Annotations: 3GFZ

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Acylphosphatase/BLUF domain-like	8087187	3000165	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Acylphosphatase/BLUF domain-like	8087187	3000165	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	BLUF	e3gfzA1	A: a+b two layers	X: Alpha-beta plaits	H: Acylphosphatase-like (From Topology)	T: Acylphosphatase-like	F: BLUF	ECOD (1.6)
A	EAL	e3gfzA2	A: a/b barrels	X: TIM beta/alpha-barrel	H: EAL domain (From Topology)	T: EAL domain	F: EAL	ECOD (1.6)
B	BLUF	e3gfzB4	A: a+b two layers	X: Alpha-beta plaits	H: Acylphosphatase-like (From Topology)	T: Acylphosphatase-like	F: BLUF	ECOD (1.6)
B	EAL	e3gfzB3	A: a/b barrels	X: TIM beta/alpha-barrel	H: EAL domain (From Topology)	T: EAL domain	F: EAL	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.20.20.450	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	EAL domain	CATH (4.3.0)
B	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.20.20.450	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	EAL domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04940	Sensors of blue-light using FAD (BLUF)	Sensors of blue-light using FAD	The BLUF domain has been shown to bind FAD in the AppA protein (Swiss:Q53119). AppA is involved in the repression of photosynthesis genes in response to blue-light.	Domain
A, B	PF00563	EAL domain (EAL)	EAL domain	This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function [1]. The domain contains many conserved acidic residues tha ...	This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function [1]. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Klebsiella pneumoniae BlrP1	blue light photoreceptor activity molecular transducer activity photoreceptor activity signaling receptor activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding blue light photoreceptor activity molecular transducer activity photoreceptor activity signaling receptor activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding cation binding metal ion binding identical protein binding protein binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007024	BLUF domain	Domain
A, B	IPR036046	Acylphosphatase-like domain superfamily	Homologous Superfamily
A, B	IPR001633	EAL domain	Domain
A, B	IPR035919	EAL domain superfamily	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.