1H4X

Structure of the Bacillus Cell Fate Determinant SpoIIAA in the Phosphorylated Form

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1h4xa_	Alpha and beta proteins (a/b)	SpoIIaa-like	SpoIIaa-like	Anti-sigma factor antagonist SpoIIaa	Anti-sigma factor antagonist SpoIIaa	(Lysinibacillus sphaericus ) [TaxId: 1421 ],	SCOPe (2.08)
B	d1h4xb_	Alpha and beta proteins (a/b)	SpoIIaa-like	SpoIIaa-like	Anti-sigma factor antagonist SpoIIaa	Anti-sigma factor antagonist SpoIIaa	(Lysinibacillus sphaericus ) [TaxId: 1421 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Anti-sigma factor antagonist SpoIIaa	8020530	4003567	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SpoIIaa-like	8032910	3001065	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	SpoIIaa-like	8032910	3001065	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	PF01740	e1h4xA1	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: PF01740	ECOD (1.6)
B	PF01740	e1h4xB1	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: PF01740	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.750.24	Alpha Beta	2-Layer Sandwich	Transcription Regulator spoIIAA	STAS domain	CATH (4.3.0)
B	3.30.750.24	Alpha Beta	2-Layer Sandwich	Transcription Regulator spoIIAA	STAS domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01740	STAS domain (STAS)	STAS domain	The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding ...	The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ANTI-SIGMA F FACTOR ANTAGONIST	transcription regulator activity anti-sigma factor antagonist activity protein binding binding antisigma factor binding	sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036513	STAS domain superfamily	Homologous Superfamily
A, B	IPR014237	Anti-sigma F factor antagonist	Family
A, B	IPR002645	STAS domain	Domain
A, B	IPR003658	Anti-sigma factor antagonist	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	SEP	Parent Component: SER RESID: AA0037 PSI-MOD : O-phospho-L-serine MOD:00046

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 R01GM133198.