Annotations: 1NSL

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1nsla1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	N-acetyl transferase, NAT	Probable acetyltransferase YdaF	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
A	d1nsla2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
B	d1nslb1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	N-acetyl transferase, NAT	Probable acetyltransferase YdaF	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
B	d1nslb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
C	d1nslc1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	N-acetyl transferase, NAT	Probable acetyltransferase YdaF	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
C	d1nslc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
D	d1nsld1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	N-acetyl transferase, NAT	Probable acetyltransferase YdaF	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
D	d1nsld2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
E	d1nsle1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	N-acetyl transferase, NAT	Probable acetyltransferase YdaF	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
E	d1nsle2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
F	d1nslf1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	N-acetyl transferase, NAT	Probable acetyltransferase YdaF	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
F	d1nslf2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	N-acetyltransferase NAT	8021200	4001800	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Acyl-CoA N-acyltransferases (Nat)	8033580	3000403	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8033580	3000403	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8033580	3000403	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8033580	3000403	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8033580	3000403	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8033580	3000403	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	Acetyltransf_3_1	e1nslA1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
B	Acetyltransf_3_1	e1nslB1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
C	Acetyltransf_3_1	e1nslC1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
D	Acetyltransf_3_1	e1nslD1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
E	Acetyltransf_3_1	e1nslE1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
F	Acetyltransf_3_1	e1nslF1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
B	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
C	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
D	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
E	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
F	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00583	Acetyltransferase (GNAT) family (Acetyltransf_1)	Acetyltransferase (GNAT) family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Probable acetyltransferase	acetyltransferase activity N-acetyltransferase activity acyltransferase activity peptide-serine-alpha-N-acetyltransferase activity peptide alpha-N-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity peptide N-acetyltransferase activity catalytic activity N-acyltransferase activity peptide-alanine-alpha-N-acetyltransferase activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR000182	GNAT domain	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.