4B0T

Structure of the Pup Ligase PafA of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pup_ligase_N	e4b0tA1	A: a+b two layers	X: Glutamine synthetase-like	H: Glutamine synthetase/guanido kinase (From Topology)	T: Glutamine synthetase/guanido kinase	F: Pup_ligase_N	ECOD (1.6)
A	Pup_ligase_C	e4b0tA2	A: a+b two layers	X: PafA/Dop C-terminal domain (From Topology)	H: PafA/Dop C-terminal domain (From Topology)	T: PafA/Dop C-terminal domain	F: Pup_ligase_C	ECOD (1.6)
B	Pup_ligase_N	e4b0tB1	A: a+b two layers	X: Glutamine synthetase-like	H: Glutamine synthetase/guanido kinase (From Topology)	T: Glutamine synthetase/guanido kinase	F: Pup_ligase_N	ECOD (1.6)
B	Pup_ligase_C	e4b0tB2	A: a+b two layers	X: PafA/Dop C-terminal domain (From Topology)	H: PafA/Dop C-terminal domain (From Topology)	T: PafA/Dop C-terminal domain	F: Pup_ligase_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03136	Pup-ligase protein (Pup_ligase)	Pup-ligase protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PUP--PROTEIN LIGASE	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity transferase activity	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process peptidyl-lysine modification macromolecule modification protein pupylation peptidyl-amino acid modification protein modification process post-translational protein modification protein modification by small protein conjugation protein modification by small protein conjugation or removal proteasomal protein catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004347	Pup ligase/deamidase	Family
A, B	IPR022279	Pup--protein ligase	Family

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.