2CNW

GDPALF4 complex of the SRP GTPases Ffh 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)
D	d2cnwd1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	automated matches	automated matches	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
D	d2cnwd2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
E	d2cnwe1	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	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
E	d2cnwe2	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	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
F	d2cnwf1	All alpha proteins	Four-helical up-and-down bundle	Domain of the SRP/SRP receptor G-proteins	automated matches	automated matches	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
F	d2cnwf2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
A	d2cnwa1	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 sequence recognition protein Ffh	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
A	d2cnwa2	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 sequence recognition protein Ffh	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
B	d2cnwb1	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 sequence recognition protein Ffh	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
B	d2cnwb2	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 sequence recognition protein Ffh	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
C	d2cnwc1	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 sequence recognition protein Ffh	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)
C	d2cnwc2	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 sequence recognition protein Ffh	(Thermus aquaticus ) [TaxId: 271 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2 Family	SRP54-like	8056570	4003997	SCOP2 (2022-06-29)
D	SCOP2 Superfamily	SRP/SRP receptor N-terminal domain-like	8056571	3001834	SCOP2 (2022-06-29)
D	SCOP2 Superfamily	Simibi-like P-loop NTPases	8056572	3002018	SCOP2 (2022-06-29)
E	SCOP2B Superfamily	Simibi-like P-loop NTPases	8056572	3002018	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8056571	3001834	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Simibi-like P-loop NTPases	8056572	3002018	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8056571	3001834	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8089711	3001834	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Simibi-like P-loop NTPases	8089712	3002018	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8089711	3001834	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Simibi-like P-loop NTPases	8089712	3002018	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SRP/SRP receptor N-terminal domain-like	8089711	3001834	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Simibi-like P-loop NTPases	8089712	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)
D	PF02881	e2cnwD1	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: PF02881	ECOD (1.6)
D	PF00448	e2cnwD2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00448	ECOD (1.6)
E	PF02881	e2cnwE1	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: PF02881	ECOD (1.6)
E	PF00448	e2cnwE2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00448	ECOD (1.6)
F	PF02881	e2cnwF1	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: PF02881	ECOD (1.6)
F	PF00448	e2cnwF2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00448	ECOD (1.6)
A	PF02881	e2cnwA1	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: PF02881	ECOD (1.6)
A	PF00448	e2cnwA2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00448	ECOD (1.6)
B	PF02881	e2cnwB1	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: PF02881	ECOD (1.6)
B	PF00448	e2cnwB2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00448	ECOD (1.6)
C	PF02881	e2cnwC1	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: PF02881	ECOD (1.6)
C	PF00448	e2cnwC2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00448	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

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

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
D, E, F	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
D, E, F	PF02881	SRP54-type protein, helical bundle domain (SRP54_N)	SRP54-type protein, helical bundle domain	-	Domain
A, B, C	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, B, C	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
D, E, F	CELL DIVISION PROTEIN 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
A, B, C	SIGNAL RECOGNITION PARTICLE 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

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
D, E, F	IPR004390	Signal-recognition particle receptor FtsY	Family
D, E, F	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain	Domain
D, E, F	IPR036225	SRP/SRP receptor, N-terminal	Homologous Superfamily
D, E, F	IPR042101	Signal recognition particle SRP54, N-terminal domain superfamily	Homologous Superfamily
D, E, F	IPR003593	AAA+ ATPase domain	Domain
D, E, F	IPR013822	Signal recognition particle SRP54, helical bundle	Domain
D, E, F	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B, C	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain	Domain
A, B, C	IPR022941	Signal recognition particle, SRP54 subunit	Family
A, B, C	IPR036225	SRP/SRP receptor, N-terminal	Homologous Superfamily
A, B, C	IPR004125	Signal recognition particle, SRP54 subunit, M-domain	Domain
A, B, C	IPR042101	Signal recognition particle SRP54, N-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR003593	AAA+ ATPase domain	Domain
A, B, C	IPR004780	Signal recognition particle protein	Family
A, B, C	IPR013822	Signal recognition particle SRP54, helical bundle	Domain
A, B, C	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B, C	IPR036891	Signal recognition particle, SRP54 subunit, M-domain superfamily	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 R01GM133198.