5L3S

Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY

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	d5l3sa1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	automated matches	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
A	d5l3sa2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
C	d5l3sc1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	automated matches	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
C	d5l3sc2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
E	d5l3se1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	automated matches	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
E	d5l3se2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
G	d5l3sg1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	automated matches	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	SCOPe (2.08)
G	d5l3sg2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Saccharolobus solfataricus P2 ) [TaxId: 273057 ],	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	8056554	3002018	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8056553	3001834	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Simibi-like P-loop NTPases	8056554	3002018	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Simibi-like P-loop NTPases	8056554	3002018	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8056553	3001834	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Simibi-like P-loop NTPases	8056554	3002018	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	e5l3sA1	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	e5l3sA2	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)
C	SRP54_N	e5l3sC2	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)
C	SRP54	e5l3sC1	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)
E	SRP54_N	e5l3sE2	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)
E	SRP54	e5l3sE1	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)
G	SRP54_N	e5l3sG2	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)
G	SRP54	e5l3sG1	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)
F	SRP54_N	e5l3sF1	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)
F	SRP54	e5l3sF2	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)
B	SRP54_N	e5l3sB1	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)
B	SRP54	e5l3sB2	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)
D	SRP54_N	e5l3sD1	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)
D	SRP54	e5l3sD2	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)
H	SRP54_N	e5l3sH2	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)
H	SRP54	e5l3sH1	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	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
C	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
E	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
G	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
F	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
B	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, C, E, G	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
B, D, F, H	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C, E, G	Signal recognition particle 54 kDa protein	RNA binding 7S RNA binding binding organic cyclic compound binding nucleic acid binding 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 RNA binding 7S RNA binding binding organic cyclic compound binding nucleic acid binding 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 purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding GTPase activity	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 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 cellular process establishment of protein localization to endoplasmic reticulum protein localization to endoplasmic reticulum protein targeting to ER	signal recognition particle protein-containing complex intracellular anatomical structure ribonucleoprotein complex cytoplasm cellular anatomical entity
B, D, F, H	Signal recognition particle receptor FtsY	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 binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding 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 binding 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	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 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 cellular process establishment of protein localization to endoplasmic reticulum protein localization to endoplasmic reticulum protein targeting to ER	cell periphery plasma membrane membrane cellular anatomical entity intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C, E, G	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain	Domain
A, C, E, G	IPR022941	Signal recognition particle, SRP54 subunit	Family
A, C, E, G	IPR036225	SRP/SRP receptor, N-terminal	Homologous Superfamily
A, C, E, G	IPR004125	Signal recognition particle, SRP54 subunit, M-domain	Domain
A, C, E, G	IPR042101	Signal recognition particle SRP54, N-terminal domain superfamily	Homologous Superfamily
A, C, E, G	IPR003593	AAA+ ATPase domain	Domain
A, C, E, G	IPR013822	Signal recognition particle SRP54, helical bundle	Domain
A, C, E, G	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, C, E, G	IPR036891	Signal recognition particle, SRP54 subunit, M-domain superfamily	Homologous Superfamily
B, D, F, H	IPR004390	Signal-recognition particle receptor FtsY	Family
B, D, F, H	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain	Domain
B, D, F, H	IPR036225	SRP/SRP receptor, N-terminal	Homologous Superfamily
B, D, F, H	IPR042101	Signal recognition particle SRP54, N-terminal domain superfamily	Homologous Superfamily
B, D, F, H	IPR003593	AAA+ ATPase domain	Domain
B, D, F, H	IPR013822	Signal recognition particle SRP54, helical bundle	Domain
B, D, F, H	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.