Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyRibonucleotide reductase-like8030424 4000846 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyFerritin-like8042803 3001658 SCOP2 (2022-06-29)
BSCOP2 FamilyRibonucleotide reductase-like8030425 4000846 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyFerritin-like8042804 3001658 SCOP2 (2022-06-29)
CSCOP2 FamilyTmoB-like8030426 4002430 SCOP2 (2022-06-29)
CSCOP2 SuperfamilyTmoB-like8042805 3001226 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APhenol_Hydroxe2incA1 A: alpha bundlesX: Ferritin/Heme oxygenase/4-helical cytokinesH: Ferritin/Heme oxygenaseT: Heme oxygenase/Ribonucleotide reductaseF: Phenol_HydroxECOD (1.6)
BPhenol_Hydroxe2incB1 A: alpha bundlesX: Ferritin/Heme oxygenase/4-helical cytokinesH: Ferritin/Heme oxygenaseT: Heme oxygenase/Ribonucleotide reductaseF: Phenol_HydroxECOD (1.6)
CTmoBe2incC1 A: a+b two layersX: beta-GraspH: Ubiquitin-relatedT: Ubiquitin-likeF: TmoBECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF04945YHS domain (YHS)YHS domainThis short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterised membr ...This short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterised membrane proteins including Swiss:Q9CNI0. This domain is named after three of the most conserved amino acids it contains. The domain may be metal binding, possibly copper ions. This domain is duplicated in some copper transporting ATPases.
Domain
PF02332Methane/Phenol/Alkene Hydroxylase (Phenol_Hydrox)Methane/Phenol/Alkene HydroxylaseThis protein family includes several components of multicomponent enzyme systems predominantly found in Proteobacteria and Actinobacteria, including subunits alpha and beta of a methane monooxygenase and an alkene monooxygenase system, small and larg ...This protein family includes several components of multicomponent enzyme systems predominantly found in Proteobacteria and Actinobacteria, including subunits alpha and beta of a methane monooxygenase and an alkene monooxygenase system, small and large subunits of propane 2-monooxygenase system and P1 protein of phenol hydroxylase [1-4].
Domain
PF02332Methane/Phenol/Alkene Hydroxylase (Phenol_Hydrox)Methane/Phenol/Alkene HydroxylaseThis protein family includes several components of multicomponent enzyme systems predominantly found in Proteobacteria and Actinobacteria, including subunits alpha and beta of a methane monooxygenase and an alkene monooxygenase system, small and larg ...This protein family includes several components of multicomponent enzyme systems predominantly found in Proteobacteria and Actinobacteria, including subunits alpha and beta of a methane monooxygenase and an alkene monooxygenase system, small and large subunits of propane 2-monooxygenase system and P1 protein of phenol hydroxylase [1-4].
Domain
PF06234Toluene-4-monooxygenase system protein B (TmoB) (TmoB)Toluene-4-monooxygenase system protein B (TmoB)This family consists of several Toluene-4-monooxygenase system protein B (TmoB) sequences. Pseudomonas mendocina KR1 metabolises toluene as a carbon source. The initial step of the pathway is hydroxylation of toluene to form p-cresol by a multicompon ...This family consists of several Toluene-4-monooxygenase system protein B (TmoB) sequences. Pseudomonas mendocina KR1 metabolises toluene as a carbon source. The initial step of the pathway is hydroxylation of toluene to form p-cresol by a multicomponent toluene-4-monooxygenase (T4MO) system [1]. TmoB adopts a ubiquitin fold [2]. Although TmoB is a component of the T4MO system, its precise role remains unclear.
Domain