|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
3-493 |
0e+00 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 789.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 3 AIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347 1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 83 AQDDVTGDGTTSNVLIIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKE--MKRKILLDVARTSLQTKV 160
Cdd:TIGR02347 81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 161 HAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTK----------------------------------- 205
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTlirglvldhgarhpdmprrvknayiltcnvsleye 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 206 --EVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQS-NKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRR 282
Cdd:TIGR02347 241 ktEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 283 NMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIK 362
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 363 NAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGV 442
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 302058290 443 DLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 493
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-489 |
0e+00 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 769.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK--RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 180
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDtdRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 181 RPGYPIDLFMVEIMEMKHKLGTDTK-------------------------------------EVNSGFFYKtaeekeklv 223
Cdd:cd03342 177 KPDEPIDLHMVEIMQMQHKSDSDTKlirglvldhgarhpdmpkrvenayiltcnvsleyektEVNSGFFYS--------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 224 kaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLT 303
Cdd:cd03342 248 -----------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 304 VDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAE 383
Cdd:cd03342 299 PECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 384 ALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCV 463
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|....*.
gi 302058290 464 KKQLLHSCTVIATNILLVDEIMRAGM 489
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
23-486 |
2.47e-174 |
|
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: 498.11 E-value: 2.47e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd00309 13 NINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:cd00309 93 LKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEdREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 PGYPIDLFMVEIMEMKHKLGTDTkEVNSGFfyktAEEKEKLVKAERKFIEDrvQKIidlkdkVCAQSNKGFVVINQKGID 261
Cdd:cd00309 173 ENGDVDLGVIRVEKKKGGSLEDS-ELVVGM----VFDKGYLSPYMPKRLEN--AKI------LLLDCKLEYVVIAEKGID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 262 PFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKG 341
Cdd:cd00309 240 DEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 342 PNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYD 421
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302058290 422 PQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 486
Cdd:cd00309 400 PIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
30-488 |
5.89e-174 |
|
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: 498.27 E-value: 5.89e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLY 109
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 110 ISEGLHPRIIAEGFEAAKIKALEVLEEVKV--TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPID 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 188 LFMVEIMEMKHKLGTDTK-------------------------------------EVNSGFFYKTAEEKEKLVKAERKFI 230
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSElvdgvvldkgplhpdmpkrlenakvlllncsleyektETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 231 EDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHA 310
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 311 GLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKN 390
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 391 SIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHS 470
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 302058290 471 CTVIATNILLVDEIMRAG 488
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
23-488 |
4.77e-121 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 364.21 E-value: 4.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:NF041082 22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:NF041082 102 LKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 P--GYPIDLFMVEImeMKHKLGT--DT---------KE-VNSGFFYKTAEEKEKLVKA--ERKFIE----------DRVQ 235
Cdd:NF041082 182 KdgGYNVDLDNIKV--EKKVGGSieDSelvegvvidKErVHPGMPKRVENAKIALLDAplEVKKTEidakisitdpDQLQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 236 KIID-----LKDKVCAQSNKGF-VVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGH 309
Cdd:NF041082 260 AFLDqeekmLKEMVDKIADSGAnVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 310 AGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYK 389
Cdd:NF041082 340 AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 390 NSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLH 469
Cdd:NF041082 420 ASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIK 499
|
490
....*....|....*....
gi 302058290 470 SCTVIATNILLVDEIMRAG 488
Cdd:NF041082 500 SATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
23-488 |
1.00e-119 |
|
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: 360.81 E-value: 1.00e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03343 20 NIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEE--VKVTKEmKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV- 179
Cdd:cd03343 100 LEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 --RRPGYPIDLFMVEIMemKHKLGT--DT---------KE-VNSGFFYK---------------------------TAEE 218
Cdd:cd03343 179 ekRDGKYVVDLDNIKIE--KKTGGSvdDTelirgividKEvVHPGMPKRvenakialldaplevkkteidakiritSPDQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 219 KEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 298
Cdd:cd03343 257 LQAFLEQEEAMLKEMVDKIAD------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 299 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 378
Cdd:cd03343 328 IDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 379 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 458
Cdd:cd03343 408 IELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVI 487
|
490 500 510
....*....|....*....|....*....|
gi 302058290 459 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 488
Cdd:cd03343 488 EPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
23-488 |
2.67e-119 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 359.65 E-value: 2.67e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:NF041083 22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV-- 179
Cdd:NF041083 102 LKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKvDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVae 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 -RRPGYPIDLFMVEIMEMKHKLGTDT---------KE-VNSGFFYKTAEEKEKLVKA--ERKFIE----------DRVQK 236
Cdd:NF041083 182 kRDGKYYVDLDNIQIEKKHGGSIEDTqliygividKEvVHPGMPKRVENAKIALLDAplEVKKTEidaeiritdpDQLQK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 237 IID-----LKDKVCAQSNKGF-VVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHA 310
Cdd:NF041083 262 FLDqeekmLKEMVDKIKATGAnVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 311 GLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKN 390
Cdd:NF041083 342 ELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLREYAA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 391 SIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHS 470
Cdd:NF041083 422 TVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKS 501
|
490
....*....|....*...
gi 302058290 471 CTVIATNILLVDEIMRAG 488
Cdd:NF041083 502 ATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
23-487 |
1.35e-114 |
|
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: 347.83 E-value: 1.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02339 21 NIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEE--VKVTKEmKRKILLDVARTSLQTKVHAELA-DVLTEVVVDSVLAV 179
Cdd:TIGR02339 101 LEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEiaTKISPE-DRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 RRP----GYPIDLFMVEIMEMKHKLGTDTKEVNSGFFYKTA---------------------EEKEKLVKAERKFIE-DR 233
Cdd:TIGR02339 180 AELrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVvhpgmpkrvenakialldaplEVEKTEIDAKIRITDpDQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 234 VQKIID-----LKDKVCAQSNKGF-VVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCL 307
Cdd:TIGR02339 260 IKKFLDqeeamLKEMVDKIASAGAnVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 308 GHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVT 387
Cdd:TIGR02339 340 GYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLRS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 388 YKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQL 467
Cdd:TIGR02339 420 YARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEPLRVKEQA 499
|
490 500
....*....|....*....|
gi 302058290 468 LHSCTVIATNILLVDEIMRA 487
Cdd:TIGR02339 500 IKSATEAATMILRIDDVIAA 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-484 |
3.91e-83 |
|
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: 265.31 E-value: 3.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03337 21 NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:cd03337 101 LAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 pgypidlfmveimemkhKLGTDTKEVNSGFFYKTaeekEKLVKAErkfIED-RVQKIIDL-KDKVCAQ------------ 247
Cdd:cd03337 181 -----------------EENGRKKEIDIKRYAKV----EKIPGGE---IEDsRVLDGVMLnKDVTHPKmrrrienprivl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 248 --SNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTL-GEEKFT 324
Cdd:cd03337 237 ldCPLEYLVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 325 FIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFA 404
Cdd:cd03337 317 FITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 405 DALLIIPKVLAQNAGYDPQETLVKVQAEHVES-KQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDE 483
Cdd:cd03337 397 SALEVIPRTLAQNCGANVIRTLTELRAKHAQGeNSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDD 476
|
.
gi 302058290 484 I 484
Cdd:cd03337 477 I 477
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-484 |
2.29e-81 |
|
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: 261.85 E-value: 2.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03339 28 HILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKE---MKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV 179
Cdd:cd03339 108 LEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 ----RRPgypIDLfmvEIMEMKHKLG---TDTKEVNSGFFYK-------------------------------------T 215
Cdd:cd03339 188 adleRKD---VNF---ELIKVEGKVGgrlEDTKLVKGIVIDKdfshpqmpkevkdakiailtcpfeppkpktkhklditS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 216 AEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 295
Cdd:cd03339 262 VEDYKKLQEYEQKYFREMVEQVKD------AGAN---LVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 296 VNSFEDLTVDCLGHAGLVYEYTLG--EEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPG 373
Cdd:cd03339 333 VPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 374 AGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQ-LVGVDLNTGEPMVA 452
Cdd:cd03339 413 GGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNpHLGIDCLGRGTNDM 492
|
490 500 510
....*....|....*....|....*....|..
gi 302058290 453 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEI 484
Cdd:cd03339 493 KEQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
23-487 |
5.62e-80 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 257.31 E-value: 5.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAK----VATAQDDVTGDGTTSNVLI 98
Cdd:COG0459 15 NIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTTATVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 99 IGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEE--VKVTkemKRKILLDVARTSLQTKvhaelaDVLTEVVVDSV 176
Cdd:COG0459 95 AGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD------EEIGELIAEAM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 177 LAVRRPGYpidlFMVEimemKHK-LGTDT---------KEVNSGFFYKTAEEKEKLVKA------ERKfIEDrVQKIIDL 240
Cdd:COG0459 166 EKVGKDGV----ITVE----EGKgLETELevvegmqfdKGYLSPYFVTDPEKMPAELENayilltDKK-ISS-IQDLLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 241 KDKVcAQSNKGfVVINQKGIDPFSLDSLAKHGIVALRRA---------KRRN--MERLSLACGGMAVN-----SFEDLTV 304
Cdd:COG0459 236 LEKV-AQSGKP-LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgDRRKamLEDIAILTGGRVISedlglKLEDVTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 305 DCLGHAGLVYEytlGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCmVPGAGAIEVAMAEA 384
Cdd:COG0459 314 DDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVEEGI-VPGGGAALLRAARA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 385 LVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAehvESKQLVGVDLNTGEPMVAADAGVWDNYCVK 464
Cdd:COG0459 390 LRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA---AKDKGFGFDAATGEYVDMLEAGVIDPAKVK 466
|
490 500
....*....|....*....|...
gi 302058290 465 KQLLHSCTVIATNILLVDEIMRA 487
Cdd:COG0459 467 RSALQNAASVAGLILTTEAVIAD 489
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-484 |
7.00e-77 |
|
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: 250.04 E-value: 7.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02344 21 NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:TIGR02344 101 LSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNdDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 -------------------PGYPIDLFMVEIMEMKHKLGTDTKE-----------VNSGFFYKTAE-------EKEK--- 221
Cdd:TIGR02344 181 dengrkeidikryakvekiPGGDIEDSCVLKGVMINKDVTHPKMrryienprivlLDCPLEYKKGEsqtnieiTKEEdwn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 222 -LVKAERKFIEDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFE 300
Cdd:TIGR02344 261 rILQMEEEYVQLMCEDIIAVKPDL---------VITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 301 DLTVDCLG-HAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEV 379
Cdd:TIGR02344 332 ELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 380 AMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHV-ESKQLVGVDLNTGEPMVAADAGVW 458
Cdd:TIGR02344 412 AVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDGETGKIVDMKEKGIW 491
|
490 500
....*....|....*....|....*.
gi 302058290 459 DNYCVKKQLLHSCTVIATNILLVDEI 484
Cdd:TIGR02344 492 EPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-487 |
8.75e-76 |
|
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: 247.20 E-value: 8.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-----KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVL 177
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNidkedKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 178 AVRRPgypIDLFMVEIMEMKHKLGTDTKEVNSGFFYKT-----AEEKEKL--------------VKAERKFIEDRV---- 234
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyagFEQQPKKfknpkilllnveleLKAEKDNAEVRVedpe 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 235 --QKIID-----LKDKVCAQSNKGF-VVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDC 306
Cdd:cd03340 258 eyQAIVDaewkiIYDKLEKIVKSGAnVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 307 LGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALV 386
Cdd:cd03340 338 LGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 387 TYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQL-VGVDLNTGEPMVAADAGVWDNYCVKK 465
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490 500
....*....|....*....|..
gi 302058290 466 QLLHSCTVIATNILLVDEIMRA 487
Cdd:cd03340 498 NALTAATEAACLILSVDETIKN 519
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
23-486 |
7.02e-75 |
|
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: 245.40 E-value: 7.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02340 17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTK--EMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 180
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSvdELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 181 ------RPGYPI-----------------------------DLFMVEIME-----------MKHKLGTDTKEVnsgffYK 214
Cdd:TIGR02340 177 ttnengETKYPIkainilkahgksaresmlvkgyalnctvaSQQMPKRIKnakiacldfnlQKAKMALGVQIV-----VD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 215 TAEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGM 294
Cdd:TIGR02340 252 DPEKLEQIRQREADITKERIKKILD------AGAN---VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 295 AVNSFEDLTVD------CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDG 368
Cdd:TIGR02340 323 LVSTLADLEGEetfeasYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 369 CMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVES------KQL--V 440
Cdd:TIGR02340 403 SVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAqlkpekKHLkwY 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 302058290 441 GVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 486
Cdd:TIGR02340 483 GLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
23-488 |
7.60e-75 |
|
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: 245.10 E-value: 7.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02343 32 NIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEV--KVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV 179
Cdd:TIGR02343 112 LEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 ----RRPgypIDLfmvEIMEMKHKLG---TDTKEVNSGFFYK-------------------------------------T 215
Cdd:TIGR02343 192 admeRRD---VDF---DLIKVEGKVGgslEDTKLIKGIIIDKdfshpqmpkevedakiailtcpfeppkpktkhkldisS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 216 AEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 295
Cdd:TIGR02343 266 VEEYKKLQKYEQQKFKEMIDDIKK------SGAN---LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 296 VNSFEDLTVDCLGHAGLVYEYTLG--EEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPG 373
Cdd:TIGR02343 337 VPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 374 AGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQ-LVGVDLNTGEPMVA 452
Cdd:TIGR02343 417 GGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNpNLGVDCLGYGTNDM 496
|
490 500 510
....*....|....*....|....*....|....*.
gi 302058290 453 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 488
Cdd:TIGR02343 497 KEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
23-486 |
1.87e-74 |
|
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: 243.73 E-value: 1.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTK--EMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 180
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISvdNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 181 R------PGYPI--------------DLFMVE----------------------------IMEMKHKLGTDTkEVNSgff 212
Cdd:cd03335 173 TtnekgkTKYPIkavnilkahgksakESYLVNgyalnctrasqgmptrvknakiacldfnLQKTKMKLGVQV-VVTD--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 213 yktAEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACG 292
Cdd:cd03335 249 ---PEKLEKIRQRESDITKERIKKILA------AGAN---VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 293 GMAVNSFEDLTVD------CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIE 366
Cdd:cd03335 317 ATLVSTLANLEGEetfdpsYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 367 DGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQL------- 439
Cdd:cd03335 397 SNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKpdkkhlk 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 302058290 440 -VGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 486
Cdd:cd03335 477 wYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-487 |
2.10e-74 |
|
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: 243.90 E-value: 2.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLA 178
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTideeKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 179 VRRPGypIDLFMVEIMEMKHKLGTDTKEVNSGFFYKT-----AEEKEKLV--------------KAERKFIEDRVQKIID 239
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyagFEQQPKKFanpkilllnvelelKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 240 LKDKVCAQSNKGF------------VVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCL 307
Cdd:TIGR02345 261 YQAIVDAEWAIIFrklekivesganVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 308 GHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVT 387
Cdd:TIGR02345 341 GTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 388 YKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQL 467
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINA 500
|
490 500
....*....|....*....|
gi 302058290 468 LHSCTVIATNILLVDEIMRA 487
Cdd:TIGR02345 501 LKAAFEAACTILSVDETITN 520
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-449 |
1.29e-73 |
|
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: 241.42 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 PGYP--IDLFMVEIMEmkhKLG---TDTKEVNSGFFYKTAEEK------------------------------------- 219
Cdd:cd03338 173 PATAtnVDLKDIRIVK---KLGgtiEDTELVDGLVFTQKASKKaggptriekakigliqfclsppktdmdnnivvndyaq 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 220 -EKLVKAERKFIEDRVQKIidlKDKVCAqsnkgfVVINQKGI-----DPFSLDSLAKHGIVALRRAKRRNMERLSLACGG 293
Cdd:cd03338 250 mDRILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 294 MAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPC-SVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVP 372
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGkTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIP 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302058290 373 GAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEP 449
Cdd:cd03338 401 GGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
32-487 |
7.72e-69 |
|
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: 228.75 E-value: 7.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 32 DVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLY 109
Cdd:cd03336 27 DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 110 ISEGLHPRIIAEGFEAAKIKALEVLEE----VKVTKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGyp 185
Cdd:cd03336 107 VAQKIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSG-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 186 iDLFMVEIMEmkhKLGTDTKE--VNSGFFYK--------------------TAEEKEK------------------LVKA 225
Cdd:cd03336 185 -NLDAIQIIK---KLGGSLKDsyLDEGFLLDkkigvnqpkrienakilianTPMDTDKikifgakvrvdstakvaeIEEA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 226 ERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVD 305
Cdd:cd03336 261 EKEKMKNKVEKIL---------KHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 306 CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEAL 385
Cdd:cd03336 332 KLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 386 VTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKK 465
Cdd:cd03336 412 EELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGITESFKVKR 491
|
490 500
....*....|....*....|..
gi 302058290 466 QLLHSCTVIATNILLVDEIMRA 487
Cdd:cd03336 492 QVLLSASEAAEMILRVDDIIKC 513
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-485 |
2.04e-68 |
|
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: 227.74 E-value: 2.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02342 14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:TIGR02342 94 LGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSdREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVID 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 PGYPIDLFMVEIMEMKHKLGT--DTKEVNSGFFYKTAEEK--------------------------------------EK 221
Cdd:TIGR02342 174 PENAKNVDLNDIKVVKKLGGTidDTELIEGLVFTQKASKSaggptriekakigliqfqisppktdmenqiivndyaqmDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 222 LVKAERKFIEDRVQKIidlkdkvcaQSNKGFVVINQKGI-----DPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAV 296
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---------KKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 297 NSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPC-SVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAG 375
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 376 AIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADA 455
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
|
490 500 510
....*....|....*....|....*....|
gi 302058290 456 GVWDNYCVKKQLLHSCTVIATNILLVDEIM 485
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
23-487 |
7.55e-66 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 221.44 E-value: 7.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVL 97
Cdd:PTZ00212 27 SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 98 IIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVV 173
Cdd:PTZ00212 107 LAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDhgsdEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 174 DSVLAVRRPGypiDLFMVEIME----------------MKHKLGT------------------DTKE-------VNSGFF 212
Cdd:PTZ00212 187 DAVLRLKGSG---NLDYIQIIKkpggtlrdsyledgfiLEKKIGVgqpkrlenckilvantpmDTDKikiygakVKVDSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 213 YKTAEekekLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACG 292
Cdd:PTZ00212 264 EKVAE----IEAAEKEKMKNKVDKILA------HGCN---VFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 293 GMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVP 372
Cdd:PTZ00212 331 AEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 373 GAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVA 452
Cdd:PTZ00212 411 GGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGTVGDM 490
|
490 500 510
....*....|....*....|....*....|....*
gi 302058290 453 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 487
Cdd:PTZ00212 491 KELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-487 |
1.11e-63 |
|
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: 215.74 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEM---KRKILLDVARTSLQTKVHAElADVLTEVVVDSVLAV 179
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKdlrDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 RrPGYPIDlFMVE-----------------IMEM--------------KHK-------LGTDTKEVNSGFFYKTAEEKEK 221
Cdd:TIGR02346 182 L-PKNPQN-FNVDnirvckilggslsnsevLKGMvfnreaegsvksvkNAKvavfscpLDTATTETKGTVLIHNAEELLN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 222 LVKAERKFIEDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFED 301
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNV---------IVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 302 LTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSV-TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVA 380
Cdd:TIGR02346 331 PTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 381 MAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMV--AADAGVW 458
Cdd:TIGR02346 411 LASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVkdASEAGIY 490
|
490 500
....*....|....*....|....*....
gi 302058290 459 DNYCVKKQLLHSCTVIATNILLVDEIMRA 487
Cdd:TIGR02346 491 DMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-487 |
1.20e-63 |
|
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: 214.01 E-value: 1.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKILLDVA---RTSLQTKVhAELADVLTEVVVDSVLAV 179
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSkalKTAIASKQ-YGNEDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 rrpgYPIDL--FMVEIMEMKHKLG---TDTKEVNSGFFYKTAEEKEKLVKaerkfiedrvqkiidlKDKV----CAQSNK 250
Cdd:cd03341 172 ----LPENIgnFNVDNIRVVKILGgslEDSKVVRGMVFKREPEGSVKRVK----------------KAKVavfsCPFDIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 251 GFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECV 330
Cdd:cd03341 232 VNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 331 NPCSV-TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLI 409
Cdd:cd03341 312 EDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 410 IPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMV--AADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 487
Cdd:cd03341 392 VPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
32-487 |
8.45e-54 |
|
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: 188.91 E-value: 8.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 32 DVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLY 109
Cdd:TIGR02341 28 DLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 110 ISEGLHPRIIAEGFEAAKIKALEVLEEVKV----TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRP--- 182
Cdd:TIGR02341 108 INQKIHPQTIIAGYREATKAARDALLKSAVdngsDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSgnl 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 183 ----------GYPIDLFMVEIMEMKHKLGT------------------DTKEVN---SGFFYKTAEEKEKLVKAERKFIE 231
Cdd:TIGR02341 188 eaiqiikklgGSLADSYLDEGFLLDKKIGVnqpkrienakiliantgmDTDKVKifgSRVRVDSTAKVAELEHAEKEKMK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 232 DRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAG 311
Cdd:TIGR02341 268 EKVEKIL---------KHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 312 LVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNS 391
Cdd:TIGR02341 339 LIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 392 IKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSC 471
Cdd:TIGR02341 419 TPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSA 498
|
490
....*....|....*.
gi 302058290 472 TVIATNILLVDEIMRA 487
Cdd:TIGR02341 499 AEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
145-367 |
1.81e-53 |
|
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: 178.81 E-value: 1.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 145 RKILLDVARTSLQTKVhAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTkEVNSGFFYKtaeeKEKLVK 224
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDS-ELVVGVVFD----KGYASP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 225 AERKFIEDrvQKIidlkdkVCAQSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTV 304
Cdd:cd03333 75 YMPKRLEN--AKI------LLLDCPLEYVVIAEKGIDDLALHYLAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302058290 305 DCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIED 367
Cdd:cd03333 147 EDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
30-485 |
1.71e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 63.22 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHP----TASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK12851 23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 106 ADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKvTKEMKRKILLDVARTSLQ--TKVHAELADVLTEVVVDSVLAVRR-P 182
Cdd:PRK12851 103 GAKAVAAGANPMDLKRGIDRAVAAVVEELKANA-RPVTTNAEIAQVATISANgdAEIGRLVAEAMEKVGNEGVITVEEsK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 183 GYPIDLFMVEIMEMKhklgtdtKEVNSGFFYKTAEEKEKLVKAERKFIEDR----VQKIIDLKDKVcAQSNKGFVVINQK 258
Cdd:PRK12851 182 TAETELEVVEGMQFD-------RGYLSPYFVTDADKMEAELEDPYILIHEKkisnLQDLLPVLEAV-VQSGKPLLIIAED 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 259 gIDPFSLDSLAKHGI-----VALRRA-----KRRNM-ERLSLACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEK 322
Cdd:PRK12851 254 -VEGEALATLVVNKLrgglkVAAVKApgfgdRRKAMlEDIAILTGGTVISedlgiKLENVTLEQLGRAKKV---VVEKEN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 323 FTF--------------------IEECVNPCSVTLL---------------VKGPNKHTLTQVKDAIRDGLRAIKNAIED 367
Cdd:PRK12851 330 TTIidgagskteiegrvaqiraqIEETTSDYDREKLqerlaklaggvavirVGASTEVEVKEKKDRVDDALHATRAAVEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 368 GcMVPGAGAIEVAMAEALVTyKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQaehvESKQLVGVDLNTG 447
Cdd:PRK12851 410 G-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLR----EKPGGYGFNAATN 483
|
490 500 510
....*....|....*....|....*....|....*...
gi 302058290 448 EPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIM 485
Cdd:PRK12851 484 EYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-459 |
4.90e-10 |
|
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: 61.70 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPT----ASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLARAIIKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 106 ADLYISEGLHPRIIAEGFEAAKIKALEVLeevkvtKEMKRKI-----LLDVARTSLQTKVH--AELADVLTEVVVDSVLA 178
Cdd:cd03344 100 GLKAVAAGANPMDLKRGIEKAVEAVVEEL------KKLSKPVktkeeIAQVATISANGDEEigELIAEAMEKVGKDGVIT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 179 VRRPGYPID-LFMVEIMemkhklgtdtkEVNSGF---FYKTAEEKEKlVKAERKFIEDRVQKIIDLKDKV-----CAQSN 249
Cdd:cd03344 174 VEEGKTLETeLEVVEGM-----------QFDRGYlspYFVTDPEKME-VELENPYILLTDKKISSIQELLpilelVAKAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 250 KGFVVINQKgIDPFSLDSLAKHGI-----VALRRA-----KRRNM-ERLSLACGGMAVN-----SFEDLTVDCLGHAGLV 313
Cdd:cd03344 242 RPLLIIAED-VEGEALATLVVNKLrgglkVCAVKApgfgdRRKAMlEDIAILTGGTVISeelglKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 314 yeyTLGEEKFTFIEECVNPCSV-----------------------------------TLLVKGPNKHTLTQVKDAIRDGL 358
Cdd:cd03344 321 ---VVTKDDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 359 RAIKNAIEDGCmVPGAGAIEVAMAEALVTYKNSIKGrARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVqaehVESKQ 438
Cdd:cd03344 398 NATRAAVEEGI-VPGGGVALLRASPALDKLKALNGD-EKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKV----LESPD 471
|
490 500
....*....|....*....|.
gi 302058290 439 LVGVDLNTGEPMVAADAGVWD 459
Cdd:cd03344 472 GFGYDAATGEYVDMIEAGIID 492
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
30-421 |
1.79e-09 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 59.93 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDG-----NVLLdEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLK 104
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvakAIEF-SDRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 105 QADLYISEGLHPRIIAEGFEAAKIKALEVLEEVK---VTKEMkrkiLLDVARTSlqtkvhAELADVLTEVVVDSVLAVRR 181
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSrpvKTKED----ILNVATIS------ANGDVEIGSLIADAMDKVGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 182 PGYpidlfmVEIME---MKHKLG-TDTKEVNSGFF--YKTAEEKEKLVKAERKFIEDRVQKIIDLKDKV-----CAQSNK 250
Cdd:PTZ00114 183 DGT------ITVEDgktLEDELEvVEGMSFDRGYIspYFVTNEKTQKVELENPLILVTDKKISSIQSILpilehAVKNKR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 251 GFVVINqkgiDPFSLDSLAKHGIVALR--------RA------KRRNMERLSLACGGMAVNS------FEDLTVDCLGHA 310
Cdd:PTZ00114 257 PLLIIA----EDVEGEALQTLIINKLRgglkvcavKApgfgdnRKDILQDIAVLTGATVVSEdnvglkLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 311 GLV------------YEYT-LGEEKFTFIEECVNPCSV-------------------TLLVKGPNKHTLTQVKDAIRDGL 358
Cdd:PTZ00114 333 KKVtvtkdetviltgGGDKaEIKERVELLRSQIERTTSeydkeklkerlaklsggvaVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302058290 359 RAIKNAIEDGcMVPGAGAIEVAMAEAL--VTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYD 421
Cdd:PTZ00114 413 NATRAAVEEG-IVPGGGVALLRASKLLdkLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-487 |
3.82e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 55.81 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQI----QHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 106 ADLYISEGLHPRIIAEGFEAAkIKALeVLEEVKVTKEM-KRKILLDVARTSLQ--TKVHAELADVLTEVVVDSVLAVRRP 182
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLA-VEAV-VADLVKNSKKVtSNDEIAQVGTISANgdAEIGKFLADAMKKVGNEGVITVEEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 183 -GYPIDLFMVEIMEMKhklgtdtKEVNSGFFYKTAEEKEklVKAERKFIEDRVQKIIDLKD-----KVCAQSNKGFVVIN 256
Cdd:PRK14104 181 kSLETELDVVEGMQFD-------RGYISPYFVTNADKMR--VEMDDAYILINEKKLSSLNEllpllEAVVQTGKPLVIVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 257 Q----KGIDPFSLDSLAKHGIVALRRA-----KRRNM-ERLSLACGGMAVNS-----FEDLTVDCLGHAGLVY---EYTL 318
Cdd:PRK14104 252 EdvegEALATLVVNRLRGGLKVAAVKApgfgdRRKAMlQDIAILTGGQAISEdlgikLENVTLQMLGRAKKVMidkENTT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 319 ---GEEKFTFIEECVNPCS--------------------------VTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGc 369
Cdd:PRK14104 332 ivnGAGKKADIEARVAQIKaqieettsdydreklqerlaklaggvAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEG- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 370 MVPGAGAIEVAMAEALVTYKNSIKGRaRLGVQAFADALLIIPKVLAQNAGYDPQETLVKVqaehVESKQLV-GVDLNTGE 448
Cdd:PRK14104 411 IVPGGGVALLRASEQLKGIKTKNDDQ-KTGVEIVRKALSAPARQIAINAGEDGSVIVGKI----LEKEQYSyGFDSQTGE 485
|
490 500 510
....*....|....*....|....*....|....*....
gi 302058290 449 PMVAADAGVWDNYCVKKQLLHSCTVIATnILLVDEIMRA 487
Cdd:PRK14104 486 YGNLVSKGIIDPTKVVRTAIQNAASVAA-LLITTEAMVA 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
30-487 |
6.42e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 55.11 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHP----TASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 106 ADLYISEGLHPRIIAEGFEAAKIKALEVLE----EVKVTKEMKRkilldVARTSL--QTKVHAELADVLTEVVVDSVLAV 179
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKkiakKVTSSKEIAQ-----VATISAngDESIGEMIAEAMDKVGKEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 RRP-GYPIDLFMVEIMEMKHKLgtdtkevNSGFFYKTAEEKEklVKAERKFIEDRVQKIIDLKD-----KVCAQSNKGFV 253
Cdd:PRK12850 178 EEAkTLGTELDVVEGMQFDRGY-------LSPYFVTNPEKMR--AELEDPYILLHEKKISNLQDllpilEAVVQSGRPLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 254 VINQKgIDPFSLDSLAKHGI-----VALRRA-----KRRNM-ERLSLACGGMAVN-----SFEDLTVDCLGHAGLVyeyT 317
Cdd:PRK12850 249 IIAED-VEGEALATLVVNKLrgglkSVAVKApgfgdRRKAMlEDIAVLTGGQVISedlgiKLENVTLDMLGRAKRV---L 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 318 LGEEKFTFIEECVNPCSVTLLVK-----------------------------------GPNKHTLTQVKDAIRDGLRAIK 362
Cdd:PRK12850 325 ITKENTTIIDGAGDKKNIEARVKqiraqieettsdydreklqerlaklaggvavirvgGATEVEVKEKKDRVDDALHATR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 363 NAIEDGcMVPGAGaieVAMAEAL--VTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVqaehVESKQLV 440
Cdd:PRK12850 405 AAVEEG-IVPGGG---VALLRARsaLRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKV----AELPGNF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 302058290 441 GVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATnILLVDEIMRA 487
Cdd:PRK12850 477 GFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAA-LLITTEAMVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
38-479 |
7.24e-08 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 54.73 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 38 LGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQ----IQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLYISEG 113
Cdd:CHL00093 30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 114 LHPRIIAEGFE-AAKIKALEVLEEVKVTKEMKRkiLLDVARTSL--QTKVHAELADVLTEVVVDSVLAVRR-PGYPIDLF 189
Cdd:CHL00093 110 ANPISLKRGIEkATQYVVSQIAEYARPVEDIQA--ITQVASISAgnDEEVGSMIADAIEKVGREGVISLEEgKSTVTELE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 190 MVEIMEMKhklgtdtKEVNSGFFYKTAEEKEklVKAERKFI---EDRV----QKIIDLKDKVcAQSNKGFVVINQKgIDP 262
Cdd:CHL00093 188 ITEGMRFE-------KGFISPYFVTDTERME--VVQENPYIlltDKKItlvqQDLLPILEQV-TKTKRPLLIIAED-VEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 263 FSLDSLAKH---GI---VALR-----RAKRRNMERLSLACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEKFTFI 326
Cdd:CHL00093 257 EALATLVLNklrGIvnvVAVRapgfgDRRKAMLEDIAILTGGQVITedaglSLETIQLDLLGQARRI---IVTKDSTTII 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 327 EE---------C----------------------VNPCSVTLLVKGPNKHTLTQVKDA---IRDGLRAIKNAIEDGcMVP 372
Cdd:CHL00093 334 ADgneeqvkarCeqlrkqieiadssyekeklqerLAKLSGGVAVIKVGAATETEMKDKklrLEDAINATKAAVEEG-IVP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 373 GAGAIEVAMAEALVTY-KNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVEskqlVGVDLNTGEPMV 451
Cdd:CHL00093 413 GGGATLVHLSENLKTWaKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFE----IGYNAANNKFVN 488
|
490 500
....*....|....*....|....*...
gi 302058290 452 AADAGVWDNYCVKKQLLHSCTVIATNIL 479
Cdd:CHL00093 489 MYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
220-351 |
1.64e-07 |
|
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: 52.61 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 220 EKLVKAERKFIEDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSF 299
Cdd:cd03334 109 DPVILQEKEYLKNLVSRIVALRPDV---------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSM 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 302058290 300 EDLtVDC--LGHAGLVYEYTLGEEK-----FTFIEECVNPCSVTLLVKGPNKHTLTQVK 351
Cdd:cd03334 180 DDL-LTSpkLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVK 237
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
30-487 |
1.94e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 47.15 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQI----QHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 106 ADLYISEGLHPRIIAEGFE---AAKIKALEVL-EEVKVTKEMKRkilldVARTSLQ--TKVHAELADVLTEVVVDSVLAV 179
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDiavAAVVKDIEKRaKPVASSAEIAQ-----VGTISANgdAAIGKMIAQAMQKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 180 RR-PGYPIDLFMVEIMEMKhklgtdtKEVNSGFFYKTAEEKEklVKAERKFIEDRVQKIIDLKD-----KVCAQSNKGFV 253
Cdd:PRK12852 178 EEnKSLETEVDIVEGMKFD-------RGYLSPYFVTNAEKMT--VELDDAYILLHEKKLSGLQAmlpvlEAVVQSGKPLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 254 VINQKgIDPFSLDSLAKHGI-----VALRRA-----KRRNM-ERLSLACGGMAVN-----SFEDLTVDCLGHAGLVY--- 314
Cdd:PRK12852 249 IIAED-VEGEALATLVVNRLrgglkVAAVKApgfgdRRKAMlEDIAILTGGQLISedlgiKLENVTLKMLGRAKKVVidk 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 315 EYTL---GEEKFTFIEECVNPCS--------------------------VTLLVKGPNKHTLTQVKDAIRDGLRAIKNAI 365
Cdd:PRK12852 328 ENTTivnGAGKKADIEARVGQIKaqieettsdydreklqerlaklaggvAVIRVGGATEVEVKEKKDRVEDALNATRAAV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 366 EDGcMVPGaGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESkqlVGVDLN 445
Cdd:PRK12852 408 QEG-IVPG-GGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSET---FGFDAQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 302058290 446 TGEPMVAADAGVWDNYCVKKQLLHSCTVIAtNILLVDEIMRA 487
Cdd:PRK12852 483 TEEYVDMVAKGIIDPAKVVRTALQDAASVA-GLLVTTEAMVA 523
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
30-147 |
2.86e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 40.11 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058290 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPT----ASLIAKVATAQDDVTGDG-TTSNVL---IIGE 101
Cdd:PRK00013 22 LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGtTTATVLaqaIVRE 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 302058290 102 LLKqadlYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKI 147
Cdd:PRK00013 102 GLK----NVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEI 143
|
|
| |
