Annotations: 1FTS

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ftsa1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	Domain of the SRP/SRP receptor G-proteins	Signal recognition particle receptor, FtsY	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1ftsa2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	GTPase domain of the signal recognition particle receptor FtsY	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Simibi-like P-loop NTPases	8056575	3002018	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8056574	3001834	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	SRP54_N	e1ftsA1	A: alpha bundles	X: Domain of the SRP/SRP receptor G proteins-like	H: Domain of the SRP/SRP receptor G-proteins (From Topology)	T: Domain of the SRP/SRP receptor G-proteins	F: SRP54_N	ECOD (1.6)
A	SRP54	e1ftsA2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: SRP54	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.120.140	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	SRP54, nucleotide-binding domain	CATH (4.3.0)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00448	SRP54-type protein, GTPase domain (SRP54)	SRP54-type protein, GTPase domain	This family includes relatives of the G-domain of the SRP54 family of proteins.	Domain
A	PF02881	SRP54-type protein, helical bundle domain (SRP54_N)	SRP54-type protein, helical bundle domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	FTSY	ribonucleoprotein complex binding protein-containing complex binding binding signal recognition particle binding identical protein binding protein binding protein homodimerization activity protein dimerization activity pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides ribonucleoprotein complex binding protein-containing complex binding binding signal recognition particle binding identical protein binding protein binding protein homodimerization activity protein dimerization activity pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding GTPase activity	cellular response to stimulus cellular response to nutrient levels response to nutrient levels response to stimulus cellular response to stress response to stress stringent response cellular process response to starvation cellular response to starvation protein localization establishment of protein localization cellular localization establishment of protein localization to membrane cellular response to stimulus cellular response to nutrient levels response to nutrient levels response to stimulus cellular response to stress response to stress stringent response cellular process response to starvation cellular response to starvation protein localization establishment of protein localization cellular localization establishment of protein localization to membrane protein targeting localization within membrane protein localization to membrane establishment of localization protein targeting to membrane localization SRP-dependent cotranslational protein targeting to membrane establishment of protein localization to organelle cellular macromolecule localization macromolecule localization protein localization to organelle cotranslational protein targeting to membrane establishment of protein localization to endoplasmic reticulum protein localization to endoplasmic reticulum protein targeting to ER	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane cytoplasmic side of plasma membrane cytoplasmic side of membrane side of membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR004390	Signal-recognition particle receptor FtsY	Family
A	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain	Domain
A	IPR036225	SRP/SRP receptor, N-terminal	Homologous Superfamily
A	IPR042101	Signal recognition particle SRP54, N-terminal domain superfamily	Homologous Superfamily
A	IPR003593	AAA+ ATPase domain	Domain
A	IPR013822	Signal recognition particle SRP54, helical bundle	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	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.