|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-501 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 836.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:NF041082 16 RDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:NF041082 96 VLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAVVDDEG--KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDP 238
Cdd:NF041082 176 VKAVAEKDGgyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 239 AKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 318
Cdd:NF041082 256 DQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 319 DLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKL 398
Cdd:NF041082 336 DLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 399 REYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGVVEPLRVK 478
Cdd:NF041082 416 REYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTGKVVDMLEIGVVEPLRVK 494
|
490 500
....*....|....*....|...
7R9J_J 479 TQAIQSAAESTEMLLRIDDVIAA 501
Cdd:NF041082 495 TQAIKSATEAAVMILRIDDVIAA 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-501 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 813.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:NF041083 16 RDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:NF041083 96 VLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITD 237
Cdd:NF041083 176 VKQVAEKRDgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 238 PAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSA 317
Cdd:NF041083 256 PDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 318 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 397
Cdd:NF041083 336 EDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 398 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGVVEPLRV 477
Cdd:NF041083 416 LREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTGEVVDMWELGVIEPLRV 494
|
490 500
....*....|....*....|....
7R9J_J 478 KTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:NF041083 495 KTQAIKSATEAATMILRIDDVIAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-501 |
0e+00 |
|
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: 782.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:cd03343 94 VLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITD 237
Cdd:cd03343 174 VLQVAEKRDgkyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 238 PAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSA 317
Cdd:cd03343 254 PDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 318 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 397
Cdd:cd03343 334 EDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 398 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 477
Cdd:cd03343 414 LREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE-KGNKNAGLDVYTGEVVDMLEKGVIEPLRV 492
|
490 500
....*....|....*....|....
7R9J_J 478 KTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:cd03343 493 KKQAIKSATEAATMILRIDDVIAA 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-501 |
0e+00 |
|
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: 700.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:TIGR02339 15 RDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKG-AEKAKEKLAEIIVE 159
Cdd:TIGR02339 95 VLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAsAEVAKDKLADLVVE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 160 AVSAVV----DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRI 235
Cdd:TIGR02339 175 AVKQVAelrgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 236 TDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDL 315
Cdd:TIGR02339 255 TDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 316 SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELS 395
Cdd:TIGR02339 335 TESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 396 MKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPL 475
Cdd:TIGR02339 415 LRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE-KGNKNAGINVFTGEIEDMLELGVIEPL 493
|
490 500
....*....|....*....|....*.
7R9J_J 476 RVKTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:TIGR02339 494 RVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
14-501 |
0e+00 |
|
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: 616.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 14 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL 93
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 94 LDQNVHPTIVVKGYQAAAQKAQELLKTIAC-EVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVD 172
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISiPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 173 KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLMEFIEQEEKML 252
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 253 KDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKIS 332
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 333 GDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLA 412
Cdd:pfam00118 321 DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 413 VRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEML 492
Cdd:pfam00118 401 IEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA-SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
|
....*....
7R9J_J 493 LRIDDVIAA 501
Cdd:pfam00118 480 LRIDDIIKA 488
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-500 |
0e+00 |
|
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: 588.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:cd00309 7 EEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:cd00309 87 VLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEiketetdaeiritdpak 240
Cdd:cd00309 167 VLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE----------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 241 lmefieqeekmlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDL 320
Cdd:cd00309 230 ------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 321 GDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLRE 400
Cdd:cd00309 286 GTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 401 YAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQ 480
Cdd:cd00309 366 LAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHA-EGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQ 444
|
490 500
....*....|....*....|
7R9J_J 481 AIQSAAESTEMLLRIDDVIA 500
Cdd:cd00309 445 ALKSATEAASLILTIDDIIV 464
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-503 |
3.09e-175 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 502.30 E-value: 3.09e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGT 76
Cdd:COG0459 9 EDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 77 TTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEI 156
Cdd:COG0459 89 TTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANG------DEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 157 IVEAVSAVVDDegkvdkDLIKIEKKSGASiDDTELIKGVLVDKERVSAQ-------MPKKVTDAKIALLNCAIEIketet 229
Cdd:COG0459 161 IAEAMEKVGKD------GVITVEEGKGLE-TELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISS----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 230 daeiritdpaklmefieqeEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDME 298
Cdd:COG0459 229 -------------------IQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 299 KLAKATGANVITN-----IKDLSAQDLGDAGLVEERKisgDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGV 373
Cdd:COG0459 290 DIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 374 VGCTIEDGrIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAhasnGNKC 453
Cdd:COG0459 367 TRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA----KDKG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
7R9J_J 454 AGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 503
Cdd:COG0459 442 FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKP 491
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
2-500 |
3.20e-165 |
|
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: 477.95 E-value: 3.20e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 2 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:cd03339 23 EAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIA--CEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVE 159
Cdd:cd03339 103 LAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 160 AVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDP 238
Cdd:cd03339 183 AVLSVADLERKdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 239 AKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 318
Cdd:cd03339 263 EDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 319 DLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSM 396
Cdd:cd03339 343 KLGKAGLVREISFgtTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 397 KLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLR 476
Cdd:cd03339 423 AVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMKEQKVFETLI 502
|
490 500
....*....|....*....|....
7R9J_J 477 VKTQAIQSAAESTEMLLRIDDVIA 500
Cdd:cd03339 503 SKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
7-501 |
9.17e-155 |
|
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: 450.97 E-value: 9.17e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 7 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 86
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 87 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVD 166
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 167 DEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERV-SAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME 243
Cdd:cd03338 173 PATATNVDLkdIRIVKKLGGTIEDTELVDGLVFTQKASkKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 244 FIEQEEKMLKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 318
Cdd:cd03338 253 ILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 319 DLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 397
Cdd:cd03338 333 KLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 398 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 477
Cdd:cd03338 413 LSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA-QGEKNAGINVRKGAITNILEENVVQPLLV 491
|
490 500
....*....|....*....|....
7R9J_J 478 KTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:cd03338 492 STSAITLATETVRMILKIDDIVLA 515
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
7-503 |
2.31e-151 |
|
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: 442.50 E-value: 2.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 7 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 86
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 87 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDK----EILTKIAMTSITGKGAEKAKEKLAEIIVEAVS 162
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 163 AVVDDegkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEIKETETDAEIRITDPA 239
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAgfeQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 240 KLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQD 319
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 320 LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLR 399
Cdd:cd03340 338 LGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 400 EYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKT 479
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490 500
....*....|....*....|....
7R9J_J 480 QAIQSAAESTEMLLRIDDVIAAEK 503
Cdd:cd03340 498 NALTAATEAACLILSVDETIKNPK 521
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
2-502 |
2.36e-150 |
|
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: 440.39 E-value: 2.36e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 2 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD--KEILTKIAMTSITGKGAEKAKEKLAEIIVE 159
Cdd:TIGR02343 107 LAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVSKCHRRFAEIAVD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 160 AVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDP 238
Cdd:TIGR02343 187 AVLNVADMERRdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 239 AKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 318
Cdd:TIGR02343 267 EEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 319 DLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSM 396
Cdd:TIGR02343 347 KLGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 397 KLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLR 476
Cdd:TIGR02343 427 AVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLI 506
|
490 500
....*....|....*....|....*.
7R9J_J 477 VKTQAIQSAAESTEMLLRIDDVIAAE 502
Cdd:TIGR02343 507 GKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
2-499 |
5.63e-143 |
|
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: 421.31 E-value: 5.63e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 2 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:cd03335 8 DVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:cd03335 88 IAAELLKRANELVKQKIHPTTIISGYRLACKEAvKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRIT 236
Cdd:cd03335 168 ILAVktTNEKGKTKYPIkaVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 237 DPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDL- 315
Cdd:cd03335 248 DPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLe 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 316 -----SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGST 390
Cdd:cd03335 328 geetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 391 EVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLNVFTGAV 463
Cdd:cd03335 408 ETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAaqvkpdkKHLKWYGLDLINGKV 487
|
490 500 510
....*....|....*....|....*....|....*.
7R9J_J 464 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 499
Cdd:cd03335 488 RDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
1-503 |
2.76e-141 |
|
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: 416.83 E-value: 2.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:TIGR02344 15 RKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:TIGR02344 95 ILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAVVDDEG---KVD-KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRIT 236
Cdd:TIGR02344 175 VRTVQRDENgrkEIDiKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEIT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 237 DPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLS 316
Cdd:TIGR02344 255 KEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 317 AQDLG-DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELS 395
Cdd:TIGR02344 335 ESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 396 MKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPL 475
Cdd:TIGR02344 415 VALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIVDMKEKGIWEPL 494
|
490 500
....*....|....*....|....*...
7R9J_J 476 RVKTQAIQSAAESTEMLLRIDDVIAAEK 503
Cdd:TIGR02344 495 AVKLQTYKTAIESACLLLRIDDIVSGVK 522
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-501 |
1.30e-140 |
|
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: 413.23 E-value: 1.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAV 80
Cdd:cd03337 15 RKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 81 VVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:cd03337 95 ILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAV-VDDEGKVD----KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIketetdaeiri 235
Cdd:cd03337 175 VKTVaVEENGRKKeidiKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY----------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 236 tdpaklmefieqeekmlkdmvaeikasganVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDL 315
Cdd:cd03337 244 ------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 316 SAQDLGDAGLVEERKISGDSMI-FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVEL 394
Cdd:cd03337 294 TESDVGTGAGLFEVKKIGDEYFtFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 395 SMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEP 474
Cdd:cd03337 374 SHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDIVDMKELGIWDP 453
|
490 500
....*....|....*....|....*..
7R9J_J 475 LRVKTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:cd03337 454 LAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
7-503 |
6.09e-139 |
|
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: 410.69 E-value: 6.09e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 7 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 86
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 87 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSA 163
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 164 VVDDEgkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAK 240
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAgfeQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 241 LMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDL 320
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 321 GDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLRE 400
Cdd:TIGR02345 341 GTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 401 YAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQ 480
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA-KGGKWYGVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|...
7R9J_J 481 AIQSAAESTEMLLRIDDVIAAEK 503
Cdd:TIGR02345 500 ALKAAFEAACTILSVDETITNPK 522
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
2-501 |
5.99e-136 |
|
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: 403.01 E-value: 5.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 2 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 161
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 162 SAVVDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVD-KERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDP 238
Cdd:TIGR02342 169 LKVIDPENAKNVDLndIKVVKKLGGTIDDTELIEGLVFTqKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 239 AKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIK 313
Cdd:TIGR02342 249 AQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASID 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 314 DLSAQDLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEV 392
Cdd:TIGR02342 329 HFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 393 ELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVV 472
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHA-NGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*....
7R9J_J 473 EPLRVKTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIVFT 516
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
2-499 |
2.23e-135 |
|
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: 402.18 E-value: 2.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 2 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:TIGR02340 12 DVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEA 160
Cdd:TIGR02340 92 IAAELLKRADELVKNKIHPTSVISGYRLACKEAvKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 161 VSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRIT 236
Cdd:TIGR02340 172 VLAVktTNENGETKYPIkaINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 237 DPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLS 316
Cdd:TIGR02340 252 DPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 317 AQD------LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGST 390
Cdd:TIGR02340 332 GEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 391 EVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLNVFTGAV 463
Cdd:TIGR02340 412 EAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekKHLKWYGLDLVNGKI 491
|
490 500 510
....*....|....*....|....*....|....*.
7R9J_J 464 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 499
Cdd:TIGR02340 492 RDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
5-501 |
2.21e-121 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 365.89 E-value: 2.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAGRI-IAETVRSTLGPKGMDKMLV-----DDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTT 78
Cdd:PTZ00212 24 RLQSFVGAIaVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 79 AVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAE 155
Cdd:PTZ00212 104 VVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSKLLTVEKDHFAK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 156 IiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIEiketeTD----- 230
Cdd:PTZ00212 184 L---AVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKRLENCKILVANTPMD-----TDkikiy 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 231 -AEIRITDPAKLMEfIEQEEKM-LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANV 308
Cdd:PTZ00212 255 gAKVKVDSMEKVAE-IEAAEKEkMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 309 ITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGG 388
Cdd:PTZ00212 334 VSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 389 STEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCE 468
Cdd:PTZ00212 414 CSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY-KGNKTAGIDMEKGTVGDMKE 492
|
490 500 510
....*....|....*....|....*....|...
7R9J_J 469 NGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:PTZ00212 493 LGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
5-501 |
4.08e-119 |
|
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: 359.72 E-value: 4.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAGRI-IAETVRSTLGPKGMDKML--VDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:cd03336 15 RLSSFVGAIaIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAEIiv 158
Cdd:cd03336 95 LAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKILTQDKEHFAEL-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 159 eAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIEiketeTD------AE 232
Cdd:cd03336 173 -AVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTPMD-----TDkikifgAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 233 IRITDPAKLMEfIEQEEKM-LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 311
Cdd:cd03336 246 VRVDSTAKVAE-IEEAEKEkMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIAST 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 312 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTE 391
Cdd:cd03336 325 FDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 392 VELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGV 471
Cdd:cd03336 405 MLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY-NGNTTAGLDMRKGTVGDMKELGI 483
|
490 500 510
....*....|....*....|....*....|
7R9J_J 472 VEPLRVKTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:cd03336 484 TESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
3-501 |
4.16e-119 |
|
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: 358.49 E-value: 4.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 3 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 82
Cdd:cd03342 13 ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 83 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVG-AQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 161
Cdd:cd03342 93 IGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 162 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEiritdpakl 241
Cdd:cd03342 173 LAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSG--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 242 meFIeqeekmlkdmvaeikasgANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLG 321
Cdd:cd03342 244 --FF------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 322 DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREY 401
Cdd:cd03342 304 YAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 402 AEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQA 481
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAE-GGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490 500
....*....|....*....|
7R9J_J 482 IQSAAESTEMLLRIDDVIAA 501
Cdd:cd03342 463 LHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
3-501 |
1.73e-116 |
|
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: 353.27 E-value: 1.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 3 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 82
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 83 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-DKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 161
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 162 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKL 241
Cdd:TIGR02347 177 LAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 242 MEFIEQEEKMLKDMVAEI-----KASGAN-----VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 311
Cdd:TIGR02347 257 EKLVKAERKFVDDRVKKIielkkKVCGKSpdkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 312 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTE 391
Cdd:TIGR02347 337 VEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 392 VELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGV 471
Cdd:TIGR02347 417 IAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH-DEGGEVVGVDLNTGEPIDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|
7R9J_J 472 VEPLRVKTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:TIGR02347 496 WDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
7-501 |
2.51e-114 |
|
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: 345.74 E-value: 2.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 7 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 86
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 87 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACE--VGAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 164
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 165 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKErVSAQMpKKVTDAKIALLNCAIEIketetdaeiritdpaklme 243
Cdd:cd03341 172 LpENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFDI------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 244 fieqeekmlkdmvaeikasGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDA 323
Cdd:cd03341 231 -------------------GVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 324 GLVEERKISGDSMIFVEECKHPKAV-TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYA 402
Cdd:cd03341 292 DSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 403 EGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQ 480
Cdd:cd03341 372 EKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAH-QKGNKSAGVDIESGdeGTKDAKEAGIFDHLATKKW 450
|
490 500
....*....|....*....|.
7R9J_J 481 AIQSAAESTEMLLRIDDVIAA 501
Cdd:cd03341 451 AIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
7-503 |
1.66e-113 |
|
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: 345.93 E-value: 1.66e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 7 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 86
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 87 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKT-IACEV-GAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 164
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElVVWEVkDLRDKDELIKALKASISSKQYGNE-DFLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 165 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQmpKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME 243
Cdd:TIGR02346 182 LpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSV--KSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 244 FIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDA 323
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 324 GLVEERKISGDSM-IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYA 402
Cdd:TIGR02346 340 DSVYVSEIGGDKVtVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 403 EGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQ 480
Cdd:TIGR02346 420 EKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKK-GNKSKGIDIEAEsdGVKDASEAGIYDMLATKKW 498
|
490 500
....*....|....*....|...
7R9J_J 481 AIQSAAESTEMLLRIDDVIAAEK 503
Cdd:TIGR02346 499 AIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
5-501 |
1.46e-93 |
|
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: 294.07 E-value: 1.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAGRI-IAETVRSTLGPKGMDKMLVDD--LGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 81
Cdd:TIGR02341 16 RLSSFVGAIaIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 82 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEI---LTKIAMTSITGKGAEKAKEKLAEIiv 158
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFrqdLMNIARTTLSSKILSQHKDHFAQL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 159 eAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIEIKETET-DAEIRITD 237
Cdd:TIGR02341 174 -AVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKVKIfGSRVRVDS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 238 PAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSA 317
Cdd:TIGR02341 252 TAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPEL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 318 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 397
Cdd:TIGR02341 332 VKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 398 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 477
Cdd:TIGR02341 412 VTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDMNEGTIADMRQLGITESYKV 490
|
490 500
....*....|....*....|....
7R9J_J 478 KTQAIQSAAESTEMLLRIDDVIAA 501
Cdd:TIGR02341 491 KRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
130-380 |
1.47e-71 |
|
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: 226.19 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 130 KEILTKIAMTSITGKGaEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKK 209
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 210 VTDAKIALLNCAIEiketetdaeiritdpaklmefieqeekmlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAA 289
Cdd:cd03333 80 LENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 290 RRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDD 369
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHD 198
|
250
....*....|.
7R9J_J 370 AVGVVGCTIED 380
Cdd:cd03333 199 ALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
5-486 |
6.61e-34 |
|
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: 134.12 E-value: 6.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 79
Cdd:cd03344 10 RKALLRGvNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 80 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 159
Cdd:cd03344 90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 160 AVSavvddegKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDAK---IALLNCAIEIketeTDAEIR 234
Cdd:cd03344 162 AME-------KVGKDgVITVE--EGKTLETElEVVEGMQFDRGYLS---PYFVTDPEkmeVELENPYILL----TDKKIS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 235 -ITDPAKLMEFIEQEEKMLKdMVAEikasganvlfcqkgidDLAQHYLA------KEGIVAARRVK--------KSDMEK 299
Cdd:cd03344 226 sIQELLPILELVAKAGRPLL-IIAE----------------DVEGEALAtlvvnkLRGGLKVCAVKapgfgdrrKAMLED 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 300 LAKATGANVITN-----IKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV-------------------------- 348
Cdd:cd03344 289 IAILTGGTVISEelglkLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqer 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 349 -------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADA 419
Cdd:cd03344 366 laklsggVAVIKvgGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVRRA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
7R9J_J 420 LEVIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA 486
Cdd:cd03344 444 LEAPLRQIAENAGVDGSVVVEKVL-----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAA 505
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-500 |
6.36e-31 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 125.69 E-value: 6.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 75
Cdd:PRK12849 8 DEEARRALERGvNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 76 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 155
Cdd:PRK12849 88 TTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 156 IIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAK--IALL-NCAIEIketeTDA 231
Cdd:PRK12849 160 LIAEAME-------KVGKDgVITVEESKTLE-TELEVTEGMQFDRGYLSPYF---VTDPErmEAVLeDPLILL----TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 232 EIR-ITDPAKLMEFIEQEEKMLKdMVAEikasganvlfcqkgidDLAQHYLA-------KEGI-VAA--------RRvkK 294
Cdd:PRK12849 225 KISsLQDLLPLLEKVAQSGKPLL-IIAE----------------DVEGEALAtlvvnklRGGLkVAAvkapgfgdRR--K 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 295 SDMEKLAKATGANVIT-----NIKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV--------------------- 348
Cdd:PRK12849 286 AMLEDIAILTGGTVISedlglKLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIearvaqirrqieettsdydre 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 349 ------------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAeGISGREQLAVR 414
Cdd:PRK12849 363 klqerlaklaggVAVIKvgAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELA-GLNGDQAAGVE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 415 AFADALEVIPRTLAENAGLDAIEILVKVRAahasnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLR 494
Cdd:PRK12849 441 IVRRALEAPLRQIAENAGLDGSVVVAKVLE-----LEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLT 515
|
....*.
7R9J_J 495 IDDVIA 500
Cdd:PRK12849 516 TEALVA 521
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
143-374 |
1.02e-27 |
|
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: 111.54 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 143 GKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLI----KIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALL 218
Cdd:cd03334 13 ISNDESWLDILLPLVWKAASNVKPDVRAGDDMDIrqyvKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 219 NCAIEIKETETdaeiritdpaKLMEF---IEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKS 295
Cdd:cd03334 93 QGPLEYQRVEN----------KLLSLdpvILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 296 DMEKLAKATGANVITNIKDLSA-QDLGDAGLVEERKI-----SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDD 369
Cdd:cd03334 163 VLERISRCTGADIISSMDDLLTsPKLGTCESFRVRTYveehgRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEF 242
|
....*
7R9J_J 370 AVGVV 374
Cdd:cd03334 243 MVFAA 247
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
5-500 |
1.07e-26 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 113.16 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 79
Cdd:TIGR02348 11 RKALLRGvDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 80 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGaqDKEILTKIAMTSITGkgaekaKEKLAEIIVE 159
Cdd:TIGR02348 91 TVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN------DEEIGSLIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 160 AVSavvddegKVDKD-LIKIEKKSGAsIDDTELIKGVLVDKERVSaqmPKKVTDAkiallncaiEIKETE-TDAEIRITD 237
Cdd:TIGR02348 163 AME-------KVGKDgVITVEESKSL-ETELEVVEGMQFDRGYIS---PYFVTDA---------EKMEVElENPYILITD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 238 paklmefieQEEKMLKDMV---AEIKASGANVLFCQKGIDDLAQHYLA---KEGIVAARRVK--------KSDMEKLAKA 303
Cdd:TIGR02348 223 ---------KKISNIKDLLpllEKVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrKAMLEDIAIL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 304 TGANVIT-----NIKDLSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVTMLIR------------------------- 353
Cdd:TIGR02348 294 TGGQVISeelglKLEEVTLDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKARVAqikaqieettsdydreklqerlakl 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 354 ----------GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALEVI 423
Cdd:TIGR02348 371 aggvavikvgAATETEMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAAL-EGLKGDGEDEAIGIDIVKRALEAP 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7R9J_J 424 PRTLAENAGLDAIEILVKVRaahASNGNKcaGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 500
Cdd:TIGR02348 449 LRQIAENAGLDGAVVAEKVK---ELKGNF--GFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVA 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
13-505 |
6.08e-24 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 105.19 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 13 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 88
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 89 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAEIIVEAVSavvdde 168
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANG------DESIGEMIAEAMD------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 169 gKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSaqmPKKVTDAKiallncaieiketetDAEIRITDPAKLMEfiEQ 247
Cdd:PRK12850 168 -KVGKEgVITVEEAKTLG-TELDVVEGMQFDRGYLS---PYFVTNPE---------------KMRAELEDPYILLH--EK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 248 EEKMLKDMVAEIKA---SGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSDMEKLAKATGANVI---T 310
Cdd:PRK12850 226 KISNLQDLLPILEAvvqSGRPLLIIAEDVEGEALATLVVNKLrgglkSVAVKApgfgdrRKAMLEDIAVLTGGQVIsedL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 311 NIK--DLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV---------------------------------TMLIR-- 353
Cdd:PRK12850 306 GIKleNVTLDMLGRAKRVL---ITKENTTIIDGAGDKKNIearvkqiraqieettsdydreklqerlaklaggVAVIRvg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 354 GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGL 433
Cdd:PRK12850 383 GATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRG-LKGANADETAGIDIVRRALEEPLRQIATNAGF 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7R9J_J 434 DAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLR 505
Cdd:PRK12850 461 EGSVVVGKVA-----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKK 527
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
5-493 |
2.40e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 97.29 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILR--EMS--VEHPAAKMLIEVAKTQEKEVGDGTTTA 79
Cdd:PTZ00114 24 RQSLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiEFSdrFENVGAQLIRQVASKTNDKAGDGTTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 80 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 159
Cdd:PTZ00114 104 TILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANG------DVEIGSLIAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 160 AVsavvddeGKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEIKETETDAeir 234
Cdd:PTZ00114 176 AM-------DKVGKDgTITVE--DGKTLEDElEVVEGMSFDRGYIS---PYFVTNEktqKVELENPLILVTDKKISS--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 235 ITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKgiddlaqhylAKEGI-VAARRV------KKSDMEKLAKATGAN 307
Cdd:PTZ00114 241 IQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINK----------LRGGLkVCAVKApgfgdnRKDILQDIAVLTGAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 308 VITN------IKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV--------------------------------- 348
Cdd:PTZ00114 311 VVSEdnvglkLDDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsgg 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 349 --TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEG--ISGREQLAVRAFADALEVIP 424
Cdd:PTZ00114 388 vaVIKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEEDneLTPDQRTGVKIVRNALRLPT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7R9J_J 425 RTLAENAGLDAIEILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 493
Cdd:PTZ00114 467 KQIAENAGVEGAVVVEKI----LEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-500 |
3.90e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 96.35 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 1 RDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 75
Cdd:PRK12851 9 HVEAREKMLRGvNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 76 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltKIAMTSITGKGAEKAKEKLAE 155
Cdd:PRK12851 89 TTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE----IAQVATISANGDAEIGRLVAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 156 IIveavsavvddeGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSaqmPKKVTDAKiallncaieiketetDAEIRI 235
Cdd:PRK12851 165 AM-----------EKVGNEGVITVEESKTAETELEVVEGMQFDRGYLS---PYFVTDAD---------------KMEAEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 236 TDPAKLMefIEQEEKMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDMEKLA 301
Cdd:PRK12851 216 EDPYILI--HEKKISNLQDLLPvleAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVaavkapgfgdrRKAMLEDIA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 302 KATGANVIT-----NIKDLSAQDLGDAGLVEERKI-------SGDSMIFVEECKHPKAV--------------------- 348
Cdd:PRK12851 294 ILTGGTVISedlgiKLENVTLEQLGRAKKVVVEKEnttiidgAGSKTEIEGRVAQIRAQieettsdydreklqerlakla 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 349 --TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIP 424
Cdd:PRK12851 374 ggVAVIRvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRALEAPV 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7R9J_J 425 RTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 500
Cdd:PRK12851 452 RQIAENAGAEGSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
13-503 |
3.41e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 90.55 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 13 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKM---LIEVAKTQEKEV-GDGTTTAVVVAGELLR 88
Cdd:CHL00093 21 ILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 89 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSiTGKGAEkakekLAEIIVEAVSavvdde 168
Cdd:CHL00093 101 QGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV--EDIQAITQVASIS-AGNDEE-----VGSMIADAIE------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 169 gKVDKD-LIKIEKKSGASIdDTELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEIketeTDAEIRIT--DPAKLM 242
Cdd:CHL00093 167 -KVGREgVISLEEGKSTVT-ELEITEGMRFEKGFIS---PYFVTDTermEVVQENPYILL----TDKKITLVqqDLLPIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 243 EFIEQEEKMLKDMVAEIKASGANVLFCQK--GIDDlaqhylakegIVAAR-----RVKKSDMEKLAKATGANVITNIKDL 315
Cdd:CHL00093 238 EQVTKTKRPLLIIAEDVEKEALATLVLNKlrGIVN----------VVAVRapgfgDRRKAMLEDIAILTGGQVITEDAGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 316 SAQDLGDAGLVEERKI--SGDSMIFVEEcKHPKAVTM---------------------------------LIR--GTTEH 358
Cdd:CHL00093 308 SLETIQLDLLGQARRIivTKDSTTIIAD-GNEEQVKArceqlrkqieiadssyekeklqerlaklsggvaVIKvgAATET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 359 VIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAE-GISGREQLAVRAFADALEVIPRTLAENAGLDAIE 437
Cdd:CHL00093 387 EMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAKnNLKEDELIGALIVARAILAPLKRIAENAGKNGSV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7R9J_J 438 ILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 503
Cdd:CHL00093 466 IIEKVQ-----EQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKK 526
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
5-500 |
7.05e-19 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 89.41 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 5 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVA-KTQEKeVGDGTTT 78
Cdd:PRK00013 12 RRKLLRGvNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVAsKTNDV-AGDGTTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 79 AVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDkeiltKIAMT-SITGKGaekaKEKLAEII 157
Cdd:PRK00013 91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKE-----EIAQVaTISANG----DEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 158 VEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAkiallncaiEIKETE-TDAEIRI 235
Cdd:PRK00013 162 AEAME-------KVGKEgVITVEESKGFE-TELEVVEGMQFDRGYLSPYF---VTDP---------EKMEAElENPYILI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 236 TDpAKLmefieqeeKMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAA--------RRvkKSDMEK 299
Cdd:PRK00013 222 TD-KKI--------SNIQDLLPvleQVAQSGKPLLIIAEDVEGEALATLVVNKLrgtlkVVAvkapgfgdRR--KAMLED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 300 LAKATGANVIT-----NIKDLSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVT---MLIRGTTEH------------- 358
Cdd:PRK00013 291 IAILTGGTVISeelglKLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKarvAQIKAQIEEttsdydreklqer 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 359 ---------VI-----------EEVARaVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFAD 418
Cdd:PRK00013 368 laklaggvaVIkvgaatevemkEKKDR-VEDALHATRAAVEEG-IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 419 ALEVIPRTLAENAGLDAIEILVKVRAAHASNgnkcAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDV 498
Cdd:PRK00013 445 ALEAPLRQIAENAGLEGSVVVEKVKNGKGKG----YGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAV 520
|
..
7R9J_J 499 IA 500
Cdd:PRK00013 521 VA 522
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
13-500 |
8.47e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 79.89 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 13 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 88
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 89 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-------------DKEILTKI--AMTSITGKGAEKAKE-K 152
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSaeiaqvgtisangDAAIGKMIaqAMQKVGNEGVITVEEnK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 153 LAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVS---AQMP--KKVTDAKIALLNCAIEIkET 227
Cdd:PRK12852 182 SLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAY----ILLHEKKLSglqAMLPvlEAVVQSGKPLLIIAEDV-EG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 228 ETDAEIRITD--------PAKLMEFIEQEEKMLKDMVAeikASGANVLFCQKGIDdlaqhyLAKEGIVAARRVKKSDMEK 299
Cdd:PRK12852 257 EALATLVVNRlrgglkvaAVKAPGFGDRRKAMLEDIAI---LTGGQLISEDLGIK------LENVTLKMLGRAKKVVIDK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 300 lAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVGVVGCT 377
Cdd:PRK12852 328 -ENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKEKKDRVEDALNATRAA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 378 IEDGrIVSGGGsteVELsMKLREYAEGISGR---EQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahaSNGNKCA 454
Cdd:PRK12852 407 VQEG-IVPGGG---VAL-LRAKKAVGRINNDnadVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIL----ENKSETF 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
7R9J_J 455 GLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 500
Cdd:PRK12852 478 GFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
14-499 |
3.70e-15 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 78.04 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 14 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRK 89
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 90 AEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEiLTKIAMTSiTGKGAEkakekLAEIIVEAVS------A 163
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV--EDSE-LADVAAVS-AGNNYE-----VGNMIAEAMSkvgrkgV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 164 VVDDEGK-VDKDLIKIEkksGASIDDTELIKGVLVDKERVSAQMPK---KVTDAKIALLNCAIEIKEtetDAeIRITDPA 239
Cdd:PLN03167 229 VTLEEGKsAENNLYVVE---GMQFDRGYISPYFVTDSEKMSVEYDNcklLLVDKKITNARDLIGILE---DA-IRGGYPL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 240 KLM-EFIEQeEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSD----MEKLAK---ATGANVI-- 309
Cdd:PLN03167 302 LIIaEDIEQ-EALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEvglsLDKVGKevlGTAAKVVlt 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 310 ----TNIKDLSAQDlgdagLVEERKISGDSMIFVEECKHPK-------------AVTMLIRGTTEHVIEEVARAVDDAVG 372
Cdd:PLN03167 381 kdttTIVGDGSTQE-----AVNKRVAQIKNLIEAAEQDYEKeklneriaklsggVAVIQVGAQTETELKEKKLRVEDALN 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 373 VVGCTIEDGrIVSGGGSTEVELSMKLREYAEGISGREQ-LAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGN 451
Cdd:PLN03167 456 ATKAAVEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKV----LSNDN 530
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
7R9J_J 452 KCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 499
Cdd:PLN03167 531 PKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVV 578
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
13-500 |
1.95e-13 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 72.76 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 13 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 88
Cdd:PRK14104 22 ILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 89 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAEIIVEAVSAvVDDE 168
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE--IAQVGTISANG------DAEIGKFLADAMKK-VGNE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 169 GkvdkdLIKIEKksgASIDDTEL--IKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAeirITDPAKLMEFIE 246
Cdd:PRK14104 173 G-----VITVEE---AKSLETELdvVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSS---LNELLPLLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 247 QEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKL--AKATGANVITNIKDLSAQDLGDA- 323
Cdd:PRK14104 242 QTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILtgGQAISEDLGIKLENVTLQMLGRAk 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 324 -----------------------------GLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVG 372
Cdd:PRK14104 322 kvmidkenttivngagkkadiearvaqikAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKERKDRVDDAMH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7R9J_J 373 VVGCTIEDGrIVSGGGSTEVELSMKLREYAEGiSGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGNK 452
Cdd:PRK14104 402 ATRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKI----LEKEQY 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
7R9J_J 453 CAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 500
Cdd:PRK14104 476 SYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVA 523
|
|
| |
