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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Bd5ecib2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Bd5ecib1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Cd5ecic2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Cd5ecic1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Ed5ecie2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Ed5ecie1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Fd5ecif2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)
Fd5ecif1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ], SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGH3_2nde5eciA3 A: beta barrelsX: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)T: beta-barrel domain in acetyl-CoA synthetase-like proteinsF: GH3_2ndECOD (1.6)
AGH3_3rde5eciA1 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)T: a+b domain in acetyl-CoA synthetase-like proteinsF: GH3_3rdECOD (1.6)
AGH3_1ste5eciA2 A: a/b three-layered sandwichesX: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)T: Rossmann-like domain in Acetyl-CoA synthetase-like proteinsF: GH3_1stECOD (1.6)
DGH3_2nde5eciD3 A: beta barrelsX: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)T: beta-barrel domain in acetyl-CoA synthetase-like proteinsF: GH3_2ndECOD (1.6)
DGH3_3rde5eciD1 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)T: a+b domain in acetyl-CoA synthetase-like proteinsF: GH3_3rdECOD (1.6)
DGH3_1ste5eciD2 A: a/b three-layered sandwichesX: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)T: Rossmann-like domain in Acetyl-CoA synthetase-like proteinsF: GH3_1stECOD (1.6)
BGST_C_3e5eciB1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
BGST_Ne5eciB2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
CGST_C_3e5eciC2 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
CGST_Ne5eciC1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
EGST_C_3e5eciE1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
EGST_Ne5eciE2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
FGST_C_3e5eciF1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
FGST_Ne5eciF2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, D
PF03321GH3 auxin-responsive promoter (GH3)GH3 auxin-responsive promoter- Family
B, C, E, F
PF13410Glutathione S-transferase, C-terminal domain (GST_C_2)Glutathione S-transferase, C-terminal domainThis domain is closely related to Pfam:PF00043.Domain
B, C, E, F
PF02798Glutathione S-transferase, N-terminal domain (GST_N)Glutathione S-transferase, N-terminal domainFunction: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity a ...Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognised); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognised). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, D
Jasmonic acid-amido synthetase JAR1
B, C, E, F
Glutathione S-transferase U20