Annotations: 1R8D

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C [auth A]	d1r8da_	All alpha proteins	Putative DNA-binding domain	Putative DNA-binding domain	DNA-binding N-terminal domain of transcription activators	Multidrug transporter activator MtaN	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
D [auth B]	d1r8db_	All alpha proteins	Putative DNA-binding domain	Putative DNA-binding domain	DNA-binding N-terminal domain of transcription activators	Multidrug transporter activator MtaN	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C [auth A]	SCOP2 Family	DNA-binding N-terminal domain of transcription activators	8026402	4000766	SCOP2 (2022-06-29)
C [auth A]	SCOP2 Superfamily	Putative DNA-binding domain	8038781	3000158	SCOP2 (2022-06-29)
C [auth A]	SCOP2 Superfamily	Dimerization domain of Mer-like transcriptional regulators	8061312	3002692	SCOP2 (2022-06-29)
D [auth B]	SCOP2B Superfamily	Putative DNA-binding domain	8038781	3000158	SCOP2B (2022-06-29)
D [auth B]	SCOP2B Superfamily	Dimerization domain of Mer-like transcriptional regulators	8061312	3002692	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)
C [auth A]	MerR_1	e1r8dA1	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: MerR_1	ECOD (1.6)
D [auth B]	MerR_1	e1r8dB1	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: MerR_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C [auth A]	1.10.1660.10	Mainly Alpha	Orthogonal Bundle	Multidrug-efflux Transporter Regulator	Chain: A	CATH (4.3.0)
D [auth B]	1.10.1660.10	Mainly Alpha	Orthogonal Bundle	Multidrug-efflux Transporter Regulator	Chain: A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
C [auth A], D [auth B]	PF09278	MerR, DNA binding (MerR-DNA-bind)	MerR, DNA binding	Members of this family of DNA-binding domains are predominantly found in the prokaryotic transcriptional regulator MerR. They adopt a structure consisting of a core of three alpha helices, with an architecture that is similar to that of the 'winged h ...	Members of this family of DNA-binding domains are predominantly found in the prokaryotic transcriptional regulator MerR. They adopt a structure consisting of a core of three alpha helices, with an architecture that is similar to that of the 'winged helix' fold [1].	Domain
C [auth A], D [auth B]	PF00376	MerR family regulatory protein (MerR)	MerR family regulatory protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B [auth D]	26-MER	-	-	-
C [auth A], D [auth B]	transcription activator MtaN	DNA binding binding organic cyclic compound binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity
A [auth C]	26-MER	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
C [auth A], D [auth B]	IPR009061	Putative DNA-binding domain superfamily	Homologous Superfamily
C [auth A], D [auth B]	IPR047057	MerR transcriptional regulator	Family
C [auth A], D [auth B]	IPR012925	TipAS antibiotic-recognition domain	Domain
C [auth A], D [auth B]	IPR036244	TipA-like multidrug resistance regulator, antibiotic-recognition domain	Homologous Superfamily
C [auth A], D [auth B]	IPR000551	MerR-type HTH domain	Domain

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.