|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
1-464 |
0e+00 |
|
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: 768.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKE--MK 78
Cdd:TIGR02347 65 MQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRKQ 158
Cdd:TIGR02347 145 REFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 159 VRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVCAES-NKGFVVINQKGIDPVSLE 237
Cdd:TIGR02347 225 VKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 238 MLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHT 317
Cdd:TIGR02347 305 LLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHT 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 318 LIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETL 397
Cdd:TIGR02347 385 IAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTL 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971415 398 IKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAGMSSLR 464
Cdd:TIGR02347 465 VKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
1-460 |
0e+00 |
|
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: 745.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-- 78
Cdd:cd03342 61 MQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDtd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRKQ 158
Cdd:cd03342 141 RELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 159 VRDAYILTCNVSLEYEKTEVSSGFFYKtveekeklvkaerkfiedrvqkiidlkqkvcaesnkgfVVINQKGIDPVSLEM 238
Cdd:cd03342 221 VENAYILTCNVSLEYEKTEVNSGFFYS--------------------------------------VVINQKGIDPPSLDM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 239 LAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHTL 318
Cdd:cd03342 263 LAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 319 IQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLI 398
Cdd:cd03342 343 TQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLV 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971415 399 KIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAGM 460
Cdd:cd03342 423 KLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
1-459 |
2.58e-175 |
|
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: 500.58 E-value: 2.58e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ--KEMK 78
Cdd:pfam00118 38 LEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSIISIpvEDVD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRKQ 158
Cdd:pfam00118 118 REDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 159 VRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVcaesnkgfvVINQKGIDPVSLEM 238
Cdd:pfam00118 198 LENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNV---------VVCQKGIDDLALHF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 239 LAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHTL 318
Cdd:pfam00118 269 LAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 319 IQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLI 398
Cdd:pfam00118 349 DEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971415 399 KIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAG 459
Cdd:pfam00118 429 ELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-457 |
1.03e-160 |
|
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: 462.28 E-value: 1.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-R 79
Cdd:cd00309 57 IEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEdR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRKQV 159
Cdd:cd00309 137 EELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 160 RDAYILTCNVSLEYektevssgffyktveekeklvkaerkfiedrvqkiidlkqkvcaesnkgfVVINQKGIDPVSLEML 239
Cdd:cd00309 217 ENAKILLLDCKLEY--------------------------------------------------VVIAEKGIDDEALHYL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 240 AKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHTLI 319
Cdd:cd00309 247 AKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 320 QIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLIK 399
Cdd:cd00309 327 EAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTK 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 568971415 400 IQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMR 457
Cdd:cd00309 407 LRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-459 |
2.12e-116 |
|
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: 351.18 E-value: 2.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-R 79
Cdd:cd03343 64 MDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAI---RRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMR 156
Cdd:cd03343 144 DTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVaekRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 157 KQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVcaesnkgfvVINQKGIDPVSL 236
Cdd:cd03343 224 KRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANV---------VFCQKGIDDLAQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 237 EMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKH 316
Cdd:cd03343 295 HYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEH 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 317 TLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQET 396
Cdd:cd03343 375 VVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDT 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971415 397 LIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAG 459
Cdd:cd03343 455 LVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-459 |
1.99e-115 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 348.80 E-value: 1.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ-KEMKR 79
Cdd:NF041082 66 MDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRP--GVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRK 157
Cdd:NF041082 146 ETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAEKdgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 158 QVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDlkqkvcAESNkgfVVINQKGIDPVSLE 237
Cdd:NF041082 226 RVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIAD------SGAN---VVFCQKGIDDLAQH 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 238 MLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHT 317
Cdd:NF041082 297 YLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 318 LIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETL 397
Cdd:NF041082 377 VDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDAL 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971415 398 IKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAG 459
Cdd:NF041082 457 VELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-459 |
1.24e-114 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 346.94 E-value: 1.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ-KEMKR 79
Cdd:NF041083 66 MDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKvDPDDR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAI---RRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMR 156
Cdd:NF041083 146 ETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVaekRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 157 KQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDlkqkvcAESNkgfVVINQKGIDPVSL 236
Cdd:NF041083 226 KRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKA------TGAN---VVFCQKGIDDLAQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 237 EMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKH 316
Cdd:NF041083 297 HYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEH 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 317 TLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQET 396
Cdd:NF041083 377 VVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDI 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971415 397 LIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAG 459
Cdd:NF041083 457 LVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-458 |
1.89e-113 |
|
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: 343.59 E-value: 1.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-R 79
Cdd:TIGR02339 65 MDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEdR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELA-DILTEAVVDSVLAIRRP----GVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPR 154
Cdd:TIGR02339 145 DLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQVAELrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 155 MRKQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKvcaesnkgfVVINQKGIDPV 234
Cdd:TIGR02339 225 MPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGAN---------VVICQKGIDDV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 235 SLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPN 314
Cdd:TIGR02339 296 AQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 315 KHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQ 394
Cdd:TIGR02339 376 EHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPI 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568971415 395 ETLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:TIGR02339 456 DALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
1-455 |
1.93e-76 |
|
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: 248.37 E-value: 1.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKE---M 77
Cdd:cd03339 72 MDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 78 KREILLDVARTSLQTKV----HAELADILTEAVVdSVLAIRRPGVPIDLFMVEivEMRHKSETDTQLIRGLVLDHGARHP 153
Cdd:cd03339 152 NKEPLIQTAMTSLGSKIvsrcHRQFAEIAVDAVL-SVADLERKDVNFELIKVE--GKVGGRLEDTKLVKGIVIDKDFSHP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 154 RMRKQVRDAYI--LTCnvSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDlkqkvcAESNkgfVVINQKGI 231
Cdd:cd03339 229 QMPKEVKDAKIaiLTC--PFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKD------AGAN---LVICQWGF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 232 DPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALG--EEKFTFIEDCVNPLSVTLL 309
Cdd:cd03339 298 DDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIF 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 310 VKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNS 389
Cdd:cd03339 378 IRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENS 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971415 390 GYDLQETLIKIQTKHAESKE-LLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEI 455
Cdd:cd03339 458 GLNPIETLSEVKARQVKEKNpHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-457 |
1.15e-73 |
|
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: 241.16 E-value: 1.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDE--IKVQKEMK 78
Cdd:TIGR02340 61 LEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnlSVSVDELG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIR------RPGVPIDlfMVEIVEMRHKSETDTQLIRGLVLDHGARH 152
Cdd:TIGR02340 141 REALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKttnengETKYPIK--AINILKAHGKSARESMLVKGYALNCTVAS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 153 PRMRKQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDlkqkvcAESNkgfVVINQKGID 232
Cdd:TIGR02340 219 QQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILD------AGAN---VVLTTGGID 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 233 PVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSF------EGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSV 306
Cdd:TIGR02340 290 DMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 307 TLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLA 386
Cdd:TIGR02340 370 SIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLA 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971415 387 QNSGYDLQETLIKIQTKHAES------KEL--LGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMR 457
Cdd:TIGR02340 450 VNAAKDSTELVAKLRAYHAAAqlkpekKHLkwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
1-457 |
1.39e-73 |
|
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: 240.65 E-value: 1.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQK--EMK 78
Cdd:cd03335 57 LEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISvdNLG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIRR---PGV---PIDlfMVEIVEMRHKSETDTQLIRGLVLDHGARH 152
Cdd:cd03335 137 KESLINVAKTSMSSKIIGADSDFFANMVVDAILAVKTtneKGKtkyPIK--AVNILKAHGKSAKESYLVNGYALNCTRAS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 153 PRMRKQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDlkqkvcAESNkgfVVINQKGID 232
Cdd:cd03335 215 QGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILA------AGAN---VVLTTGGID 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 233 PVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSF------EGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSV 306
Cdd:cd03335 286 DMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLanlegeETFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 307 TLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLA 386
Cdd:cd03335 366 SIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLA 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971415 387 QNSGYDLQETLIKIQTKHAES------KEL--LGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMR 457
Cdd:cd03335 446 VNAAKDATELVAKLRAYHAAAqvkpdkKHLkwYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
1-455 |
5.41e-73 |
|
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: 239.25 E-value: 5.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-R 79
Cdd:TIGR02344 65 IDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNdD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVP---IDLFMVEIVEMRHKSE-TDTQLIRGLVLDHGARHPRM 155
Cdd:TIGR02344 145 AAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDENGrkeIDIKRYAKVEKIPGGDiEDSCVLKGVMINKDVTHPKM 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 156 RKQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVcaesnkgfvVINQKGIDPVS 235
Cdd:TIGR02344 225 RRYIENPRIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDL---------VITEKGVSDLA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 236 LEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLG-HAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPN 314
Cdd:TIGR02344 296 QHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGAS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 315 KHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQ 394
Cdd:TIGR02344 376 KDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVI 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971415 395 ETLIKIQTKHA-ESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEI 455
Cdd:TIGR02344 456 RTLTELRAKHAqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
1-458 |
2.11e-72 |
|
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: 237.57 E-value: 2.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ-----K 75
Cdd:cd03340 65 LDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNidkedK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 76 EMKREILLDVARTSLQTKVHAELADILTEAVVDSVLAIrrpGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHG---ARH 152
Cdd:cd03340 145 EEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSL---DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 153 PRMRKQVRDAYILTCNVSLEY--EKT--EVSSGffykTVEEKEKLVKAERKFIEDRVQKIIDLKQKVcaesnkgfvVINQ 228
Cdd:cd03340 222 EQQPKKFKNPKILLLNVELELkaEKDnaEVRVE----DPEEYQAIVDAEWKIIYDKLEKIVKSGANV---------VLSK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 229 KGIDPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTL 308
Cdd:cd03340 289 LPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 309 LVKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQN 388
Cdd:cd03340 369 ILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDN 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971415 389 SGYDLQETLIKIQTKHAESKEL-LGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:cd03340 449 AGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
1-459 |
7.57e-72 |
|
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: 236.24 E-value: 7.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEI--KVQKEMK 78
Cdd:TIGR02343 76 MDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIsdEISADNN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 -REILLDVARTSLQTKV----HAELADILTEAVVdSVLAIRRPGVPIDLFMVEivEMRHKSETDTQLIRGLVLDHGARHP 153
Cdd:TIGR02343 156 nREPLIQAAKTSLGSKIvskcHRRFAEIAVDAVL-NVADMERRDVDFDLIKVE--GKVGGSLEDTKLIKGIIIDKDFSHP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 154 RMRKQVRDAY--ILTCnvSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIidlkQKVCAEsnkgfVVINQKGI 231
Cdd:TIGR02343 233 QMPKEVEDAKiaILTC--PFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDI----KKSGAN-----LVICQWGF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 232 DPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALG--EEKFTFIEDCVNPLSVTLL 309
Cdd:TIGR02343 302 DDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 310 VKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNS 389
Cdd:TIGR02343 382 IRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENS 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971415 390 GYDLQETLIKIQTKHAESKE-LLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAG 459
Cdd:TIGR02343 462 GLDPIGTLSTLKSLQLKEKNpNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
1-458 |
9.73e-72 |
|
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: 235.81 E-value: 9.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKV----QKE 76
Cdd:TIGR02345 67 LDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVtideEKG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 77 MKREILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGvpIDLFMVEIVEMRHKSETDTQLIRGLVLDHG---ARHP 153
Cdd:TIGR02345 147 EQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 154 RMRKQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIdlkqkvcaeSNKGFVVINQKGIDP 233
Cdd:TIGR02345 225 QQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIV---------ESGANVVLSKLPIGD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 234 VSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGP 313
Cdd:TIGR02345 296 LATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 314 NKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDL 393
Cdd:TIGR02345 376 AEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDS 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971415 394 QETLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:TIGR02345 456 IEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
2-455 |
5.37e-71 |
|
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: 232.57 E-value: 5.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 2 QIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ-KEMKRE 80
Cdd:cd03337 66 DVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 81 ILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRP----GVPIDLFMVEIVEMRHKSE-TDTQLIRGLVLDHGARHPRM 155
Cdd:cd03337 146 QMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAVEengrKKEIDIKRYAKVEKIPGGEiEDSRVLDGVMLNKDVTHPKM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 156 RKQVRDAYILTCNVSLEYektevssgffyktveekeklvkaerkfiedrvqkiidlkqkvcaesnkgfVVINQKGIDPVS 235
Cdd:cd03337 226 RRRIENPRIVLLDCPLEY--------------------------------------------------LVITEKGVSDLA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 236 LEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYAL-GEEKFTFIEDCVNPLSVTLLVKGPN 314
Cdd:cd03337 256 QHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGAS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 315 KHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQ 394
Cdd:cd03337 336 KDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVI 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971415 395 ETLIKIQTKHAESKEL-LGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEI 455
Cdd:cd03337 416 RTLTELRAKHAQGENStWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-458 |
6.11e-70 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 230.35 E-value: 6.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAK----VAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKE 76
Cdd:COG0459 59 IELEDPFENMGAQlvkeVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 77 mKREILLDVARTSLQTKvhAELADIlteaVVDSVLAIRRPGVpidlFMVEivemRHKS-ETDTQLIRGLVLDHGARHP-- 153
Cdd:COG0459 139 -DKEELAQVATISANGD--EEIGEL----IAEAMEKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPyf 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 154 -----RMRKQVRDAYILTCNvsleyektevssgffyKTVEEKEKLVKAerkfiedrVQKIIDLKQKvcaesnkgfVVINQ 228
Cdd:COG0459 204 vtdpeKMPAELENAYILLTD----------------KKISSIQDLLPL--------LEKVAQSGKP---------LLIIA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 229 KGIDPVSLEMLAKHNIVALRRA---------KRRN--LERLTLACGGLAVN-----SFEGLSEECLGHAGLVFEyalGEE 292
Cdd:COG0459 251 EDIDGEALATLVVNGIRGVLRVvavkapgfgDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 293 KFTFIEDCVNPLSVTLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGcVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQ 372
Cdd:COG0459 328 NTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 373 AFADALLIIPKVLAQNSGYDLQETLIKIqtKHAESKElLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLV 452
Cdd:COG0459 407 IVARALEAPLRQIAENAGLDGSVVVEKV--RAAKDKG-FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTT 483
|
....*.
gi 568971415 453 DEIMRA 458
Cdd:COG0459 484 EAVIAD 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
79-338 |
3.35e-67 |
|
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: 213.87 E-value: 3.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVhAELADILTEAVVDSVLAIRRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRKQ 158
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 159 VRDAYILTCNVSLEYektevssgffyktveekeklvkaerkfiedrvqkiidlkqkvcaesnkgfVVINQKGIDPVSLEM 238
Cdd:cd03333 80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 239 LAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHTL 318
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 568971415 319 IQIKDALRDGLRAVKNAIED 338
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
1-420 |
8.32e-67 |
|
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: 222.55 E-value: 8.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-R 79
Cdd:cd03338 57 MSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVP--IDLFMVEIVEMRHKSETDTQLIRGLVLDHGARH-PRMR 156
Cdd:cd03338 137 ESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVIDPATAtnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 157 KQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIidlKQKVCAesnkgfVVINQKGI--DPV 234
Cdd:cd03338 217 TRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDRILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrDAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 235 S---LEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNP-LSVTLLV 310
Cdd:cd03338 288 SdlaLHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 311 KGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSG 390
Cdd:cd03338 368 RGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAG 447
|
410 420 430
....*....|....*....|....*....|
gi 568971415 391 YDLQETLIKIQTKHAESKELLGIDLNTGEP 420
Cdd:cd03338 448 LNPISIVTELRNRHAQGEKNAGINVRKGAI 477
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
3-458 |
8.02e-66 |
|
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: 220.28 E-value: 8.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 3 IQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ----KEMK 78
Cdd:cd03336 66 VDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDhssdEEAF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGvpiDLFMVEIVEMRHKSETDTQLIRGLVLDH--GARHPrmr 156
Cdd:cd03336 146 REDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSG---NLDAIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 157 KQVRDAYILTCNVSLEYEKTEV-SSGFFYKTVEEKEKLVKAERKFIEDRVQKIIdlkqkvcaeSNKGFVVINQKGIDPVS 235
Cdd:cd03336 220 KRIENAKILIANTPMDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKIL---------KHGINCFINRQLIYNYP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 236 LEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNK 315
Cdd:cd03336 291 EQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 316 HTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQE 395
Cdd:cd03336 371 QILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAE 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971415 396 TLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:cd03336 451 LVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-458 |
1.27e-65 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 219.90 E-value: 1.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKV----QKE 76
Cdd:PTZ00212 76 VWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFdhgsDEE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 77 MKREILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGvpiDLFMVEIVEMRHKSETDTQLIRGLVLDH--GARHPr 154
Cdd:PTZ00212 156 KFKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSG---NLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 155 mrKQVRDAYILTCNVSLEYEKTEVSSG-FFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVcaesnkgfvVINQKGIDP 233
Cdd:PTZ00212 232 --KRLENCKILVANTPMDTDKIKIYGAkVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNV---------FINRQLIYN 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 234 VSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGP 313
Cdd:PTZ00212 301 YPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 314 NKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDL 393
Cdd:PTZ00212 381 STHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDS 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971415 394 QETLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:PTZ00212 461 AELVSKLRAEHYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
1-456 |
1.41e-63 |
|
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.
Pssm-ID: 274083 Cd Length: 517 Bit Score: 214.26 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMK-R 79
Cdd:TIGR02342 58 MAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSdR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 80 EILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVP--IDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPR-MR 156
Cdd:TIGR02342 138 EQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVIDPENAknVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 157 KQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIidlKQKVCAesnkgfVVINQKGI----- 231
Cdd:TIGR02342 218 TRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDRVLKEERAYILNIVKKI---KKTGCN------VLLIQKSIlrdav 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 232 DPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNP-LSVTLLV 310
Cdd:TIGR02342 289 NDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 311 KGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSG 390
Cdd:TIGR02342 369 RGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAG 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568971415 391 YDLQETLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIM 456
Cdd:TIGR02342 449 LNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
1-458 |
1.63e-56 |
|
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: 195.70 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEM--- 77
Cdd:TIGR02346 67 LEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKdlr 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 78 KREILLDVARTSLQTKVHAElADILTEAVVDSVLAIRrPGVP--IDLFMVEIVEMRHKSETDTQLIRGLVLdhgARHPRM 155
Cdd:TIGR02346 147 DKDELIKALKASISSKQYGN-EDFLAQLVAQACSTVL-PKNPqnFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 156 R-KQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVcaesnkgfvVINQKGIDPV 234
Cdd:TIGR02346 222 SvKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNV---------IVTGGSVGDM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 235 SLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSV-TLLVKGP 313
Cdd:TIGR02346 293 ALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 314 NKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDL 393
Cdd:TIGR02346 373 TDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNA 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971415 394 QETLIKIQTKHAESKELLGIDLNTGEPMA--AAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:TIGR02346 453 NEVIPKLYAAHKKGNKSKGIDIEAESDGVkdASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
3-458 |
8.19e-51 |
|
T-complex protein 1, beta 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 beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 180.06 E-value: 8.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 3 IQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQ----KEMK 78
Cdd:TIGR02341 67 VDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDngsdEVKF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 79 REILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGvpiDLFMVEIVEMRHKSETDTQLIRGLVLDH--GARHPrmr 156
Cdd:TIGR02341 147 RQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSG---NLEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP--- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 157 KQVRDAYILTCNVSLEYEKTEV-SSGFFYKTVEEKEKLVKAERKFIEDRVQKIIdlkqkvcaeSNKGFVVINQKGIDPVS 235
Cdd:TIGR02341 221 KRIENAKILIANTGMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKIL---------KHGINCFINRQLIYNYP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 236 LEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNK 315
Cdd:TIGR02341 292 EQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQ 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 316 HTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQE 395
Cdd:TIGR02341 372 QILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAE 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971415 396 TLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:TIGR02341 452 LVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
1-458 |
1.44e-48 |
|
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: 173.18 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 1 MQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMKRE 80
Cdd:cd03341 57 LEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 81 ILLDVA---RTSLQTKVhAELADILTEAVVDSVLAIrrpgVPIDLFM-----VEIVEMRHKSETDTQLIRGLVLDHGARH 152
Cdd:cd03341 137 NKEEVSkalKTAIASKQ-YGNEDFLSPLVAEACISV----LPENIGNfnvdnIRVVKILGGSLEDSKVVRGMVFKREPEG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 153 PRMRKQVRDAYILTCNvsleyektevssgffyktveekeklvkaerkfiedrvqkiIDLKQKVcaesnkgfvVINQKGID 232
Cdd:cd03341 212 SVKRVKKAKVAVFSCP----------------------------------------FDIGVNV---------IVAGGSVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 233 PVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSV-TLLVK 311
Cdd:cd03341 243 DLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 312 GPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGY 391
Cdd:cd03341 323 GATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971415 392 DLQETLIKIQTKHAESKELLGIDLNTGEP--MAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRA 458
Cdd:cd03341 403 DATEVLSELYAAHQKGNKSAGVDIESGDEgtKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
137-322 |
4.44e-11 |
|
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: 63.01 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 137 DTQLIRGLVLDHGARHPRMRKQVRDAYILTCNVSLEYEKtevssgffyktVEEK----EKLVKAERKFIEDRVQKIIDLK 212
Cdd:cd03334 62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR-----------VENKllslDPVILQEKEYLKNLVSRIVALR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 213 QKVcaesnkgfvVINQKGIDPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEEC-LGHAGLV----FEY 287
Cdd:cd03334 131 PDV---------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSPkLGTCESFrvrtYVE 201
|
170 180 190
....*....|....*....|....*....|....*.
gi 568971415 288 ALGEEK-FTFIEDCVNPLSVTLLVKGPNKHTLIQIK 322
Cdd:cd03334 202 EHGRSKtLMFFEGCPKELGCTILLRGGDLEELKKVK 237
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
8-444 |
3.32e-06 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 49.53 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 8 ASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMKREIlLDVAR 87
Cdd:PTZ00114 82 AQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDI-LNVAT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 88 TSLQTKVHaeladiLTEAVVDSVLAIRRPGVpIdlfmveIVEMRHKSETDTQLIRGLVLDHGARHPR-------MRKQVR 160
Cdd:PTZ00114 161 ISANGDVE------IGSLIADAMDKVGKDGT-I------TVEDGKTLEDELEVVEGMSFDRGYISPYfvtnektQKVELE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 161 DAYILTCNVSLEYEKTEVSsgFFYKTVEEKEKLVKAERKFIEDRVQKII----DLKQKVCAESNKGF------------- 223
Cdd:PTZ00114 228 NPLILVTDKKISSIQSILP--ILEHAVKNKRPLLIIAEDVEGEALQTLIinklRGGLKVCAVKAPGFgdnrkdilqdiav 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 224 ----VVINQKG----IDPVSLEML--AKHNIV----------------------ALRRAKRRNL---------ERLTLAC 262
Cdd:PTZ00114 306 ltgaTVVSEDNvglkLDDFDPSMLgsAKKVTVtkdetviltgggdkaeikerveLLRSQIERTTseydkeklkERLAKLS 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 263 GGLAVNSFEGLSEeclghaglvFEyaLGEekftfiedcvnplsvtllvkgpnkhtliqIKDALRDGLRAVKNAIEDGcVV 342
Cdd:PTZ00114 386 GGVAVIKVGGASE---------VE--VNE-----------------------------KKDRIEDALNATRAAVEEG-IV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 343 PGAGAVEVAIAEAL-----VNYKHRVQgrvRLGIQAFADALLIIPKVLAQNSGYDLQETLIKIQTKHAESKellGIDLNT 417
Cdd:PTZ00114 425 PGGGVALLRASKLLdkleeDNELTPDQ---RTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSF---GYDAQT 498
|
490 500
....*....|....*....|....*...
gi 568971415 418 GEPMAAAEAGIWDNYCVKKH-LLHSCTV 444
Cdd:PTZ00114 499 GEYVNMFEAGIIDPTKVVRSaLVDAASV 526
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
8-456 |
4.97e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 48.97 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 8 ASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMKREIlldvAR 87
Cdd:PRK12851 71 AQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEI----AQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 88 T-SLQTKVHAELADILTEAVVDsvlaIRRPGVPIdlfmveiVEMRHKSETDTQLIRGLVLDHGARHP-------RMRKQV 159
Cdd:PRK12851 147 VaTISANGDAEIGRLVAEAMEK----VGNEGVIT-------VEESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 160 RDAYILTCNVSLEYEKTevssgffykTVEEKEKLVKAERKFI---ED--------RVQKIIDLKQKVCAESNKGF----- 223
Cdd:PRK12851 216 EDPYILIHEKKISNLQD---------LLPVLEAVVQSGKPLLiiaEDvegealatLVVNKLRGGLKVAAVKAPGFgdrrk 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 224 -------------VVINQKGI--DPVSLEMLAkhnivalrRAKRRNLER--LTLACGGlavnsfeGLSEECLGHAGLV-- 284
Cdd:PRK12851 287 amlediailtggtVISEDLGIklENVTLEQLG--------RAKKVVVEKenTTIIDGA-------GSKTEIEGRVAQIra 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 285 -FEYALGEEKFTFIEDCVNPLS---VTLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGcVVPGAGAVEVAIAEALVNYK 360
Cdd:PRK12851 352 qIEETTSDYDREKLQERLAKLAggvAVIRVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 361 HRvQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLIKIqtkhAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLH 440
Cdd:PRK12851 431 TA-NGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKL----REKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQ 505
|
490
....*....|....*.
gi 568971415 441 SCTVIATNILLVDEIM 456
Cdd:PRK12851 506 NAASVAGLLLTTEAMV 521
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
8-430 |
1.19e-04 |
|
GroEL_like type I chaperonin. 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. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 44.37 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 8 ASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMKREIlLDVAR 87
Cdd:cd03344 68 AQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEI-AQVAT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 88 TSlqTKVHAELADILTEAvvdsVLAIRRPGVpIDlfmveiVEMRHKSETDTQLIRGLVLDHGARHP-------RMRKQVR 160
Cdd:cd03344 147 IS--ANGDEEIGELIAEA----MEKVGKDGV-IT------VEEGKTLETELEVVEGMQFDRGYLSPyfvtdpeKMEVELE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 161 DAYILTCNvsleyekTEVSSgffyktveekeklvkaerkfiedrVQKIIDLKQKvCAESNKGFVVInQKGIDPVSLEMLA 240
Cdd:cd03344 214 NPYILLTD-------KKISS------------------------IQELLPILEL-VAKAGRPLLII-AEDVEGEALATLV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 241 KH------NIVALR----RAKRRN-LERLTLACGGLAVN-----SFEGLSEECLGHAGLVfeyALGEEKFTFIEDCVNPL 304
Cdd:cd03344 261 VNklrgglKVCAVKapgfGDRRKAmLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKV---VVTKDDTTIIGGAGDKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 305 SV-----------------------------------TLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGcVVPGAGAVE 349
Cdd:cd03344 338 AIkariaqirkqieettsdydkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVAL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 350 VAIAEALVNYKhRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLIKIQtkhaESKELLGIDLNTGEPMAAAEAGIW 429
Cdd:cd03344 417 LRASPALDKLK-ALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEYVDMIEAGII 491
|
.
gi 568971415 430 D 430
Cdd:cd03344 492 D 492
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
8-458 |
1.87e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 43.94 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 8 ASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMKREIlldvAR 87
Cdd:PRK12850 71 AQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEI----AQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 88 T-SLQTKVHAELADILTEAVvDSVlaiRRPGVPIdlfmveiVEMRHKSETDTQLIRGLVLDHGARHP-------RMRKQV 159
Cdd:PRK12850 147 VaTISANGDESIGEMIAEAM-DKV---GKEGVIT-------VEEAKTLGTELDVVEGMQFDRGYLSPyfvtnpeKMRAEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 160 RDAYILTCNVSLeyektevssgffyktveekeklvkaerkfieDRVQKIIDLKQKVcAESNKGFVVINQKgIDPVSLEML 239
Cdd:PRK12850 216 EDPYILLHEKKI-------------------------------SNLQDLLPILEAV-VQSGRPLLIIAED-VEGEALATL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 240 AKHNI-----VALRRA----KRRN--LERLTLACGGLAVNSFEG--LSEECLGHAGLVFEYALGEEKFTF---------I 297
Cdd:PRK12850 263 VVNKLrgglkSVAVKApgfgDRRKamLEDIAVLTGGQVISEDLGikLENVTLDMLGRAKRVLITKENTTIidgagdkknI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 298 EDCVNPLSV--------------------------TLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGcVVPGAGaveVA 351
Cdd:PRK12850 343 EARVKQIRAqieettsdydreklqerlaklaggvaVIRVGGATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGG---VA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 352 IAEAL--VNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLIKIqtkhAESKELLGIDLNTGEPMAAAEAGIW 429
Cdd:PRK12850 419 LLRARsaLRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKV----AELPGNFGFNAQTGEYGDMVEAGII 494
|
490 500
....*....|....*....|....*....
gi 568971415 430 DNYCVKKHLLHSCTVIATnILLVDEIMRA 458
Cdd:PRK12850 495 DPAKVTRTALQDAASIAA-LLITTEAMVA 522
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
8-458 |
3.23e-04 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 43.10 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 8 ASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKAleVLDEIKVQKEM-KREILLDVA 86
Cdd:PRK14104 71 AQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAV--VADLVKNSKKVtSNDEIAQVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 87 RTSLQ--TKVHAELADILTEAVVDSVLAirrpgvpidlfmveiVEMRHKSETDTQLIRGLVLDHGARHP-------RMRK 157
Cdd:PRK14104 149 TISANgdAEIGKFLADAMKKVGNEGVIT---------------VEEAKSLETELDVVEGMQFDRGYISPyfvtnadKMRV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 158 QVRDAYIL-------TCNVSLEYEKTEVSSGFFYKTVEEKEKlVKAERKFIEDRVQ---KIIDLKQKVCAESNK------ 221
Cdd:PRK14104 214 EMDDAYILinekklsSLNELLPLLEAVVQTGKPLVIVAEDVE-GEALATLVVNRLRgglKVAAVKAPGFGDRRKamlqdi 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 222 -----GFVVINQKGI--DPVSLEMLAKHNIVALRRakrrnlERLTLACGG-------LAVNSFEGLSEECLGHaglvFEY 287
Cdd:PRK14104 293 ailtgGQAISEDLGIklENVTLQMLGRAKKVMIDK------ENTTIVNGAgkkadieARVAQIKAQIEETTSD----YDR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 288 ALGEEKFTFIEDCVnplsVTLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGcVVPGAGAVEVAIAEALVNYKHRVQGRv 367
Cdd:PRK14104 363 EKLQERLAKLAGGV----AVIRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTKNDDQ- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971415 368 RLGIQAFADALLIIPKVLAQNSGYDLQETLIKIQTKHAESkelLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIAT 447
Cdd:PRK14104 437 KTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYS---YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAA 513
|
490
....*....|.
gi 568971415 448 nILLVDEIMRA 458
Cdd:PRK14104 514 -LLITTEAMVA 523
|
|
| |
