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Bardet-Biedl syndrome 10 protein [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||||
Cpn60_TCP1 super family | cl28953 | TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
21-427 | 5.38e-19 | |||||||
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family. The actual alignment was detected with superfamily member pfam00118: Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 90.72 E-value: 5.38e-19
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chaperonin_like super family | cl02777 | chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
597-644 | 6.53e-04 | |||||||
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. The actual alignment was detected with superfamily member cd03342: Pssm-ID: 351886 [Multi-domain] Cd Length: 484 Bit Score: 43.02 E-value: 6.53e-04
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chap_CCT_zeta super family | cl28957 | T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
597-705 | 9.08e-04 | |||||||
T-complex protein 1, zeta 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 zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. The actual alignment was detected with superfamily member TIGR02347: Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 42.41 E-value: 9.08e-04
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Name | Accession | Description | Interval | E-value | |||||||
Cpn60_TCP1 | pfam00118 | TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
21-427 | 5.38e-19 | |||||||
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family. Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 90.72 E-value: 5.38e-19
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chap_CCT_epsi | TIGR02343 | T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
12-100 | 1.63e-06 | |||||||
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. Pssm-ID: 274084 [Multi-domain] Cd Length: 532 Bit Score: 51.34 E-value: 1.63e-06
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TCP1_epsilon | cd03339 | TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-100 | 2.49e-04 | |||||||
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. Pssm-ID: 239455 Cd Length: 526 Bit Score: 44.21 E-value: 2.49e-04
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thermosome_beta | NF041083 | thermosome subunit beta; |
13-95 | 2.80e-04 | |||||||
thermosome subunit beta; Pssm-ID: 469010 Cd Length: 519 Bit Score: 44.17 E-value: 2.80e-04
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TCP1_zeta | cd03342 | TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
597-644 | 6.53e-04 | |||||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta 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. Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 43.02 E-value: 6.53e-04
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chap_CCT_zeta | TIGR02347 | T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
597-705 | 9.08e-04 | |||||||
T-complex protein 1, zeta 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 zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 42.41 E-value: 9.08e-04
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Name | Accession | Description | Interval | E-value | |||||||
Cpn60_TCP1 | pfam00118 | TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
21-427 | 5.38e-19 | |||||||
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family. Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 90.72 E-value: 5.38e-19
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chap_CCT_epsi | TIGR02343 | T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
12-100 | 1.63e-06 | |||||||
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. Pssm-ID: 274084 [Multi-domain] Cd Length: 532 Bit Score: 51.34 E-value: 1.63e-06
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chap_CCT_zeta | TIGR02347 | T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
2-95 | 4.91e-05 | |||||||
T-complex protein 1, zeta 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 zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 46.65 E-value: 4.91e-05
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chap_CCT_alpha | TIGR02340 | T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
11-95 | 5.15e-05 | |||||||
T-complex protein 1, alpha 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. Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 46.64 E-value: 5.15e-05
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TCP1_epsilon | cd03339 | TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-100 | 2.49e-04 | |||||||
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. Pssm-ID: 239455 Cd Length: 526 Bit Score: 44.21 E-value: 2.49e-04
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TCP1_alpha | cd03335 | TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
11-95 | 2.66e-04 | |||||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha 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. Pssm-ID: 239451 Cd Length: 527 Bit Score: 44.20 E-value: 2.66e-04
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thermosome_beta | NF041083 | thermosome subunit beta; |
13-95 | 2.80e-04 | |||||||
thermosome subunit beta; Pssm-ID: 469010 Cd Length: 519 Bit Score: 44.17 E-value: 2.80e-04
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cpn60 | cd03343 | cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
13-95 | 6.32e-04 | |||||||
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. Pssm-ID: 239459 [Multi-domain] Cd Length: 517 Bit Score: 43.02 E-value: 6.32e-04
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TCP1_zeta | cd03342 | TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
597-644 | 6.53e-04 | |||||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta 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. Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 43.02 E-value: 6.53e-04
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TCP1_delta | cd03338 | TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
2-98 | 7.31e-04 | |||||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta 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. Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 42.66 E-value: 7.31e-04
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chap_CCT_zeta | TIGR02347 | T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
597-705 | 9.08e-04 | |||||||
T-complex protein 1, zeta 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 zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 42.41 E-value: 9.08e-04
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TCP1_zeta | cd03342 | TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
13-98 | 9.38e-04 | |||||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta 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. Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 42.25 E-value: 9.38e-04
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chap_CCT_eta | TIGR02345 | T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
11-246 | 1.25e-03 | |||||||
T-complex protein 1, eta 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 eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 42.05 E-value: 1.25e-03
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chap_CCT_gamma | TIGR02344 | T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
6-107 | 4.62e-03 | |||||||
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. Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 40.11 E-value: 4.62e-03
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Blast search parameters | ||||
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