Annotations: 1AYF

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ayfa_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin-related	Adrenodoxin	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B	d1ayfb_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin-related	Adrenodoxin	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	2Fe-2S ferredoxin-like	8038589	3000113	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	2Fe-2S ferredoxin-like	8038589	3000113	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	Fer2	e1ayfA1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: Fer2	ECOD (1.6)
B	Fer2	e1ayfB1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: Fer2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)
B	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00111	2Fe-2S iron-sulfur cluster binding domain (Fer2)	2Fe-2S iron-sulfur cluster binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ADRENODOXIN	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding metal cluster binding small molecule binding electron transfer activity cation binding ion binding metal ion binding	cellular metabolic process electron transport chain metabolic process cellular process generation of precursor metabolites and energy biosynthetic process regulation of hormone levels biological regulation regulation of biological quality hormone biosynthetic process hormone metabolic process steroid metabolic process lipid biosynthetic process primary metabolic process cellular metabolic process electron transport chain metabolic process cellular process generation of precursor metabolites and energy biosynthetic process regulation of hormone levels biological regulation regulation of biological quality hormone biosynthetic process hormone metabolic process steroid metabolic process lipid biosynthetic process primary metabolic process steroid biosynthetic process lipid metabolic process P450-containing electron transport chain cellular respiration energy derivation by oxidation of organic compounds respiratory electron transport chain secondary alcohol metabolic process organic hydroxy compound metabolic process sterol metabolic process cholesterol metabolic process alcohol metabolic process small molecule metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
A, B	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
A, B	IPR001055	Adrenodoxin-like	Family
A, B	IPR018298	Adrenodoxin, iron-sulphur binding site	Binding Site
A, B	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily

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.