|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 869.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 7 LNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDD 86
Cdd:cd03342 1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 87 ATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV--NKKSLTDVARTSLKTKVHAAL 164
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 165 ADLLTDVCVDAVLAIRHDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKSEV 244
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 245 NSGFFYKtaeerekfvqaerdfidqrvkkiielkrkvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERL 324
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 325 ALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTIND 404
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 405 KCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTG 484
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 822092673 485 EPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRAGM 526
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| 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: 862.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 3 SISLLNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHAST 82
Cdd:TIGR02347 1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 83 AQDDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKV--PVEVNKKSLTDVARTSLKTKV 160
Cdd:TIGR02347 81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVkkEDEVDREFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 161 HAALADLLTDVCVDAVLAIRHDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 241 KSEVNSGFFYKTAEEREKFVQAERDFIDQRVKKIIELKRKVC-DGTEKSFVVINQKGIDPMSLDALAKEGILALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCgKSPDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 320 NMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAIN 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 400 NTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGL 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 822092673 480 DLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRAGMTSLK 530
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| 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: 572.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 30 LQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGELLKQADIF 109
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 110 LAEGLHPRIVTEGFEKAREQALAVLDTMK-VPVE-VNKKSLTDVARTSLKTKVHAALADLLTDVCVDAVLAIRHDEKPVD 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIIsIPVEdVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 188 LHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAEEREKFVQAERDFI 267
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 268 DQRVKKIIELKRKVcdgteksfvVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMNSVDDLEESHLGYA 347
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 348 GLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAGAFEVRAFNKLMKYKD 427
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 428 TVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEPMKPVDLGVYDNHIVKKQILNS 507
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 822092673 508 CSVIASNLLLVDEIMRAG 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: 544.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 11 AEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGD 90
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 91 GTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV-NKKSLTDVARTSLKTKVHAALADLLT 169
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVeDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 170 DVCVDAVLAIRHDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYeksevnsgff 249
Cdd:cd00309 161 ELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 250 yktaeerekfvqaerdfidqrvkkiielkrkvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACG 329
Cdd:cd00309 231 ----------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 330 GTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIP 409
Cdd:cd00309 271 ATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 410 GAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEPMKP 489
Cdd:cd00309 351 GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDM 430
|
490 500 510
....*....|....*....|....*....|....
gi 822092673 490 VDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMR 523
Cdd:cd00309 431 KEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
4-525 |
4.32e-143 |
|
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: 422.06 E-value: 4.32e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 4 ISLLNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTA 83
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 84 QDDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV-NKKSLTDVARTSLKTKVHA 162
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPdDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 163 ALADLLTDVCVDAVLAI---RHDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEY 239
Cdd:cd03343 161 AAKDKLADLVVDAVLQVaekRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 240 EKSEVNSGFFYKTAEEREKFVQAERDFIDQRVKKIIELKRKVcdgteksfvVINQKGIDPMSLDALAKEGILALRRAKRR 319
Cdd:cd03343 241 KKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANV---------VFCQKGIDDLAQHYLAKAGILAVRRVKKS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 320 NMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAIN 399
Cdd:cd03343 312 DMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 400 NTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLT---EEDRLNpdp 476
Cdd:cd03343 392 DALEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRaahEKGNKN--- 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 822092673 477 IGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRAG 525
Cdd:cd03343 469 AGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
18-525 |
3.95e-141 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 416.98 E-value: 3.95e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 18 NALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVL 97
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 98 LIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV-NKKSLTDVARTSLKTKVHAALADLLTDVCVDAV 176
Cdd:NF041082 97 LAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPdDKETLKKIAATAMTGKGAEAAKDKLADLVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 177 LAIRHDEKP--VDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAE 254
Cdd:NF041082 177 KAVAEKDGGynVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 255 EREKFVQAERDFIDQRVKKIIELKRKvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMN 334
Cdd:NF041082 257 QLQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 335 SVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAGAF 414
Cdd:NF041082 328 SIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 415 EVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEPMKPVDLGV 494
Cdd:NF041082 408 EVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGV 487
|
490 500 510
....*....|....*....|....*....|.
gi 822092673 495 YDNHIVKKQILNSCSVIASNLLLVDEIMRAG 525
Cdd:NF041082 488 VEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
18-525 |
7.23e-141 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 416.27 E-value: 7.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 18 NALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVL 97
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 98 LIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVN-KKSLTDVARTSLKTKVHAALADLLTDVCVDAV 176
Cdd:NF041083 97 LAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDdRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 177 LAI---RHDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTA 253
Cdd:NF041083 177 KQVaekRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 254 EEREKFVQAERDFIDQRVKKIIELkrkvcdGTEksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAM 333
Cdd:NF041083 257 DQLQKFLDQEEKMLKEMVDKIKAT------GAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 334 NSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAGA 413
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 414 FEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEPMKPVDLG 493
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
|
490 500 510
....*....|....*....|....*....|..
gi 822092673 494 VYDNHIVKKQILNSCSVIASNLLLVDEIMRAG 525
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
4-524 |
1.83e-137 |
|
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: 407.92 E-value: 1.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 4 ISLLNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTA 83
Cdd:TIGR02339 2 VFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 84 QDDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVN-KKSLTDVARTSLKTKVHA 162
Cdd:TIGR02339 82 QDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEdRDLLKKIAYTSLTSKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 163 ALA-DLLTDVCVDAVLAI---RHDEKP-VDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSL 237
Cdd:TIGR02339 162 EVAkDKLADLVVEAVKQVaelRGDGKYyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 238 EYEKSEVNSGFFYKTAEEREKFVQAERDFIDQRVKKIIELKRKvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAK 317
Cdd:TIGR02339 242 EVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGAN---------VVICQKGIDDVAQHYLAKAGILAVRRVK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 318 RRNMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRA 397
Cdd:TIGR02339 313 KSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 398 INNTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPI 477
Cdd:TIGR02339 393 VANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 822092673 478 GLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:TIGR02339 473 GINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
7-521 |
3.29e-93 |
|
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: 292.66 E-value: 3.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 7 LNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTA-SMIgHASTAQD 85
Cdd:cd03337 5 LNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAkSMI-ELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 86 DATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV-NKKSLTDVARTSLKTKVHAAL 164
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVnDRAQMLKIIKSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 165 ADLLTDVCVDAVLAIRHDE----KPVDL-HMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEY 239
Cdd:cd03337 164 SDLMCNLALDAVKTVAVEEngrkKEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 240 eksevnsgffyktaeerekfvqaerdfidqrvkkiielkrkvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRR 319
Cdd:cd03337 244 --------------------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 320 NMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVL-GENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAI 398
Cdd:cd03337 274 DNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 399 NNTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDP-I 477
Cdd:cd03337 354 RNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENStW 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 822092673 478 GLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEI 521
Cdd:cd03337 434 GIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
18-524 |
1.09e-92 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 291.60 E-value: 1.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 18 NALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHP----TASMIGHASTAQDDATGDGTT 93
Cdd:COG0459 10 DARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 94 STVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTSLKTKvhaalaDLLTDVCV 173
Cdd:COG0459 90 TATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD-DKEELAQVATISANGD------EEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 174 DAVLAIrhDEKPVdlhmIEImEMQHKTATDTTLIKGLVMDHGARHPD-------MPKRLENAYILTCNVSLEyeksevns 246
Cdd:COG0459 163 EAMEKV--GKDGV----ITV-EEGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 247 gffyktaeerekfvqAERDFIDQrVKKIIELKRKvcdgteksfVVINQKGIDPMSLDALAKEGILALRRA---------K 317
Cdd:COG0459 228 ---------------SIQDLLPL-LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 318 RRN--MERLALACGGTAMN-----SVDDLEESHLGYAGLVYEhvlGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDA 390
Cdd:COG0459 283 RRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 391 IRDGLRAINNTINDKCViPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEED 470
Cdd:COG0459 360 VEDALHATRAAVEEGIV-PGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAK 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 822092673 471 RLNpdpIGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:COG0459 439 DKG---FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
19-521 |
1.30e-91 |
|
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: 289.97 E-value: 1.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 19 ALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLL 98
Cdd:cd03339 24 AHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 99 IGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV---NKKSLTDVARTSLKTKVHAALADLLTDVCVDA 175
Cdd:cd03339 104 AGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFspdNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 176 VLAIRHDE-KPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYI--LTCnvSLEYEKSEVNSGFFYKT 252
Cdd:cd03339 184 VLSVADLErKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIaiLTC--PFEPPKPKTKHKLDITS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 253 AEEREKFVQAERDFIDQRVKKIIElkrkvcdgtEKSFVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTA 332
Cdd:cd03339 262 VEDYKKLQEYEQKYFREMVEQVKD---------AGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 333 MNSVDDLEESHLGYAGLVYEHVLG--ENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPG 410
Cdd:cd03339 333 VPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 411 AGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDP-IGLD-LSTGE-PM 487
Cdd:cd03339 413 GGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPhLGIDcLGRGTnDM 492
|
490 500 510
....*....|....*....|....*....|....
gi 822092673 488 KpvDLGVYDNHIVKKQILNSCSVIASNLLLVDEI 521
Cdd:cd03339 493 K--EQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
4-521 |
5.31e-91 |
|
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: 288.17 E-value: 5.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 4 ISLLNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTA-SMIgHAST 82
Cdd:TIGR02344 2 VLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAkSMI-ELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 83 AQDDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNKKS-LTDVARTSLKTKVH 161
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAaMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 162 AALADLLTDVCVDAVLAIRHDE---KPVDL-HMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSL 237
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDEngrKEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 238 EYEKSEVNSGFFYKTAEEREKFVQAERDFIDQRVKKIIELKrkvCDgteksfVVINQKGIDPMSLDALAKEGILALRRAK 317
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVK---PD------LVITEKGVSDLAQHYLLKANITAIRRVR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 318 RRNMERLALACGGTAMNSVDDLEESHLGY-AGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLR 396
Cdd:TIGR02344 312 KTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 397 AINNTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKL----TEEDRL 472
Cdd:TIGR02344 392 VARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELrakhAQENNC 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 822092673 473 NpdpIGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEI 521
Cdd:TIGR02344 472 T---WGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
23-523 |
7.94e-88 |
|
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: 279.94 E-value: 7.94e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVL-DTMKVPVE-VNKKSLTDVARTSLKTKVHAALADLLTDVCVDAVLAIR 180
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIkEHLSISVDnLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 181 H-DEK-----PVDlhMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAE 254
Cdd:cd03335 173 TtNEKgktkyPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 255 EREKFVQAERDFIDQRVKKIIElkrkvcDGTEksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMN 334
Cdd:cd03335 251 KLEKIRQRESDITKERIKKILA------AGAN---VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 335 SVDDLE------ESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVI 408
Cdd:cd03335 322 TLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 409 PGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKL--------TEEDRLNPDPIGLD 480
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLrayhaaaqVKPDKKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 822092673 481 LSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMR 523
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
23-523 |
3.91e-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: 278.53 E-value: 3.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:TIGR02340 17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVL-DTMKVPVE-VNKKSLTDVARTSLKTKVHAALADLLTDVCVDAVLAIR 180
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIkENLSVSVDeLGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 181 H-DEKPVDLHMIE---IMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAEER 256
Cdd:TIGR02340 177 TtNENGETKYPIKainILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPEKL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 257 EKFVQAERDFIDQRVKKIIElkrkvcdgtEKSFVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMNSV 336
Cdd:TIGR02340 257 EQIRQREADITKERIKKILD---------AGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 337 DDLE------ESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPG 410
Cdd:TIGR02340 328 ADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 411 AGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKL--------TEEDRLNPDPIGLDLS 482
Cdd:TIGR02340 408 GGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLrayhaaaqLKPEKKHLKWYGLDLV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 822092673 483 TGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMR 523
Cdd:TIGR02340 488 NGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
15-525 |
2.98e-85 |
|
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: 273.60 E-value: 2.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 15 RAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTS 94
Cdd:TIGR02343 24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 95 TVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV---NKKSLTDVARTSLKTKVHAALADLLTDV 171
Cdd:TIGR02343 104 VVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAdnnNREPLIQAAKTSLGSKIVSKCHRRFAEI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 172 CVDAVLAIRH-DEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKRLENAY--ILTCnvSLEYEKSEVNSGF 248
Cdd:TIGR02343 184 AVDAVLNVADmERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKiaILTC--PFEPPKPKTKHKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 249 FYKTAEEREKFVQAERDFIDQRVKKIielKRKVCDgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALAC 328
Cdd:TIGR02343 262 DISSVEEYKKLQKYEQQKFKEMIDDI---KKSGAN------LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 329 GGTAMNSVDDLEESHLGYAGLVYEHVLG--ENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKC 406
Cdd:TIGR02343 333 GGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 407 VIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTI--VKLTEEDRLNPDpIGLD-LST 483
Cdd:TIGR02343 413 IVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLstLKSLQLKEKNPN-LGVDcLGY 491
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 822092673 484 GE-PMKpvDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRAG 525
Cdd:TIGR02343 492 GTnDMK--EQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
3.14e-83 |
|
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: 267.80 E-value: 3.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:TIGR02342 14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEV-NKKSLTDVARTSLKTKVHAALADLLTDVCVDAVLAIRH 181
Cdd:TIGR02342 94 LGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLsDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVID 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 182 DE--KPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPD-MPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAEEREK 258
Cdd:TIGR02342 174 PEnaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 259 FVQAERDFIDQRVKKIielKRKVCDgteksfVVINQKGI-----DPMSLDALAKEGILALRRAKRRNMERLALACGGTAM 333
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---KKTGCN------VLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 334 NSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNP-QSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAG 412
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 413 AFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEPMKPVDL 492
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
|
490 500 510
....*....|....*....|....*....|
gi 822092673 493 GVYDNHIVKKQILNSCSVIASNLLLVDEIM 522
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-469 |
4.67e-83 |
|
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: 267.23 E-value: 4.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVN-KKSLTDVARTSLKTKVHAALADLLTDVCVDAVLAIRH 181
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 182 DEKP--VDLHMIEIMEMQHKTATDTTLIKGLVMDHGARH-PDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAEEREK 258
Cdd:cd03338 173 PATAtnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 259 FVQAERDFIDQRVKKIielKRKVCDgteksfVVINQKGI-----DPMSLDALAKEGILALRRAKRRNMERLALACGGTAM 333
Cdd:cd03338 253 ILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 334 NSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNP-QSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAG 412
Cdd:cd03338 324 ASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 822092673 413 AFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEE 469
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNR 460
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-524 |
2.14e-80 |
|
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: 260.46 E-value: 2.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNKKSLTDV----ARTSLKTKVHAALADLLTDVCVDAVLA 178
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELlekcAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 179 IRHDEkpVDLHMIEIMEMQHKTATDTTLIKGLVMDHG---ARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAEE 255
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 256 REKFVQAERDFIDQRVKKIIELKRKvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMNS 335
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGAN---------VVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 336 VDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAGAFE 415
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 416 VRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEPMKPVDLGVY 495
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
|
490 500
....*....|....*....|....*....
gi 822092673 496 DNHIVKKQILNSCSVIASNLLLVDEIMRA 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 |
1.23e-79 |
|
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: 258.37 E-value: 1.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNKKS-----LTDVARTSLKTKVHAALADLLTDVCVDAVL 177
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEeqrelLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 178 AIRHDekpVDLHMIEIMEMQHKTATDTTLIKGLVMDHG---ARHPDMPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAE 254
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 255 EREKFVQAERDFIDQRVKKIIELKRKvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMN 334
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGAN---------VVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 335 SVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIK----DAIRDGLRAINNtindKCVIPG 410
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAErslhDAIMIVRRAIKN----DSVVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 411 AGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDP-IGLDLSTGEPMKP 489
Cdd:cd03340 405 GGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADN 484
|
490 500 510
....*....|....*....|....*....|....*
gi 822092673 490 VDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:cd03340 485 FEAFVWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
7-524 |
5.18e-76 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 249.18 E-value: 5.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 7 LNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVS-----GAGDIKITKDGNILLHEMQIQHPTASMIGHAS 81
Cdd:PTZ00212 11 LKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 82 TAQDDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNKKS----LTDVARTSLK 157
Cdd:PTZ00212 91 KTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfkedLLNIARTTLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 158 TKVHAALADLLTDVCVDAVLAIRHDekpVDLHMIEIMEMQHKTATDTTLIKGLVMDH--GArhpDMPKRLENAYILTCNV 235
Cdd:PTZ00212 171 SKLLTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGV---GQPKRLENCKILVANT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 236 SLEYEK-----SEVNSGFFYKTAEerekFVQAERDFIDQRVKKIIELKrkvCDgteksfVVINQKGIDPMSLDALAKEGI 310
Cdd:PTZ00212 245 PMDTDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKILAHG---CN------VFINRQLIYNYPEQLFAEAGI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 311 LALRRAKRRNMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDA 390
Cdd:PTZ00212 312 MAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 391 IRDGLRAINNTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEED 470
Cdd:PTZ00212 392 LHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEH 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 822092673 471 RLNPDPIGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:PTZ00212 472 YKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
7-524 |
9.33e-75 |
|
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: 245.70 E-value: 9.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 7 LNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSG--AGDIKITKDGNILLHEMQIQHPTASMIGHASTAQ 84
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 85 DDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVN----KKSLTDVARTSLKTKV 160
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDeeafREDLLNIARTTLSSKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 161 HAALADLLTDVCVDAVLAIRHDekpVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARhPDMPKRLENAYILTCNVSLEYE 240
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGS---GNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIG-VNQPKRIENAKILIANTPMDTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 241 K-----SEVNSGFFYKTAEEREkfvqAERDFIDQRVKKIIELKrkvCDgteksfVVINQKGIDPMSLDALAKEGILALRR 315
Cdd:cd03336 238 KikifgAKVRVDSTAKVAEIEE----AEKEKMKNKVEKILKHG---IN------CFINRQLIYNYPEQLFADAGIMAIEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 316 AKRRNMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGL 395
Cdd:cd03336 305 ADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 396 RAINNTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPD 475
Cdd:cd03336 385 CVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNT 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 822092673 476 PIGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:cd03336 465 TAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
145-404 |
2.44e-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: 229.27 E-value: 2.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 145 KKSLTDVARTSLKTKVhAALADLLTDVCVDAVLAIRHDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMDHGARHPDMPKR 224
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 225 LENAYILTCNVSLEYeksevnsgffyktaeerekfvqaerdfidqrvkkiielkrkvcdgteksfVVINQKGIDPMSLDA 304
Cdd:cd03333 80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 305 LAKEGILALRRAKRRNMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTI 384
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 822092673 385 VQIKDAIRDGLRAINNTIND 404
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-524 |
7.36e-64 |
|
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: 217.28 E-value: 7.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 23 NISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGEL 102
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 103 LKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTM---KVPVEVNKKSLTDVARTSLKTKVHAAlADLLTDVCVDAVLAI 179
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELvvwEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 180 R-HDEKPVDLHMIEIMEMQHKTATDTTLIKGLVMdhgARHPD-MPKRLENAYILTCNVSLEYEKSEVNSGFFYKTAEERE 257
Cdd:TIGR02346 182 LpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEgSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 258 KFVQAERDFIDQRVKKIIELKRKvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMNSVD 337
Cdd:TIGR02346 259 NYSKGEENQIEAMIKAIADSGVN---------VIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 338 DLEESHLGYAGLVYEHVLGENKFT-FVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCVIPGAGAFEV 416
Cdd:TIGR02346 330 APTPEEIGYVDSVYVSEIGGDKVTvFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 417 RAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEP--MKPVDLGV 494
Cdd:TIGR02346 410 ELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDgvKDASEAGI 489
|
490 500 510
....*....|....*....|....*....|
gi 822092673 495 YDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
18-524 |
4.96e-60 |
|
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: 205.53 E-value: 4.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 18 NALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPTASMIGHASTAQDDATGDGTTSTVL 97
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 98 LIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTM---KVPVEVNKKSLTDVARTSLKTKVHAAlADLLTDVCVD 174
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELvvyKIEDLRNKEEVSKALKTAIASKQYGN-EDFLSPLVAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 175 AVLAIRHDEKP---VDlhMIEIMEMQHKTATDTTLIKGLVMdhgARHPD-MPKRLENAYI--LTCNvsleyeksevnsgf 248
Cdd:cd03341 167 ACISVLPENIGnfnVD--NIRVVKILGGSLEDSKVVRGMVF---KREPEgSVKRVKKAKVavFSCP-------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 249 fyktaeerekfvqaerdfIDQRVKkiielkrkvcdgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALAC 328
Cdd:cd03341 228 ------------------FDIGVN-----------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 329 GGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSV-TILVKGPNKHTIVQIKDAIRDGLRAINNTINDKCV 407
Cdd:cd03341 273 GATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 408 IPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDPIGLDLSTGEP- 486
Cdd:cd03341 353 VPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEg 432
|
490 500 510
....*....|....*....|....*....|....*....
gi 822092673 487 -MKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:cd03341 433 tKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
6-524 |
8.80e-58 |
|
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: 200.47 E-value: 8.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 6 LLNPKAEYARAANALAFNISAAKGLQDVMRTNLGPKGTMKMLVSGA--GDIKITKDGNILLHEMQIQHPTASMIGHASTA 83
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 84 QDDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNK----KSLTDVARTSLKTK 159
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEvkfrQDLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 160 VHAALADLLTDVCVDAVLAIRHDekpVDLHMIEIMEMQHKTATDTTLIKGLVMDhgaRHPDM--PKRLENAYILTCNVSL 237
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRLKGS---GNLEAIQIIKKLGGSLADSYLDEGFLLD---KKIGVnqPKRIENAKILIANTGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 238 EYEKSEV-NSGFFYKTAEEREKFVQAERDFIDQRVKKIielKRKVCDgteksfVVINQKGIDPMSLDALAKEGILALRRA 316
Cdd:TIGR02341 236 DTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKI---LKHGIN------CFINRQLIYNYPEQLFADAGVMAIEHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 317 KRRNMERLALACGGTAMNSVDDLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSVTILVKGPNKHTIVQIKDAIRDGLR 396
Cdd:TIGR02341 307 DFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 397 AINNTINDKCVIPGAGAFEVRAFNKLMKYKDTVKGKVRLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEDRLNPDP 476
Cdd:TIGR02341 387 VLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTT 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 822092673 477 IGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLLLVDEIMRA 524
Cdd:TIGR02341 467 MGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
203-388 |
2.50e-13 |
|
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: 69.94 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 203 DTTLIKGLVMDHGARHPDMPKRLENAYILTCNVSLEYEKseVNSGFFYktaeeREKFVQAERDFIDQRVKKIIELKRKvc 282
Cdd:cd03334 62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLS-----LDPVILQEKEYLKNLVSRIVALRPD-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 283 dgteksfVVINQKGIDPMSLDALAKEGILALRRAKRRNMERLALACGGTAMNSVDDL-EESHLGYAGL------VYEHVL 355
Cdd:cd03334 133 -------VILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLlTSPKLGTCESfrvrtyVEEHGR 205
|
170 180 190
....*....|....*....|....*....|...
gi 822092673 356 GENkFTFVEECKNPQSVTILVKGPNKHTIVQIK 388
Cdd:cd03334 206 SKT-LMFFEGCPKELGCTILLRGGDLEELKKVK 237
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-524 |
8.17e-13 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 70.83 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 30 LQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQI----QHPTASMIGHASTAQDDATGDGTTSTVLLIGELLKQ 105
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 106 ADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNKKsLTDVARTSLK--TKVHAALADLLTDVCVDAVLAIrhde 183
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE-IAQVGTISANgdAEIGKFLADAMKKVGNEGVITV---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 184 kpvdlhmieimEMQHKTATDTTLIKGLVMDHGARHP-------DMPKRLENAYILTCnvslEYEKSEVNsgffyktaeER 256
Cdd:PRK14104 178 -----------EEAKSLETELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYILIN----EKKLSSLN---------EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 257 EKFVQAerdfIDQRVKKIIELKRKVcDGTEKSFVVINQ-KGidPMSLDALAKEGILALRRAKrrnMERLALACGGTAMnS 335
Cdd:PRK14104 234 LPLLEA----VVQTGKPLVIVAEDV-EGEALATLVVNRlRG--GLKVAAVKAPGFGDRRKAM---LQDIAILTGGQAI-S 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 336 VD---DLEESHLGYAGLVYEHVLGENKFTFVE--------ECKNPQ---------------------------SVTILVK 377
Cdd:PRK14104 303 EDlgiKLENVTLQMLGRAKKVMIDKENTTIVNgagkkadiEARVAQikaqieettsdydreklqerlaklaggVAVIRVG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 378 GPNKHTIVQIKDAIRDGLRAINNTInDKCVIPGAGAFEVRAFNKLMKYKdTVKGKVRLGIQAFAEALLVIPKNLAINSGY 457
Cdd:PRK14104 383 GATEVEVKERKDRVDDAMHATRAAV-EEGIVPGGGVALLRASEQLKGIK-TKNDDQKTGVEIVRKALSAPARQIAINAGE 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822092673 458 DAQDTIVKLTEEDRLNpdpIGLDLSTGEPMKPVDLGVYD-NHIVKKQILNSCSVIAsnLLLVDEIMRA 524
Cdd:PRK14104 461 DGSVIVGKILEKEQYS---YGFDSQTGEYGNLVSKGIIDpTKVVRTAIQNAASVAA--LLITTEAMVA 523
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
30-522 |
8.66e-13 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 70.71 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 30 LQDVMRTNLGPKGTMKMLVSGAGDIKITKDG-----NILLHEmQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGELLK 104
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvakAIEFSD-RFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 105 QADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTSLKTKVH--AALADLLTDVCVDAVLAIrhD 182
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVK-TKEDILNVATISANGDVEigSLIADAMDKVGKDGTITV--E 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 183 EKPVDLHMIEIMEmqhktatdttlikGLVMDHGARHP-------DMPKRLENAYILTCNVSLEYEKSEVNS-GFFYKT-- 252
Cdd:PTZ00114 190 DGKTLEDELEVVE-------------GMSFDRGYISPyfvtnekTQKVELENPLILVTDKKISSIQSILPIlEHAVKNkr 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 253 -----AEEREKfvQAERDFIDQRVKKIIelkrKVCdgteksfvvinqkgidpmsldALAKEGILALRRAkrrNMERLALA 327
Cdd:PTZ00114 257 plliiAEDVEG--EALQTLIINKLRGGL----KVC---------------------AVKAPGFGDNRKD---ILQDIAVL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 328 CGGTAMNSV------DDLEESHLGYAGLVY----EHVL---GENKFTFVEECKNPQS----------------------- 371
Cdd:PTZ00114 307 TGATVVSEDnvglklDDFDPSMLGSAKKVTvtkdETVIltgGGDKAEIKERVELLRSqierttseydkeklkerlaklsg 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 372 --VTILVKGPNKHTIVQIKDAIRDGLRAINNTInDKCVIPGAGAFEVRAfNKLMKYKDTVKGKV---RLGIQAFAEALLV 446
Cdd:PTZ00114 387 gvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLRA-SKLLDKLEEDNELTpdqRTGVKIVRNALRL 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092673 447 IPKNLAINSGYDAQDTIVKLTEEdrlNPDPIGLDLSTGEPMKPVDLGVYD-NHIVKKQILNSCSViASnLLLVDEIM 522
Cdd:PTZ00114 465 PTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDpTKVVRSALVDAASV-AS-LMLTTEAA 536
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
16-522 |
1.63e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 66.69 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 16 AANALAFNISAAKG-------LQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHP----TASMIGHASTAQ 84
Cdd:PRK12851 2 AAKEVKFHVEAREKmlrgvniLADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 85 DDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTSLK--TKVHA 162
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVT-TNAEIAQVATISANgdAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 163 ALADLLTDVCVDAVLAIrhdekpvdlhmieimEMQHKTATDTTLIKGLVMDHGARHP-------DMPKRLENAYILTCNV 235
Cdd:PRK12851 161 LVAEAMEKVGNEGVITV---------------EESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 236 SLEYEKSEVnsgffyktaEEREKFVQAERDFIdqrvkkIIElkrKVCDGTEKSFVVINQ-KGIdpMSLDALAKEGILALR 314
Cdd:PRK12851 226 KISNLQDLL---------PVLEAVVQSGKPLL------IIA---EDVEGEALATLVVNKlRGG--LKVAAVKAPGFGDRR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 315 RAKrrnMERLALACGGTAMnSVD---DLEESHLGYAGLVYEHVLGENKFTFVEECKNPQSV------------------- 372
Cdd:PRK12851 286 KAM---LEDIAILTGGTVI-SEDlgiKLENVTLEQLGRAKKVVVEKENTTIIDGAGSKTEIegrvaqiraqieettsdyd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 373 ----------------TILVKGPNKHTIVQIKDAIRDGLRAINNTINDKcVIPGAGAFEVRAFNKLMKyKDTVKGKVRLG 436
Cdd:PRK12851 362 reklqerlaklaggvaVIRVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 437 IQAFAEALLVIPKNLAINSGYDAQDTIVKLTEEdrlnPDPIGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIASNLL 516
Cdd:PRK12851 440 VEIVRRALEAPVRQIAENAGAEGSVVVGKLREK----PGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLL 515
|
....*.
gi 822092673 517 LVDEIM 522
Cdd:PRK12851 516 TTEAMV 521
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
16-524 |
1.44e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 60.50 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 16 AANALAFNISAAKG-------LQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHP----TASMIGHASTAQ 84
Cdd:PRK12850 2 AAKEIRFSTDARDRllrgvniLANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 85 DDATGDGTTSTVLLIGELLKQADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTSLK--TKVHA 162
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT-SSKEIAQVATISANgdESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 163 ALADLLTDVCVDAVLAIRhdekpvdlhmieimemQHKTA-TDTTLIKGLVMDHGARHPDM---PKR----LENAYILTCN 234
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVE----------------EAKTLgTELDVVEGMQFDRGYLSPYFvtnPEKmraeLEDPYILLHE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 235 VSLEYEKSEVNSgffyktaeeREKFVQAERdfidqrvkKIIELKRKVCDGTEKSFVVINQKGIdpMSLDALAKEGILALR 314
Cdd:PRK12850 225 KKISNLQDLLPI---------LEAVVQSGR--------PLLIIAEDVEGEALATLVVNKLRGG--LKSVAVKAPGFGDRR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 315 RAKrrnMERLALACGGTaMNSVD---DLEE---SHLGYAGLVyehVLGENKFTFVEECKNPQSV---------------- 372
Cdd:PRK12850 286 KAM---LEDIAVLTGGQ-VISEDlgiKLENvtlDMLGRAKRV---LITKENTTIIDGAGDKKNIearvkqiraqieetts 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 373 -------------------TILVKGPNKHTIVQIKDAIRDGLRAINNTInDKCVIPGAGAFEVRAFNKLMKyKDTVKGKV 433
Cdd:PRK12850 359 dydreklqerlaklaggvaVIRVGGATEVEVKEKKDRVDDALHATRAAV-EEGIVPGGGVALLRARSALRG-LKGANADE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 434 RLGIQAFAEALLVIPKNLAINSGYDAQDTIVKLTEedrlNPDPIGLDLSTGEPMKPVDLGVYDNHIVKKQILNSCSVIAS 513
Cdd:PRK12850 437 TAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAE----LPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAA 512
|
570
....*....|.
gi 822092673 514 nLLLVDEIMRA 524
Cdd:PRK12850 513 -LLITTEAMVA 522
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-155 |
6.16e-09 |
|
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: 58.24 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 30 LQDVMRTNLGPKGTMKMLVSGAGDIKITKDG-----NILLhEMQIQHPTASMIGHASTAQDDATGDGTTSTVLLIGELLK 104
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGvtvakEIEL-EDPFENMGAQLVKEVASKTNDVAGDGTTTATVLARAIIK 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 822092673 105 QADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTS 155
Cdd:cd03344 99 EGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVK-TKEEIAQVATIS 148
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
38-231 |
1.23e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 51.26 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 38 LGPKGTMKMLVSGAGDIKITKDGNILLHEMQ----IQHPTASMIGHASTAQDDATGDGTTSTVLLIGELLKQADIFLAEG 113
Cdd:CHL00093 30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 114 LHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTSL--KTKVHAALADLLTDVCVDAVLAIRHDEKPV-DLHM 190
Cdd:CHL00093 110 ANPISLKRGIEKATQYVVSQIAEYARPVE-DIQAITQVASISAgnDEEVGSMIADAIEKVGREGVISLEEGKSTVtELEI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 822092673 191 IEIMEMQhktatdttliKGLVMDHGARHPD-MPKRLENAYIL 231
Cdd:CHL00093 189 TEGMRFE----------KGFISPYFVTDTErMEVVQENPYIL 220
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
16-234 |
3.19e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 49.81 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 16 AANALAFNISA----AKG---LQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHP----TASMIGHASTAQ 84
Cdd:PRK12849 1 MAKIIKFDEEArralERGvnkLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 85 DDATGDG-TTSTVL---LIGELLKQadifLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVARTS--LKT 158
Cdd:PRK12849 81 NDVAGDGtTTATVLaqaLVQEGLKN----VAAGANPMDLKRGIDKAVEAVVEELKALARPVS-GSEEIAQVATISanGDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822092673 159 KVHAALADLLTDVCVDAVLAIRhDEKPVDLHMiEIME-MQHKtatdttliKGLVMDHGARHPD-MPKRLENAYILTCN 234
Cdd:PRK12849 156 EIGELIAEAMEKVGKDGVITVE-ESKTLETEL-EVTEgMQFD--------RGYLSPYFVTDPErMEAVLEDPLILLTD 223
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
30-231 |
3.47e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 49.84 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 30 LQDVMRTNLGPKGTMKMLVSGAGDIKITKDGNILLHEMQI----QHPTASMIGHASTAQDDATGDGTTSTVLLIGELLKQ 105
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 106 ADIFLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEVNKKsLTDVARTSLK--TKVHAALADLLTDVCVDAVLAIRhde 183
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAE-IAQVGTISANgdAAIGKMIAQAMQKVGNEGVITVE--- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822092673 184 kpvdlhmieimemQHKTA-TDTTLIKGLVMDHGARHP-------DMPKRLENAYIL 231
Cdd:PRK12852 179 -------------ENKSLeTEVDIVEGMKFDRGYLSPyfvtnaeKMTVELDDAYIL 221
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
16-152 |
4.17e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 46.27 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092673 16 AANALAFNISAAKGLQDVMRT-------NLGPKGTMKMLVSGAGDIKITKDGNILLHEMQIQHPT----ASMIGHASTAQ 84
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKladavkvTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822092673 85 DDATGDG-TTSTVL---LIGELLKQadifLAEGLHPRIVTEGFEKAREQALAVLDTMKVPVEvNKKSLTDVA 152
Cdd:PRK00013 81 NDVAGDGtTTATVLaqaIVREGLKN----VAAGANPMDLKRGIDKAVEAAVEELKKISKPVE-DKEEIAQVA 147
|
|
| |
