1IB8

SOLUTION STRUCTURE AND FUNCTION OF A CONSERVED PROTEIN SP14.3 ENCODED BY AN ESSENTIAL STREPTOCOCCUS PNEUMONIAE GENE

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	d1ib8a1	All beta proteins	Sm-like fold	YhbC-like, C-terminal domain	YhbC-like, C-terminal domain	Hypothetical protein SP14.3 (SP0552)	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
A	d1ib8a2	Alpha and beta proteins (a+b)	Alpha-lytic protease prodomain-like	YhbC-like, N-terminal domain	YhbC-like, N-terminal domain	Hypothetical protein SP14.3 (SP0552)	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	YhbC-like N-terminal domain	8027176	4002612	SCOP2 (2022-06-29)
A	SCOP2 Family	YhbC-like C-terminal domain	8027175	4002169	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	YhbC-like N-terminal domain	8039555	3001482	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	YhbC-like C-terminal domain	8039554	3000906	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	DUF150_C	e1ib8A1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: DUF150_C	ECOD (1.6)
A	DUF150	e1ib8A2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: YhbC-like, N-terminal domain (From Topology)	T: YhbC-like, N-terminal domain	F: DUF150	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.300.70	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
A	2.30.30.180	Mainly Beta	Roll	SH3 type barrels.	Ribosome maturation factor RimP, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF17384	RimP C-terminal SH3 domain (DUF150_C)	RimP C-terminal SH3 domain	This family represents the C-terminal domain from RimP.	Domain
A	PF02576	RimP N-terminal domain (RimP_N)	RimP N-terminal domain	This entry represents the N-terminal domain of the ribosome maturation factor RimP (also known as yhbC). RimP facilitates the maturation of the 30S ribosomal subunit [1]. The N-terminal domain contains two alpha-helices and a three-stranded beta-shee ...	This entry represents the N-terminal domain of the ribosome maturation factor RimP (also known as yhbC). RimP facilitates the maturation of the 30S ribosomal subunit [1]. The N-terminal domain contains two alpha-helices and a three-stranded beta-sheet. It is suggested that the N-terminal domain of SP14.3 (RimP orthologue) could function as a protein module that binds to other proteins, especially those that contain highly positively charged surfaces. [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CONSERVED PROTEIN SP14.3	-	cellular component biogenesis ribosome biogenesis ribonucleoprotein complex biogenesis cellular process cellular component organization or biogenesis ribosomal small subunit biogenesis	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR028989	Ribosome maturation factor RimP, N-terminal	Domain
A	IPR003728	Ribosome maturation factor RimP	Family
A	IPR036847	Ribosome maturation factor RimP, C-terminal domain superfamily	Homologous Superfamily
A	IPR035956	RimP, N-terminal domain superfamily	Homologous Superfamily
A	IPR028998	Ribosome maturation factor RimP, C-terminal	Domain

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.