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Conserved domains on  [gi|157830060|pdb|1ASS|A]
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Chain A, THERMOSOME

Protein Classification

TCP-1/cpn60 chaperonin family protein( domain architecture ID 16)

TCP-1/cpn60 chaperonin family protein similar to mycobacterial 60 kDa chaperonin (GroEL) that together with its co-chaperonin GroES, plays an essential role in assisting protein folding

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thermosome_beta super family cl46127
thermosome subunit beta;
3-153 7.65e-94

thermosome subunit beta;


The actual alignment was detected with superfamily member NF041083:

Pssm-ID: 469010  Cd Length: 519  Bit Score: 281.07  E-value: 7.65e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:NF041083 212 GIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI 291

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:NF041083 292 DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKN 362
 
Name Accession Description Interval E-value
thermosome_beta NF041083
thermosome subunit beta;
3-153 7.65e-94

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 281.07  E-value: 7.65e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:NF041083 212 GIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI 291

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:NF041083 292 DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKN 362
thermosome_alpha NF041082
thermosome subunit alpha;
3-153 1.44e-92

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 277.54  E-value: 1.44e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:NF041082 211 GVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGI 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:NF041082 291 DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKN 361
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 3-153 3.80e-86

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: 261.04  E-value: 3.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:cd03343 210 GIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGI 289

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd03343 290 DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKN 360
thermosome_arch TIGR02339
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
 3-153 3.57e-76

thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274080  Cd Length: 519  Bit Score: 235.73  E-value: 3.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:TIGR02339 213 GIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGI 292

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A         83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:TIGR02339 293 DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKN 363
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 3-153 1.12e-63

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: 202.43  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:pfam00118 182 GVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQKGI 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A         83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:pfam00118 262 DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIGDEKYTFIEGCKS 332
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 3-153 4.58e-37

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 132.51  E-value: 4.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHS-------KMPDVVKNAKIALIDSALEIkkteieakvqisdpskIQDFLnqetntfkQMVEKIKKSGANV 75
Cdd:COG0459 191 GMQFDKGYLSPyfvtdpeKMPAELENAYILLTDKKISS----------------IQDLL--------PLLEKVAQSGKPL 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A       76 VLCQKGIDDVAQHYLAKEGIYAVRRV-----------KKSDMEKLAKATGAKIVTD-----LDDLTPSVLGEAETVEerk 139
Cdd:COG0459 247 LIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVE--- 323

                       170
                ....*....|....
1ASS_A      140 IGDDRMTFVMGCKN 153
Cdd:COG0459 324 VDKDNTTIVEGAGN 337
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 3-152 2.68e-16

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 74.68  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKeKVHSKMPDVVKNAKIALIDSALEIKKTEI-EAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKG 81
Cdd:PTZ00212 219 GFILEK-KIGVGQPKRLENCKILVANTPMDTDKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQL 297

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        82 IDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCK 152
Cdd:PTZ00212 298 IYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCA 368
 
Name Accession Description Interval E-value
thermosome_beta NF041083
thermosome subunit beta;
3-153 7.65e-94

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 281.07  E-value: 7.65e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:NF041083 212 GIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI 291

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:NF041083 292 DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKN 362
thermosome_alpha NF041082
thermosome subunit alpha;
3-153 1.44e-92

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 277.54  E-value: 1.44e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:NF041082 211 GVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGI 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:NF041082 291 DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKN 361
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 3-153 3.80e-86

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: 261.04  E-value: 3.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:cd03343 210 GIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGI 289

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd03343 290 DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKN 360
thermosome_arch TIGR02339
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
 3-153 3.57e-76

thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274080  Cd Length: 519  Bit Score: 235.73  E-value: 3.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:TIGR02339 213 GIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGI 292

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A         83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:TIGR02339 293 DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKN 363
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 3-153 1.12e-63

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: 202.43  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:pfam00118 182 GVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQKGI 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A         83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:pfam00118 262 DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIGDEKYTFIEGCKS 332
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 3-153 1.76e-40

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.


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 134.90  E-value: 1.76e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEikkteieakvqisdpskiqdflnqetntfkqmvekikksgaNVVLCQKGI 82
Cdd:cd03333  64 GVVFDKGYASPYMPKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd03333 103 DDLALHYLAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKG 173
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 3-153 6.49e-40

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.


Pssm-ID: 238189  Cd Length: 464  Bit Score: 139.49  E-value: 6.49e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEikkteieakvqisdpskiqdflnqetntfkqmvekikksgaNVVLCQKGI 82
Cdd:cd00309 200 GMVFDKGYLSPYMPKRLENAKILLLDCKLE-----------------------------------------YVVIAEKGI 238

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd00309 239 DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKG 309
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 3-153 7.45e-40

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: 140.51  E-value: 7.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:cd03339 218 GIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGF 297

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIG--DDRMTFVMGCKN 153
Cdd:cd03339 298 DDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPN 370
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
 15-153 4.26e-38

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: 135.87  E-value: 4.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A       15 MPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEG 94
Cdd:cd03335 217 MPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAG 296

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1ASS_A       95 IYAVRRVKKSDMEKLAKATGAKIVTDLDDL------TPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd03335 297 AMAVRRVKKEDLRRIAKATGATLVSTLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKK 361
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 3-153 4.58e-37

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 132.51  E-value: 4.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHS-------KMPDVVKNAKIALIDSALEIkkteieakvqisdpskIQDFLnqetntfkQMVEKIKKSGANV 75
Cdd:COG0459 191 GMQFDKGYLSPyfvtdpeKMPAELENAYILLTDKKISS----------------IQDLL--------PLLEKVAQSGKPL 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A       76 VLCQKGIDDVAQHYLAKEGIYAVRRV-----------KKSDMEKLAKATGAKIVTD-----LDDLTPSVLGEAETVEerk 139
Cdd:COG0459 247 LIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVE--- 323

                       170
                ....*....|....
1ASS_A      140 IGDDRMTFVMGCKN 153
Cdd:COG0459 324 VDKDNTTIVEGAGN 337
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 15-153 9.36e-35

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: 126.76  E-value: 9.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         15 MPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEG 94
Cdd:TIGR02340 221 MPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAG 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
1ASS_A         95 IYAVRRVKKSDMEKLAKATGAKIVTDLDDLT------PSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:TIGR02340 301 AMGVRRCKKEDLKRIAKATGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKK 365
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
 1-153 1.72e-34

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: 126.01  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          1 MSGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQK 80
Cdd:TIGR02344 210 LKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEK 289

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ASS_A         81 GIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGE-AETVEERKIGDDRMTFVMGCKN 153
Cdd:TIGR02344 290 GVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKD 363
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 3-153 1.19e-33

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: 123.76  E-value: 1.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:TIGR02343 222 GIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGF 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ASS_A         83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIG--DDRMTFVMGCKN 153
Cdd:TIGR02343 302 DDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKN 374
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 16-153 9.03e-29

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.


Pssm-ID: 239456 [Multi-domain]  Cd Length: 522  Bit Score: 110.07  E-value: 9.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A       16 PDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGI 95
Cdd:cd03340 225 PKKFKNPKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDI 304

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
1ASS_A       96 YAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd03340 305 FCAGRVPEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPK 362
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
 12-153 4.93e-26

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: 102.53  E-value: 4.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         12 HSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLA 91
Cdd:TIGR02345 223 FEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFA 302

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1ASS_A         92 KEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:TIGR02345 303 DRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPH 364
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 3-153 2.20e-25

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: 100.41  E-value: 2.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISdpskiqdflnqetntfkqmvekikksganVVLCQKGI 82
Cdd:cd03342 205 GLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSGFFYS-----------------------------VVINQKGI 255

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKN 153
Cdd:cd03342 256 DPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKN 326
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
 3-153 5.00e-25

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.


Pssm-ID: 239453 [Multi-domain]  Cd Length: 480  Bit Score: 99.29  E-value: 5.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIkkteieakvqisdpskiqdflnqetntfkqmvekikksganVVLCQKGI 82
Cdd:cd03337 213 GVMLNKDVTHPKMRRRIENPRIVLLDCPLEY-----------------------------------------LVITEKGV 251

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1ASS_A       83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEE-RKIGDDRMTFVMGCKN 153
Cdd:cd03337 252 SDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGTGAGLFEvKKIGDEYFTFITECKD 323
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 3-153 2.87e-21

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: 89.02  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKI----KKSGAN---- 74
Cdd:TIGR02347 209 GLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIielkKKVCGKspdk 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         75 --VVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCK 152
Cdd:TIGR02347 289 gfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECK 368


                  .
1ASS_A        153 N 153
Cdd:TIGR02347 369 N 369
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
 2-143 3.20e-18

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 78.42  E-value: 3.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        2 SGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKteIEAKVQISDPskiqdFLNQETNTFKQMVEKIKKSGANVVLCQKG 81
Cdd:cd03334  67 DGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLSLDP-----VILQEKEYLKNLVSRIVALRPDVILVEKS 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1ASS_A       82 IDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDL-TPSVLGEAETVEERKIGDD 143
Cdd:cd03334 140 VSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLlTSPKLGTCESFRVRTYVEE 202
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
 3-146 1.19e-17

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.


Pssm-ID: 274087 [Multi-domain]  Cd Length: 531  Bit Score: 78.60  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A          3 GIVIDKEKVHSKMPdvVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI 82
Cdd:TIGR02346 212 GMVFNREAEGSVKS--VKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSV 289

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1ASS_A         83 DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMT 146
Cdd:TIGR02346 290 GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVT 353
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 3-152 2.68e-16

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 74.68  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A         3 GIVIDKeKVHSKMPDVVKNAKIALIDSALEIKKTEI-EAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKG 81
Cdd:PTZ00212 219 GFILEK-KIGVGQPKRLENCKILVANTPMDTDKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQL 297

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A        82 IDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCK 152
Cdd:PTZ00212 298 IYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCA 368
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 3-152 1.75e-13

TCP-1 (CTT or eukaryotic type II) chaperonin family, beta 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: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 66.58  E-value: 1.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A        3 GIVIDKeKVHSKMPDVVKNAKIALIDSALEIKKTEI-EAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKG 81
Cdd:cd03336 207 GFLLDK-KIGVNQPKRIENAKILIANTPMDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQL 285

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ASS_A       82 IDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCK 152
Cdd:cd03336 286 IYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVA 356
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
 72-153 4.10e-10

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.


Pssm-ID: 239457 [Multi-domain]  Cd Length: 472  Bit Score: 56.85  E-value: 4.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ASS_A       72 GANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGC 151
Cdd:cd03341 231 GVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQN 310


                ..
1ASS_A      152 KN 153
Cdd:cd03341 311 KE 312
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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