Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyADC-like 8101088 3001132 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8099846 3001453 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyADC-like 8101088 3001132 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8099846 3001453 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8099846 3001453 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyADC-like 8101088 3001132 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyADC-like 8101088 3001132 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8099846 3001453 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyISP domain 8099848 3000233 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyISP domain 8099848 3000233 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyISP domain 8099848 3000233 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyISP domain 8099848 3000233 SCOP2B (2022-06-29)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, C, E, G
PF01568Molydopterin dinucleotide binding domain (Molydop_binding)Molydopterin dinucleotide binding domainThis domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entir ...This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2].
Domain
A, C, E, G
PF18465Rieske 3Fe-4S (Rieske_3)Rieske 3Fe-4SThis domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of ...This domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of Gram-negative organisms. The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes. The large subunit of arsenite oxidase is divided into four domains, with domain I binding the [3Fe-4S] cluster . Domain I, consists of three antiparallel beta sheets and six helices. The [3Fe-4S] cluster is coordinated by the motif Cys21-X2-Cys24-X3-Cys28 near the interface with domains III and IV. A large, flattened funnel-like cavity bounded by domains I, II, and III leads to the molybdenum center Pfam:PF00384 located near the center of the molecule [1].
Domain
A, C, E, G
PF00384Molybdopterin oxidoreductase (Molybdopterin)Molybdopterin oxidoreductase- Family
B, D, F, H
PF00355Rieske [2Fe-2S] domain (Rieske)Rieske [2Fe-2S] domainThe rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in ...The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilises the protein [4].
Domain