6SJ5

Crystal structure of the uL14-RsfS complex from Staphylococcus aureus

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	d6sj5a_	Alpha and beta proteins (a+b)	Nucleotidyltransferase	Nucleotidyltransferase	Iojap/YbeB-like	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d6sj5b_	Alpha and beta proteins (a+b)	Nucleotidyltransferase	Nucleotidyltransferase	Iojap/YbeB-like	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	50S Ribosomal protein L14-like	8093892	3000433	SCOP2B (2022-06-29)
D	SCOP2 Family	Ribosomal protein L14	8093891	4001826	SCOP2 (2022-06-29)
D	SCOP2 Superfamily	50S Ribosomal protein L14-like	8093892	3000433	SCOP2 (2022-06-29)
A	SCOP2 Family	Iojap/YbeB-like	8094846	4001878	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotidyltransferase-like	8094847	3000129	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Nucleotidyltransferase-like	8094847	3000129	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	PF00238	e6sj5C1	A: beta barrels	X: Ribosomal protein L14-like	H: Ribosomal protein L14-related (From Topology)	T: Ribosomal protein L14-related	F: PF00238	ECOD (1.6)
D	PF00238	e6sj5D1	A: beta barrels	X: Ribosomal protein L14-like	H: Ribosomal protein L14-related (From Topology)	T: Ribosomal protein L14-related	F: PF00238	ECOD (1.6)
A	PF02410	e6sj5A1	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: PF02410	ECOD (1.6)
B	PF02410	e6sj5B1	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: PF02410	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	2.40.150.20	Mainly Beta	Beta Barrel	Ribosomal Protein L14	Ribosomal protein L14/L23	CATH (utative)
D	2.40.150.20	Mainly Beta	Beta Barrel	Ribosomal Protein L14	Ribosomal protein L14/L23	CATH (utative)
A	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (utative)
B	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
C, D	PF00238	Ribosomal protein L14p/L23e (Ribosomal_L14)	Ribosomal protein L14p/L23e	-	Domain
A, B	PF02410	Ribosomal silencing factor during starvation (RsfS)	Ribosomal silencing factor during starvation	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
C, D	50S ribosomal protein L14	structural molecule activity structural constituent of ribosome RNA binding binding organic cyclic compound binding rRNA binding nucleic acid binding large ribosomal subunit rRNA binding	organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process primary metabolic process translation gene expression macromolecule biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process primary metabolic process translation gene expression macromolecule biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process	protein-containing complex intracellular anatomical structure cellular anatomical entity intracellular organelle ribosomal subunit cytosolic large ribosomal subunit cytosolic ribosome organelle ribonucleoprotein complex intracellular non-membrane-bounded organelle ribosome cytoplasm cytosol large ribosomal subunit protein-containing complex intracellular anatomical structure cellular anatomical entity intracellular organelle ribosomal subunit cytosolic large ribosomal subunit cytosolic ribosome organelle ribonucleoprotein complex intracellular non-membrane-bounded organelle ribosome cytoplasm cytosol large ribosomal subunit non-membrane-bounded organelle
A, B	Ribosomal silencing factor RsfS	-	regulation of biological process ribonucleoprotein complex biogenesis regulation of cellular process biological regulation negative regulation of biological process regulation of ribosome biogenesis regulation of cellular component biogenesis cellular component biogenesis ribosome biogenesis negative regulation of cellular process negative regulation of ribosome biogenesis cellular process cellular component organization or biogenesis cellular biosynthetic process regulation of biological process ribonucleoprotein complex biogenesis regulation of cellular process biological regulation negative regulation of biological process regulation of ribosome biogenesis regulation of cellular component biogenesis cellular component biogenesis ribosome biogenesis negative regulation of cellular process negative regulation of ribosome biogenesis cellular process cellular component organization or biogenesis cellular biosynthetic process organonitrogen compound biosynthetic process negative regulation of cellular metabolic process regulation of primary metabolic process post-transcriptional regulation of gene expression negative regulation of translation organic substance metabolic process organic substance biosynthetic process protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biosynthetic process organonitrogen compound metabolic process cellular metabolic process regulation of protein metabolic process negative regulation of metabolic process regulation of cellular metabolic process primary metabolic process regulation of macromolecule metabolic process gene expression translation macromolecule biosynthetic process negative regulation of cellular biosynthetic process regulation of cellular biosynthetic process regulation of gene expression negative regulation of gene expression biosynthetic process negative regulation of biosynthetic process regulation of translation negative regulation of macromolecule biosynthetic process regulation of macromolecule biosynthetic process metabolic process macromolecule metabolic process regulation of metabolic process organelle assembly non-membrane-bounded organelle assembly cellular component organization organelle organization cellular component assembly cytosolic ribosome assembly ribosome assembly	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
C, D	IPR005745	Large ribosomal subunit protein uL14, bacterial-type	Family
C, D	IPR036853	Large ribosomal subunit protein uL14 superfamily	Homologous Superfamily
C, D	IPR000218	Large ribosomal subunit protein uL14	Family
C, D	IPR019972	Large ribosomal subunit protein uL14, conserved site	Conserved Site
A, B	IPR043519	Nucleotidyltransferase superfamily	Homologous Superfamily
A, B	IPR004394	Protein Iojap/ribosomal silencing factor RsfS	Family

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.