4R3A

Erythrobacter litoralis EL346 blue-light activated histidine kinase

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)
B	SCOP2B Superfamily	PYP-like sensor domain (PAS domain)	8084698	3000471	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	PYP-like sensor domain (PAS domain)	8084698	3000471	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	HisKA_2	e4r3aB3	A: alpha duplicates or obligate multimers	X: ROP-like	H: Homodimeric domain of signal transducing histidine kinase (From Topology)	T: Homodimeric domain of signal transducing histidine kinase	F: HisKA_2	ECOD (1.6)
B	HATPase_c_2	e4r3aB2	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: HATPase_c_2	ECOD (1.6)
B	PAS	e4r3aB1	A: a+b three layers	X: Profilin-like	H: sensor domains (From Topology)	T: sensor domains	F: PAS	ECOD (1.6)
A	HisKA_2	e4r3aA3	A: alpha duplicates or obligate multimers	X: ROP-like	H: Homodimeric domain of signal transducing histidine kinase (From Topology)	T: Homodimeric domain of signal transducing histidine kinase	F: HisKA_2	ECOD (1.6)
A	HATPase_c_2	e4r3aA1	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: HATPase_c_2	ECOD (1.6)
A	PAS	e4r3aA2	A: a+b three layers	X: Profilin-like	H: sensor domains (From Topology)	T: sensor domains	F: PAS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.450.20	Alpha Beta	2-Layer Sandwich	Beta-Lactamase	PAS domain	CATH (4.3.0)
B	3.30.565.10	Alpha Beta	2-Layer Sandwich	Heat Shock Protein 90	Histidine kinase-like ATPase, C-terminal domain	CATH (4.3.0)
A	3.30.450.20	Alpha Beta	2-Layer Sandwich	Beta-Lactamase	PAS domain	CATH (4.3.0)
A	3.30.565.10	Alpha Beta	2-Layer Sandwich	Heat Shock Protein 90	Histidine kinase-like ATPase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13426	PAS domain (PAS_9)	PAS domain	This domain is found in many signalling proteins in which it functions as a sensor domain. It recognises FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).	Domain
A, B	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (HATPase_c)	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase	This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.	Domain
A, B	PF07568	Histidine kinase (HisKA_2)	Histidine kinase	This is the dimerisation and phosphoacceptor domain of a sub-family of histidine kinases [1]. It shares sequence similarity with Pfam:PF00512 and Pfam:PF07536 [2]. It is usually found adjacent to a C-terminal ATPase domain (Pfam:PF02518). This domain ...	This is the dimerisation and phosphoacceptor domain of a sub-family of histidine kinases [1]. It shares sequence similarity with Pfam:PF00512 and Pfam:PF07536 [2]. It is usually found adjacent to a C-terminal ATPase domain (Pfam:PF02518). This domain is found in a wide range of Bacteria and also several Archaea.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Blue-light-activated histidine kinase 2	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity catalytic activity phosphotransferase activity, nitrogenous group as acceptor phosphotransferase activity, alcohol group as acceptor protein histidine kinase activity transferase activity, transferring phosphorus-containing groups molecular transducer activity photoreceptor activity signaling receptor activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR035965	PAS domain superfamily	Homologous Superfamily
A, B	IPR003594	Histidine kinase/HSP90-like ATPase domain	Domain
A, B	IPR000700	PAS-associated, C-terminal	Domain
A, B	IPR005467	Histidine kinase domain	Domain
A, B	IPR000014	PAS domain	Domain
A, B	IPR004358	Signal transduction histidine kinase-related protein, C-terminal	Domain
A, B	IPR011495	Signal transduction histidine kinase, subgroup 2, dimerisation and phosphoacceptor domain	Domain
A, B	IPR036890	Histidine kinase/HSP90-like ATPase 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.