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        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79374903     2 ALAFDEFGRPFIILREQDQKTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:TIGR02343   1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDK 54

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79374903     2 ALAFDEFGRPFIILREQDQKTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:TIGR02343   1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDK 54

thermosome subunit alpha;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 79374903   11 PFIILREQDQKTRlkGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:NF041082   2 PILILKEGTQRTS--GRDAQRNNIMAAKAVAEAVRTTLGPKGMDK 44

TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon 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 79374903  78 LRSIPMALALNSGLQPIETLSAVKSQQIKE 107
Cdd:cd03339 446 LESIPLALAENSGLNPIETLSEVKARQVKE 475

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];

                        10        20        30
                ....*....|....*....|....*....|....*
gi 79374903  21 KTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:COG0459   3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNV 37

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 79374903     2 ALAFDEFGRPFIILREQDQKTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:TIGR02343   1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDK 54

thermosome subunit alpha;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 79374903   11 PFIILREQDQKTRlkGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:NF041082   2 PILILKEGTQRTS--GRDAQRNNIMAAKAVAEAVRTTLGPKGMDK 44

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        30        40
                ....*....|....*....|....*....|....*....|...
gi 79374903  13 IILREQDQKTrlKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:cd03343   2 LILKEGTQRT--SGRDAQRMNIAAAKAVAEAVRTTLGPKGMDK 42

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 79374903  21 KTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:cd00309   1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDK 35

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];

                        10        20        30
                ....*....|....*....|....*....|....*
gi 79374903  21 KTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:COG0459   3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNV 37

T-complex protein 1, delta 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 delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 79374903    20 QKTRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:TIGR02342   1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDK 36

T-complex protein 1, gamma 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 gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 79374903    13 IILREQDQKtRLKGIDAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:TIGR02344   2 VLVLNQNTK-RESGRKAQLSNIQAAKAVADIIRTCLGPRSMLK 43

TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 79374903  11 PFIILREqdqktrlkGIDAQK------ANISAGKAVARILRSSLGPKGMEK 55
Cdd:cd03340   1 PIILLKE--------GTDTSQgkgqliSNINACQAIADAVRTTLGPRGMDK 43

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        30
                ....*....|....*....|....*....|....*
gi 79374903  77 SLRSIPMALALNSGLQPIETLSAVKSQQIKERRTF 111
Cdd:cd03343 435 ALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNA 469

T-complex protein 1, theta 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 alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.

                          10        20
                  ....*....|....*....|....*...
gi 79374903    28 DAQKANISAGKAVARILRSSLGPKGMEK 55
Cdd:TIGR02346  18 EAVIKNIEACKELSQITRTSLGPNGMNK 45