chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.

                        10        20        30
                ....*....|....*....|....*....|...
gi 992595     1 IQACKELAQTTRTAYGPNGMNKMVINHLEKLFV 33
Cdd:cd03341  14 IEACKELSQITRTSYGPNGMNKMVINHLEKLFV 46

TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.

                        10        20        30
                ....*....|....*....|....*....|...
gi 992595     1 IQACKELAQTTRTAYGPNGMNKMVINHLEKLFV 33
Cdd:cd03341  14 IEACKELSQITRTSYGPNGMNKMVINHLEKLFV 46

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.

                          10        20
                  ....*....|....*....|....*..
gi 992595       7 LAQTTRTAYGPNGMNKMVINHLEKLFV 33
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTV 27

TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.

                        10        20        30
                ....*....|....*....|....*....|...
gi 992595     1 IQACKELAQTTRTAYGPNGMNKMVINHLEKLFV 33
Cdd:cd03341  14 IEACKELSQITRTSYGPNGMNKMVINHLEKLFV 46

chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.

                        10        20        30
                ....*....|....*....|....*....|...
gi 992595     1 IQACKELAQTTRTAYGPNGMNKMVINHLEKLFV 33
Cdd:cd00309  14 INAAKALADAVKTTLGPKGMDKMLVDSLGDPTI 46

cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.

                        10        20
                ....*....|....*....|....*...
gi 992595     1 IQACKELAQTTRTAYGPNGMNKMVINHL 28
Cdd:cd03343  21 IAAAKAVAEAVRTTLGPKGMDKMLVDSL 48

T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.

                          10        20
                  ....*....|....*....|....*
gi 992595       1 IQACKELAQTTRTAYGPNGMNKMVI 25
Cdd:TIGR02343  33 IAAAKSVASILRTSLGPKGMDKMLI 57

TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.

                        10        20
                ....*....|....*....|....*
gi 992595     1 IQACKELAQTTRTAYGPNGMNKMVI 25
Cdd:cd03337  22 IQAAKTVADVIRTCLGPRAMLKMLL 46