Annotations: 2QZA

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pentapeptide_4	e2qzaA1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pentapeptide repeats (From Topology)	T: Pentapeptide repeats	F: Pentapeptide_4	ECOD (1.6)
A	SopA_C	e2qzaA2	A: a+b complex topology	X: E3 ubiquitin-protein ligase SopA catalytic domain (From Topology)	H: E3 ubiquitin-protein ligase SopA catalytic domain (From Topology)	T: E3 ubiquitin-protein ligase SopA catalytic domain	F: SopA_C	ECOD (1.6)
B	Pentapeptide_4	e2qzaB1	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Pentapeptide repeats (From Topology)	T: Pentapeptide repeats	F: Pentapeptide_4	ECOD (1.6)
B	SopA_C	e2qzaB2	A: a+b complex topology	X: E3 ubiquitin-protein ligase SopA catalytic domain (From Topology)	H: E3 ubiquitin-protein ligase SopA catalytic domain (From Topology)	T: E3 ubiquitin-protein ligase SopA catalytic domain	F: SopA_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.160.20.80	Mainly Beta	3 Solenoid	Pectate Lyase C-like	E3 ubiquitin-protein ligase SopA	CATH (4.3.0)
A	1.25.40.300	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Putative secreted effector protein	CATH (4.3.0)
A	3.40.1850.10	Alpha Beta	3-Layer(aba) Sandwich	HECT-like ubiquitin ligase fold	HECT-like ubiquitin ligase	CATH (4.3.0)
A	1.10.4140.10	Mainly Alpha	Orthogonal Bundle	effector protein (NleL) fold	effector protein (NleL)	CATH (4.3.0)
B	2.160.20.80	Mainly Beta	3 Solenoid	Pectate Lyase C-like	E3 ubiquitin-protein ligase SopA	CATH (4.3.0)
B	1.25.40.300	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Putative secreted effector protein	CATH (4.3.0)
B	3.40.1850.10	Alpha Beta	3-Layer(aba) Sandwich	HECT-like ubiquitin ligase fold	HECT-like ubiquitin ligase	CATH (4.3.0)
B	1.10.4140.10	Mainly Alpha	Orthogonal Bundle	effector protein (NleL) fold	effector protein (NleL)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13979	SopA-like catalytic domain (SopA_C)	SopA-like catalytic domain	This domain is found in the E. coli Type III secretion effector proteins SopA and NleL [1,2]. These proteins have been shown to act as E3 ubiquitin ligase enzymes. This domain contains the active site cysteine residue.	Domain
A, B	PF13981	SopA-like central domain (SopA)	SopA-like central domain	This domain is found in the E. coli Type III secretion effector proteins SopA and NleL [1,2]. These proteins have been shown to act as E3 ubiquitin ligase enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Secreted effector protein	aminoacyltransferase activity ubiquitin-like protein transferase activity catalytic activity, acting on a protein acyltransferase activity transferase activity catalytic activity ubiquitin-protein transferase activity	primary metabolic process protein ubiquitination macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein modification by small protein conjugation protein modification by small protein conjugation or removal	host cellular component cellular anatomical structure host cell extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR025726	E3 ubiquitin ligase SopA-like central domain	Domain
A, B	IPR038270	SopA-like, catalytic domain superfamily	Homologous Superfamily
A, B	IPR025725	E3 ubiquitin-protein ligase SopA-like, catalytic 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.