|
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 ... |
3-530 |
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: 974.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347 1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 83 AQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKE--MDRETLIDVARTSLRTKV 160
Cdd:TIGR02347 81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 161 HAELADVLTEAVVDSILAIKKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 241 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKVCGDS-DKGFVVINQKGIDPFSLDALAKEGIIALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 320 NMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVK 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 400 NAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGV 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
4B2T_Z 480 DLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 530
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
7-526 |
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: 936.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDD 86
Cdd:cd03342 1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 87 ITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEM--DRETLIDVARTSLRTKVHAEL 164
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 165 ADVLTEAVVDSILAIKKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEV 244
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 245 NSGFFYKsaeereklvkaerkfiedrvkkiielkkkvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERL 324
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 325 TLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDD 404
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 405 GCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTG 484
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
4B2T_Z 485 EPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRAGM 526
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
30-525 |
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: 589.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLY 109
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 110 ISEGLHPRIITEGFEAAKEKALQFLEQVKV--SKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPID 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 188 LFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFI 267
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 268 EDRVKKIIELKKKVcgdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALNSLDDLNPDCLGHA 347
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 348 GLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALVKYKP 427
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 428 SVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHS 507
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
4B2T_Z 508 CTVIATNILLVDEIMRAG 525
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
11-523 |
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: 567.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 11 AEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGD 90
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 91 GTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSK-EMDRETLIDVARTSLRTKVHAELADVLT 169
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIdVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 170 EAVVDSILAIKKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYektevnsgff 249
Cdd:cd00309 161 ELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 250 yksaeereklvkaerkfiedrvkkiielkkkvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACG 329
Cdd:cd00309 231 ----------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 330 GIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVP 409
Cdd:cd00309 271 ATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 410 GAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVA 489
Cdd:cd00309 351 GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDM 430
|
490 500 510
....*....|....*....|....*....|....
4B2T_Z 490 AEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd00309 431 KEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
19-525 |
3.13e-144 |
|
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: 425.14 E-value: 3.13e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:cd03343 16 AQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQ--VKVSKEmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 176
Cdd:cd03343 96 AGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 177 LAIKKQDEP---IDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:cd03343 175 LQVAEKRDGkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 254 EEREKLVKAERKFIEDRVKKIIELKKKVcgdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIAL 333
Cdd:cd03343 255 DQLQAFLEQEEAMLKEMVDKIADTGANV---------VFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 334 NSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGA 413
Cdd:cd03343 326 TNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 414 VEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAG 493
Cdd:cd03343 406 VEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKG 485
|
490 500 510
....*....|....*....|....*....|..
4B2T_Z 494 IWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:cd03343 486 VIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
19-525 |
1.05e-143 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 423.53 E-value: 1.05e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041082 18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVS-KEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:NF041082 98 AGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 178 AI--KKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:NF041082 178 AVaeKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 256 REKLVKAERKFIEDRVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALNS 335
Cdd:NF041082 258 LQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 336 LDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:NF041082 329 IDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 416 VAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAGIW 495
Cdd:NF041082 409 VELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVV 488
|
490 500 510
....*....|....*....|....*....|
4B2T_Z 496 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041082 489 EPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
19-525 |
1.34e-142 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 420.90 E-value: 1.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041083 18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVS-KEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:NF041083 98 AGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKvDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 178 AIKKQDEP---IDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:NF041083 178 QVAEKRDGkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 255 EREKLVKAERKFIEDRVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALN 334
Cdd:NF041083 258 QLQKFLDQEEKMLKEMVDKIKATGAN---------VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 335 SLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAV 414
Cdd:NF041083 329 NIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 415 EVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAGI 494
Cdd:NF041083 409 EVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGV 488
|
490 500 510
....*....|....*....|....*....|.
4B2T_Z 495 WDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041083 489 IEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
19-524 |
1.47e-138 |
|
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: 410.62 E-value: 1.47e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:TIGR02339 17 AQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQ--VKVSKEmDRETLIDVARTSLRTKVHAELA-DVLTEAVVDS 175
Cdd:TIGR02339 97 AGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEiaTKISPE-DRDLLKKIAYTSLTSKASAEVAkDKLADLVVEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 176 ILAIKKQDE----PIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK 251
Cdd:TIGR02339 176 VKQVAELRGdgkyYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRIT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 252 SAEEREKLVKAERKFIEDRVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGI 331
Cdd:TIGR02339 256 DPDQIKKFLDQEEAMLKEMVDKIASAGAN---------VVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 332 ALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGA 411
Cdd:TIGR02339 327 IVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 412 GAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAE 491
Cdd:TIGR02339 407 GAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLE 486
|
490 500 510
....*....|....*....|....*....|...
4B2T_Z 492 AGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02339 487 LGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
23-523 |
4.85e-94 |
|
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: 296.12 E-value: 4.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFL-EQVKVSKE-MDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIK 180
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIkEHLSISVDnLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 181 KQDE------PIDlfMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:cd03335 173 TTNEkgktkyPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 255 EREKLVKAERKFIEDRVKKIIELKKKVcgdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALN 334
Cdd:cd03335 251 KLEKIRQRESDITKERIKKILAAGANV---------VLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 335 SLDDLN------PDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVV 408
Cdd:cd03335 322 TLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 409 PGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESgQL---------VGV 479
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAA-QVkpdkkhlkwYGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
4B2T_Z 480 DLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd03335 481 DLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
14-521 |
5.48e-94 |
|
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: 296.13 E-value: 5.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 14 ARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTT 93
Cdd:cd03339 19 LKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 94 SNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKE---MDRETLIDVARTSLRTKVHAELADVLTE 170
Cdd:cd03339 99 GVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspDNKEPLIQTAMTSLGSKIVSRCHRQFAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 171 AVVDSILA---IKKQDEPIDLFMVE-----IMEmkhksetDTSLIRGLVLDHGARHPDMKKRVEDAYI--LTCnvSLEYE 240
Cdd:cd03339 179 IAVDAVLSvadLERKDVNFELIKVEgkvggRLE-------DTKLVKGIVIDKDFSHPQMPKEVKDAKIaiLTC--PFEPP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 241 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIielkkKVCGDSdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRN 320
Cdd:cd03339 250 KPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQV-----KDAGAN----LVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 321 MERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAV 398
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 399 KNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEH-SESGQLV 477
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
4B2T_Z 478 GVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03339 481 GIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
23-523 |
2.88e-92 |
|
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: 292.01 E-value: 2.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02340 17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEQ--VKVSKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIK 180
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnlSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 181 KQDE------PIDlfMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:TIGR02340 177 TTNEngetkyPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 255 EREKLVKAERKFIEDRVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALN 334
Cdd:TIGR02340 255 KLEQIRQREADITKERIKKILDAGAN---------VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 335 SLDDL------NPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVV 408
Cdd:TIGR02340 326 TLADLegeetfEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 409 PGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESgQL---------VGV 479
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAA-QLkpekkhlkwYGL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....
4B2T_Z 480 DLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
4-521 |
3.54e-92 |
|
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: 289.97 E-value: 3.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 4 VKTLNPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATA 83
Cdd:cd03337 4 VLNQNTKRESGR-KAQLG-NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 84 QDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVS-KEMDRETLIDVARTSLRTKVHA 162
Cdd:cd03337 82 QDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 163 ELADVLTEAVVDSILAIKKQDE----PIDL-FMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSL 237
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAVEENgrkkEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 238 EYektevnsgffyksaeereklvkaerkfiedrvkkiielkkkvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAK 317
Cdd:cd03337 242 EY--------------------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 318 RRNMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTL-GEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLR 396
Cdd:cd03337 272 KTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 397 AVKNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQL 476
Cdd:cd03337 352 VARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENS 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
4B2T_Z 477 V-GVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03337 432 TwGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-521 |
8.22e-92 |
|
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: 290.49 E-value: 8.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 8 NPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDI 87
Cdd:TIGR02344 8 NTKRESGR-KAQLS-NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEM-DRETLIDVARTSLRTKVHAELAD 166
Cdd:TIGR02344 86 VGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVnDDAAMLKLIQSCIGTKFVSRWSD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 167 VLTEAVVDSILAIKKQDEPIdlFMVEIMEMKhKSE-------TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEY 239
Cdd:TIGR02344 166 LMCDLALDAVRTVQRDENGR--KEIDIKRYA-KVEkipggdiEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 240 EKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRR 319
Cdd:TIGR02344 243 KKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPD---------LVITEKGVSDLAQHYLLKANITAIRRVRKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 320 NMERLTLACGGIALNSLDDLNPDCLG-HAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAV 398
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 399 KNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHS-ESGQLV 477
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
4B2T_Z 478 GVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
15-525 |
3.43e-89 |
|
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: 284.00 E-value: 3.43e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 15 RAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTS 94
Cdd:TIGR02343 24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQV--KVSKEMD-RETLIDVARTSLRTKVHAELADVLTEA 171
Cdd:TIGR02343 104 VVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 172 VVDSILAI-KKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAY--ILTCnvSLEYEKTEVNSGF 248
Cdd:TIGR02343 184 AVDAVLNVaDMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKiaILTC--PFEPPKPKTKHKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 249 FYKSAEEREKLVKAERKFIEDRVKKIielkKKVCGDsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLAC 328
Cdd:TIGR02343 262 DISSVEEYKKLQKYEQQKFKEMIDDI----KKSGAN-----LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 329 GGIALNSLDDLNPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGC 406
Cdd:TIGR02343 333 GGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 407 VVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEH-SESGQLVGVDLNTGE 485
Cdd:TIGR02343 413 IVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYG 492
|
490 500 510 520
....*....|....*....|....*....|....*....|
4B2T_Z 486 PMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:TIGR02343 493 TNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-524 |
5.19e-88 |
|
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: 280.49 E-value: 5.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVS----KEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILA 178
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTideeKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 179 IKKQDepIDLFMVEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 256 REKLVKAERKFIEDRVKKIIELKKKVcgdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALNS 335
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANV---------VLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 336 LDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 416 VAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEAGIW 495
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
|
490 500
....*....|....*....|....*....
4B2T_Z 496 DNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
19-524 |
7.17e-87 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 276.57 E-value: 7.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAK----VATAQDDITGDGTTS 94
Cdd:COG0459 11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQ--VKVSkemDRETLIDVARTSLRTKvhAELADVLTEAV 172
Cdd:COG0459 91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD--EEIGELIAEAM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 173 vdsiLAIKKQDEpidlFMVEimemKHKS-ETDTSLIRGLVLDHGARHPD-------MKKRVEDAYILTCNVSLEyektev 244
Cdd:COG0459 166 ----EKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 245 nsgffykSAEEREKLvkaerkfiedrVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRA-------- 316
Cdd:COG0459 228 -------SIQDLLPL-----------LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 317 -KRRN--MERLTLACGGIALN-----SLDDLNPDCLGHAGLVYEytlGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIK 388
Cdd:COG0459 281 gDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 389 DAIRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQA 468
Cdd:COG0459 358 RRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
4B2T_Z 469 EHSESgqlVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:COG0459 437 AKDKG---FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-524 |
9.06e-86 |
|
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: 274.55 E-value: 9.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKV-----SKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVnidkeDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 178 AIkkqDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:cd03340 181 SL---DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 255 EREKLVKAERKFIEDRVKKIIELKKKVcgdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALN 334
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANV---------VLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 335 SLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAGAV 414
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 415 EVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQL-VGVDLNTGEPMVAAEAG 493
Cdd:cd03340 409 EMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAF 488
|
490 500 510
....*....|....*....|....*....|.
4B2T_Z 494 IWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03340 489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-486 |
2.23e-85 |
|
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: 273.39 E-value: 2.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 179
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLnDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVid 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 180 KKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARH-PDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 258
Cdd:cd03338 173 PATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 259 LVKAERKFIEDRVKKIielKKKVCGdsdkgfVVINQKGI-----DPFSLDALAKEGIIALRRAKRRNMERLTLACGGIAL 333
Cdd:cd03338 253 ILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 334 NSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNP-RSVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAG 412
Cdd:cd03338 324 ASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4B2T_Z 413 AVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEP 486
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
8.33e-82 |
|
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: 263.95 E-value: 8.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02342 14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 179
Cdd:TIGR02342 94 LGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLsDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVid 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 180 KKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPD-MKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 258
Cdd:TIGR02342 174 PENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 259 LVKAERKFIEDRVKKIielKKKVCGdsdkgfVVINQKGI-----DPFSLDALAKEGIIALRRAKRRNMERLTLACGGIAL 333
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---KKTGCN------VLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 334 NSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPR-SVTLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAG 412
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 413 AVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMVAAEA 492
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
|
490 500 510
....*....|....*....|....*....|
4B2T_Z 493 GIWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
16-524 |
1.31e-78 |
|
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: 256.18 E-value: 1.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 16 AQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSN 95
Cdd:TIGR02346 16 LEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 96 VLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEMD---RETLIDVARTSLRTKVHAElADVLTEAV 172
Cdd:TIGR02346 96 LVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDlrdKDELIKALKASISSKQYGN-EDFLAQLV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 173 VDSILAIK-KQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYILTCNVSLEYEKTEVNSGFFY 250
Cdd:TIGR02346 175 AQACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 251 KSAEEREKLVKAERKFIEDRVKKIIELKKKvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGG 330
Cdd:TIGR02346 252 HNAEELLNYSKGEENQIEAMIKAIADSGVN---------VIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 331 IALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVP 409
Cdd:TIGR02346 323 TPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 410 GAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMV- 488
Cdd:TIGR02346 403 GAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVk 482
|
490 500 510
....*....|....*....|....*....|....*..
4B2T_Z 489 -AAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02346 483 dASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-524 |
9.25e-78 |
|
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: 253.41 E-value: 9.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 10 KAEVARAQA---ALAVNisaarglqDVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:cd03336 10 KGETARLSSfvgAIAIG--------DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQ----VKVSKEMDRETLIDVARTSLRTKV 160
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 161 HAELADVLTEAVVDSILAIKKQDepiDLFMVEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGSG---NLDAIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 239 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKVcgdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAK 317
Cdd:cd03336 236 TDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINC---------FINRQLIYNYPEQLFADAGIMAIEHAD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 318 RRNMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRA 397
Cdd:cd03336 307 FDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 398 VKNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLV 477
Cdd:cd03336 387 LAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
4B2T_Z 478 GVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03336 467 GLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
10-524 |
1.73e-76 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 250.72 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 10 KAEVARAQaalavNISAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:PTZ00212 19 KGETARLQ-----SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVS----KEMDRETLIDVARTSLRTKV 160
Cdd:PTZ00212 94 DEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDhgsdEEKFKEDLLNIARTTLSSKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 161 HAELADVLTEAVVDSILAIKKQdepIDLFMVEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 239 YEK-----TEVNSGFFYKSAEerekLVKAERKFIEDRVKKIIelkKKVCGdsdkgfVVINQKGIDPFSLDALAKEGIIAL 313
Cdd:PTZ00212 248 TDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKIL---AHGCN------VFINRQLIYNYPEQLFAEAGIMAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 314 RRAKRRNMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRD 393
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 394 GLRAVKNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSES 473
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
4B2T_Z 474 GQLVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:PTZ00212 475 NKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
145-404 |
5.44e-72 |
|
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: 228.12 E-value: 5.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 145 RETLIDVARTSLRTKVhAELADVLTEAVVDSILAIKKQDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKR 224
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 225 VEDAYILTCNVSLEYektevnsgffyksaeereklvkaerkfiedrvkkiielkkkvcgdsdkgfVVINQKGIDPFSLDA 304
Cdd:cd03333 80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 305 LAKEGIIALRRAKRRNMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTL 384
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
4B2T_Z 385 TQIKDAIRDGLRAVKNAIDD 404
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-524 |
5.98e-70 |
|
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: 231.73 E-value: 5.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEMDRETLIDVA---RTSLRTKVhAELADVLTEAVVDSILAI 179
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSkalKTAIASKQ-YGNEDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 180 KKQDepIDLFMVE---IMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYI--LTCNVSleyekTEVNsgffyksa 253
Cdd:cd03341 172 LPEN--IGNFNVDnirVVKILGGSLEDSKVVRGMVF---KREPEGSvKRVKKAKVavFSCPFD-----IGVN-------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 254 eereklvkaerkfiedrvkkiielkkkvcgdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIAL 333
Cdd:cd03341 234 ------------------------------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 334 NSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGCVVPGAG 412
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 413 AVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLVGVDLNTGEPMV--AA 490
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAK 437
|
490 500 510
....*....|....*....|....*....|....
4B2T_Z 491 EAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
7-524 |
4.06e-63 |
|
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: 215.11 E-value: 4.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:TIGR02341 3 FKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKV----SKEMDRETLIDVARTSLRTKV 160
Cdd:TIGR02341 83 DDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVdngsDEVKFRQDLMNIARTTLSSKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 161 HAELADVLTEAVVDSILAIKKQDepiDLFMVEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:TIGR02341 163 LSQHKDHFAQLAVDAVLRLKGSG---NLEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 239 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIielKKKVCGdsdkgfVVINQKGIDPFSLDALAKEGIIALRRAK 317
Cdd:TIGR02341 237 TDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKI---LKHGIN------CFINRQLIYNYPEQLFADAGVMAIEHAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 318 RRNMERLTLACGGIALNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAIRDGLRA 397
Cdd:TIGR02341 308 FEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 398 VKNAIDDGCVVPGAGAVEVAMAEALVKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESGQLV 477
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
4B2T_Z 478 GVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
203-388 |
1.54e-12 |
|
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: 67.63 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 203 DTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKteVNSGFFYksaeeREKLVKAERKFIEDRVKKIIELKKKVc 282
Cdd:cd03334 62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLS-----LDPVILQEKEYLKNLVSRIVALRPDV- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 283 gdsdkgfvVINQKGIDPFSLDALAKEGIIALRRAKRRNMERLTLACGGIALNSLDDL-NPDCLGHAGLVYEYTLGEEK-- 359
Cdd:cd03334 134 --------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLlTSPKLGTCESFRVRTYVEEHgr 205
|
170 180 190
....*....|....*....|....*....|..
4B2T_Z 360 ---FTFIEKCNNPRSVTLLIKGPNKHTLTQIK 388
Cdd:cd03334 206 sktLMFFEGCPKELGCTILLRGGDLEELKKVK 237
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
30-510 |
4.61e-11 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 65.32 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDG-----NVLLHEmQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLK 104
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvakAIEFSD-RFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 105 QADLYISEGLHPRIITEGFEAAKEKALQFLEqvKVSKEM-DRETLIDVARTSlrtkvhAELADVLTEAVVDSILAIKKqD 183
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLK--EQSRPVkTKEDILNVATIS------ANGDVEIGSLIADAMDKVGK-D 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 184 EPIDLfmveimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVNS-GFFYKS--- 252
Cdd:PTZ00114 184 GTITV------EDGKTLEDELEVVEGMSFDRGYISPyfvtnekTQKVELENPLILVTDKKISSIQSILPIlEHAVKNkrp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 253 ----AEEREKLVKAErkFIEDRVKKIIelkkKVC-------GDSDK----------GFVVINQKGIDpFSLDALAKEgii 311
Cdd:PTZ00114 258 lliiAEDVEGEALQT--LIINKLRGGL----KVCavkapgfGDNRKdilqdiavltGATVVSEDNVG-LKLDDFDPS--- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 312 ALRRAKRRNMERL-TLACGGIalNSLDDLNPDCLGHAGLVYEYTLGEEKftfiEKCN------NPRSVTLLIKGPNKHTL 384
Cdd:PTZ00114 328 MLGSAKKVTVTKDeTVILTGG--GDKAEIKERVELLRSQIERTTSEYDK----EKLKerlaklSGGVAVIKVGGASEVEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 385 TQIKDAIRDGLRAVKNAIDDGcVVPGAGAVEVAMAEAL--VKYKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDlQET 462
Cdd:PTZ00114 402 NEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLdkLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVE-GAV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
4B2T_Z 463 LVKVQAEHSESGqlVGVDLNTGEPMVAAEAGIWDNY-CVKKQLLHSCTV 510
Cdd:PTZ00114 480 VVEKILEKKDPS--FGYDAQTGEYVNMFEAGIIDPTkVVRSALVDAASV 526
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
12-496 |
6.09e-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: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDI 87
Cdd:cd03344 7 EEARKALLRGVNK-----LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEqvKVSKEM-DRETLIDVARTSlrTKVHAELAD 166
Cdd:cd03344 82 AGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELK--KLSKPVkTKEEIAQVATIS--ANGDEEIGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 167 VLTEavvdsilAIKK--QDEPIDLfmveimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSL 237
Cdd:cd03344 158 LIAE-------AMEKvgKDGVITV------EEGKTLETELEVVEGMQFDRGYLSPyfvtdpeKMEVELENPYILLTDKKI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 238 EYEKTEVNSgffyksaeeREKLVKAERKFI---EDrvkkiielkkkVCGDSDKGFVVINQKGIdpfsLDALAKegiialr 314
Cdd:cd03344 225 SSIQELLPI---------LELVAKAGRPLLiiaED-----------VEGEALATLVVNKLRGG----LKVCAV------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 315 RA-----KRRNM-ERLTLACGGIALN-----SLDDLNPDCLGHAGLVyeyTLGEEKFTFIEKCNNPRSV----------- 372
Cdd:cd03344 274 KApgfgdRRKAMlEDIAILTGGTVISeelglKLEDVTLEDLGRAKKV---VVTKDDTTIIGGAGDKAAIkariaqirkqi 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 373 ------------------------TLLIKGPNKHTLTQIKDAIRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALVKYKPS 428
Cdd:cd03344 351 eettsdydkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKAL 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4B2T_Z 429 vKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQaehsESGQLVGVDLNTGEPMVAAEAGIWD 496
Cdd:cd03344 430 -NGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEYVDMIEAGIID 492
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
30-155 |
1.19e-09 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 60.71 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
4B2T_Z 106 ADLYISEGLHPRIITEGFEaaKEKALQFLEQVKVSKEMDRETLIDVARTS 155
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIE--KTAKALVKELKKMSKEVEDSELADVAAVS 205
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
30-522 |
2.78e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 59.37 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHP----TASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PRK12851 23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 106 ADLYISEGLHPRIITEGFEAAKEKALQFLEqvKVSKEMDRETliDVART-SLRTKVHAELADVLTEAVvdsilaikkqdE 184
Cdd:PRK12851 103 GAKAVAAGANPMDLKRGIDRAVAAVVEELK--ANARPVTTNA--EIAQVaTISANGDAEIGRLVAEAM-----------E 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 185 PIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVnsgffyksaEERE 257
Cdd:PRK12851 168 KVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEKKISNLQDLL---------PVLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 258 KLVKAERKFIedrvkkIIelKKKVCGDSDKGFVVINQKGIdpFSLDALAKEGIIALRRAKRRNMERLTlacGGIALN--- 334
Cdd:PRK12851 239 AVVQSGKPLL------II--AEDVEGEALATLVVNKLRGG--LKVAAVKAPGFGDRRKAMLEDIAILT---GGTVISedl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 335 --SLDDLNPDCLGHAGLVyeyTLGEEKFTF--------------------IEKCNNP--------RSVTL-----LIK-- 377
Cdd:PRK12851 306 giKLENVTLEQLGRAKKV---VVEKENTTIidgagskteiegrvaqiraqIEETTSDydreklqeRLAKLaggvaVIRvg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 378 GPNKHTLTQIKDAIRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALVKYKpSVKGRAQLGVQAFADALLIIPKVLAQNSGF 457
Cdd:PRK12851 383 ASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLE-TANGDQRTGVEIVRRALEAPVRQIAENAGA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
4B2T_Z 458 DLQETLVKVqAEHSESgqlVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:PRK12851 461 EGSVVVGKL-REKPGG---YGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-524 |
6.50e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 58.50 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQI----QHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 106 ADLYISEGLHPRIITEGFEAAKEKALQFLeqVKVSKEM-DRETLIDVARTSLR--TKVHAELADVLTEAVVDSILAIkkq 182
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADL--VKNSKKVtSNDEIAQVGTISANgdAEIGKFLADAMKKVGNEGVITV--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 183 depidlfmveimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYIL-------TCNVSLEYEKTEVNSGF 248
Cdd:PRK14104 178 ------------EEAKSLETELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYILinekklsSLNELLPLLEAVVQTGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 249 -FYKSAEEREKlvKAERKFIEDRVK---KIIELKKKVCGDSDKGFV--VINQKGIDPFSLD---ALAKEGIIALRRAKRR 319
Cdd:PRK14104 246 pLVIVAEDVEG--EALATLVVNRLRgglKVAAVKAPGFGDRRKAMLqdIAILTGGQAISEDlgiKLENVTLQMLGRAKKV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 320 --NMERLTLACGGialNSLDDLNPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIK--GPNKHTLTQIKDAIRDGL 395
Cdd:PRK14104 324 miDKENTTIVNGA---GKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 396 RAVKNAIDDGcVVPGAGAVEVAMAEALVKYKpSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQAEHSESgq 475
Cdd:PRK14104 401 HATRAAVEEG-IVPGGGVALLRASEQLKGIK-TKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYS-- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
4B2T_Z 476 lVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATnILLVDEIMRA 524
Cdd:PRK14104 477 -YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAA-LLITTEAMVA 523
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
14-231 |
5.28e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 52.15 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 14 ARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQI----QHPTASLIAKVATAQDDITG 89
Cdd:PRK12852 12 ARDRMLRGVDI-----LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 90 DGTTSNVLIIGELLKQADLYISEGLHPriitegfeaakekalqfleqvkvskeMDRETLIDVARTSLRTKVHAELADVLT 169
Cdd:PRK12852 87 DGTTTATVLAQAIVREGAKAVAAGMNP--------------------------MDLKRGIDIAVAAVVKDIEKRAKPVAS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 170 EAVVDSILAIKKQ-DEPIDLFMVEIM-----------EMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYI 230
Cdd:PRK12852 141 SAEIAQVGTISANgDAAIGKMIAQAMqkvgnegvitvEENKSLETEVDIVEGMKFDRGYLSPyfvtnaeKMTVELDDAYI 220
|
.
4B2T_Z 231 L 231
Cdd:PRK12852 221 L 221
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
12-524 |
7.40e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 51.64 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHP----TASLIAKVATAQDDI 87
Cdd:PRK12850 10 TDARDRLLRGVNI-----LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQfleqvkvskemdretliDVARTSLRTKVHAELADV 167
Cdd:PRK12850 85 AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVD-----------------ELKKIAKKVTSSKEIAQV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 168 LTEAVVDsilaikkqDEPIDLFMVEIMEMKHKS-----------ETDTSLIRGLVLDHGARHPDM-----KKRV--EDAY 229
Cdd:PRK12850 148 ATISANG--------DESIGEMIAEAMDKVGKEgvitveeaktlGTELDVVEGMQFDRGYLSPYFvtnpeKMRAelEDPY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 230 ILTCNVSLEYEKTEVNSgffyksaeeREKLVKAERKFIedrvkkIIelKKKVCGDSDKGFVVINQKGIdpFSLDALAKEG 309
Cdd:PRK12850 220 ILLHEKKISNLQDLLPI---------LEAVVQSGRPLL------II--AEDVEGEALATLVVNKLRGG--LKSVAVKAPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 310 IIALRRAKrrnMERLTLACGGIALN-----SLDDLNPDCLGHAGLVyeyTLGEEKFTFIEKCNNPRsvtlLIKGPNKHTL 384
Cdd:PRK12850 281 FGDRRKAM---LEDIAVLTGGQVISedlgiKLENVTLDMLGRAKRV---LITKENTTIIDGAGDKK----NIEARVKQIR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 385 TQI---------------------------------------KDAIRDGLRAVKNAIDDGcVVPGaGAVEVAMAEALVKY 425
Cdd:PRK12850 351 AQIeettsdydreklqerlaklaggvavirvggatevevkekKDRVDDALHATRAAVEEG-IVPG-GGVALLRARSALRG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 426 KPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKVQaeHSESGQlvGVDLNTGEPMVAAEAGIWDNYCVKKQLL 505
Cdd:PRK12850 429 LKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVA--ELPGNF--GFNAQTGEYGDMVEAGIIDPAKVTRTAL 504
|
570
....*....|....*....
4B2T_Z 506 HSCTVIATnILLVDEIMRA 524
Cdd:PRK12850 505 QDAASIAA-LLITTEAMVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
38-516 |
4.89e-04 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 42.78 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 38 LGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQ----IQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEG 113
Cdd:CHL00093 30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 114 LHPRIITEGFeaakEKALQFL-EQV-KVSKEM-DRETLIDVARTSL--RTKVHAELADVLTEAVVDSILAikkqdepidl 188
Cdd:CHL00093 110 ANPISLKRGI----EKATQYVvSQIaEYARPVeDIQAITQVASISAgnDEEVGSMIADAIEKVGREGVIS---------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 189 fmveiMEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVNSGFfyksaeerEKLVK 261
Cdd:CHL00093 176 -----LEEGKSTVTELEITEGMRFEKGFISPyfvtdteRMEVVQENPYILLTDKKITLVQQDLLPIL--------EQVTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 262 AERKF--IEDRVKKiielkkkvcgDSDKGFVVINQKGIdpFSLDALAKEGIIALRRAkrrNMERLTLACGGIALN----- 334
Cdd:CHL00093 243 TKRPLliIAEDVEK----------EALATLVLNKLRGI--VNVVAVRAPGFGDRRKA---MLEDIAILTGGQVITedagl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 335 SLDDLNPDCLGHAGLVyeyTLGEEKFTFIEKCNNP----------RSVTLLIKGPNKHTL-------------------- 384
Cdd:CHL00093 308 SLETIQLDLLGQARRI---IVTKDSTTIIADGNEEqvkarceqlrKQIEIADSSYEKEKLqerlaklsggvavikvgaat 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 385 -TQIKDA---IRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALVKY-KPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDL 459
Cdd:CHL00093 385 eTEMKDKklrLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWaKNNLKEDELIGALIVARAILAPLKRIAENAGKNG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
4B2T_Z 460 QETLVKVQAEHSEsgqlVGVDLNTGEPMVAAEAGIWDNYCVKKQLLHSCTVIATNIL 516
Cdd:CHL00093 464 SVIIEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
12-142 |
2.79e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 40.49 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4B2T_Z 12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDI 87
Cdd:PRK00013 9 EDARRKLLRGVNK-----LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
4B2T_Z 88 TGDG-TTSNVL---IIGELLKqadlYISEGLHPRIITEGFEAAKEKALQFLEqvKVSKE 142
Cdd:PRK00013 84 AGDGtTTATVLaqaIVREGLK----NVAAGANPMDLKRGIDKAVEAAVEELK--KISKP 136
|
|
| |
