|
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: 962.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347 1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 83 AQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 160
Cdd:TIGR02347 81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 161 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 241 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 320 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 400 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 4502643 480 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 530
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
7-526 |
0e+00 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 935.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDD 86
Cdd:cd03342 1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 87 ITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM--DRETLIDVARTSLRTKVHAEL 164
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 165 ADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEV 244
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 245 NSGFFYKsaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERL 324
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 325 TLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDD 404
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 405 GCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTG 484
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 4502643 485 EPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGM 526
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
30-525 |
0e+00 |
|
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 589.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLY 109
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 110 ISEGLHPRIITEGFEAAKEKALQFLEEVKV--SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPID 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 188 LFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFI 267
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 268 EDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHA 347
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 348 GLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKP 427
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 428 SVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHS 507
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 4502643 508 CTVIATNILLVDEIMRAG 525
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
11-523 |
0e+00 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 565.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 11 AEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGD 90
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 91 GTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLT 169
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPiDVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 170 EAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYektevnsgff 249
Cdd:cd00309 161 ELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 250 yksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACG 329
Cdd:cd00309 231 ----------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 330 GVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVP 409
Cdd:cd00309 271 ATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 410 GAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVA 489
Cdd:cd00309 351 GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDM 430
|
490 500 510
....*....|....*....|....*....|....
gi 4502643 490 AEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd00309 431 KEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
19-525 |
1.44e-142 |
|
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: 420.90 E-value: 1.44e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:cd03343 16 AQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 176
Cdd:cd03343 96 AGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 177 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:cd03343 175 LQVAEKRDGkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 254 EEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03343 255 DQLQAFLEQEEAMLKEMVDKIADTGANV---------VFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 413
Cdd:cd03343 326 TNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 414 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 493
Cdd:cd03343 406 VEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKG 485
|
490 500 510
....*....|....*....|....*....|..
gi 4502643 494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:cd03343 486 VIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
19-525 |
6.19e-142 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 419.29 E-value: 6.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041082 18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:NF041082 98 AGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 178 AI--KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:NF041082 178 AVaeKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 256 REKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 335
Cdd:NF041082 258 LQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 336 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:NF041082 329 IDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 416 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 495
Cdd:NF041082 409 VELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVV 488
|
490 500 510
....*....|....*....|....*....|
gi 4502643 496 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041082 489 EPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
19-525 |
2.19e-141 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 417.81 E-value: 2.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041083 18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV--KVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 176
Cdd:NF041083 98 AGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIaeKVDPD-DRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 177 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:NF041083 177 KQVAEKRDGkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 254 EEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:NF041083 257 DQLQKFLDQEEKMLKEMVDKIKATGAN---------VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 413
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 414 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 493
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
|
490 500 510
....*....|....*....|....*....|..
gi 4502643 494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
19-524 |
2.98e-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: 407.15 E-value: 2.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:TIGR02339 17 AQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSREmDRETLIDVARTSLRTKVHAELA-DVLTEAVVDS 175
Cdd:TIGR02339 97 AGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEiaTKISPE-DRDLLKKIAYTSLTSKASAEVAkDKLADLVVEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 176 ILAIKKQDE----PIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK 251
Cdd:TIGR02339 176 VKQVAELRGdgkyYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRIT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 252 SAEEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGV 331
Cdd:TIGR02339 256 DPDQIKKFLDQEEAMLKEMVDKIASAGAN---------VVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 332 ALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGA 411
Cdd:TIGR02339 327 IVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 412 GAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAE 491
Cdd:TIGR02339 407 GAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLE 486
|
490 500 510
....*....|....*....|....*....|...
gi 4502643 492 VGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02339 487 LGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
14-521 |
3.50e-96 |
|
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: 301.91 E-value: 3.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 14 ARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTT 93
Cdd:cd03339 19 LKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 94 SNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS---REMDRETLIDVARTSLRTKVHAELADVLTE 170
Cdd:cd03339 99 GVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKiefSPDNKEPLIQTAMTSLGSKIVSRCHRQFAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 171 AVVDSILA---IKKQDepIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYI--LTCnvSLEYEKTEVN 245
Cdd:cd03339 179 IAVDAVLSvadLERKD--VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIaiLTC--PFEPPKPKTK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 246 SGFFYKSAEEREKLVKAERKFIEDRVKKIielkrKVCGDSdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLT 325
Cdd:cd03339 255 HKLDITSVEDYKKLQEYEQKYFREMVEQV-----KDAGAN----LVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 326 LACGGVALNSFDDLSPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAID 403
Cdd:cd03339 326 IATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 404 DGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEH-SESGQLVGVDLN 482
Cdd:cd03339 406 DNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCL 485
|
490 500 510
....*....|....*....|....*....|....*....
gi 4502643 483 TGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03339 486 GRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
23-523 |
1.57e-92 |
|
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: 292.27 E-value: 1.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEE---VKVSrEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI 179
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhlsISVD-NLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 180 KKQDE------PIDlfMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:cd03335 172 KTTNEkgktkyPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 254 EEREKLVKAERKFIEDRVKKIIElkrkvCGDSdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03335 250 EKLEKIRQRESDITKERIKKILA-----AGAN----VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 334 NSFDDL------SPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCV 407
Cdd:cd03335 321 STLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 408 VPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgQL---------VG 478
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAA-QVkpdkkhlkwYG 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 4502643 479 VDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd03335 480 LDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
4-521 |
5.67e-92 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 289.20 E-value: 5.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 4 VKTLNPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATA 83
Cdd:cd03337 4 VLNQNTKRESGR-KAQLG-NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 84 QDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHA 162
Cdd:cd03337 82 QDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 163 ELADVLTEAVVDSILAIKKQDE----PIDL-FMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSL 237
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAVEENgrkkEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 238 EYektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAK 317
Cdd:cd03337 242 EY--------------------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 318 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTL-GEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLR 396
Cdd:cd03337 272 KTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 397 AVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQL 476
Cdd:cd03337 352 VARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENS 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 4502643 477 V-GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03337 432 TwGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-521 |
1.42e-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: 289.72 E-value: 1.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 8 NPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDI 87
Cdd:TIGR02344 8 NTKRESGR-KAQLS-NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELAD 166
Cdd:TIGR02344 86 VGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVnDDAAMLKLIQSCIGTKFVSRWSD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 167 VLTEAVVDSILAIKKQDEPIdlFMIEIMEMKhKSE-------TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEY 239
Cdd:TIGR02344 166 LMCDLALDAVRTVQRDENGR--KEIDIKRYA-KVEkipggdiEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 240 EKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRR 319
Cdd:TIGR02344 243 KKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPD---------LVITEKGVSDLAQHYLLKANITAIRRVRKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 320 NMERLTLACGGVALNSFDDLSPDCLG-HAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAV 398
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 399 KNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHS-ESGQLV 477
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 4502643 478 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
23-523 |
1.53e-91 |
|
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: 290.08 E-value: 1.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02340 17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIK 180
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnlSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 181 KQDE------PIDlfMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:TIGR02340 177 TTNEngetkyPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 255 EREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALN 334
Cdd:TIGR02340 255 KLEQIRQREADITKERIKKILDAGAN---------VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 335 SFDDLS------PDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVV 408
Cdd:TIGR02340 326 TLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 409 PGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgQL---------VGV 479
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAA-QLkpekkhlkwYGL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 4502643 480 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
15-525 |
2.90e-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: 289.39 E-value: 2.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 15 RAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTS 94
Cdd:TIGR02343 24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV--KVSREMD-RETLIDVARTSLRTKVHAELADVLTEA 171
Cdd:TIGR02343 104 VVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 172 VVDSILAI-KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAY--ILTCnvSLEYEKTEVNSGF 248
Cdd:TIGR02343 184 AVDAVLNVaDMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKiaILTC--PFEPPKPKTKHKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 249 FYKSAEEREKLVKAERKFIEDRVKKIielkRKVCGDsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLAC 328
Cdd:TIGR02343 262 DISSVEEYKKLQKYEQQKFKEMIDDI----KKSGAN-----LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 329 GGVALNSFDDLSPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGC 406
Cdd:TIGR02343 333 GGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 407 VVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEH-SESGQLVGVDLNTGE 485
Cdd:TIGR02343 413 IVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYG 492
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 4502643 486 PMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:TIGR02343 493 TNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-524 |
5.90e-88 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 280.49 E-value: 5.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKVHAELADVLTEAVVDSILA 178
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEkgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 179 IKKQDepIDLFMIEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 256 REKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 335
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANV---------VLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 336 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 416 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 495
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
|
490 500
....*....|....*....|....*....
gi 4502643 496 DNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
19-524 |
1.94e-84 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 270.41 E-value: 1.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAK----VATAQDDITGDGTTS 94
Cdd:COG0459 11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSremDRETLIDVARTSLRTKvhAELADVLTEAV 172
Cdd:COG0459 91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD--EEIGELIAEAM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 173 vdsiLAIKKQDEpidlFMIEimemKHKS-ETDTSLIRGLVLDHGARHPD-------MKKRVEDAYILTCNVSLEyektev 244
Cdd:COG0459 166 ----EKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 245 nsgffykSAEEREKLvkaerkfiedrVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRA-------- 316
Cdd:COG0459 228 -------SIQDLLPL-----------LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 317 -KRRN--MERLTLACGGVALN-----SFDDLSPDCLGHAGLVYEytlGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIK 388
Cdd:COG0459 281 gDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 389 DAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQA 468
Cdd:COG0459 358 RRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 4502643 469 EHSESgqlVGVDLNTGEP--MVAAevGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:COG0459 437 AKDKG---FGFDAATGEYvdMLEA--GVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-524 |
2.37e-84 |
|
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: 270.70 E-value: 2.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKV-----SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVnidkeDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 178 AIkkqDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:cd03340 181 SL---DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 255 EREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALN 334
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANV---------VLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 335 SFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAV 414
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 415 EVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQL-VGVDLNTGEPMVAAEVG 493
Cdd:cd03340 409 EMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAF 488
|
490 500 510
....*....|....*....|....*....|.
gi 4502643 494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03340 489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-486 |
1.26e-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: 268.77 E-value: 1.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 179
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLnDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVid 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 180 KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARH-PDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 258
Cdd:cd03338 173 PATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 259 LVKAERKFIEDRVKKIielKRKVCGdsdkgfVVINQKGI-----DPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03338 253 ILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNP-RSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 412
Cdd:cd03338 324 ASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4502643 413 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEP 486
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
6.09e-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: 259.33 E-value: 6.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02342 14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 179
Cdd:TIGR02342 94 LGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLsDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVid 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 180 KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPD-MKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 258
Cdd:TIGR02342 174 PENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 259 LVKAERKFIEDRVKKIielKRKVCGdsdkgfVVINQKGI-----DPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---KKTGCN------VLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPR-SVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 412
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 413 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEV 492
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
|
490 500 510
....*....|....*....|....*....|
gi 4502643 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 ... |
10-524 |
1.42e-78 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 255.72 E-value: 1.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 10 KAEVARAQA---ALAVNisaarglqDVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:cd03336 10 KGETARLSSfvgAIAIG--------DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE----VKVSREMDRETLIDVARTSLRTKV 160
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 161 HAELADVLTEAVVDSILAIKKQDepiDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGSG---NLDAIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 239 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAK 317
Cdd:cd03336 236 TDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINC---------FINRQLIYNYPEQLFADAGIMAIEHAD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 318 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRA 397
Cdd:cd03336 307 FDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 398 VKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLV 477
Cdd:cd03336 387 LAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 4502643 478 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03336 467 GLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
10-524 |
6.91e-78 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 254.18 E-value: 6.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 10 KAEVARAQaalavNISAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:PTZ00212 19 KGETARLQ-----SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 160
Cdd:PTZ00212 94 DEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDeekfKEDLLNIARTTLSSKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 161 HAELADVLTEAVVDSILAIKKQdepIDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 239 YEK-----TEVNSGFFYKSAEerekLVKAERKFIEDRVKKIIELKrkvCGdsdkgfVVINQKGIDPFSLDALSKEGIVAL 313
Cdd:PTZ00212 248 TDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKILAHG---CN------VFINRQLIYNYPEQLFAEAGIMAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 314 RRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRD 393
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 394 GLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSES 473
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 4502643 474 GQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:PTZ00212 475 NKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
16-524 |
6.87e-77 |
|
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: 251.56 E-value: 6.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 16 AQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSN 95
Cdd:TIGR02346 16 LEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 96 VLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD---RETLIDVARTSLRTKVHAElADVLTEAV 172
Cdd:TIGR02346 96 LVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDlrdKDELIKALKASISSKQYGN-EDFLAQLV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 173 VDSILAIK-KQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYILTCNVSLEYEKTEVNSGFFY 250
Cdd:TIGR02346 175 AQACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 251 KSAEEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGG 330
Cdd:TIGR02346 252 HNAEELLNYSKGEENQIEAMIKAIADSGVN---------VIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 331 VALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVP 409
Cdd:TIGR02346 323 TPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 410 GAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMV- 488
Cdd:TIGR02346 403 GAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVk 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 4502643 489 -AAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02346 483 dASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
145-404 |
4.20e-72 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 228.50 E-value: 4.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 145 RETLIDVARTSLRTKVhAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKR 224
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 225 VEDAYILTCNVSLEYektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDA 304
Cdd:cd03333 80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 305 LSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTL 384
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 4502643 385 TQIKDAVRDGLRAVKNAIDD 404
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-524 |
3.47e-67 |
|
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: 224.41 E-value: 3.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV---KVSREMDRETLIDVARTSLRTKVhAELADVLTEAVVDSILAI 179
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELvvyKIEDLRNKEEVSKALKTAIASKQ-YGNEDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 180 KKQDepIDLFMIE---IMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYI--LTCNVSleyekTEVNsgffyksa 253
Cdd:cd03341 172 LPEN--IGNFNVDnirVVKILGGSLEDSKVVRGMVF---KREPEGSvKRVKKAKVavFSCPFD-----IGVN-------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 254 eereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03341 234 ------------------------------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 412
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 413 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMV--AA 490
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAK 437
|
490 500 510
....*....|....*....|....*....|....
gi 4502643 491 EVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
7-524 |
3.70e-64 |
|
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: 217.80 E-value: 3.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:TIGR02341 3 FKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 160
Cdd:TIGR02341 83 DDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDevkfRQDLMNIARTTLSSKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 161 HAELADVLTEAVVDSILAIKKQDepiDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:TIGR02341 163 LSQHKDHFAQLAVDAVLRLKGSG---NLEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 239 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAK 317
Cdd:TIGR02341 237 TDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINC---------FINRQLIYNYPEQLFADAGVMAIEHAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 318 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRA 397
Cdd:TIGR02341 308 FEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 398 VKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLV 477
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 4502643 478 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
203-391 |
1.95e-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: 70.33 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 203 DTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKteVNSGFFYksaeeREKLVKAERKFIEDRVKKIIELKRKVc 282
Cdd:cd03334 62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLS-----LDPVILQEKEYLKNLVSRIVALRPDV- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 283 gdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLS-PDCLGHAGLVYEYTLGEEK-- 359
Cdd:cd03334 134 --------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLtSPKLGTCESFRVRTYVEEHgr 205
|
170 180 190
....*....|....*....|....*....|....*
gi 4502643 360 ---FTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAV 391
Cdd:cd03334 206 sktLMFFEGCPKELGCTILLRGGDLEELKKVKRVV 240
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
30-510 |
2.73e-11 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 66.09 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDG-----NVLLHEmQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLK 104
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvakAIEFSD-RFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 105 QADLYISEGLHPRIITEGFEAAKEKALQFLEEvkVSREM-DRETLIDVARTSLRTKVhaELADVLTEAV----VDSILAI 179
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLKE--QSRPVkTKEDILNVATISANGDV--EIGSLIADAMdkvgKDGTITV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 180 kkQDEPIDLFMIEIMEmkhksetdtslirGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVNS-GFFYK 251
Cdd:PTZ00114 189 --EDGKTLEDELEVVE-------------GMSFDRGYISPyfvtnekTQKVELENPLILVTDKKISSIQSILPIlEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 252 S-------AEEREKLVKAerKFIEDRVKKIIelkrKVC-------GDSDK----------GFVVINQKG----IDPFSLD 303
Cdd:PTZ00114 254 NkrplliiAEDVEGEALQ--TLIINKLRGGL----KVCavkapgfGDNRKdilqdiavltGATVVSEDNvglkLDDFDPS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 304 ALS------------------------KEGIVALRRAKRRNM---------ERLTLACGGVALnsfddlspdclghaglv 350
Cdd:PTZ00114 328 MLGsakkvtvtkdetviltgggdkaeiKERVELLRSQIERTTseydkeklkERLAKLSGGVAV----------------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 351 yeytlgeekftfiekcnnprsvtLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEAL--IKHKPS 428
Cdd:PTZ00114 391 -----------------------IKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLdkLEEDNE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 429 VKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgqlVGVDLNTGEPMVAAEVGVWDNY-CVKKQLLHS 507
Cdd:PTZ00114 447 LTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPS---FGYDAQTGEYVNMFEAGIIDPTkVVRSALVDA 523
|
...
gi 4502643 508 CTV 510
Cdd:PTZ00114 524 ASV 526
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
12-496 |
2.71e-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: 59.39 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDI 87
Cdd:cd03344 7 EEARKALLRGVNK-----LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEevKVSREM-DRETLIDVARTSlrTKVHAELAD 166
Cdd:cd03344 82 AGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELK--KLSKPVkTKEEIAQVATIS--ANGDEEIGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 167 VLTEavvdsilAIKK--QDEPIDLfmieimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSL 237
Cdd:cd03344 158 LIAE-------AMEKvgKDGVITV------EEGKTLETELEVVEGMQFDRGYLSPyfvtdpeKMEVELENPYILLTDKKI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 238 EYEKTEVNSgffyksaeeREKLVKAERKFI---EDrvkkiielkrkVCGDSDKGFVVINQKGIDPfsldalskegIVALR 314
Cdd:cd03344 225 SSIQELLPI---------LELVAKAGRPLLiiaED-----------VEGEALATLVVNKLRGGLK----------VCAVK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 315 ----RAKRRNM-ERLTLACGGVALN-----SFDDLSPDCLGHAGLVyeyTLGEEKFTFIEKCNNPRSV------------ 372
Cdd:cd03344 275 apgfGDRRKAMlEDIAILTGGTVISeelglKLEDVTLEDLGRAKKV---VVTKDDTTIIGGAGDKAAIkariaqirkqie 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 373 -----------------------TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSv 429
Cdd:cd03344 352 ettsdydkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKAL- 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4502643 430 KGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQaehsESGQLVGVDLNTGE--PMVAAevGVWD 496
Cdd:cd03344 430 NGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEyvDMIEA--GIID 492
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
30-522 |
8.84e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 57.83 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHP----TASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PRK12851 23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 106 ADLYISEGLHPRIITEGFEAAKEKALQFLEevKVSREMDRETliDVART-SLRTKVHAELADVLTEAVVdsilaiKKQDE 184
Cdd:PRK12851 103 GAKAVAAGANPMDLKRGIDRAVAAVVEELK--ANARPVTTNA--EIAQVaTISANGDAEIGRLVAEAME------KVGNE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 185 PIdlfmIEIMEMKhKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVnsgffyksaEERE 257
Cdd:PRK12851 173 GV----ITVEESK-TAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEKKISNLQDLL---------PVLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 258 KLVKAERKFI---EDrvkkiielkrkVCGDSDKGFVVINQKGIdpFSLDALSKEGIVALRRAKRRNMERLTlacGGVALN 334
Cdd:PRK12851 239 AVVQSGKPLLiiaED-----------VEGEALATLVVNKLRGG--LKVAAVKAPGFGDRRKAMLEDIAILT---GGTVIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 335 -----SFDDLSPDCLGHAGLVyeyTLGEEKFTF--------------------IEKCNNP--------RSVTL-----LI 376
Cdd:PRK12851 303 edlgiKLENVTLEQLGRAKKV---VVEKENTTIidgagskteiegrvaqiraqIEETTSDydreklqeRLAKLaggvaVI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 377 K--GPNKHTLTQIKDAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKpSVKGRAQLGVQAFADALLIIPKVLAQN 454
Cdd:PRK12851 380 RvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLE-TANGDQRTGVEIVRRALEAPVRQIAEN 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4502643 455 SGFDLQETLVKIqAEHSESgqlVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:PRK12851 458 AGAEGSVVVGKL-REKPGG---YGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-524 |
2.69e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 56.58 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQI----QHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 106 ADLYISEGLHPRIITEGFEAAKEKALQFLeeVKVSREM-DRETLIDVARTSLR--TKVHAELADVLTEAVVDSILAIkkq 182
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADL--VKNSKKVtSNDEIAQVGTISANgdAEIGKFLADAMKKVGNEGVITV--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 183 depidlfmieimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYIL-------TCNVSLEYEKTEVNSGF 248
Cdd:PRK14104 178 ------------EEAKSLETELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYILinekklsSLNELLPLLEAVVQTGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 249 -FYKSAEEREKlvKAERKFIEDRVK---KIIELKRKVCGDSDKGFV--VINQKGIDPFSLD---ALSKEGIVALRRAKRR 319
Cdd:PRK14104 246 pLVIVAEDVEG--EALATLVVNRLRgglKVAAVKAPGFGDRRKAMLqdIAILTGGQAISEDlgiKLENVTLQMLGRAKKV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 320 --NMERLTLACGGvalNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIK--GPNKHTLTQIKDAVRDGL 395
Cdd:PRK14104 324 miDKENTTIVNGA---GKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 396 RAVKNAIDDGcVVPGAGAVEVAMAEALiKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgq 475
Cdd:PRK14104 401 HATRAAVEEG-IVPGGGVALLRASEQL-KGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYS-- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 4502643 476 lVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATnILLVDEIMRA 524
Cdd:PRK14104 477 -YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAA-LLITTEAMVA 523
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
14-231 |
6.39e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 52.15 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 14 ARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQI----QHPTASLIAKVATAQDDITG 89
Cdd:PRK12852 12 ARDRMLRGVDI-----LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 90 DGTTSNVLIIGELLKQADLYISEGLHPriitegfeaakekalqfleevkvsreMDRETLIDVARTSLRTKVHAELADVLT 169
Cdd:PRK12852 87 DGTTTATVLAQAIVREGAKAVAAGMNP--------------------------MDLKRGIDIAVAAVVKDIEKRAKPVAS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 170 EAVVDSILAIKKQ-DEPIDLFMIEIM-----------EMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYI 230
Cdd:PRK12852 141 SAEIAQVGTISANgDAAIGKMIAQAMqkvgnegvitvEENKSLETEVDIVEGMKFDRGYLSPyfvtnaeKMTVELDDAYI 220
|
.
gi 4502643 231 L 231
Cdd:PRK12852 221 L 221
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
12-231 |
2.37e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 50.10 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHP----TASLIAKVATAQDDI 87
Cdd:PRK12850 10 TDARDRLLRGVNI-----LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQfleevkvsremdretliDVARTSLRTKVHAELADV 167
Cdd:PRK12850 85 AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVD-----------------ELKKIAKKVTSSKEIAQV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 168 LTEAVVDsilaikkqDEPIDLFMIEIMEMKHKS-----------ETDTSLIRGLVLDHGARHPDM-----KKRV--EDAY 229
Cdd:PRK12850 148 ATISANG--------DESIGEMIAEAMDKVGKEgvitveeaktlGTELDVVEGMQFDRGYLSPYFvtnpeKMRAelEDPY 219
|
..
gi 4502643 230 IL 231
Cdd:PRK12850 220 IL 221
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
38-134 |
6.67e-04 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 42.40 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 38 LGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQ----IQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEG 113
Cdd:CHL00093 30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
|
90 100
....*....|....*....|.
gi 4502643 114 LHPRIITEGFeaakEKALQFL 134
Cdd:CHL00093 110 ANPISLKRGI----EKATQYV 126
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
12-136 |
4.45e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 39.72 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643 12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDI 87
Cdd:PRK00013 9 EDARRKLLRGVNK-----LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 4502643 88 TGDG-TTSNVL---IIGELLKqadlYISEGLHPRIITEGFEAAKEKALQFLEE 136
Cdd:PRK00013 84 AGDGtTTATVLaqaIVREGLK----NVAAGANPMDLKRGIDKAVEAAVEELKK 132
|
|
| |
