flagellar cap protein FliD helical bundle domain	F: UNK_F_TYPE	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C [auth D]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
C [auth D]	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
G [auth H]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
G [auth H]	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
C [auth D], G [auth H]	PF00009	Elongation factor Tu GTP binding domain (GTP_EFTU)	Elongation factor Tu GTP binding domain	This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.	Domain
C [auth D], G [auth H]	PF03143	Elongation factor Tu C-terminal domain (GTP_EFTU_D3)	Elongation factor Tu C-terminal domain	Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA [1] and binding to EF-Ts Pfam:PF00889 [2].	Domain
C [auth D], G [auth H]	PF03144	Elongation factor Tu domain 2 (GTP_EFTU_D2)	Elongation factor Tu domain 2	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, E	Contact-dependent inhibitor A	endonuclease activity nuclease activity hydrolase activity, acting on ester bonds hydrolase activity catalytic activity toxin activity	-	cellular anatomical structure extracellular region
B [auth C], F [auth G]	Elongation factor Tu	guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding translation regulator activity translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding RNA binding GTP binding purine ribonucleoside triphosphate 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	response to stimulus response to chemical response to antibiotic biosynthetic process translational elongation metabolic process cellular process primary metabolic process macromolecule metabolic process protein metabolic process translation gene expression macromolecule biosynthetic process	cell periphery cellular anatomical structure plasma membrane membrane intracellular anatomical structure cytoplasm protein-containing complex guanyl-nucleotide exchange factor complex intracellular protein-containing complex
C [auth D], G [auth H]	Elongation factor Tu	guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding translation regulator activity translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding RNA binding GTP binding purine ribonucleoside triphosphate 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	response to stimulus response to chemical response to antibiotic biosynthetic process translational elongation metabolic process cellular process primary metabolic process macromolecule metabolic process protein metabolic process translation gene expression macromolecule biosynthetic process	cell periphery cellular anatomical structure plasma membrane membrane intracellular anatomical structure cytoplasm protein-containing complex guanyl-nucleotide exchange factor complex intracellular protein-containing complex
D [auth B], H [auth F]	Contact-dependent inhibitor I	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, E	IPR006626	Parallel beta-helix repeat	Repeat
A, E	IPR008638	Filamentous haemagglutinin FhaB/tRNA nuclease CdiA-like, TPS domain	Domain
A, E	IPR012334	Pectin lyase fold	Homologous Superfamily
A, E	IPR049271	Domain of unknown function DUF6862	Domain
A, E	IPR006914	VENN motif-containing domain	Domain
A, E	IPR025157	Hemagglutinin repeat	Repeat
A, E	IPR010069	Toxin CdiA-like, Filamentous hemagglutinin motif repeats	Repeat
A, E	IPR011050	Pectin lyase fold/virulence factor	Homologous Superfamily
B [auth C], F [auth G]	IPR005225	Small GTP-binding domain	Domain
B [auth C], F [auth G]	IPR000795	Translational (tr)-type GTP-binding domain	Domain
B [auth C], F [auth G]	IPR033720	Elongation factor Tu, domain 2	Domain
B [auth C], F [auth G]	IPR009001	Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal	Homologous Superfamily
B [auth C], F [auth G]	IPR031157	Tr-type G domain, conserved site	Conserved Site
B [auth C], F [auth G]	IPR004541	Translation elongation factor EFTu/EF1A, bacterial/organelle	Family
B [auth C], F [auth G]	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
B [auth C], F [auth G]	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
B [auth C], F [auth G]	IPR004160	Translation elongation factor EFTu/EF1A, C-terminal	Domain
B [auth C], F [auth G]	IPR050055	Elongation factor Tu GTPase	Family
B [auth C], F [auth G]	IPR041709	Elongation factor Tu (EF-Tu), GTP-binding domain	Domain
B [auth C], F [auth G]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
C [auth D], G [auth H]	IPR005225	Small GTP-binding domain	Domain
C [auth D], G [auth H]	IPR000795	Translational (tr)-type GTP-binding domain	Domain
C [auth D], G [auth H]	IPR033720	Elongation factor Tu, domain 2	Domain
C [auth D], G [auth H]	IPR009001	Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal	Homologous Superfamily
C [auth D], G [auth H]	IPR031157	Tr-type G domain, conserved site	Conserved Site
C [auth D], G [auth H]	IPR004541	Translation elongation factor EFTu/EF1A, bacterial/organelle	Family
C [auth D], G [auth H]	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
C [auth D], G [auth H]	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
C [auth D], G [auth H]	IPR004160	Translation elongation factor EFTu/EF1A, C-terminal	Domain
C [auth D], G [auth H]	IPR050055	Elongation factor Tu GTPase	Family
C [auth D], G [auth H]	IPR041709	Elongation factor Tu (EF-Tu), GTP-binding domain	Domain
C [auth D], G [auth H]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
D [auth B], H [auth F]	IPR049759	Immunity protein CdiI-like	Family