1DOQ | pdb_00001doq

THE C-TERMINAL DOMAIN OF THE RNA POLYMERASE ALPHA SUBUNIT FROM THERMUS THERMOPHILUS

External Resource: Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1doqa_	All alpha proteins	SAM domain-like	C-terminal domain of RNA polymerase alpha subunit	C-terminal domain of RNA polymerase alpha subunit	C-terminal domain of RNA polymerase alpha subunit	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	C-terminal domain of RNA polymerase alpha subunit	8025343	4001030	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	C-terminal domain of RNA polymerase alpha subunit	8037722	3000519	SCOP2 (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	RNA_pol_A_CTD	e1doqA1	A: alpha arrays	X: HhH/H2TH	H: SAM/DNA-glycosylase	T: SAM domain-like	F: RNA_pol_A_CTD	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.150.20	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF03118	Bacterial RNA polymerase, alpha chain C terminal domain (RNA_pol_A_CTD)	Bacterial RNA polymerase, alpha chain C terminal domain	The alpha subunit of RNA polymerase consists of two independently folded domains, referred to as amino-terminal and carboxyl terminal domains. The amino terminal domain is involved in the interaction with the other subunits of the RNA polymerase. T ...	The alpha subunit of RNA polymerase consists of two independently folded domains, referred to as amino-terminal and carboxyl terminal domains. The amino terminal domain is involved in the interaction with the other subunits of the RNA polymerase. The carboxyl-terminal domain interacts with the DNA and activators. The amino acid sequence of the alpha subunit is conserved in prokaryotic and chloroplast RNA polymerases. There are three regions of particularly strong conservation, two in the amino-terminal and one in the carboxyl- terminal [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	RNA POLYMERASE ALPHA SUBUNIT	DNA binding binding nucleic acid binding protein binding protein dimerization activity	-	cellular anatomical structure intracellular anatomical structure cytoplasm transferase complex, transferring phosphorus-containing groups protein-containing complex catalytic complex RNA polymerase complex DNA-directed RNA polymerase complex transferase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011773	DNA-directed RNA polymerase, alpha subunit	Family
A	IPR011262	DNA-directed RNA polymerase, insert domain	Domain
A	IPR011260	RNA polymerase, alpha subunit, C-terminal	Domain
A	IPR011263	DNA-directed RNA polymerase, RpoA/D/Rpb3-type	Domain
A	IPR036643	DNA-directed RNA polymerase, insert domain superfamily	Homologous Superfamily
A	IPR036603	RNA polymerase, RBP11-like subunit	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.