Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
C [auth T]SCOP2B SuperfamilyGST C-terminal domain-like 8037552 3000305 SCOP2B (2022-06-29)
C [auth T]SCOP2B SuperfamilyThioredoxin-like 8044378 3000031 SCOP2B (2022-06-29)
D [auth S]SCOP2B SuperfamilyGST C-terminal domain-like 8037552 3000305 SCOP2B (2022-06-29)
D [auth S]SCOP2B SuperfamilyThioredoxin-like 8044378 3000031 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BAAA_9_Ce3qmzB3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: AAA_9_CECOD (1.6)
BAAA_7_Ce3qmzB10 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: AAA_7_CECOD (1.6)
BDYN1e3qmzB9 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: DYN1ECOD (1.6)
BKOG3595e3qmzB7 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: KOG3595ECOD (1.6)
BDynein_heavy_2nde3qmzB4 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: Dynein_heavy_2ndECOD (1.6)
BDHC_N2e3qmzB1 A: alpha superhelicesX: Linker domain of cytoplasmic dynein heavy chain (From Topology)H: Linker domain of cytoplasmic dynein heavy chain (From Topology)T: Linker domain of cytoplasmic dynein heavy chainF: DHC_N2ECOD (1.6)
BAAA_7_Ne3qmzB6 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_7_NECOD (1.6)
BAAA_8e3qmzB2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_8ECOD (1.6)
BAAA_6_Ne3qmzB8 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_6_NECOD (1.6)
BDynein_heavy_1ste3qmzB11 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Dynein_heavy_1stECOD (1.6)
BAAA_5e3qmzB5 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_5ECOD (1.6)
BAAA_9_Ne3qmzB12 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_9_NECOD (1.6)
AAAA_9_Ce3qmzA3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: AAA_9_CECOD (1.6)
AAAA_7_Ce3qmzA10 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: AAA_7_CECOD (1.6)
ADYN1e3qmzA9 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: DYN1ECOD (1.6)
AKOG3595e3qmzA7 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: KOG3595ECOD (1.6)
ADynein_heavy_2nde3qmzA4 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: Dynein_heavy_2ndECOD (1.6)
ADHC_N2e3qmzA1 A: alpha superhelicesX: Linker domain of cytoplasmic dynein heavy chain (From Topology)H: Linker domain of cytoplasmic dynein heavy chain (From Topology)T: Linker domain of cytoplasmic dynein heavy chainF: DHC_N2ECOD (1.6)
AAAA_7_Ne3qmzA6 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_7_NECOD (1.6)
AAAA_8e3qmzA2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_8ECOD (1.6)
AAAA_6_Ne3qmzA8 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_6_NECOD (1.6)
ADynein_heavy_1ste3qmzA11 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Dynein_heavy_1stECOD (1.6)
AAAA_5e3qmzA5 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_5ECOD (1.6)
AAAA_9_Ne3qmzA12 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_9_NECOD (1.6)
C [auth T]GST_C_3e3qmzT1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
C [auth T]GST_N_5e3qmzT2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
D [auth S]GST_C_3e3qmzS1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
D [auth S]GST_N_5e3qmzS2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF22597Dynein heavy chain, ATPase lid domain (DYN_lid)Dynein heavy chain, ATPase lid domainDyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport and comprise cytoplasmic and axonemal isoforms. They consist of a motor domain that contains a ring-shaped head ...Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport and comprise cytoplasmic and axonemal isoforms. They consist of a motor domain that contains a ring-shaped head with six AAA-domains, a coiled-coil stalk with a microtubule binding domain (MTBD) and a linker [1-5] This entry represents the lid domain found at the C-terminal of the third AAA+ ATPase domain in dyneins [1-5].
Domain
A, B
PF18198Dynein heavy chain AAA lid domain (AAA_lid_11)Dynein heavy chain AAA lid domainThis family represents the AAA lid domain found neat the C-terminal region of dynein heavy chain.Domain
A, B
PF12775P-loop containing dynein motor region (AAA_7)P-loop containing dynein motor regionThis domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliophathies. Dyneins share a conserved motor domain that couples cycles of ATP hydr ...This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliophathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs) [1].
Domain
A, B
PF21499DYN1, AAA+ ATPase lid domain (DYN1_lid)DYN1, AAA+ ATPase lid domainThis entry includes dynein heavy chain (DYN1) from yeast, which is a cytoplasmic dynein that acts as a motor for intracellular retrograde motility of vesicles and organelles along microtubules. This entry represents the AAA+ ATPase lid domain [1-5].Domain
A, B
PF12781ATP-binding dynein motor region (AAA_9)ATP-binding dynein motor regionThis domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydro ...This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk [1].
Domain
A, B
PF08393Dynein heavy chain, N-terminal region 2 (DHC_N2)Dynein heavy chain, N-terminal region 2- Family
A, B
PF12777Microtubule-binding stalk of dynein motor (MT)Microtubule-binding stalk of dynein motorthe 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures describ ...the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component [1].
Domain
A, B
PF03028Dynein heavy chain region D6 P-loop domain (Dynein_heavy)Dynein heavy chain region D6 P-loop domainThis family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved i ...This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains [1]. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained [2].
Domain
C [auth T],
D [auth S]
PF14497Glutathione S-transferase, C-terminal domain (GST_C_3)Glutathione S-transferase, C-terminal domainThis domain is closely related to Pfam:PF00043.Domain
C [auth T],
D [auth S]
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, B
Cytoplasmic dynein heavy chain
C [auth T],
D [auth S]
Glutathione-S-transferase -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B
IPR026983Dynein heavy chainFamily
A, B
IPR013602Dynein heavy chain, linkerDomain
A, B
IPR035706Dynein heavy chain, ATP-binding dynein motor regionDomain
A, B
IPR054354Dynein 2 heavy chain 1, cytoplasmic, ATPase lid domainDomain
A, B
IPR003593AAA+ ATPase domainDomain
A, B
IPR041658Dynein heavy chain AAA lid domainDomain
A, B
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
A, B
IPR042228Dynein heavy chain, linker, subdomain 3Homologous Superfamily
A, B
IPR035699Dynein heavy chain, hydrolytic ATP-binding dynein motor regionDomain
A, B
IPR042219Dynein heavy chain AAA lid domain superfamilyHomologous Superfamily
A, B
IPR024743Dynein heavy chain, coiled coil stalkDomain
A, B
IPR013594Dynein heavy chain, tailDomain
A, B
IPR048404DYN1, AAA+ ATPase lid domainDomain
A, B
IPR043157Dynein heavy chain, AAA1 domain, small subdomainHomologous Superfamily
A, B
IPR042222Dynein heavy chain, domain 2, N-terminalHomologous Superfamily
A, B
IPR004273Dynein heavy chain region D6 P-loop domainDomain
A, B
IPR024317Dynein heavy chain, AAA module D4Domain
C [auth T],
D [auth S]
IPR004046Glutathione S-transferase, C-terminalDomain
C [auth T],
D [auth S]
IPR050213Glutathione S-transferase superfamilyFamily
C [auth T],
D [auth S]
IPR010987Glutathione S-transferase, C-terminal-likeDomain
C [auth T],
D [auth S]
IPR036282Glutathione S-transferase, C-terminal domain superfamilyHomologous Superfamily
C [auth T],
D [auth S]
IPR004045Glutathione S-transferase, N-terminalDomain
C [auth T],
D [auth S]
IPR036249Thioredoxin-like superfamilyHomologous Superfamily
C [auth T],
D [auth S]
IPR040079Glutathione transferase familyFamily