Annotations: 4GT2

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth A]	PF04261	e4gt2A2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF04261	ECOD (1.6)
B [auth A]	PF20628	e4gt2A1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF20628	ECOD (1.6)
C [auth E]	PF04261	e4gt2E4	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF04261	ECOD (1.6)
C [auth E]	PF20628	e4gt2E3	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF20628	ECOD (1.6)
D [auth G]	PF04261	e4gt2G4	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF04261	ECOD (1.6)
D [auth G]	PF20628	e4gt2G3	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF20628	ECOD (1.6)
A [auth B]	PF04261	e4gt2B4	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF04261	ECOD (1.6)
A [auth B]	PF20628	e4gt2B3	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: PF20628	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A], C [auth E], D [auth G]	PF04261	Dyp-type peroxidase, N-terminal (Dyp_perox_N)	Dyp-type peroxidase, N-terminal	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much ...	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much lower pH conditions compared with the other plant peroxidases [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the N-terminal domain [2,3,4].	Domain
A [auth B], B [auth A], C [auth E], D [auth G]	PF20628	Dyp-type peroxidase, C-terminal (Dyp_perox_C)	Dyp-type peroxidase, C-terminal	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much ...	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much lower pH conditions compared with the other plant peroxidases [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the C-terminal domain, which possess a large hydrophobic cavity for heme binding [2,3,4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A], C [auth E], D [auth G]	Putative uncharacterized protein SCO3963	lyase activity ferrochelatase activity catalytic activity peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding lyase activity ferrochelatase activity catalytic activity peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	cellular localization inorganic ion homeostasis iron import into cell homeostatic process transport iron ion transport establishment of localization metal ion transport localization intracellular iron ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis establishment of localization in cell monoatomic ion homeostasis cellular localization inorganic ion homeostasis iron import into cell homeostatic process transport iron ion transport establishment of localization metal ion transport localization intracellular iron ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis establishment of localization in cell monoatomic ion homeostasis intracellular chemical homeostasis transition metal ion transport monoatomic ion transport cellular process monoatomic cation homeostasis monoatomic cation transport intracellular monoatomic ion homeostasis	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A], C [auth E], D [auth G]	IPR048327	Dyp-type peroxidase, N-terminal domain	Domain
A [auth B], B [auth A], C [auth E], D [auth G]	IPR006314	Dyp-type peroxidase	Family
A [auth B], B [auth A], C [auth E], D [auth G]	IPR006313	Deferrochelatase	Family
A [auth B], B [auth A], C [auth E], D [auth G]	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A [auth B], B [auth A], C [auth E], D [auth G]	IPR048328	Dyp-type peroxidase, C-terminal domain	Domain
A [auth B], B [auth A], C [auth E], D [auth G]	IPR011008	Dimeric alpha-beta barrel	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 R01GM133198.