Annotations: 4FFP

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ATP-grasp	e4ffpA3	A: a+b complex topology	X: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)	H: Protein kinase/SAICAR synthase/ATP-grasp	T: ATP-grasp	F: ATP-grasp	ECOD (1.6)
A	ATPgrasp_Ter	e4ffpA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: PreATP-grasp domain	F: ATPgrasp_Ter	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.30.470.20	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21360	PylC-like, N-terminal domain (PylC-like_N)	PylC-like, N-terminal domain	This domain is found in 3-methyl-D-ornithine--L-lysine ligase from Methanosarcina barkeri (PylC) and similar sequences from prokaryotes. PylC is required for the biosynthesis of pyrrolysine. This ATP-grasp enzyme is composed of three domains. This en ...	This domain is found in 3-methyl-D-ornithine--L-lysine ligase from Methanosarcina barkeri (PylC) and similar sequences from prokaryotes. PylC is required for the biosynthesis of pyrrolysine. This ATP-grasp enzyme is composed of three domains. This entry represents the N-terminal domain, which is composed of a central four-stranded beta-sheet that is faced on both sides by two helices. It shows an adenine binding pocket that has not been observed in any homologous structure determined before [1].	Domain
A	PF02655	ATP-grasp domain (ATP-grasp_3)	ATP-grasp domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Putative uncharacterized protein	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding catalytic activity ligase activity cation binding metal ion binding	oxoacid metabolic process small molecule biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process carboxylic acid metabolic process amide biosynthetic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process oxoacid metabolic process small molecule biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process carboxylic acid metabolic process amide biosynthetic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process small molecule metabolic process pyrrolysine biosynthetic process amide metabolic process pyrrolysine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011761	ATP-grasp fold	Domain
A	IPR003806	ATP-grasp fold, PylC-type	Domain
A	IPR023890	Pyrrolysine biosynthesis protein PylC	Family
A	IPR048764	PylC, N-terminal domain	Domain

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.