|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
5-517 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 732.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 5 QSNYTISENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIA 84
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 85 KTQESEVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQ--DRNVLKNIAITAMTGKG 162
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDpdDKETLKKIAATAMTGKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 163 AEGNKEHLAELIVNAVDQVS---NGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIE 239
Cdd:NF041082 161 AEAAKDKLADLVVDAVKAVAekdGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 240 LRNPDAEAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARA 319
Cdd:NF041082 241 VKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 320 TSGKVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTI 399
Cdd:NF041082 321 TGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 400 VAGGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIE 479
Cdd:NF041082 401 VAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVV 480
|
490 500 510
....*....|....*....|....*....|....*...
gi 1276430170 480 DTLQAGIIEPIKVKIQAITSASEVATMILRIDDVLISK 517
Cdd:NF041082 481 DMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
8-517 |
0e+00 |
|
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: 709.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 8 YTISENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQ 87
Cdd:cd03343 2 LILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 88 ESEVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKI--QDRNVLKNIAITAMTGKGAEG 165
Cdd:cd03343 82 DEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVdpDDKDTLRKIAKTSLTGKGAEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 166 NKEHLAELIVNAVDQVS----NGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELR 241
Cdd:cd03343 162 AKDKLADLVVDAVLQVAekrdGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 242 NPDAEAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATS 321
Cdd:cd03343 242 KTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 322 GKVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVA 401
Cdd:cd03343 322 AKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 402 GGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDT 481
Cdd:cd03343 402 GGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDM 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 1276430170 482 LQAGIIEPIKVKIQAITSASEVATMILRIDDVLISK 517
Cdd:cd03343 482 LEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
12-517 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 708.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEV 91
Cdd:NF041083 8 EGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKN--QSVKIQDRNVLKNIAITAMTGKGAEGNKEH 169
Cdd:NF041083 88 GDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEiaEKVDPDDRETLKKIAETSLTSKGVEEARDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 170 LAELIVNAVDQVSNGQE----VNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDA 245
Cdd:NF041083 168 LAEIAVKAVKQVAEKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 246 EAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVI 325
Cdd:NF041083 248 DAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 326 STLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGA 405
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 406 IEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAG 485
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
|
490 500 510
....*....|....*....|....*....|..
gi 1276430170 486 IIEPIKVKIQAITSASEVATMILRIDDVLISK 517
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-514 |
0e+00 |
|
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: 666.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 8 YTISENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQ 87
Cdd:TIGR02339 3 FILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 88 ESEVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKN--QSVKIQDRNVLKNIAITAMTGKG-AE 164
Cdd:TIGR02339 83 DEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEiaTKISPEDRDLLKKIAYTSLTSKAsAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 165 GNKEHLAELIVNAVDQVS-----NGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIE 239
Cdd:TIGR02339 163 VAKDKLADLVVEAVKQVAelrgdGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 240 LRNPDAEAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARA 319
Cdd:TIGR02339 243 VEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 320 TSGKVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTI 399
Cdd:TIGR02339 323 TGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 400 VAGGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIE 479
Cdd:TIGR02339 403 VAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIE 482
|
490 500 510
....*....|....*....|....*....|....*
gi 1276430170 480 DTLQAGIIEPIKVKIQAITSASEVATMILRIDDVL 514
Cdd:TIGR02339 483 DMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
33-517 |
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: 586.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 33 IANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAVLLAGKLLENAERL 112
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 113 LDKKIHPTVIIKGYRLAAQKALEILKN---QSVKIQDRNVLKNIAITAMTGKGAEGNKEHLAELIVNAVDQV-SNGQEVN 188
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSiisIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIpKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 189 SEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDAEAKISVSTPEQLENFIESEEIYL 268
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 269 KNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLSLETLGSAERVEEVKHG 348
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 349 DESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELSKELNLFSRTLGGREQLA 428
Cdd:pfam00118 321 DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 429 VQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:pfam00118 401 IEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTIL 480
|
....*....
gi 1276430170 509 RIDDVLISK 517
Cdd:pfam00118 481 RIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
16-513 |
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: 569.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 16 RSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGT 95
Cdd:cd00309 3 REFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 96 TTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQ--DRNVLKNIAITAMTGKGAEGNKEHLAEL 173
Cdd:cd00309 83 TTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDveDREELLKVATTSLNSKLVSGGDDFLGEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 174 IVNAVDQVSNGQE-VNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELrnpdaeakisvs 252
Cdd:cd00309 163 VVDAVLKVGKENGdVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 253 tpeqlenfieseeiylknmtdkiialgakAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLS 332
Cdd:cd00309 231 -----------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 333 LETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELSK 412
Cdd:cd00309 282 PEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 413 ELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAGIIEPIKV 492
Cdd:cd00309 362 ALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKV 441
|
490 500
....*....|....*....|.
gi 1276430170 493 KIQAITSASEVATMILRIDDV 513
Cdd:cd00309 442 KRQALKSATEAASLILTIDDI 462
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
18-517 |
1.11e-174 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 501.92 E-value: 1.11e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEVGD 93
Cdd:COG0459 7 FGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 94 GTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIAITAMTGkgaegnKEHLAEL 173
Cdd:COG0459 87 GTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANG------DEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 174 IVNAVDQVsnGQEVNsedITLEKLKGeSISDSELVSGIVLQKERANAD-------MPLRVDNPKILLVDFPIELRNPdae 246
Cdd:COG0459 161 IAEAMEKV--GKDGV---ITVEEGKG-LETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISSIQD--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 247 akisvstpeqlenfieseeiyLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIP-----------KSEMEK 315
Cdd:COG0459 232 ---------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgdrrKAMLED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 316 LARATSGKVIS-----TLRDLSLETLGSAERVEEvkhGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDV 390
Cdd:COG0459 291 IAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHAT 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 391 ISAIKSGtIVAGGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDiglKFHG 470
Cdd:COG0459 368 RAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKD---KGFG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1276430170 471 LNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVLISK 517
Cdd:COG0459 444 FDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADK 490
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
16-515 |
1.42e-152 |
|
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: 446.73 E-value: 1.42e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 16 RSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGT 95
Cdd:cd03335 3 RTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 96 TTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALE-ILKNQSVKIQD--RNVLKNIAITAMTGKGAEGNKEHLAE 172
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKyIKEHLSISVDNlgKESLINVAKTSMSSKIIGADSDFFAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 173 LIVNAVDQV----SNGQEVNS-EDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDAEA 247
Cdd:cd03335 163 MVVDAILAVkttnEKGKTKYPiKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 248 KISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVIST 327
Cdd:cd03335 243 QVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVST 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 328 LRDLSLE------TLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVA 401
Cdd:cd03335 323 LANLEGEetfdpsYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 402 GGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHD--------IGLKFHGLNL 473
Cdd:cd03335 403 GGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKHLKWYGLDL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1276430170 474 FSDKIEDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVLI 515
Cdd:cd03335 483 INGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
26-516 |
1.57e-147 |
|
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: 433.25 E-value: 1.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 26 NILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAVLLAGKL 105
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 106 LENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKI--QDRNVLKNIAITAMTGKGAEGNKEHLAELIVNAVDQVSN 183
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 184 GQE---VNSEDITLEKLKGESISDSELVSGIVLQKERAN-ADMPLRVDNPKILLVDFPIELRNPDAEAKISVSTPEQLEN 259
Cdd:cd03338 173 PATatnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 260 FIESEEIYLKNMTDKIIALGAKAIFCQKGI-----DDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLSLE 334
Cdd:cd03338 253 ILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 335 TLGSAERVEEVKHGDESFVYIRGCSNP-RAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELSKE 413
Cdd:cd03338 333 KLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 414 LNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAGIIEPIKVK 493
Cdd:cd03338 413 LSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQPLLVS 492
|
490 500
....*....|....*....|...
gi 1276430170 494 IQAITSASEVATMILRIDDVLIS 516
Cdd:cd03338 493 TSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
16-515 |
1.80e-147 |
|
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: 434.15 E-value: 1.80e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 16 RSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGT 95
Cdd:TIGR02340 7 RTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 96 TTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALE-ILKNQSVKIQD--RNVLKNIAITAMTGKGAEGNKEHLAE 172
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKyIKENLSVSVDElgREALINVAKTSMSSKIIGLDSDFFSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 173 LIVNAVDQV----SNGQEVNS-EDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDAEA 247
Cdd:TIGR02340 167 IVVDAVLAVkttnENGETKYPiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 248 KISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVIST 327
Cdd:TIGR02340 247 QIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVST 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 328 LRDLSLE------TLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVA 401
Cdd:TIGR02340 327 LADLEGEetfeasYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 402 GGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDI--------GLKFHGLNL 473
Cdd:TIGR02340 407 GGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekkHLKWYGLDL 486
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1276430170 474 FSDKIEDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVLI 515
Cdd:TIGR02340 487 VNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
12-519 |
5.52e-144 |
|
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: 424.39 E-value: 5.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEV 91
Cdd:cd03340 7 EGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKI------QDRNVLKNIAITAMTGKGAEG 165
Cdd:cd03340 87 GDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIdkedkeEQRELLEKCAATALNSKLIAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 166 NKEHLAELIVNAVDQVsnGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANA---DMPLRVDNPKILLVDFPIELRN 242
Cdd:cd03340 167 EKEFFAKMVVDAVLSL--DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAgfeQQPKKFKNPKILLLNVELELKA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 243 PDAEAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSG 322
Cdd:cd03340 245 EKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 323 KVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAG 402
Cdd:cd03340 325 SIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 403 GGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIG-LKFHGLNLFSDKIEDT 481
Cdd:cd03340 405 GGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDINNEGIADN 484
|
490 500 510
....*....|....*....|....*....|....*...
gi 1276430170 482 LQAGIIEPIKVKIQAITSASEVATMILRIDDVLISKGS 519
Cdd:cd03340 485 FEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
12-513 |
6.44e-138 |
|
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: 409.00 E-value: 6.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEV 91
Cdd:cd03339 14 EKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKI----QDRNVLKNIAITAMTGKGAEGNK 167
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIefspDNKEPLIQTAMTSLGSKIVSRCH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 168 EHLAELIVNAVDQVSNGQ--EVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDA 245
Cdd:cd03339 174 RQFAEIAVDAVLSVADLErkDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 246 EAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVI 325
Cdd:cd03339 254 KHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 326 STLRDLSLETLGSAERVEEVKHGDES--FVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGG 403
Cdd:cd03339 334 PRFEDLSPEKLGKAGLVREISFGTTKdkMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 404 GAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFH-GLNLFSDKIEDTL 482
Cdd:cd03339 414 GAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHlGIDCLGRGTNDMK 493
|
490 500 510
....*....|....*....|....*....|.
gi 1276430170 483 QAGIIEPIKVKIQAITSASEVATMILRIDDV 513
Cdd:cd03339 494 EQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
12-519 |
2.12e-130 |
|
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: 389.89 E-value: 2.12e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEV 91
Cdd:TIGR02345 9 EGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQD-----RNVLKNIAITAMTGKGAEGN 166
Cdd:TIGR02345 89 GDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEekgeqRELLEKCAATALSSKLISHN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 167 KEHLAELIVNAVDQVsNGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANA---DMPLRVDNPKILLVDFPIELRNP 243
Cdd:TIGR02345 169 KEFFSKMIVDAVLSL-DRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAgfeQQPKKFANPKILLLNVELELKAE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 244 DAEAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGK 323
Cdd:TIGR02345 248 KDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 324 VISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGG 403
Cdd:TIGR02345 328 IQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 404 GAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQ 483
Cdd:TIGR02345 408 GAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFE 487
|
490 500 510
....*....|....*....|....*....|....*.
gi 1276430170 484 AGIIEPIKVKIQAITSASEVATMILRIDDVLISKGS 519
Cdd:TIGR02345 488 AFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
20-517 |
8.28e-130 |
|
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: 387.99 E-value: 8.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 20 KDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAV 99
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 100 LLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQS--VKIQDRNVLKNIAITAMTGKGAEGNKEHLAELIVNA 177
Cdd:TIGR02342 88 ILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSipVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 178 VDQVSNGQE---VNSEDITLEKLKGESISDSELVSGIVL-QKERANADMPLRVDNPKILLVDFPIELRNPDAEAKISVST 253
Cdd:TIGR02342 168 VLKVIDPENaknVDLNDIKVVKKLGGTIDDTELIEGLVFtQKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVND 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 254 PEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGI-----DDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTL 328
Cdd:TIGR02342 248 YAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 329 RDLSLETLGSAERVEEVKHGDESFVYIRGCSNPR-AVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIE 407
Cdd:TIGR02342 328 DHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 408 IELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAGII 487
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVL 487
|
490 500 510
....*....|....*....|....*....|
gi 1276430170 488 EPIKVKIQAITSASEVATMILRIDDVLISK 517
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
11-514 |
1.50e-126 |
|
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: 378.56 E-value: 1.50e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 11 SENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESE 90
Cdd:cd03337 6 NQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 91 VGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQS--VKIQDRNVLKNIAITAMTGKGAEGNKE 168
Cdd:cd03337 86 VGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISipVDVNDRAQMLKIIKSCIGTKFVSRWSD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 169 HLAELIVNAVDQVSNGQEVNSEDITL------EKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIElrn 242
Cdd:cd03337 166 LMCNLALDAVKTVAVEENGRKKEIDIkryakvEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 243 pdaeakisvstpeqlenfieseeiYLknmtdkiialgakaIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSG 322
Cdd:cd03337 243 ------------------------YL--------------VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 323 KVISTLRDLSLETLGSAERVEEVKH-GDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVA 401
Cdd:cd03337 285 TIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 402 GGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFH-GLNLFSDKIED 480
Cdd:cd03337 365 GGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTwGIDGETGDIVD 444
|
490 500 510
....*....|....*....|....*....|....
gi 1276430170 481 TLQAGIIEPIKVKIQAITSASEVATMILRIDDVL 514
Cdd:cd03337 445 MKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
10-513 |
3.09e-125 |
|
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: 376.77 E-value: 3.09e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 10 ISENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQES 89
Cdd:TIGR02344 5 LNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 90 EVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQS--VKIQDRNVLKNIAITAMTGKGAEGNK 167
Cdd:TIGR02344 85 EVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISipVDVNDDAAMLKLIQSCIGTKFVSRWS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 168 EHLAELIVNAVDQVSNGQEVNSE-DIT----LEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRN 242
Cdd:TIGR02344 165 DLMCDLALDAVRTVQRDENGRKEiDIKryakVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 243 PDAEAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSG 322
Cdd:TIGR02344 245 GESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 323 KVISTLRDLSLETLGSAERVEEVKH-GDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVA 401
Cdd:TIGR02344 325 TIVNRPEELRESDVGTGCGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 402 GGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFH-GLNLFSDKIED 480
Cdd:TIGR02344 405 GGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTwGIDGETGKIVD 484
|
490 500 510
....*....|....*....|....*....|...
gi 1276430170 481 TLQAGIIEPIKVKIQAITSASEVATMILRIDDV 513
Cdd:TIGR02344 485 MKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
12-516 |
1.47e-124 |
|
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: 375.29 E-value: 1.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEV 91
Cdd:TIGR02343 18 DNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKN----IAITAMTGKGAEGNK 167
Cdd:TIGR02343 98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREpliqAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 168 EHLAELIVNAVDQVSNGQ--EVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDA 245
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMErrDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 246 EAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVI 325
Cdd:TIGR02343 258 KHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 326 STLRDLSLETLGSAERVEEVKHG--DESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGG 403
Cdd:TIGR02343 338 PRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 404 GAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFH-GLNLFSDKIEDTL 482
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVDCLGYGTNDMK 497
|
490 500 510
....*....|....*....|....*....|....
gi 1276430170 483 QAGIIEPIKVKIQAITSASEVATMILRIDDVLIS 516
Cdd:TIGR02343 498 EQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
12-514 |
3.80e-120 |
|
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: 363.19 E-value: 3.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKML--VDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQES 89
Cdd:cd03336 4 DGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 90 EVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQD-----RNVLKNIAITAMTGKGAE 164
Cdd:cd03336 84 EVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSdeeafREDLLNIARTTLSSKILT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 165 GNKEHLAELIVNAVDQVsnGQEVNSEDITLEKLKGESISDSELVSGIVLQKeRANADMPLRVDNPKILLVDFPIelrnpD 244
Cdd:cd03336 164 QDKEHFAELAVDAVLRL--KGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTPM-----D 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 245 AE------AKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLAR 318
Cdd:cd03336 236 TDkikifgAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 319 ATSGKVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGT 398
Cdd:cd03336 316 VTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 399 IVAGGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKI 478
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 1276430170 479 EDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVL 514
Cdd:cd03336 476 GDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
12-514 |
5.08e-119 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 360.88 E-value: 5.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDS-----TGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKT 86
Cdd:PTZ00212 13 QGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLDNPAAKILVDISKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 87 QESEVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLA---AQKALEILK--NQSVKIQDRNVLKNIAITAMTGK 161
Cdd:PTZ00212 93 QDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMAldvARKALEEIAfdHGSDEEKFKEDLLNIARTTLSSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 162 GAEGNKEHLAELIVNAVDQVSNgqEVNSEDITLEKLKGESISDSELVSGIVLQKeRANADMPLRVDNPKILLVDFPIelr 241
Cdd:PTZ00212 173 LLTVEKDHFAKLAVDAVLRLKG--SGNLDYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKRLENCKILVANTPM--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 242 npDAE------AKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEK 315
Cdd:PTZ00212 247 --DTDkikiygAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 316 LARATSGKVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIK 395
Cdd:PTZ00212 325 LAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 396 SGTIVAGGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFS 475
Cdd:PTZ00212 405 DTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEK 484
|
490 500 510
....*....|....*....|....*....|....*....
gi 1276430170 476 DKIEDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVL 514
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
26-514 |
4.36e-106 |
|
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: 326.14 E-value: 4.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 26 NILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAVLLAGKL 105
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 106 LENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQ---DRNVLKNIAITAMTGKGAEGNKEHLAELIVNAVDQV- 181
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEidtDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIy 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 182 SNGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDaeakisvstpeqlenfI 261
Cdd:cd03342 177 KPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTE----------------V 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 262 ESEEIYlknmtdkiialgaKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLSLETLGSAER 341
Cdd:cd03342 241 NSGFFY-------------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 342 VEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELSKELNLFSRTL 421
Cdd:cd03342 308 VYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 422 GGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSAS 501
Cdd:cd03342 388 KGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSAT 467
|
490
....*....|...
gi 1276430170 502 EVATMILRIDDVL 514
Cdd:cd03342 468 VIASQLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
26-514 |
2.47e-105 |
|
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: 325.54 E-value: 2.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 26 NILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAVLLAGKL 105
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 106 LENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQ---DRNVLKNIAITAMTGKGAEGNKEHLAELIVNAVDQV- 181
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdevDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIk 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 182 SNGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELRNPDAEAKISVSTPEQLENFI 261
Cdd:TIGR02347 181 KDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 262 ESEEIYLKNMTDKIIALGAK----------AIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDL 331
Cdd:TIGR02347 261 KAERKFVDDRVKKIIELKKKvcgkspdkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 332 SLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELS 411
Cdd:TIGR02347 341 TPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 412 KELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQAGIIEPIK 491
Cdd:TIGR02347 421 RHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYR 500
|
490 500
....*....|....*....|...
gi 1276430170 492 VKIQAITSASEVATMILRIDDVL 514
Cdd:TIGR02347 501 VKKQLIQSATVIASQLLLVDEVM 523
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
25-517 |
2.54e-104 |
|
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: 321.09 E-value: 2.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 25 NNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAVLLAGK 104
Cdd:cd03341 12 RNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 105 LLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSV-KIQDRNVLKNIAI---TAMTGKGAeGNKEHLAELIVNAVDQ 180
Cdd:cd03341 92 LLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVyKIEDLRNKEEVSKalkTAIASKQY-GNEDFLSPLVAEACIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 181 V--SNGQEVNSEDITLEKLKGESISDSELVSGIVLQKErANADMpLRVDNPKILLVDFPIElrnpdaeakisvstpeqle 258
Cdd:cd03341 171 VlpENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFD------------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 259 nfieseeiylknmtdkiiaLGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLSLETLGS 338
Cdd:cd03341 230 -------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 339 AERVEEVKHGDESFVYIRGCSNPRAVS-LILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELSKELNLF 417
Cdd:cd03341 291 CDSVYVEEIGDTKVVVFRQNKEDSKIAtIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 418 SRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFS--DKIEDTLQAGIIEPIKVKIQ 495
Cdd:cd03341 371 GEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESgdEGTKDAKEAGIFDHLATKKW 450
|
490 500
....*....|....*....|..
gi 1276430170 496 AITSASEVATMILRIDDVLISK 517
Cdd:cd03341 451 AIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
21-517 |
2.61e-102 |
|
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: 317.81 E-value: 2.61e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 21 DAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQESEVGDGTTTAVL 100
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 101 LAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSV-KIQDRNVLKNI--AITAMTGKGAEGNKEHLAELIVNA 177
Cdd:TIGR02346 98 LAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVwEVKDLRDKDELikALKASISSKQYGNEDFLAQLVAQA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 178 VDQV--SNGQEVNSEDITLEKLKGESISDSELVSGIVLQKErANADMPlRVDNPKILLVDFPIELRNPDAEAKISVSTPE 255
Cdd:TIGR02346 178 CSTVlpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVK-SVKNAKVAVFSCPLDTATTETKGTVLIHNAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 256 QLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLSLET 335
Cdd:TIGR02346 256 ELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 336 LGSAERVEEVKHGDESFVYIRGCSNPRAVS-LILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGGGAIEIELSKEL 414
Cdd:TIGR02346 336 IGYVDSVYVSEIGGDKVTVFKQENGDSKIStIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 415 NLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNL--FSDKIEDTLQAGIIEPIKV 492
Cdd:TIGR02346 416 TKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIeaESDGVKDASEAGIYDMLAT 495
|
490 500
....*....|....*....|....*
gi 1276430170 493 KIQAITSASEVATMILRIDDVLISK 517
Cdd:TIGR02346 496 KKWAIKLATEAAVTVLRVDQIIMAK 520
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
12-514 |
9.81e-96 |
|
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: 300.24 E-value: 9.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 12 ENVSRSFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLV--DSTGNIIVTNDGVTILEEMEIDHPAAKMMVDIAKTQES 89
Cdd:TIGR02341 5 DGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 90 EVGDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSV-----KIQDRNVLKNIAITAMTGKGAE 164
Cdd:TIGR02341 85 EVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVdngsdEVKFRQDLMNIARTTLSSKILS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 165 GNKEHLAELIVNAVDQVSNgqEVNSEDITLEKLKGESISDSELVSGIVLQKERANaDMPLRVDNPKILLVDFPIELRNPD 244
Cdd:TIGR02341 165 QHKDHFAQLAVDAVLRLKG--SGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV-NQPKRIENAKILIANTGMDTDKVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 245 A-EAKISVSTPEQLENFIESEEIYLKNMTDKIIALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGK 323
Cdd:TIGR02341 242 IfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 324 VISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITDGLGDVISAIKSGTIVAGG 403
Cdd:TIGR02341 322 IVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 404 GAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGLKFHGLNLFSDKIEDTLQ 483
Cdd:TIGR02341 402 GCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQ 481
|
490 500 510
....*....|....*....|....*....|.
gi 1276430170 484 AGIIEPIKVKIQAITSASEVATMILRIDDVL 514
Cdd:TIGR02341 482 LGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
147-396 |
4.45e-61 |
|
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: 200.00 E-value: 4.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 147 RNVLKNIAITAMTGKGaEGNKEHLAELIVNAVDQVS-NGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMPLR 225
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGpDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 226 VDNPKILLVDFPIElrnpdaeakisvstpeqlenfieseeiYLknmtdkiialgakaIFCQKGIDDVAQYYLAKSGIFAC 305
Cdd:cd03333 80 LENAKILLLDCPLE---------------------------YV--------------VIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 306 RRIPKSEMEKLARATSGKVISTLRDLSLETLGSAERVEEVKHGDESFVYIRGCSNPRAVSLILRGGSSHVLDEIERAITD 385
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHD 198
|
250
....*....|.
gi 1276430170 386 GLGDVISAIKS 396
Cdd:cd03333 199 ALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
18-508 |
1.75e-40 |
|
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: 153.38 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAqRNNILA-AKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEVG 92
Cdd:cd03344 5 FGEEA-RKALLRgVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 93 DGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIA-ITAmtgkgaeGNKEHLA 171
Cdd:cd03344 84 DGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVAtISA-------NGDEEIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 172 ELIVNAVDQVSNGQEVNSEDitleklkGESISDS-ELVSGI-----------VLQKERANADMplrvDNPKILLVDFPIe 239
Cdd:cd03344 157 ELIAEAMEKVGKDGVITVEE-------GKTLETElEVVEGMqfdrgylspyfVTDPEKMEVEL----ENPYILLTDKKI- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 240 lrnpdaeakisvSTPEQ----LENFIESEEIYLknmtdkIIAlgakaifcqkgiDDVAQYYLA-------KSGIFAC--- 305
Cdd:cd03344 225 ------------SSIQEllpiLELVAKAGRPLL------IIA------------EDVEGEALAtlvvnklRGGLKVCavk 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 306 ------RRipKSEMEKLARATSGKVIS-----TLRDLSLETLGSAERVEEVKhgdESFVYIRGCSNPRA----------- 363
Cdd:cd03344 275 apgfgdRR--KAMLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVVVTK---DDTTIIGGAGDKAAikariaqirkq 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 364 -----------------------VSLILRGGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFSr 419
Cdd:cd03344 350 ieettsdydkeklqerlaklsggVAVIKVGGATEVeLKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLK- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 420 TLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDiglkFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITS 499
Cdd:cd03344 428 ALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPD----GFGYDAATGEYVDMIEAGIIDPTKVVRSALQN 503
|
....*....
gi 1276430170 500 ASEVATMIL 508
Cdd:cd03344 504 AASVASLLL 512
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
32-508 |
1.33e-34 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 136.86 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 32 IIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEVGDGTTTAVLLAGKLLE 107
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 108 NAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIAITamtgkgAEGNKEHLAELIVNAVDQVSNG--- 184
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATI------SANGDEEIGELIAEAMEKVGKDgvi 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 185 --QEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMplrvDNPKILLVDfpielrnpdaeAKIsvSTPEQ----LE 258
Cdd:PRK12849 175 tvEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVL----EDPLILLTD-----------KKI--SSLQDllplLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 259 NFIESEEIYLknmtdkIIAlgakaifcqkgiDDVAQYYLA----------------KSGIFACRRipKSEMEKLARATSG 322
Cdd:PRK12849 238 KVAQSGKPLL------IIA------------EDVEGEALAtlvvnklrgglkvaavKAPGFGDRR--KAMLEDIAILTGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 323 KVIS-----TLRDLSLETLGSAERVEEVKhgdESFVYIRGCSNPRA---------------------------------- 363
Cdd:PRK12849 298 TVISedlglKLEEVTLDDLGRAKRVTITK---DNTTIVDGAGDKEAiearvaqirrqieettsdydreklqerlaklagg 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 364 VSLILRGGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFsRTLGGREQLAVQEFSLALESIPET 442
Cdd:PRK12849 375 VAVIKVGAATEVeLKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDEL-AGLNGDQAAGVEIVRRALEAPLRQ 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276430170 443 LAENAGLDPlEVLTDLKKQHDIGlkfHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:PRK12849 453 IAENAGLDG-SVVVAKVLELEDG---FGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLL 514
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
17-508 |
7.78e-32 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 128.56 E-value: 7.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 17 SFGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEVG 92
Cdd:TIGR02348 5 KFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 93 DGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIA-ITAmtgkgaeGNKEHLA 171
Cdd:TIGR02348 85 DGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVAtISA-------NNDEEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 172 ELIVNAVDQVSNG-----QEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMplrvDNPKILLVDfpielrnpdae 246
Cdd:TIGR02348 158 SLIAEAMEKVGKDgvitvEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVEL----ENPYILITD----------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 247 AKISVSTP--EQLENFIESEEIYLknmtdkII-------ALGAKAIFCQKGIDDVAQyylAKSGIFACRRipKSEMEKLA 317
Cdd:TIGR02348 223 KKISNIKDllPLLEKVAQSGKPLL------IIaedvegeALATLVVNKLRGTLNVCA---VKAPGFGDRR--KAMLEDIA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 318 RATSGKVIS-----TLRDLSLETLGSAERVEEVKH--------GDESFVYIRgCSNPRA--------------------- 363
Cdd:TIGR02348 292 ILTGGQVISeelglKLEEVTLDDLGKAKKVTVDKDnttivegaGDKAAIKAR-VAQIKAqieettsdydreklqerlakl 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 364 ---VSLILRGGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFsRTLGGREQLAVQEFSLALESI 439
Cdd:TIGR02348 371 aggVAVIKVGAATETeMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAALEGL-KGDGEDEAIGIDIVKRALEAP 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276430170 440 PETLAENAGLDPLEVLTDLKKQHDiglkFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:TIGR02348 449 LRQIAENAGLDGAVVAEKVKELKG----NFGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLL 513
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
18-508 |
1.73e-31 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 127.91 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKM---MV-DIAKTQESEVGD 93
Cdd:PRK12850 8 FSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVkEVASKTNDLAGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 94 GTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIAITAMTGKGAEGnkehlaEL 173
Cdd:PRK12850 88 GTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIG------EM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 174 IVNAVDQVSNG-----QEVNSEDITLEKLKGESISDSELVSGIVLQKERANADMplrvDNPKILLVDFPIELRN---PDA 245
Cdd:PRK12850 162 IAEAMDKVGKEgvitvEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAEL----EDPYILLHEKKISNLQdllPIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 246 EAKISVSTPEqlenFIESEEIYLKNMT----DKIialgakaifcQKGIDDVAqyylAKSGIFACRRipKSEMEKLARATS 321
Cdd:PRK12850 238 EAVVQSGRPL----LIIAEDVEGEALAtlvvNKL----------RGGLKSVA----VKAPGFGDRR--KAMLEDIAVLTG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 322 GKVIS-----TLRDLSLETLGSAERVEEVK--------HGDESFVYIRgCSNPRA------------------------V 364
Cdd:PRK12850 298 GQVISedlgiKLENVTLDMLGRAKRVLITKenttiidgAGDKKNIEAR-VKQIRAqieettsdydreklqerlaklaggV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 365 SLILRGGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFsRTLGGREQLAVQEFSLALESIPETL 443
Cdd:PRK12850 377 AVIRVGGATEVeVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQI 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276430170 444 AENAGLDPLEVLTDLKKQHDiglkFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:PRK12850 455 ATNAGFEGSVVVGKVAELPG----NFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLI 515
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
31-517 |
1.13e-29 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 122.52 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 31 KIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPAAKMMVDI---AKTQESEV-GDGTTTAVLLAGKLL 106
Cdd:CHL00093 20 DILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqAASKTNDVaGDGTTTATVLAYAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 107 ENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIA-ITAmtgkgaeGNKEHLAELIVNAVDQVsnGQ 185
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVAsISA-------GNDEEVGSMIADAIEKV--GR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 186 EvnsEDITLEKLKGeSISDSELVSGIVLQK-----------ERanadMPLRVDNPKILLVDFPIELRNPDAEAKISVSTP 254
Cdd:CHL00093 171 E---GVISLEEGKS-TVTELEITEGMRFEKgfispyfvtdtER----MEVVQENPYILLTDKKITLVQQDLLPILEQVTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 255 EQLENFIESEEIYLKnmtdkiiALGAKAIFCQKGIDDVAQyylAKSGIFACRRipKSEMEKLARATSGKVIS-----TLR 329
Cdd:CHL00093 243 TKRPLLIIAEDVEKE-------ALATLVLNKLRGIVNVVA---VRAPGFGDRR--KAMLEDIAILTGGQVITedaglSLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 330 DLSLETLGSAERVEEVK-------HGDESFVYIRgCSNPRavSLILRGGSSHVLDEI-ER--------------AITDG- 386
Cdd:CHL00093 311 TIQLDLLGQARRIIVTKdsttiiaDGNEEQVKAR-CEQLR--KQIEIADSSYEKEKLqERlaklsggvavikvgAATETe 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 387 -------LGDVISAIKSGT---IVAGGGAIEIELSKELNLFSRT-LGGREQLAVQEFSLALESIPETLAENAGLDPLeVL 455
Cdd:CHL00093 388 mkdkklrLEDAINATKAAVeegIVPGGGATLVHLSENLKTWAKNnLKEDELIGALIVARAILAPLKRIAENAGKNGS-VI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276430170 456 TDLKKQHDIGLkfhGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVLISK 517
Cdd:CHL00093 467 IEKVQEQDFEI---GYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDK 525
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
17-508 |
2.34e-29 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 121.56 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 17 SFGKDAqRNNILA-AKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHPA----AKMMVDIAKTQESEV 91
Cdd:PTZ00114 18 RFGDEA-RQSLLKgIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIAITAmtgkgAEGNKEhLA 171
Cdd:PTZ00114 97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATIS-----ANGDVE-IG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 172 ELIVNAVDQVS-NG----QEVNSEDITLEKLKGESIsDSELVSGIVLQKEranADMPLRVDNPKILLVDFPIE-----Lr 241
Cdd:PTZ00114 171 SLIADAMDKVGkDGtitvEDGKTLEDELEVVEGMSF-DRGYISPYFVTNE---KTQKVELENPLILVTDKKISsiqsiL- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 242 nPDAEAKISVSTPEqlenFIESEEIYLKNMTDKIIalgAKAifcQKGIDDVAqyylAKSGIFACRRipKSEMEKLARATS 321
Cdd:PTZ00114 246 -PILEHAVKNKRPL----LIIAEDVEGEALQTLII---NKL---RGGLKVCA----VKAPGFGDNR--KDILQDIAVLTG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 322 GKVIS------TLRDLSLETLGSAERVEEVKhgDESFVYIRGCSNPRA-------------------------------- 363
Cdd:PTZ00114 309 ATVVSednvglKLDDFDPSMLGSAKKVTVTK--DETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsg 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 364 -VSLILRGGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELN--LFSRTLGGREQLAVQEFSLALESI 439
Cdd:PTZ00114 387 gVAVIKVGGASEVeVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDklEEDNELTPDQRTGVKIVRNALRLP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276430170 440 PETLAENAGLDPLEVLTDLKKQHDiglKFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:PTZ00114 466 TKQIAENAGVEGAVVVEKILEKKD---PSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
18-508 |
1.08e-27 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 116.76 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEVGD 93
Cdd:PRK12851 8 FHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 94 GTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLkniaitAMTGKGAEGNKEHLAEL 173
Cdd:PRK12851 88 GTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEI------AQVATISANGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 174 IVNAVDQVSNGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANAD-MPLRVDNPKILLVDFPI-ELRN--PDAEAKI 249
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADkMEAELEDPYILIHEKKIsNLQDllPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 250 SVSTPEQL--ENfIESEeiylknmtdkiiALGAKAIFCQKGIDDVAqyyLAKSGIFACRRipKSEMEKLARATSGKVIS- 326
Cdd:PRK12851 242 QSGKPLLIiaED-VEGE------------ALATLVVNKLRGGLKVA---AVKAPGFGDRR--KAMLEDIAILTGGTVISe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 327 ----TLRDLSLETLGSAERVEEVKH--------GDESFVYIRgCSNPRA------------------------VSLILRG 370
Cdd:PRK12851 304 dlgiKLENVTLEQLGRAKKVVVEKEnttiidgaGSKTEIEGR-VAQIRAqieettsdydreklqerlaklaggVAVIRVG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 371 GSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELnLFSRTLGGREQLAVQEFSLALESIPETLAENAGL 449
Cdd:PRK12851 383 ASTEVeVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKAL-DKLETANGDQRTGVEIVRRALEAPVRQIAENAGA 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1276430170 450 DPLEVLTDLKKqhdiGLKFHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:PRK12851 461 EGSVVVGKLRE----KPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLL 515
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
18-508 |
3.84e-27 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 114.84 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAqRNNILA-AKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEVG 92
Cdd:PRK00013 7 FGEDA-RRKLLRgVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 93 DGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIA-ITAmtgkgaeGNKEHLA 171
Cdd:PRK00013 86 DGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVAtISA-------NGDEEIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 172 ELIVNAVDQVsnGQE-VnsedITLEKLKGesiSDSEL--VSGI-----------VLQKERANADMplrvDNPKILLVDfp 237
Cdd:PRK00013 159 KLIAEAMEKV--GKEgV----ITVEESKG---FETELevVEGMqfdrgylspyfVTDPEKMEAEL----ENPYILITD-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 238 ielrnpdaeAKIS-------VstpeqLENFIESEEIYLknmtdkIIAlgakaifcqkgiDDVAQYYLAK------SGIFA 304
Cdd:PRK00013 224 ---------KKISniqdllpV-----LEQVAQSGKPLL------IIA------------EDVEGEALATlvvnklRGTLK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 305 C----------RRipKSEMEKLARATSGKVIS-----TLRDLSLETLGSAERVEEVK--------HGDESFVYIRgCSNP 361
Cdd:PRK00013 272 VvavkapgfgdRR--KAMLEDIAILTGGTVISeelglKLEDATLEDLGQAKKVVVTKdnttivdgAGDKEAIKAR-VAQI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 362 RA------------------------VSLILRGGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNL 416
Cdd:PRK00013 349 KAqieettsdydreklqerlaklaggVAVIKVGAATEVeMKEKKDRVEDALHATRAAVEEG-IVPGGGVALLRAAPALEA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 417 FSrTLGGREQLAVQEFSLALESIPETLAENAGLDPLEVLTDLKKQHDIGlkfHGLNLFSDKIEDTLQAGIIEPIKVKIQA 496
Cdd:PRK00013 428 LK-GLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEYVDMIEAGIIDPTKVTRSA 503
|
570
....*....|..
gi 1276430170 497 ITSASEVATMIL 508
Cdd:PRK00013 504 LQNAASVAGLLL 515
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
196-381 |
1.25e-26 |
|
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: 108.85 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 196 KLKGESISDSELVSGIVLQKERANADMPLRVDNPKILLVDFPIELrnPDAEAKISvstpeQLENFIESEEIYLKNMTDKI 275
Cdd:cd03334 54 KIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEY--QRVENKLL-----SLDPVILQEKEYLKNLVSRI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 276 IALGAKAIFCQKGIDDVAQYYLAKSGIFACRRIPKSEMEKLARATSGKVISTLRDLSLE-TLGSAER------VEEVKHG 348
Cdd:cd03334 127 VALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSpKLGTCESfrvrtyVEEHGRS 206
|
170 180 190
....*....|....*....|....*....|...
gi 1276430170 349 dESFVYIRGCSNPRAVSLILRGGSSHVLDEIER 381
Cdd:cd03334 207 -KTLMFFEGCPKELGCTILLRGGDLEELKKVKR 238
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
18-508 |
3.75e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 96.84 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEID----HPAAKMMVDIAKTQESEVGD 93
Cdd:PRK12852 8 FSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 94 GTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIAITAMTGKGAEGnkehlaEL 173
Cdd:PRK12852 88 GTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIG------KM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 174 IVNAVDQVSNG-----QEVNSEDITLEKLKGESISDSELVSGIVLQKERanadMPLRVDNPKILLVDFPIE-LRN--PDA 245
Cdd:PRK12852 162 IAQAMQKVGNEgvitvEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEK----MTVELDDAYILLHEKKLSgLQAmlPVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 246 EAKISVSTPEqlenFIESEEIYLKnmtdkiiALGAKAIFCQKGIDDVAQyylAKSGIFACRRipKSEMEKLARATSGKVI 325
Cdd:PRK12852 238 EAVVQSGKPL----LIIAEDVEGE-------ALATLVVNRLRGGLKVAA---VKAPGFGDRR--KAMLEDIAILTGGQLI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 326 S-----TLRDLSLETLGSAERVEEVKH--------GDESFV-----------------YIRGCSNPR------AVSLILR 369
Cdd:PRK12852 302 SedlgiKLENVTLKMLGRAKKVVIDKEnttivngaGKKADIearvgqikaqieettsdYDREKLQERlaklagGVAVIRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 370 GGSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFSrTLGGREQLAVQEFSLALESIPETLAENAG 448
Cdd:PRK12852 382 GGATEVeVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRIN-NDNADVQAGINIVLKALEAPIRQIAENAG 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 449 LDPLEVLTDLKKQHDIGLkfhGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:PRK12852 460 VEGSIVVGKILENKSETF---GFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLV 516
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
18-508 |
1.27e-19 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 92.02 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAQRNNILAAKIIANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEID----HPAAKMMVDIAKTQESEVGD 93
Cdd:PRK14104 8 FGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 94 GTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKiqdrnVLKNIAITAMTGKGAEGNKEhLAEL 173
Cdd:PRK14104 88 GTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKK-----VTSNDEIAQVGTISANGDAE-IGKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 174 IVNAVDQVSNGQEVNSEDITLEKLKGESISDSELVSGIVLQKERANAD-MPLRVDNPKILLVDFPIELRN---PDAEAKI 249
Cdd:PRK14104 162 LADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADkMRVEMDDAYILINEKKLSSLNellPLLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 250 SVSTPEqlenFIESEEIYLKnmtdkiiALGAKAIFCQKGIDDVAQyylAKSGIFACRRipKSEMEKLARATSGKVIS--- 326
Cdd:PRK14104 242 QTGKPL----VIVAEDVEGE-------ALATLVVNRLRGGLKVAA---VKAPGFGDRR--KAMLQDIAILTGGQAISedl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 327 --TLRDLSLETLGSAE-----------------------RVEEVKHGDESFV--YIRGCSNPR------AVSLILRGGSS 373
Cdd:PRK14104 306 giKLENVTLQMLGRAKkvmidkenttivngagkkadieaRVAQIKAQIEETTsdYDREKLQERlaklagGVAVIRVGGAT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 374 HV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFsRTLGGREQLAVQEFSLALESIPETLAENAGLDPL 452
Cdd:PRK14104 386 EVeVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGS 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276430170 453 EVLTDL--KKQHDiglkfHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMIL 508
Cdd:PRK14104 464 VIVGKIleKEQYS-----YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLI 516
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
18-516 |
5.10e-19 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 90.37 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 18 FGKDAQRNNILAAKI--IANIVKTTLGPKGMDKMLVDSTGNIIVTNDGVTILEEMEIDHP----AAKMMVDIAKTQESEV 91
Cdd:PLN03167 61 FNKDGSAIKKLQAGVnkLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 92 GDGTTTAVLLAGKLLENAERLLDKKIHPTVIIKGYRLAAQKALEILKNQSVKIQDRNVLKNIAITAmtgkgaeGNKEHLA 171
Cdd:PLN03167 141 GDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSELADVAAVSA-------GNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 172 ELIVNAVDQVSNG-----QEVNSEDITLEKLKGESISDSELVSGIVLQKERanadMPLRVDNPKILLVDFPIElrnpDAE 246
Cdd:PLN03167 214 NMIAEAMSKVGRKgvvtlEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEK----MSVEYDNCKLLLVDKKIT----NAR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 247 AKISVstpeqLENFIE--------SEEIYLKNMTD----------KIIALGAKAIFCQKG--IDDVAqyylAKSGIFACR 306
Cdd:PLN03167 286 DLIGI-----LEDAIRggyplliiAEDIEQEALATlvvnklrgslKIAALKAPGFGERKSqyLDDIA----ILTGGTVIR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 307 RIPKSEMEKLAR---ATSGKVISTLRDLSLETLGSAE-----RVEEVKHGDESFV--YIRGCSNPR------AVSLILRG 370
Cdd:PLN03167 357 EEVGLSLDKVGKevlGTAAKVVLTKDTTTIVGDGSTQeavnkRVAQIKNLIEAAEqdYEKEKLNERiaklsgGVAVIQVG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276430170 371 GSSHV-LDEIERAITDGLGDVISAIKSGtIVAGGGAIEIELSKELNLFSRTLGGREQLAVQEFSLALESIPETL-AENAG 448
Cdd:PLN03167 437 AQTETeLKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPLKLiAKNAG 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276430170 449 LDPLEVLTDLKKQHDIGlkfHGLNLFSDKIEDTLQAGIIEPIKVKIQAITSASEVATMILRIDDVLIS 516
Cdd:PLN03167 516 VNGSVVSEKVLSNDNPK---FGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVE 580
|
|
| |
