Annotations: 1B4A

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1b4aa1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
A	d1b4aa2	Alpha and beta proteins (a+b)	DCoH-like	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d1b4ab1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d1b4ab2	Alpha and beta proteins (a+b)	DCoH-like	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
C	d1b4ac1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
C	d1b4ac2	Alpha and beta proteins (a+b)	DCoH-like	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
D	d1b4ad1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
D	d1b4ad2	Alpha and beta proteins (a+b)	DCoH-like	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
E	d1b4ae1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
E	d1b4ae2	Alpha and beta proteins (a+b)	DCoH-like	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
F	d1b4af1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	Arginine repressor (ArgR), N-terminal DNA-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
F	d1b4af2	Alpha and beta proteins (a+b)	DCoH-like	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	C-terminal domain of arginine repressor	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	ArgR-like	8002672	4000153	SCOP2 (2022-06-29)
A	SCOP2 Family	C-terminal domain of arginine repressor	8091641	4001468	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Winged helix DNA-binding domain	8002673	3000034	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ArgR regulatory domain-like	8002675	3000096	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	ArgR regulatory domain-like	8002675	3000096	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Winged helix DNA-binding domain	8002673	3000034	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Winged helix DNA-binding domain	8002673	3000034	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ArgR regulatory domain-like	8002675	3000096	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ArgR regulatory domain-like	8002675	3000096	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Winged helix DNA-binding domain	8002673	3000034	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ArgR regulatory domain-like	8002675	3000096	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Winged helix DNA-binding domain	8002673	3000034	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Winged helix DNA-binding domain	8002673	3000034	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ArgR regulatory domain-like	8002675	3000096	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	Arg_repressor	e1b4aA1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Arg_repressor	ECOD (1.6)
A	Arg_repressor_C	e1b4aA2	A: a+b two layers	X: Glucose permease domain IIB-like	H: arginine repressor C terminal domain-related	T: C-terminal domain of arginine repressor	F: Arg_repressor_C	ECOD (1.6)
B	Arg_repressor	e1b4aB1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Arg_repressor	ECOD (1.6)
B	Arg_repressor_C	e1b4aB2	A: a+b two layers	X: Glucose permease domain IIB-like	H: arginine repressor C terminal domain-related	T: C-terminal domain of arginine repressor	F: Arg_repressor_C	ECOD (1.6)
C	Arg_repressor	e1b4aC1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Arg_repressor	ECOD (1.6)
C	Arg_repressor_C	e1b4aC2	A: a+b two layers	X: Glucose permease domain IIB-like	H: arginine repressor C terminal domain-related	T: C-terminal domain of arginine repressor	F: Arg_repressor_C	ECOD (1.6)
D	Arg_repressor	e1b4aD1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Arg_repressor	ECOD (1.6)
D	Arg_repressor_C	e1b4aD2	A: a+b two layers	X: Glucose permease domain IIB-like	H: arginine repressor C terminal domain-related	T: C-terminal domain of arginine repressor	F: Arg_repressor_C	ECOD (1.6)
E	Arg_repressor	e1b4aE1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Arg_repressor	ECOD (1.6)
E	Arg_repressor_C	e1b4aE2	A: a+b two layers	X: Glucose permease domain IIB-like	H: arginine repressor C terminal domain-related	T: C-terminal domain of arginine repressor	F: Arg_repressor_C	ECOD (1.6)
F	Arg_repressor	e1b4aF1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Arg_repressor	ECOD (1.6)
F	Arg_repressor_C	e1b4aF2	A: a+b two layers	X: Glucose permease domain IIB-like	H: arginine repressor C terminal domain-related	T: C-terminal domain of arginine repressor	F: Arg_repressor_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
A	3.30.1360.40	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
B	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
B	3.30.1360.40	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
C	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
C	3.30.1360.40	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
D	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
D	3.30.1360.40	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
E	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
E	3.30.1360.40	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
F	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
F	3.30.1360.40	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF02863	Arginine repressor, C-terminal domain (Arg_repressor_C)	Arginine repressor, C-terminal domain	This is the C-terminal domain of the arginine repressor, responsible for arginine binding and multimerization [1,2]. It binds mainly Arg, but also ornithine, Pro and Tyr (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.o ...	This is the C-terminal domain of the arginine repressor, responsible for arginine binding and multimerization [1,2]. It binds mainly Arg, but also ornithine, Pro and Tyr (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	ARGININE REPRESSOR	DNA binding binding organic cyclic compound binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity cation binding organic acid binding ion binding anion binding amino acid binding carboxylic acid binding arginine binding small molecule binding	cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly cellular process cellular component organization or biogenesis L-arginine biosynthetic process oxoacid metabolic process glutamine family amino acid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly cellular process cellular component organization or biogenesis L-arginine biosynthetic process oxoacid metabolic process glutamine family amino acid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process alpha-amino acid biosynthetic process regulation of cellular process regulation of arginine biosynthetic process regulation of amino acid biosynthetic process regulation of primary metabolic process regulation of small molecule metabolic process regulation of arginine metabolic process regulation of amino acid metabolic process regulation of biosynthetic process regulation of biological process biological regulation regulation of metabolic process regulation of glutamine family amino acid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR001669	Arginine repressor	Family
A, B, C, D, E A, B, C, D, E, F	IPR020899	Arginine repressor, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR020900	Arginine repressor, DNA-binding domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036251	Arginine repressor, C-terminal domain 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.