Annotations: 1A16

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1a16a1	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Creatinase/prolidase N-terminal domain	Creatinase/prolidase N-terminal domain	Aminopeptidase P	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1a16a2	Alpha and beta proteins (a+b)	Creatinase/aminopeptidase	Creatinase/aminopeptidase	Creatinase/aminopeptidase	Aminopeptidase P, C-terminal domain	(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	Creatinase/prolidase N-terminal domain-like	8037176	3000538	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Creatinase/aminopeptidase catalytic domain-like	8037177	3000126	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	Peptidase_M24	e1a16A1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Peptidase_M24	ECOD (1.6)
A	AMP_N	e1a16A2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Creatinase/prolidase N-terminal domain (From Topology)	T: Creatinase/prolidase N-terminal domain	F: AMP_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.350.10	Alpha Beta	3-Layer(aba) Sandwich	Creatine Amidinohydrolase	Chain A, domain 1	CATH (4.3.0)
A	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05195	Aminopeptidase P, N-terminal domain (AMP_N)	Aminopeptidase P, N-terminal domain	This domain is structurally very similar [1] to the creatinase N-terminal domain (Pfam:PF01321). However, little or no sequence similarity exists between the two families.	Domain
A	PF00557	Metallopeptidase family M24 (Peptidase_M24)	Metallopeptidase family M24	This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	AMINOPEPTIDASE P	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity identical protein binding protein binding	protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis proteolysis metabolic process primary metabolic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001714	Peptidase M24, methionine aminopeptidase	Family
A	IPR001131	Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site	Conserved Site
A	IPR007865	Aminopeptidase P, N-terminal	Domain
A	IPR029149	Creatinase/Aminopeptidase P/Spt16, N-terminal	Homologous Superfamily
A	IPR036005	Creatinase/aminopeptidase-like	Homologous Superfamily
A	IPR000994	Peptidase M24	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	Xaa-Pro aminopeptidase M-CSA #379	Aminopeptidase P cleaves an Xaa-Pro bond at the N-terminal of a polypeptide (even a dipeptide or tripeptide), where Xaa can be any amino acid. This substrate specificity is important as many biologically active peptides have Xaa-Pro at the N-terminus. This protein is part of the peptidase M24B family.	Defined by 11 residues: ASP:A_4-38HIS:A-243ASP:A-260ASP:A-271HIS:A-350HIS:A-354HIS:A-361GLU:A-383TYR:A-387ARG:A-404GLU:A-406 \| Explore in 3D: M-CSA Motif Definition Up to 10 residues are supported for Structure Motif searching, this motif has 11 residues. EC: 3.4.11.9 (PDB Primary Data)

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.