|
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: 884.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 3 AIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347 1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 83 AQDDVTGDGTTSNVLIIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKE--MKRKILLDVARTSLQTKV 160
Cdd:TIGR02347 81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 161 HAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 241 KTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQS-NKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 320 NMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIK 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 400 NAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGV 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58331173 480 DLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 530
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-526 |
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: 871.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK--RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 180
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDtdRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 181 RPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKtaeekeklv 260
Cdd:cd03342 177 KPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSGFFYS--------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 261 kaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLT 340
Cdd:cd03342 248 -----------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 341 VDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAE 420
Cdd:cd03342 299 PECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 421 ALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCV 500
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|....*.
gi 58331173 501 KKQLLHSCTVIATNILLVDEIMRAGM 526
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEIIRAGR 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: 571.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLY 109
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 110 ISEGLHPRIIAEGFEAAKIKALEVLEEVKV--TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPID 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 188 LFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEKLVKAERKFI 267
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 268 EDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHA 347
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 348 GLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKN 427
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 428 SIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHS 507
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 58331173 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 ... |
23-523 |
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: 543.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd00309 13 NINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:cd00309 93 LKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEdREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 PGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYektevnsgffyktaeekeklvk 261
Cdd:cd00309 173 ENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 262 aerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTV 341
Cdd:cd00309 231 ----------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 342 DCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEA 421
Cdd:cd00309 283 EDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 422 LVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVK 501
Cdd:cd00309 363 LEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVK 442
|
490 500
....*....|....*....|..
gi 58331173 502 KQLLHSCTVIATNILLVDEIMR 523
Cdd:cd00309 443 RQALKSATEAASLILTIDDIIV 464
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
23-525 |
6.24e-142 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 418.90 E-value: 6.24e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:NF041082 22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:NF041082 102 LKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 P--GYPIDLFMVEImeMKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKE 257
Cdd:NF041082 182 KdgGYNVDLDNIKV--EKKVGGSieDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 258 KLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFE 337
Cdd:NF041082 260 AFLDQEEKMLKEMVDKIAD------SGAN---VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSID 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 338 DLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVA 417
Cdd:NF041082 331 DLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 418 MAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDN 497
Cdd:NF041082 411 LALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEP 490
|
490 500
....*....|....*....|....*...
gi 58331173 498 YCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041082 491 LRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
23-525 |
4.61e-141 |
|
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: 416.66 E-value: 4.61e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03343 20 NIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEE--VKVTKEmKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV- 179
Cdd:cd03343 100 LEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 --RRPGYPIDLFMVEIMemKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 255
Cdd:cd03343 179 ekRDGKYVVDLDNIKIE--KKTGGSvdDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 335
Cdd:cd03343 257 LQAFLEQEEAMLKEMVDKIAD------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 336 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 415
Cdd:cd03343 328 IDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 416 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 495
Cdd:cd03343 408 IELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVI 487
|
490 500 510
....*....|....*....|....*....|
gi 58331173 496 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:cd03343 488 EPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
23-525 |
2.92e-140 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 414.73 E-value: 2.92e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:NF041083 22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV-- 179
Cdd:NF041083 102 LKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKvDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVae 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 -RRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEK 258
Cdd:NF041083 182 kRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 259 LVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFED 338
Cdd:NF041083 262 FLDQEEKMLKEMVDKIKA------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 339 LTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAM 418
Cdd:NF041083 333 LTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVEL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 419 AEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNY 498
Cdd:NF041083 413 AKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPL 492
|
490 500
....*....|....*....|....*..
gi 58331173 499 CVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041083 493 RVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
23-524 |
3.02e-136 |
|
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: 404.45 E-value: 3.02e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02339 21 NIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEE--VKVTKEmKRKILLDVARTSLQTKVHAELA-DVLTEVVVDSVLAV 179
Cdd:TIGR02339 101 LEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEiaTKISPE-DRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 RRP----GYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 255
Cdd:TIGR02339 180 AELrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 335
Cdd:TIGR02339 260 IKKFLDQEEAMLKEMVDKIAS------AGAN---VVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 336 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 415
Cdd:TIGR02339 331 IDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 416 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 495
Cdd:TIGR02339 411 IELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVI 490
|
490 500
....*....|....*....|....*....
gi 58331173 496 DNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02339 491 EPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-521 |
3.34e-98 |
|
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: 306.92 E-value: 3.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03339 28 HILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKE---MKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV 179
Cdd:cd03339 108 LEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 ----RRpgyPIDLfmvEIMEMKHKLG---TDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKT 252
Cdd:cd03339 188 adleRK---DVNF---ELIKVEGKVGgrlEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 253 AEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 332
Cdd:cd03339 262 VEDYKKLQEYEQKYFREMVEQVKD------AGAN---LVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 333 VNSFEDLTVDCLGHAGLVYEYTLG--EEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPG 410
Cdd:cd03339 333 VPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 411 AGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQ-LVGVDLNTGEPMVA 489
Cdd:cd03339 413 GGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNpHLGIDCLGRGTNDM 492
|
490 500 510
....*....|....*....|....*....|..
gi 58331173 490 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03339 493 KEQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
23-525 |
1.02e-91 |
|
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: 290.17 E-value: 1.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02343 32 NIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEV--KVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV 179
Cdd:TIGR02343 112 LEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 ----RRpgyPIDLfmvEIMEMKHKLG---TDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKT 252
Cdd:TIGR02343 192 admeRR---DVDF---DLIKVEGKVGgslEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 253 AEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 332
Cdd:TIGR02343 266 VEEYKKLQKYEQQKFKEMIDDIKK------SGAN---LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 333 VNSFEDLTVDCLGHAGLVYEYTLG--EEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPG 410
Cdd:TIGR02343 337 VPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 411 AGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQ-LVGVDLNTGEPMVA 489
Cdd:TIGR02343 417 GGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNpNLGVDCLGYGTNDM 496
|
490 500 510
....*....|....*....|....*....|....*.
gi 58331173 490 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:TIGR02343 497 KEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-521 |
4.17e-89 |
|
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: 283.17 E-value: 4.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02344 21 NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:TIGR02344 101 LSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNdDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 PGYPIdlFMVEIMEM----KHKLG--TDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 255
Cdd:TIGR02344 181 DENGR--KEIDIKRYakveKIPGGdiEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEED 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQKIIDLKDKvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 335
Cdd:TIGR02344 259 WNRILQMEEEYVQLMCEDIIAVKPD---------LVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 336 FEDLTVDCLG-HAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAI 414
Cdd:TIGR02344 330 PEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGAT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 415 EVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHV-ESKQLVGVDLNTGEPMVAADAG 493
Cdd:TIGR02344 410 EMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDGETGKIVDMKEKG 489
|
490 500
....*....|....*....|....*...
gi 58331173 494 VWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:TIGR02344 490 IWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-521 |
1.51e-88 |
|
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: 280.34 E-value: 1.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03337 21 NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:cd03337 101 LAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 P----GYPIDL--FM-VEimemKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYektevnsgffykt 252
Cdd:cd03337 181 EengrKKEIDIkrYAkVE----KIPGGEieDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY------------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 253 aeekeklvkaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 332
Cdd:cd03337 244 -------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 333 VNSFEDLTVDCLGHAGLVYEYTL-GEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGA 411
Cdd:cd03337 287 VNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 412 GAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVES-KQLVGVDLNTGEPMVAA 490
Cdd:cd03337 367 GATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGeNSTWGIDGETGDIVDMK 446
|
490 500 510
....*....|....*....|....*....|.
gi 58331173 491 DAGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03337 447 ELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
23-524 |
7.51e-88 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 279.27 E-value: 7.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAK----VATAQDDVTGDGTTSNVLI 98
Cdd:COG0459 15 NIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTTATVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 99 IGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEE--VKVTKemkRKILLDVARTSLQTKvhaelaDVLTEVVVDSV 176
Cdd:COG0459 95 AGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKiaKPVDD---KEELAQVATISANGD------EEIGELIAEAM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 177 LAVRRPGYpidlFMVEimemKHK-LGTDTKLIQGLVLDHGARHPD-------MKKRVEDAFILICNVSLEyektevnsgf 248
Cdd:COG0459 166 EKVGKDGV----ITVE----EGKgLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS---------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 249 fyktaeekeklvkaerkfiedRVQKIIDLKDKVcAQSNKGfVVINQKGIDPFSLDSLAKHGIVALRRA---------KRR 319
Cdd:COG0459 228 ---------------------SIQDLLPLLEKV-AQSGKP-LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgDRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 320 N--MERLSLACGGMAVN-----SFEDLTVDCLGHAGLVYEytlGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIR 392
Cdd:COG0459 285 KamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 393 DGLRAIKNAIEDGCmVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEhve 472
Cdd:COG0459 362 DALHATRAAVEEGI-VPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA--- 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 58331173 473 SKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:COG0459 438 KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
23-523 |
6.75e-87 |
|
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: 277.76 E-value: 6.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02340 17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTK--EMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 180
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSvdELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 181 ------RPGYPIDlfMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAE 254
Cdd:TIGR02340 177 ttnengETKYPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 255 EKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVN 334
Cdd:TIGR02340 255 KLEQIRQREADITKERIKKILD------AGAN---VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 335 SFEDLTVD------CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMV 408
Cdd:TIGR02340 326 TLADLEGEetfeasYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 409 PGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVES------KQL--VGVD 480
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAqlkpekKHLkwYGLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 58331173 481 LNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:TIGR02340 486 LVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
23-523 |
1.29e-86 |
|
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: 276.86 E-value: 1.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTK--EMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 180
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISvdNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 181 R------PGYPIDlfMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAE 254
Cdd:cd03335 173 TtnekgkTKYPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 255 EKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVN 334
Cdd:cd03335 251 KLEKIRQRESDITKERIKKILA------AGAN---VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 335 SFEDLTVD------CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMV 408
Cdd:cd03335 322 TLANLEGEetfdpsYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 409 PGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQL--------VGVD 480
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKpdkkhlkwYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 58331173 481 LNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-486 |
5.49e-84 |
|
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: 269.54 E-value: 5.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 PGYP--IDLFMVEIMEmkhKLG---TDTKLIQGLVLDHGARH-PDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 255
Cdd:cd03338 173 PATAtnVDLKDIRIVK---KLGgtiEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQKIidlKDKVCAqsnkgfVVINQKGI-----DPFSLDSLAKHGIVALRRAKRRNMERLSLACGG 330
Cdd:cd03338 250 MDRILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 331 MAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPC-SVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVP 409
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGkTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIP 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58331173 410 GAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEP 486
Cdd:cd03338 401 GGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-524 |
4.47e-81 |
|
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: 262.39 E-value: 4.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLA 178
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTideeKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 179 VRRPGypIDLFMVEIMEMKHKLGTDTKLIQGLVLDHG---ARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 255
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 335
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIV---------ESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 336 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 415
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 416 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 495
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
|
490 500
....*....|....*....|....*....
gi 58331173 496 DNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-524 |
5.49e-81 |
|
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: 262.22 E-value: 5.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT-----KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVL 177
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNidkedKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 178 AVRRpgyPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHG---ARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAE 254
Cdd:cd03340 181 SLDD---DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 255 EKEKLVKAERKFIEDRVQKIIDLKDKvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVN 334
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGAN---------VVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 335 SFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAI 414
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 415 EVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQL-VGVDLNTGEPMVAADAG 493
Cdd:cd03340 409 EMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAF 488
|
490 500 510
....*....|....*....|....*....|.
gi 58331173 494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03340 489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
2.41e-80 |
|
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: 260.10 E-value: 2.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02342 14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 181
Cdd:TIGR02342 94 LGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSdREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVID 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 PGYPIDLFMVEIMEMKHKLGT--DTKLIQGLVLDHGARHPD-MKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEK 258
Cdd:TIGR02342 174 PENAKNVDLNDIKVVKKLGGTidDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 259 LVKAERKFIEDRVQKIidlkdkvcaQSNKGFVVINQKGI-----DPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAV 333
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---------KKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 334 NSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPC-SVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAG 412
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 413 AIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADA 492
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
|
490 500 510
....*....|....*....|....*....|
gi 58331173 493 GVWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
32-524 |
7.82e-79 |
|
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: 256.10 E-value: 7.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 32 DVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLY 109
Cdd:cd03336 27 DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 110 ISEGLHPRIIAEGFEAAKIKALEVLEE----VKVTKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGyp 185
Cdd:cd03336 107 VAQKIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSG-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 186 iDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEK-----TEVNSGFFYKTAEe 255
Cdd:cd03336 185 -NLDAIQIIK---KLGgslKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMDTDKikifgAKVRVDSTAKVAE- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 kekLVKAERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 335
Cdd:cd03336 257 ---IEEAEKEKMKNKVEKIL---------KHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIAST 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 336 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 415
Cdd:cd03336 325 FDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 416 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 495
Cdd:cd03336 405 MLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGIT 484
|
490 500
....*....|....*....|....*....
gi 58331173 496 DNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03336 485 ESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
23-524 |
3.20e-76 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 249.95 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVL 97
Cdd:PTZ00212 27 SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 98 IIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVV 173
Cdd:PTZ00212 107 LAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDhgsdEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 174 DSVLAVRRPGypiDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEK-----TE 243
Cdd:PTZ00212 187 DAVLRLKGSG---NLDYIQIIK---KPGgtlRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMDTDKikiygAK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 244 VNSGFFYKTAEekekLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMER 323
Cdd:PTZ00212 258 VKVDSMEKVAE----IEAAEKEKMKNKVDKILA------HGCN---VFINRQLIYNYPEQLFAEAGIMAIEHADFDGMER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 324 LSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIE 403
Cdd:PTZ00212 325 LAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 404 DGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNT 483
Cdd:PTZ00212 405 DTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEK 484
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 58331173 484 GEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-524 |
4.53e-72 |
|
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: 238.85 E-value: 4.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEM---KRKILLDVARTSLQTKVHAElADVLTEVVVDSVLAV 179
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKdlrDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 rRPGYPIDlFMVEIMEMKHKLGT---DTKLIQGLVLdhgARHPDMK-KRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 255
Cdd:TIGR02346 182 -LPKNPQN-FNVDNIRVCKILGGslsNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQKIIDLKDKvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 335
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVN---------VIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 336 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSV-TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAI 414
Cdd:TIGR02346 328 LGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGAT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 415 EVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMV--AADA 492
Cdd:TIGR02346 408 EIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVkdASEA 487
|
490 500 510
....*....|....*....|....*....|..
gi 58331173 493 GVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02346 488 GIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
145-404 |
1.35e-68 |
|
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: 219.26 E-value: 1.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 145 RKILLDVARTSLQTKVhAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKR 224
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 225 VEDAFILICNVSLEYektevnsgffyktaeekeklvkaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDS 304
Cdd:cd03333 80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 305 LAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTL 384
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 58331173 385 TQVKDAIRDGLRAIKNAIED 404
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
32-524 |
1.14e-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: 216.26 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 32 DVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLY 109
Cdd:TIGR02341 28 DLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 110 ISEGLHPRIIAEGFEAAKIKALEVLEEVKV----TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGyp 185
Cdd:TIGR02341 108 INQKIHPQTIIAGYREATKAARDALLKSAVdngsDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSG-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 186 iDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEKTEV-NSGFFYKTAEEKEKL 259
Cdd:TIGR02341 186 -NLEAIQIIK---KLGgslADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMDTDKVKIfGSRVRVDSTAKVAEL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 260 VKAERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDL 339
Cdd:TIGR02341 259 EHAEKEKMKEKVEKIL---------KHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 340 TVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMA 419
Cdd:TIGR02341 330 ELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 420 EALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYC 499
Cdd:TIGR02341 410 KAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYK 489
|
490 500
....*....|....*....|....*
gi 58331173 500 VKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02341 490 VKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-524 |
1.40e-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: 214.78 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGEL 102
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 103 LKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKILLDVA---RTSLQTKVhAELADVLTEVVVDSVLAV 179
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSkalKTAIASKQ-YGNEDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 rrpgYPIDL--FMVEIMEMKHKLG---TDTKLIQGLVLdhgARHPDMK-KRVEDAFILICNVSLEyekTEVNsgffykta 253
Cdd:cd03341 172 ----LPENIgnFNVDNIRVVKILGgslEDSKVVRGMVF---KREPEGSvKRVKKAKVAVFSCPFD---IGVN-------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 254 eekeklvkaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAV 333
Cdd:cd03341 234 ------------------------------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 334 NSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSV-TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAG 412
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 413 AIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMV--AA 490
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAK 437
|
490 500 510
....*....|....*....|....*....|....
gi 58331173 491 DAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
203-388 |
1.38e-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: 68.02 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 203 DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKteVNSGFFYKtaeekEKLVKAERKFIEDRVQKIIDLKDKVc 282
Cdd:cd03334 62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLSL-----DPVILQEKEYLKNLVSRIVALRPDV- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 283 aqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLtVDC--LGHAGLVYEYTLGEEK- 359
Cdd:cd03334 134 --------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDL-LTSpkLGTCESFRVRTYVEEHg 204
|
170 180 190
....*....|....*....|....*....|...
gi 58331173 360 ----FTFIEECVNPCSVTLLVKGPNKHTLTQVK 388
Cdd:cd03334 205 rsktLMFFEGCPKELGCTILLRGGDLEELKKVK 237
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-496 |
8.76e-12 |
|
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: 67.48 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPT----ASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLARAIIKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 106 ADLYISEGLHPRIIAEGFEAAKIKALEVLeevkvtKEMKRKI-----LLDVARTSLQTKVH--AELADVLTEVVVDSVLA 178
Cdd:cd03344 100 GLKAVAAGANPMDLKRGIEKAVEAVVEEL------KKLSKPVktkeeIAQVATISANGDEEigELIAEAMEKVGKDGVIT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 179 VrrpgypidlfmveimEMKHKLGTDTKLIQGLVLDHGARHP-------DMKKRVEDAFILICNvsleyektevnsgffyk 251
Cdd:cd03344 174 V---------------EEGKTLETELEVVEGMQFDRGYLSPyfvtdpeKMEVELENPYILLTD----------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 252 taeekeklvkaerkfiedrvQKIIDLKDKV-----CAQSNKGFVVINQKgIDPFSLDSLAKHGI-----VALRRA----- 316
Cdd:cd03344 222 --------------------KKISSIQELLpilelVAKAGRPLLIIAED-VEGEALATLVVNKLrgglkVCAVKApgfgd 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 317 KRRNM-ERLSLACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEKFTFIEECVNPCSV------------------ 372
Cdd:cd03344 281 RRKAMlEDIAILTGGTVISeelglKLEDVTLEDLGRAKKV---VVTKDDTTIIGGAGDKAAIkariaqirkqieettsdy 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 373 -----------------TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCmVPGAGAIEVAMAEALVTYKNSIKGrARL 435
Cdd:cd03344 358 dkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEGI-VPGGGVALLRASPALDKLKALNGD-EKL 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331173 436 GVQAFADALLIIPKVLAQNAGYDPQETLVKVqaehVESKQLVGVDLNTGE--PMVAadAGVWD 496
Cdd:cd03344 436 GIEIVRRALEAPLRQIAENAGVDGSVVVEKV----LESPDGFGYDAATGEyvDMIE--AGIID 492
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
30-522 |
1.89e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 66.30 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHP----TASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK12851 23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 106 ADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKvTKEMKRKILLDVARTSLQ--TKVHAELADVLTEVVVDSVLAVrrpg 183
Cdd:PRK12851 103 GAKAVAAGANPMDLKRGIDRAVAAVVEELKANA-RPVTTNAEIAQVATISANgdAEIGRLVAEAMEKVGNEGVITV---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 184 ypidlfmveimEMKHKLGTDTKLIQGLVLDHGARHP-------DMKKRVEDAFILICNvsleyektevnsgffyktaeek 256
Cdd:PRK12851 178 -----------EESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHE---------------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 257 EKLvkaerkfieDRVQKIIDLKDKVcAQSNKGFVVINQKgIDPFSLDSLAKHGI-----VALRRA-----KRRNM-ERLS 325
Cdd:PRK12851 225 KKI---------SNLQDLLPVLEAV-VQSGKPLLIIAED-VEGEALATLVVNKLrgglkVAAVKApgfgdRRKAMlEDIA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 326 LACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEKFTF--------------------IEECVNPCSVTLL----- 375
Cdd:PRK12851 294 ILTGGTVISedlgiKLENVTLEQLGRAKKV---VVEKENTTIidgagskteiegrvaqiraqIEETTSDYDREKLqerla 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 376 ----------VKGPNKHTLTQVKDAIRDGLRAIKNAIEDGcMVPGAGAIEVAMAEALVTyKNSIKGRARLGVQAFADALL 445
Cdd:PRK12851 371 klaggvavirVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRALE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58331173 446 IIPKVLAQNAGYDPQETLVKVQaehvESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:PRK12851 449 APVRQIAENAGAEGSVVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
30-458 |
4.47e-11 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 65.32 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDG-----NVLLdEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLK 104
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvakAIEF-SDRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 105 QADLYISEGLHPRIIAEGFEAAKIKALEVLEEVK---VTKEMkrkiLLDVARTSlqtkvhAELADVLTEVVVDSVLAVRR 181
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSrpvKTKED----ILNVATIS------ANGDVEIGSLIADAMDKVGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 182 PGYpidlfmVEIME---MKHKLgtdtKLIQGLVLDHGARHP-------DMKKRVEDAFILICNVSLEYEKTEVNS-GFFY 250
Cdd:PTZ00114 183 DGT------ITVEDgktLEDEL----EVVEGMSFDRGYISPyfvtnekTQKVELENPLILVTDKKISSIQSILPIlEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 251 KT-------AEEKEKLVKAErkFIEDRVQKIIdlkdKVCAQSNKGF-----------------VVINQKG----IDPFSL 302
Cdd:PTZ00114 253 KNkrplliiAEDVEGEALQT--LIINKLRGGL----KVCAVKAPGFgdnrkdilqdiavltgaTVVSEDNvglkLDDFDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 303 DSL--AKHGIV----------------------ALRRAKRRNM---------ERLSLACGGMAVnsfedltvdclghagl 349
Cdd:PTZ00114 327 SMLgsAKKVTVtkdetviltgggdkaeikerveLLRSQIERTTseydkeklkERLAKLSGGVAV---------------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 350 vyeytlgeekftfieecvnpcsvtLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGcMVPGAGAIEVAMAEAL--VTYKN 427
Cdd:PTZ00114 391 ------------------------IKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLdkLEEDN 445
|
490 500 510
....*....|....*....|....*....|.
gi 58331173 428 SIKGRARLGVQAFADALLIIPKVLAQNAGYD 458
Cdd:PTZ00114 446 ELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-524 |
1.98e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 60.04 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQI----QHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 106 ADLYISEGLHPRIIAEGFEAAkIKALeVLEEVKVTKEM-KRKILLDVARTSLQ--TKVHAELADVLTEVVVDSVLAVrrp 182
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLA-VEAV-VADLVKNSKKVtSNDEIAQVGTISANgdAEIGKFLADAMKKVGNEGVITV--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 183 gypidlfmveimEMKHKLGTDTKLIQGLVLDHGARHP-------DMKKRVEDAFILIcnvsleyektevnsgffyktAEE 255
Cdd:PRK14104 178 ------------EEAKSLETELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYILI--------------------NEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 256 KEKLVKAERKFIEDRVQK---IIDLKDKVCAQSNKGFVVINQKGidPFSLDSLAKHGIVALRRAKrrnMERLSLACGGMA 332
Cdd:PRK14104 226 KLSSLNELLPLLEAVVQTgkpLVIVAEDVEGEALATLVVNRLRG--GLKVAAVKAPGFGDRRKAM---LQDIAILTGGQA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 333 VNS-----FEDLTVDCLGHAGLVY---EYTL---GEEKFTFIEECVNPCS--------------------------VTLL 375
Cdd:PRK14104 301 ISEdlgikLENVTLQMLGRAKKVMidkENTTivnGAGKKADIEARVAQIKaqieettsdydreklqerlaklaggvAVIR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 376 VKGPNKHTLTQVKDAIRDGLRAIKNAIEDGcMVPGAGAIEVAMAEALVTYKNSIKGRaRLGVQAFADALLIIPKVLAQNA 455
Cdd:PRK14104 381 VGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTKNDDQ-KTGVEIVRKALSAPARQIAINA 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 456 GYDPQETLVKVqaehVESKQLV-GVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATnILLVDEIMRA 524
Cdd:PRK14104 459 GEDGSVIVGKI----LEKEQYSyGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAA-LLITTEAMVA 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
30-524 |
3.25e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 59.35 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHP----TASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 106 ADLYISEGLHPRIIAEGFEaakiKALEVleevkVTKEMKRKilldvartSLQTKVHAELADVLT----------EVVVDS 175
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGID----LAVAA-----VVDELKKI--------AKKVTSSKEIAQVATisangdesigEMIAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 176 VLAVRRPGypidlfmVEIMEMKHKLGTDTKLIQGLVLDHGARHPDM-----KKRV--EDAFILICNVSLeyektevnsgf 248
Cdd:PRK12850 166 MDKVGKEG-------VITVEEAKTLGTELDVVEGMQFDRGYLSPYFvtnpeKMRAelEDPYILLHEKKI----------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 249 fyktaeekeklvkaerkfieDRVQKIIDLKDKVcAQSNKGFVVINQKgIDPFSLDSLAKHGI-----VALRRA-----KR 318
Cdd:PRK12850 228 --------------------SNLQDLLPILEAV-VQSGRPLLIIAED-VEGEALATLVVNKLrgglkSVAVKApgfgdRR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 319 RNM-ERLSLACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEKFTFIEECVNPCSVTLLVK--------------- 377
Cdd:PRK12850 286 KAMlEDIAVLTGGQVISedlgiKLENVTLDMLGRAKRV---LITKENTTIIDGAGDKKNIEARVKqiraqieettsdydr 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 378 --------------------GPNKHTLTQVKDAIRDGLRAIKNAIEDGcMVPGAGaieVAMAEAL--VTYKNSIKGRARL 435
Cdd:PRK12850 363 eklqerlaklaggvavirvgGATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGG---VALLRARsaLRGLKGANADETA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 436 GVQAFADALLIIPKVLAQNAGYDPQETLVKVqaehVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATnI 515
Cdd:PRK12850 439 GIDIVRRALEEPLRQIATNAGFEGSVVVGKV----AELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAA-L 513
|
....*....
gi 58331173 516 LLVDEIMRA 524
Cdd:PRK12850 514 LITTEAMVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
38-516 |
1.21e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 54.34 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 38 LGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQ----IQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLYISEG 113
Cdd:CHL00093 30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 114 LHPRIIAEGFEaakikalevleevKVTKEMKRKIlLDVARTSLQTKVHAELA-------DVLTEVVVDSVLAVRRPGypi 186
Cdd:CHL00093 110 ANPISLKRGIE-------------KATQYVVSQI-AEYARPVEDIQAITQVAsisagndEEVGSMIADAIEKVGREG--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 187 dlfmveIMEMKHKLGTDTKL--IQGLVLDHGARHP-------DMKKRVEDAFILICNvsleyektevnsgffyktaeEKE 257
Cdd:CHL00093 173 ------VISLEEGKSTVTELeiTEGMRFEKGFISPyfvtdteRMEVVQENPYILLTD--------------------KKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 258 KLVKaerkfiedrvQKIIDLKDKVcAQSNKGFVVINQKgIDPFSLDSLAKH---GI---VALR-----RAKRRNMERLSL 326
Cdd:CHL00093 227 TLVQ----------QDLLPILEQV-TKTKRPLLIIAED-VEKEALATLVLNklrGIvnvVAVRapgfgDRRKAMLEDIAI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 327 ACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEKFTFIEE---------C----------------------VNPC 370
Cdd:CHL00093 295 LTGGQVITedaglSLETIQLDLLGQARRI---IVTKDSTTIIADgneeqvkarCeqlrkqieiadssyekeklqerLAKL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 371 SVTLLVKGPNKHTLTQVKDA---IRDGLRAIKNAIEDGcMVPGAGAIEVAMAEALVTY-KNSIKGRARLGVQAFADALLI 446
Cdd:CHL00093 372 SGGVAVIKVGAATETEMKDKklrLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWaKNNLKEDELIGALIVARAILA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 447 IPKVLAQNAGYDPQETLVKVQAEHVEskqlVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNIL 516
Cdd:CHL00093 451 PLKRIAENAGKNGSVIIEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
27-496 |
1.00e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 51.35 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 27 ARG---LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHP----TASLIAKVATAQDDVTGDGTTSNVLII 99
Cdd:PRK12849 16 ERGvnkLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 100 GELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEvKVTKEMKRKILLDVARTSLQ--TKVHAELADVLTEVVVDSVL 177
Cdd:PRK12849 96 QALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKA-LARPVSGSEEIAQVATISANgdEEIGELIAEAMEKVGKDGVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 178 AVrrpgypidlfmveimEMKHKLGTDTKLIQGLVLDHG------ARHPD-MKKRVEDAFILICNvsleyektevnsgffy 250
Cdd:PRK12849 175 TV---------------EESKTLETELEVTEGMQFDRGylspyfVTDPErMEAVLEDPLILLTD---------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 251 ktaeekEKLVkaerkfiedRVQKIIDLKDKVcAQSNKGFVVINQKgIDPFSLDSLAKHGI-----VALRRA----KRRN- 320
Cdd:PRK12849 224 ------KKIS---------SLQDLLPLLEKV-AQSGKPLLIIAED-VEGEALATLVVNKLrgglkVAAVKApgfgDRRKa 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 321 -MERLSLACGGMAVN-----SFEDLTVDCLGHAGLVyeyTLGEEKFTFIEECVNPCSV---------------------- 372
Cdd:PRK12849 287 mLEDIAILTGGTVISedlglKLEEVTLDDLGRAKRV---TITKDNTTIVDGAGDKEAIearvaqirrqieettsdydrek 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 373 -------------TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCmVPGAGAIEVAMAEALVTYKNsIKGRARLGVQA 439
Cdd:PRK12849 364 lqerlaklaggvaVIKVGAATEVELKERKDRVEDALNATRAAVEEGI-VPGGGVALLRAAKALDELAG-LNGDQAAGVEI 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 58331173 440 FADALLIIPKVLAQNAGYDPQETLVKVQaehvESKQLVGVDLNTGE--PMVAadAGVWD 496
Cdd:PRK12849 442 VRRALEAPLRQIAENAGLDGSVVVAKVL----ELEDGFGFNAATGEygDLIA--AGIID 494
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
30-524 |
2.28e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 50.23 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQI----QHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQ 105
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 106 ADLYISEGLHPRIIAEGFE---AAKIKALEVL-EEVKVTKEMKRkilldVARTSLQ--TKVHAELADVLTEVVVDSVLAV 179
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDiavAAVVKDIEKRaKPVASSAEIAQ-----VGTISANgdAAIGKMIAQAMQKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 180 rrpgypidlfmveimEMKHKLGTDTKLIQGLVLDHGARHP-------DMKKRVEDAFILIcnvsleYEKTEVNsgffykt 252
Cdd:PRK12852 178 ---------------EENKSLETEVDIVEGMKFDRGYLSPyfvtnaeKMTVELDDAYILL------HEKKLSG------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 253 aeekeklvkaerkfiedrVQKIIDLKDKVcAQSNKGFVVINQKgIDPFSLDSLAKHGI-----VALRRA-----KRRNM- 321
Cdd:PRK12852 230 ------------------LQAMLPVLEAV-VQSGKPLLIIAED-VEGEALATLVVNRLrgglkVAAVKApgfgdRRKAMl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 322 ERLSLACGGMAVN-----SFEDLTVDCLGHAGLVY---EYTL---GEEKFTFIEECVNPCS------------------- 371
Cdd:PRK12852 290 EDIAILTGGQLISedlgiKLENVTLKMLGRAKKVVidkENTTivnGAGKKADIEARVGQIKaqieettsdydreklqerl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 372 -------VTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGcMVPGaGAIEVAMAEALVTYKNSIKGRARLGVQAFADAL 444
Cdd:PRK12852 370 aklaggvAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPG-GGVALLRAKKAVGRINNDNADVQAGINIVLKAL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 445 LIIPKVLAQNAGYDPQETLVKVQAEHVESkqlVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIAtNILLVDEIMRA 524
Cdd:PRK12852 448 EAPIRQIAENAGVEGSIVVGKILENKSET---FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVA-GLLVTTEAMVA 523
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
30-147 |
2.83e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 40.49 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331173 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPT----ASLIAKVATAQDDVTGDG-TTSNVL---IIGE 101
Cdd:PRK00013 22 LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGtTTATVLaqaIVRE 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 58331173 102 LLKqadlYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKI 147
Cdd:PRK00013 102 GLK----NVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEI 143
|
|
| |
