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T-complex protein 1 subunit theta-like 2 [Rattus norvegicus]
Protein Classification
TCP-1/cpn60 chaperonin family protein ( domain architecture ID 16 )
TCP-1/cpn60 chaperonin family protein similar to mycobacterial 60 kDa chaperonin (GroEL) that together with its co-chaperonin GroES, plays an essential role in assisting protein folding
List of domain hits
Name
Accession
Description
Interval
E-value
chaperonin_like super family
cl02777 chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
34-531
3.24e-151
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.
cd03341 :Pssm-ID: 351886 [Multi-domain]
Cd Length: 472
Bit Score: 442.43
E-value: 3.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 34 Q G E E PL c I LR ATA A AQT L AS I I R SC YGP Y G LQ K FLVSAQGETVC T GH AA A IL KA LE LE HPAA RFVQELA Q T Q A E NT GDGT 113
Cdd:cd03341 4 S G L E EA - V LR NIE A CKE L SQ I T R TS YGP N G MN K MVINHLEKLFV T SD AA T IL RE LE VQ HPAA KLLVMAS Q M Q E E EI GDGT 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 114 AF VV L L TEA LLE Q A QY LL WA GL T P AQLR E AFVT A TAEV L TA L PS L AICSLGP L --- E DP S W AL YSVMSTHTLS N AEY L TK 190
Cdd:cd03341 83 NL VV V L AGE LLE K A EE LL RM GL H P SEII E GYEK A LKKA L EI L EE L VVYKIED L rnk E EV S K AL KTAIASKQYG N EDF L SP 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 191 LVA Q AC W - ISR E PN G S F KPES I V V CILQ GG I L T DS RIIP G IAICGKLC G RKTE V LN d A R VA L F N CPF G psnpfapatlrl 269
Cdd:cd03341 163 LVA E AC I s VLP E NI G N F NVDN I R V VKIL GG S L E DS KVVR G MVFKREPE G SVKR V KK - A K VA V F S CPF D ------------ 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 270 sspeelirfrkqteqvemeiaelam M G I NV A V VL G E V NERSVDQADYC G V MVI QVK S RK E IVY L SDKL G VPL L N R ILP P L 349
Cdd:cd03341 230 ------------------------- I G V NV I V AG G S V GDLALHYCNKY G I MVI KIN S KF E LRR L CRTV G ATP L P R LGA P T 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 350 -- E P G K C HK VY RM E F G ESALIM F EWER E IAPFLSV VLRG P T IQG L RGA E Q A VYY G IDA F SQ L CQ D P R LL PGAGATE MA LA 427
Cdd:cd03341 285 pe E I G Y C DS VY VE E I G DTKVVV F RQNK E DSKIATI VLRG A T QNI L DDV E R A IDD G VNV F KS L TK D G R FV PGAGATE IE LA 364
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 428 RM L VDK G SRLD G PNGL A FQA FA Q A LSSL P K TLAENAGL A A QS VL A E MSGY HQ A GN FVI GV ---- G TD G LVNVAQE GI W D I 503
Cdd:cd03341 365 KK L KEY G EKTP G LEQY A IKK FA E A FEVV P R TLAENAGL D A TE VL S E LYAA HQ K GN KSA GV dies G DE G TKDAKEA GI F D H 444
490 500
....*....|....*....|....*...
gi 83642818 504 L R TK AQGLQAV T GLVQQLVT VDQII V A R 531
Cdd:cd03341 445 L A TK KWAIKLA T EAAVTVLR VDQII M A K 472
Name
Accession
Description
Interval
E-value
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
34-531
3.24e-151
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: 442.43
E-value: 3.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 34 Q G E E PL c I LR ATA A AQT L AS I I R SC YGP Y G LQ K FLVSAQGETVC T GH AA A IL KA LE LE HPAA RFVQELA Q T Q A E NT GDGT 113
Cdd:cd03341 4 S G L E EA - V LR NIE A CKE L SQ I T R TS YGP N G MN K MVINHLEKLFV T SD AA T IL RE LE VQ HPAA KLLVMAS Q M Q E E EI GDGT 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 114 AF VV L L TEA LLE Q A QY LL WA GL T P AQLR E AFVT A TAEV L TA L PS L AICSLGP L --- E DP S W AL YSVMSTHTLS N AEY L TK 190
Cdd:cd03341 83 NL VV V L AGE LLE K A EE LL RM GL H P SEII E GYEK A LKKA L EI L EE L VVYKIED L rnk E EV S K AL KTAIASKQYG N EDF L SP 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 191 LVA Q AC W - ISR E PN G S F KPES I V V CILQ GG I L T DS RIIP G IAICGKLC G RKTE V LN d A R VA L F N CPF G psnpfapatlrl 269
Cdd:cd03341 163 LVA E AC I s VLP E NI G N F NVDN I R V VKIL GG S L E DS KVVR G MVFKREPE G SVKR V KK - A K VA V F S CPF D ------------ 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 270 sspeelirfrkqteqvemeiaelam M G I NV A V VL G E V NERSVDQADYC G V MVI QVK S RK E IVY L SDKL G VPL L N R ILP P L 349
Cdd:cd03341 230 ------------------------- I G V NV I V AG G S V GDLALHYCNKY G I MVI KIN S KF E LRR L CRTV G ATP L P R LGA P T 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 350 -- E P G K C HK VY RM E F G ESALIM F EWER E IAPFLSV VLRG P T IQG L RGA E Q A VYY G IDA F SQ L CQ D P R LL PGAGATE MA LA 427
Cdd:cd03341 285 pe E I G Y C DS VY VE E I G DTKVVV F RQNK E DSKIATI VLRG A T QNI L DDV E R A IDD G VNV F KS L TK D G R FV PGAGATE IE LA 364
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 428 RM L VDK G SRLD G PNGL A FQA FA Q A LSSL P K TLAENAGL A A QS VL A E MSGY HQ A GN FVI GV ---- G TD G LVNVAQE GI W D I 503
Cdd:cd03341 365 KK L KEY G EKTP G LEQY A IKK FA E A FEVV P R TLAENAGL D A TE VL S E LYAA HQ K GN KSA GV dies G DE G TKDAKEA GI F D H 444
490 500
....*....|....*....|....*...
gi 83642818 504 L R TK AQGLQAV T GLVQQLVT VDQII V A R 531
Cdd:cd03341 445 L A TK KWAIKLA T EAAVTVLR VDQII M A K 472
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
51-531
4.48e-138
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: 409.28
E-value: 4.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 51 LA S I I R SCY GP Y G LQ K F LV SAQ G ETVC T GHA A A ILK A LE LE HPAA RFVQ E L A QT Q A E NT GDGT AF VV L L TEA LLE Q A QY L 130
Cdd:pfam00118 1 LA D I V R TSL GP K G MD K M LV NSG G DVTV T NDG A T ILK E LE IQ HPAA KLLV E A A KA Q D E EV GDGT TT VV V L AGE LLE E A EK L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 131 L W AG LT P AQLR E AFVT A TAEV L TA L P S la I C S LGPLEDPSWA L YS V MS T HTL S ----- NAEY L T KLV AQ A CWISREPN GS 205
Cdd:pfam00118 81 L A AG VH P TTII E GYEK A LEKA L EI L D S -- I I S IPVEDVDRED L LK V AR T SLS S kiisr ESDF L A KLV VD A VLAIPKND GS 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 206 F KPES I V V CILQ GG I L T DS RIIP G IAI - C G K L CGRKTEV L ND A R V A L F NC PFGPSNPFAP AT LR LS SP E E L I RF - RKQT E 283
Cdd:pfam00118 159 F DLGN I G V VKIL GG S L E DS ELVD G VVL d K G P L HPDMPKR L EN A K V L L L NC SLEYEKTETK AT VV LS DA E Q L E RF l KAEE E 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 284 Q VEMEIAELAMM G I NV A V VLGEVNERSVDQADYC G V M VIQVKSRKEIVY L SDKL G VPLLNRI -- L P P LEP G KCH KV YRME 361
Cdd:pfam00118 239 Q ILEIVEKIIDS G V NV V V CQKGIDDLALHFLAKN G I M ALRRVKKRDLER L AKAT G ARAVSSL dd L T P DDL G TAG KV EEEK 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 362 F G ESALIMF E w EREIAPFLSVV LRG P T IQG L RGA E QAVYYGIDAFSQLCQ DPR LL PG A GA T EM A LAR M L VDKGSRLD G PN 441
Cdd:pfam00118 319 I G DEKYTFI E - GCKSPKAATIL LRG A T DHV L DEI E RSIHDALCVVKNAIE DPR VV PG G GA V EM E LAR A L REYAKSVS G KE 397
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 442 G LA FQ AFA Q AL SSL PKTLAENAGL AAQS VLAE MSGY H QA G NFVI G VGTDG -- LVNVAQE G IW D I L RT K A Q G L QAV T GLVQ 519
Cdd:pfam00118 398 Q LA IE AFA E AL EVI PKTLAENAGL DPIE VLAE LRAA H AS G EKHA G IDVET ge IIDMKEA G VV D P L KV K R Q A L KSA T EAAS 477
490
....*....|..
gi 83642818 520 QLVTV D Q II V A R 531
Cdd:pfam00118 478 TILRI D D II K A K 489
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
41-532
1.07e-96
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: 304.33
E-value: 1.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 41 ILRATA A AQT L AS I I R SCY GP Y G LQ K FLVSAQGETVC T GH AA A IL KA LE LE HPAA RFVQELAQT Q AENT GDGT AF V VL L T 120
Cdd:TIGR02346 20 VIKNIE A CKE L SQ I T R TSL GP N G MN K MVINHLEKLFV T ND AA T IL RE LE VQ HPAA KLLVMASEM Q ENEI GDGT NL V LV L A 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 121 EA LL EQ A QY L LWA GL T P AQLREAFVT A TAEVLTA L PS L AICSLGP L E D P --- SW AL YSVM S THTLS N AEY L TK LVAQAC W 197
Cdd:TIGR02346 100 GE LL NK A EE L IRM GL H P SEIIKGYEM A LKKAMEI L EE L VVWEVKD L R D K del IK AL KASI S SKQYG N EDF L AQ LVAQAC S 179
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 198 ISREP N - GS F KPES I V VC ILQ GG I L TD S RIIP G IAICGKLC G RKTE V L N d A R VA L F N CP FGPSNPFAPA T LRLSSP EEL I 276
Cdd:TIGR02346 180 TVLPK N p QN F NVDN I R VC KIL GG S L SN S EVLK G MVFNREAE G SVKS V K N - A K VA V F S CP LDTATTETKG T VLIHNA EEL L 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 277 RFR K QT E - Q V E ME I AEL A MM G I NV A V VL G E V NERSVDQADYCGV MV IQVK S RK E IVY L SDKL G VPL L N R ILP P L -- E P G K 353
Cdd:TIGR02346 259 NYS K GE E n Q I E AM I KAI A DS G V NV I V TG G S V GDMALHYLNKYNI MV LKIP S KF E LRR L CKTV G ATP L P R LGA P T pe E I G Y 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 354 CHK VY RM E F G ESALIM F EW E REIAPFLSVV LRG P T IQG L RGA E Q A VYY G IDAFSQ L CQ D P RLLPGAGATE MA LA RM L VDK 433
Cdd:TIGR02346 339 VDS VY VS E I G GDKVTV F KQ E NGDSKISTII LRG S T DNL L DDI E R A IDD G VNTVKA L VK D G RLLPGAGATE IE LA SR L TKY 418
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 434 G SR L D G PNGL A FQA FA Q A LSSL P K TLAENAGL A A QS V LAEMSGY H QA GN FVI G V ---- GT DG LVNVAQE GI W D I L R TK AQ 509
Cdd:TIGR02346 419 G EK L P G LDQY A IKK FA E A FEII P R TLAENAGL N A NE V IPKLYAA H KK GN KSK G I diea ES DG VKDASEA GI Y D M L A TK KW 498
490 500
....*....|....*....|...
gi 83642818 510 GLQAV T GLVQQLVT VDQII V A RK 532
Cdd:TIGR02346 499 AIKLA T EAAVTVLR VDQII M A KP 521
thermosome_alpha
NF041082 thermosome subunit alpha;
47-530
1.02e-51
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 184.70
E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A SII R SCY GP Y G LQ K F LV SAQ G ET V C T GHAAA ILK ALEL EHPAA RFVQ E L A Q TQ AENT GDGT AFV V L L TEA LL EQ 126
Cdd:NF041082 25 AA KAV A EAV R TTL GP K G MD K M LV DSL G DV V I T NDGVT ILK EMDI EHPAA KMIV E V A K TQ DDEV GDGT TTA V V L AGE LL KK 104
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QY LL WAGLT P AQLR E AFVT A TAEV L TA L PSL AI c SLG P LEDP --- SW A LYSVMSTHTLSNAEY L TK LV AQ A CWISR E PN 203
Cdd:NF041082 105 A EE LL DQDIH P TIIA E GYRL A AEKA L EI L DEI AI - KVD P DDKE tlk KI A ATAMTGKGAEAAKDK L AD LV VD A VKAVA E KD 183
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 204 G SFK -- PES I V V CILQ GG ILT DS RIIP G IA I cgklcgr KT E VLN -------- D A RV AL FNC P FGPSNPFAP A TLRLSS P E 273
Cdd:NF041082 184 G GYN vd LDN I K V EKKV GG SIE DS ELVE G VV I ------- DK E RVH pgmpkrve N A KI AL LDA P LEVKKTEID A KISITD P D 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 274 E L IR F RK Q T E QVEM E IAE - L A MM G I NV AVVLGEVN ersv D Q A DY ---- C G VMVIQVKSRKEIVY L SDKL G VPLLNR I -- L 346
Cdd:NF041082 257 Q L QA F LD Q E E KMLK E MVD k I A DS G A NV VFCQKGID ---- D L A QH ylak E G ILAVRRVKKSDMEK L AKAT G ARIVTS I dd L 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 347 P P LEP G KCHK V YRMEF G ESAL I MF E w EREIAPFLSVV LRG P T IQGLRGA E Q A VYYGIDAFSQLCQ D PRLLP G A GA T E MA L 426
Cdd:NF041082 333 S P EDL G YAGL V EERKV G GDKM I FV E - GCKNPKAVTIL LRG G T EHVVDEV E R A LEDALRVVRVVLE D GKVVA G G GA P E VE L 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 427 A RM L VDKGSRLD G PNG LA FQ AFA Q AL SSL P K TLAENAGL AAQSV L A E MSGY H QA GN FVI G VG -- T DGL V NVAQE G IWDI L 504
Cdd:NF041082 412 A LR L REYAASVG G REQ LA IE AFA E AL EII P R TLAENAGL DPIDA L V E LRSA H EK GN KTA G LD vy T GKV V DMLEI G VVEP L 491
490 500
....*....|....*....|....*.
gi 83642818 505 R T K A Q GLQAV T GLVQQLVTV D QI I V A 530
Cdd:NF041082 492 R V K T Q AIKSA T EAAVMILRI D DV I A A 517
thermosome_beta
NF041083 thermosome subunit beta;
47-531
2.53e-48
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 175.52
E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A SII R SCY GP Y G LQ K F LV SAQ G ET V C T GHA A A ILK ALELE HPAA RFVQ E L A Q TQ AENT GDGT AFV V L L TEA LL EQ 126
Cdd:NF041083 25 AA KAV A EAV R TTL GP K G MD K M LV DSL G DI V I T NDG A T ILK EMDVQ HPAA KMLV E V A K TQ DDEV GDGT TTA V V L AGE LL KK 104
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QY LL WAGLT P AQLREAFVT A TAEVLTA L PSL A I c SLG P l E D PSW ---- A LY S VM S THTLSNAE YL TKLVAQ A C - WISRE 201
Cdd:NF041083 105 A EE LL DQNIH P TIIANGYRL A AEKAIEI L DEI A E - KVD P - D D RET lkki A ET S LT S KGVEEARD YL AEIAVK A V k QVAEK 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 202 PN G SFK -- PES I VVCILQ GG ILT D SRI I P GI A I CG - KLCGRKTEVLND A RV AL FNC P FGPSNPFAP A TL R LSS P EE L IR F 278
Cdd:NF041083 183 RD G KYY vd LDN I QIEKKH GG SIE D TQL I Y GI V I DK e VVHPGMPKRVEN A KI AL LDA P LEVKKTEID A EI R ITD P DQ L QK F 262
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 279 RK Q T E QVEM E IAE - LAMM G I NV AVV lgevn ERSV D Q - A DY ---- C G VM - V IQ VK s RKEIVY L SDKL G VPLLNR I -- L P P L 349
Cdd:NF041083 263 LD Q E E KMLK E MVD k IKAT G A NV VFC ----- QKGI D D l A QH ylak A G IL a V RR VK - KSDMEK L AKAT G ARIVTN I dd L T P E 336
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 350 EP G KCHK V YRMEF G ESALIMF E WERE i APFLSVVL RG P T IQGLRG AE Q A VYYGIDAFSQLCQ D PRLLP G A GA T E MA LA RM 429
Cdd:NF041083 337 DL G YAEL V EERKV G DDKMVFV E GCKN - PKAVTILI RG G T EHVVDE AE R A LEDALSVVADAVE D GKIVA G G GA P E VE LA KR 415
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 430 L VDKGSRLD G PNG LA FQ AFA Q AL SSL P K TLAENAGL AAQSV L AEMSGY H QA G NFVI G -- V G T DGL V NVAQE G IWDI LR T K 507
Cdd:NF041083 416 L REYAATVG G REQ LA VE AFA E AL EII P R TLAENAGL DPIDI L VKLRSA H EK G KKWA G in V F T GEV V DMWEL G VIEP LR V K 495
490 500
....*....|....*....|....
gi 83642818 508 A Q GLQAV T GLVQQLVTV D QI I V A R 531
Cdd:NF041083 496 T Q AIKSA T EAATMILRI D DV I A A K 519
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
14-537
7.77e-37
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 143.63
E-value: 7.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 14 QSDLEL PQ R LK L G LE knp E SQ GE ep LCI L RATAA A QTL A SIIRSCY GP Y G LQ K F L VSAQ ----- G ETVC T GHA A A ILK AL 88
Cdd:PTZ00212 2 IMANVP PQ V LK Q G AQ --- E EK GE -- TAR L QSFVG A IAV A DLVKTTL GP K G MD K I L QPMS egprs G NVTV T NDG A T ILK SV 76
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 89 E L EH PAA RFVQELAQ TQ A E NT GDGT AF VV L L TEA LL EQ A QY LL WAGLT P AQLR E AFVT A TAEVLT AL PSL A ICSLGPL E D 168
Cdd:PTZ00212 77 W L DN PAA KILVDISK TQ D E EV GDGT TS VV V L AGE LL RE A EK LL DQKIH P QTII E GWRM A LDVARK AL EEI A FDHGSDE E K 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 169 PSWA L YSVMS T h TLS N ------ AEYLT KL VAQ A cw IS R E p N GS FKPES I VVCILQ GG I L T DS RIIP G ------ I AIC gkl 236
Cdd:PTZ00212 157 FKED L LNIAR T - TLS S klltve KDHFA KL AVD A -- VL R L - K GS GNLDY I QIIKKP GG T L R DS YLED G filekk I GVG --- 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 237 CGRKT E vln DARVALF N C P -------- F G psnpfap A TLRLS S P E EL irfrkqteq V E M E I AE LAM M ---------- G I N 298
Cdd:PTZ00212 230 QPKRL E --- NCKILVA N T P mdtdkiki Y G ------- A KVKVD S M E KV --------- A E I E A AE KEK M knkvdkilah G C N 290
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 299 V AV ----------- VLG E VNERSVDQ AD YC G VMVIQVKSRK EIV YLS D K lgv P LLNRI lpplep G K C HKVYRMEF GE SA L 367
Cdd:PTZ00212 291 V FI nrqliynypeq LFA E AGIMAIEH AD FD G MERLAAALGA EIV STF D T --- P EKVKL ------ G H C DLIEEIMI GE DK L 361
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 368 I M F E - WEREI A pf LSV VLRG PTIQG L RG AE QAVYYGIDAF SQ LCQ D P R LLP G A G AT EM AL A RMLVDKGSRLD G PNG LA FQ 446
Cdd:PTZ00212 362 I R F S g CAKGE A -- CTI VLRG ASTHI L DE AE RSLHDALCVL SQ TVK D T R VVL G G G CS EM LM A NAVEELAKKVE G KKS LA IE 439
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 447 AFA Q AL SSL P KTL A E N A G LAAQSVLAEMSGY H QA GN FVI G VG - TD G L V - NVAQE GI WDILRT K AQG L QAV T GLVQQLVT V 524
Cdd:PTZ00212 440 AFA K AL RQI P TII A D N G G YDSAELVSKLRAE H YK GN KTA G ID m EK G T V g DMKEL GI TESYKV K LSQ L CSA T EAAEMILR V 519
570
....*....|...
gi 83642818 525 D Q II va R KT PR Y R 537
Cdd:PTZ00212 520 D D II -- R CA PR Q R 530
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
46-534
4.43e-29
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 120.57
E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 46 AAAQT LA SIIRSCY GP Y G LQKF LV SAQ G ETVC T GHAAA I L K AL ELE H P ---- A A RF V Q E L A QTQAENT GDGT AFVVL L TE 121
Cdd:COG0459 17 RGVKA LA DAVKVTL GP K G RNVM LV KSF G DPTI T NDGVT I A K EI ELE D P fenm G A QL V K E V A SKTNDEA GDGT TTATV L AG 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 122 ALL EQAQY L LW AG LT P AQLREAFVT A TAEVLTA L PSL A I cslg P LE D PSW a L YS V MST h TLSNA E YLTK L V A Q A cw ISR - 200
Cdd:COG0459 97 ALL KEGLK L VA AG AN P TDIKRGIDK A VEKAVEE L KKI A K ---- P VD D KEE - L AQ V ATI - SANGD E EIGE L I A E A -- MEK v 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 201 EPN G SFKP E SI vvcilq G G IL T DSRIIP G IAI -------- CGKLCGRKTEV L ND A RVA L FNCP fgpsnpfapatlr L SS P 272
Cdd:COG0459 169 GKD G VITV E EG ------ K G LE T ELEVVE G MQF dkgylspy FVTDPEKMPAE L EN A YIL L TDKK ------------- I SS I 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 273 EE L IRFRKQT ----------- E QVEM E I - A E L A --- MM G I - N V AV V -- L G EVNE R S --- V D Q A DYC G VM VI qvksrkeiv 331
Cdd:COG0459 230 QD L LPLLEKV aqsgkplliia E DIDG E A l A T L V vng IR G V l R V VA V ka P G FGDR R K aml E D I A ILT G GR VI --------- 300
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 332 yl S DK LG VP L LNRI L PP L ep G KCHK V yrm E FGESALIMF E w EREIAPFLSVVLRGP T ---------- IQ - G L RGAEQ AV Y 400
Cdd:COG0459 301 -- S ED LG LK L EDVT L DD L -- G RAKR V --- E VDKDNTTIV E - GAGNPKAIVILVGAA T evevkerkrr VE d A L HATRA AV E 372
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 401 Y GI dafsqlcqdprl L PG A GA TEMAL AR M L VDKGSR L D G PNG L AFQAF A Q AL SSLPKTL AENAGL AAQS V LAEMSG y HQA 480
Cdd:COG0459 373 E GI ------------ V PG G GA ALLRA AR A L RELAAK L E G DEQ L GIEIV A R AL EAPLRQI AENAGL DGSV V VEKVRA - AKD 439
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 83642818 481 GN F VIGVG T DGL V NVAQE G IW D ILRT K AQG LQ A --- V T GL vqq LV T VDQI I VARKTP 534
Cdd:COG0459 440 KG F GFDAA T GEY V DMLEA G VI D PAKV K RSA LQ N aas V A GL --- IL T TEAV I ADKPEK 493
Name
Accession
Description
Interval
E-value
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
34-531
3.24e-151
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: 442.43
E-value: 3.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 34 Q G E E PL c I LR ATA A AQT L AS I I R SC YGP Y G LQ K FLVSAQGETVC T GH AA A IL KA LE LE HPAA RFVQELA Q T Q A E NT GDGT 113
Cdd:cd03341 4 S G L E EA - V LR NIE A CKE L SQ I T R TS YGP N G MN K MVINHLEKLFV T SD AA T IL RE LE VQ HPAA KLLVMAS Q M Q E E EI GDGT 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 114 AF VV L L TEA LLE Q A QY LL WA GL T P AQLR E AFVT A TAEV L TA L PS L AICSLGP L --- E DP S W AL YSVMSTHTLS N AEY L TK 190
Cdd:cd03341 83 NL VV V L AGE LLE K A EE LL RM GL H P SEII E GYEK A LKKA L EI L EE L VVYKIED L rnk E EV S K AL KTAIASKQYG N EDF L SP 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 191 LVA Q AC W - ISR E PN G S F KPES I V V CILQ GG I L T DS RIIP G IAICGKLC G RKTE V LN d A R VA L F N CPF G psnpfapatlrl 269
Cdd:cd03341 163 LVA E AC I s VLP E NI G N F NVDN I R V VKIL GG S L E DS KVVR G MVFKREPE G SVKR V KK - A K VA V F S CPF D ------------ 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 270 sspeelirfrkqteqvemeiaelam M G I NV A V VL G E V NERSVDQADYC G V MVI QVK S RK E IVY L SDKL G VPL L N R ILP P L 349
Cdd:cd03341 230 ------------------------- I G V NV I V AG G S V GDLALHYCNKY G I MVI KIN S KF E LRR L CRTV G ATP L P R LGA P T 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 350 -- E P G K C HK VY RM E F G ESALIM F EWER E IAPFLSV VLRG P T IQG L RGA E Q A VYY G IDA F SQ L CQ D P R LL PGAGATE MA LA 427
Cdd:cd03341 285 pe E I G Y C DS VY VE E I G DTKVVV F RQNK E DSKIATI VLRG A T QNI L DDV E R A IDD G VNV F KS L TK D G R FV PGAGATE IE LA 364
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 428 RM L VDK G SRLD G PNGL A FQA FA Q A LSSL P K TLAENAGL A A QS VL A E MSGY HQ A GN FVI GV ---- G TD G LVNVAQE GI W D I 503
Cdd:cd03341 365 KK L KEY G EKTP G LEQY A IKK FA E A FEVV P R TLAENAGL D A TE VL S E LYAA HQ K GN KSA GV dies G DE G TKDAKEA GI F D H 444
490 500
....*....|....*....|....*...
gi 83642818 504 L R TK AQGLQAV T GLVQQLVT VDQII V A R 531
Cdd:cd03341 445 L A TK KWAIKLA T EAAVTVLR VDQII M A K 472
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
51-531
4.48e-138
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: 409.28
E-value: 4.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 51 LA S I I R SCY GP Y G LQ K F LV SAQ G ETVC T GHA A A ILK A LE LE HPAA RFVQ E L A QT Q A E NT GDGT AF VV L L TEA LLE Q A QY L 130
Cdd:pfam00118 1 LA D I V R TSL GP K G MD K M LV NSG G DVTV T NDG A T ILK E LE IQ HPAA KLLV E A A KA Q D E EV GDGT TT VV V L AGE LLE E A EK L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 131 L W AG LT P AQLR E AFVT A TAEV L TA L P S la I C S LGPLEDPSWA L YS V MS T HTL S ----- NAEY L T KLV AQ A CWISREPN GS 205
Cdd:pfam00118 81 L A AG VH P TTII E GYEK A LEKA L EI L D S -- I I S IPVEDVDRED L LK V AR T SLS S kiisr ESDF L A KLV VD A VLAIPKND GS 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 206 F KPES I V V CILQ GG I L T DS RIIP G IAI - C G K L CGRKTEV L ND A R V A L F NC PFGPSNPFAP AT LR LS SP E E L I RF - RKQT E 283
Cdd:pfam00118 159 F DLGN I G V VKIL GG S L E DS ELVD G VVL d K G P L HPDMPKR L EN A K V L L L NC SLEYEKTETK AT VV LS DA E Q L E RF l KAEE E 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 284 Q VEMEIAELAMM G I NV A V VLGEVNERSVDQADYC G V M VIQVKSRKEIVY L SDKL G VPLLNRI -- L P P LEP G KCH KV YRME 361
Cdd:pfam00118 239 Q ILEIVEKIIDS G V NV V V CQKGIDDLALHFLAKN G I M ALRRVKKRDLER L AKAT G ARAVSSL dd L T P DDL G TAG KV EEEK 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 362 F G ESALIMF E w EREIAPFLSVV LRG P T IQG L RGA E QAVYYGIDAFSQLCQ DPR LL PG A GA T EM A LAR M L VDKGSRLD G PN 441
Cdd:pfam00118 319 I G DEKYTFI E - GCKSPKAATIL LRG A T DHV L DEI E RSIHDALCVVKNAIE DPR VV PG G GA V EM E LAR A L REYAKSVS G KE 397
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 442 G LA FQ AFA Q AL SSL PKTLAENAGL AAQS VLAE MSGY H QA G NFVI G VGTDG -- LVNVAQE G IW D I L RT K A Q G L QAV T GLVQ 519
Cdd:pfam00118 398 Q LA IE AFA E AL EVI PKTLAENAGL DPIE VLAE LRAA H AS G EKHA G IDVET ge IIDMKEA G VV D P L KV K R Q A L KSA T EAAS 477
490
....*....|..
gi 83642818 520 QLVTV D Q II V A R 531
Cdd:pfam00118 478 TILRI D D II K A K 489
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
41-532
1.07e-96
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: 304.33
E-value: 1.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 41 ILRATA A AQT L AS I I R SCY GP Y G LQ K FLVSAQGETVC T GH AA A IL KA LE LE HPAA RFVQELAQT Q AENT GDGT AF V VL L T 120
Cdd:TIGR02346 20 VIKNIE A CKE L SQ I T R TSL GP N G MN K MVINHLEKLFV T ND AA T IL RE LE VQ HPAA KLLVMASEM Q ENEI GDGT NL V LV L A 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 121 EA LL EQ A QY L LWA GL T P AQLREAFVT A TAEVLTA L PS L AICSLGP L E D P --- SW AL YSVM S THTLS N AEY L TK LVAQAC W 197
Cdd:TIGR02346 100 GE LL NK A EE L IRM GL H P SEIIKGYEM A LKKAMEI L EE L VVWEVKD L R D K del IK AL KASI S SKQYG N EDF L AQ LVAQAC S 179
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 198 ISREP N - GS F KPES I V VC ILQ GG I L TD S RIIP G IAICGKLC G RKTE V L N d A R VA L F N CP FGPSNPFAPA T LRLSSP EEL I 276
Cdd:TIGR02346 180 TVLPK N p QN F NVDN I R VC KIL GG S L SN S EVLK G MVFNREAE G SVKS V K N - A K VA V F S CP LDTATTETKG T VLIHNA EEL L 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 277 RFR K QT E - Q V E ME I AEL A MM G I NV A V VL G E V NERSVDQADYCGV MV IQVK S RK E IVY L SDKL G VPL L N R ILP P L -- E P G K 353
Cdd:TIGR02346 259 NYS K GE E n Q I E AM I KAI A DS G V NV I V TG G S V GDMALHYLNKYNI MV LKIP S KF E LRR L CKTV G ATP L P R LGA P T pe E I G Y 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 354 CHK VY RM E F G ESALIM F EW E REIAPFLSVV LRG P T IQG L RGA E Q A VYY G IDAFSQ L CQ D P RLLPGAGATE MA LA RM L VDK 433
Cdd:TIGR02346 339 VDS VY VS E I G GDKVTV F KQ E NGDSKISTII LRG S T DNL L DDI E R A IDD G VNTVKA L VK D G RLLPGAGATE IE LA SR L TKY 418
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 434 G SR L D G PNGL A FQA FA Q A LSSL P K TLAENAGL A A QS V LAEMSGY H QA GN FVI G V ---- GT DG LVNVAQE GI W D I L R TK AQ 509
Cdd:TIGR02346 419 G EK L P G LDQY A IKK FA E A FEII P R TLAENAGL N A NE V IPKLYAA H KK GN KSK G I diea ES DG VKDASEA GI Y D M L A TK KW 498
490 500
....*....|....*....|...
gi 83642818 510 GLQAV T GLVQQLVT VDQII V A RK 532
Cdd:TIGR02346 499 AIKLA T EAAVTVLR VDQII M A KP 521
chaperonin_type_I_II
cd00309 chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
33-529
7.19e-92
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: 289.33
E-value: 7.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 33 SQ GEE pl CI L RATA AA QT LA SIIRSCY GP Y G LQ K F LV SAQ G ETVC T GHA A A ILK AL E L EHPAA RFVQ E L A QT Q AENT GDG 112
Cdd:cd00309 4 EF GEE -- AR L SNIN AA KA LA DAVKTTL GP K G MD K M LV DSL G DPTI T NDG A T ILK EI E V EHPAA KLLV E V A KS Q DDEV GDG 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 113 T AF VV L L TEA LL EQ A QY LL W AG LT P AQLREAFVT A TAEV L TA L PSL A IC - SLGPL E DPSWALYSVMSTHTL S - NAEY L TK 190
Cdd:cd00309 82 T TT VV V L AGE LL KE A EK LL A AG IH P TEIIRGYEK A VEKA L EI L KEI A VP i DVEDR E ELLKVATTSLNSKLV S g GDDF L GE 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 191 LV AQ A CWISREP NG SFKPES I V V CILQ GG I L T DS RIIP G IAI - C G K L CGRKTEV L ND A RVA L FN C PF gpsnpfapatlrl 269
Cdd:cd00309 162 LV VD A VLKVGKE NG DVDLGV I R V EKKK GG S L E DS ELVV G MVF d K G Y L SPYMPKR L EN A KIL L LD C KL ------------- 228
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 270 sspeelirfrkqt E Q V --- E ME I AEL A MMGINVA vvlgevnersvdqadyc G V M VIQVKSRKEIVYLSDKL G VPLLN R I - 345
Cdd:cd00309 229 ------------- E Y V via E KG I DDE A LHYLAKL ----------------- G I M AVRRVRKEDLERIAKAT G ATIVS R L e 278
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 346 - L P P LEP G KCHK V YRMEF G ESALIMF E WERE -- I A pfl SVV LRG P T IQG L RG AE QAVYYGID A FSQLCQ D PRLL PG A GA T 422
Cdd:cd00309 279 d L T P EDL G TAGL V EETKI G DEKYTFI E GCKG gk V A --- TIL LRG A T EVE L DE AE RSLHDALC A VRAAVE D GGIV PG G GA A 355
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 423 E MA L ARM L VDKGSR L D G PNG L AFQ AFA Q AL SSL P K TLAENAGL AAQS V LAEMSGY H QA G NF -- VIG V G T DGL V NVAQE GI 500
Cdd:cd00309 356 E IE L SKA L EELAKT L P G KEQ L GIE AFA D AL EVI P R TLAENAGL DPIE V VTKLRAK H AE G GG na GGD V E T GEI V DMKEA GI 435
490 500
....*....|....*....|....*....
gi 83642818 501 W D I L RT K A Q G L QAV T GLVQQLV T V D Q IIV 529
Cdd:cd00309 436 I D P L KV K R Q A L KSA T EAASLIL T I D D IIV 464
thermosome_arch
TIGR02339 thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
46-530
2.43e-61
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: 211.08
E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 46 AAA QTL A SIIR S CY GP Y G LQ K F LV SAQ G ETVC T GHA A A ILK ALEL EHPAA RFVQ E L A Q TQ A E NT GDGT AFV V L L TEA LLE 125
Cdd:TIGR02339 23 AAA KAV A EAVK S TL GP R G MD K M LV DSL G DVTI T NDG A T ILK EMDI EHPAA KMLV E V A K TQ D E EV GDGT TTA V V L AGE LLE 102
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 126 Q A QY LL WAGLT P AQLR E AFVT A TAEV L TALPSL A I c SLG P l ED PSWALYSVMSTH T ----- LSNAEY L TK LV AQ A CWISR 200
Cdd:TIGR02339 103 K A ED LL EQDIH P TVII E GYRK A AEKA L EIIDEI A T - KIS P - ED RDLLKKIAYTSL T skasa EVAKDK L AD LV VE A VKQVA 180
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 201 E PN G SF K P ---- ES I VVCILQ GG ILT D SRIIP GI AI cgklcgr KT EV LN -------- D A RV AL FNC P FGPSNPFAP A TL R 268
Cdd:TIGR02339 181 E LR G DG K Y yvdl DN I KIVKKK GG SIE D TELVE GI VV ------- DK EV VH pgmpkrve N A KI AL LDA P LEVEKTEID A KI R 253
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 269 LSS P EELIR F RK Q T E QVEM E IAE - L A MM G I NV AVVLGEVNERSVDQADYC G VMVIQVKSRKE I VY L SDKL G VPLLNR I -- 345
Cdd:TIGR02339 254 ITD P DQIKK F LD Q E E AMLK E MVD k I A SA G A NV VICQKGIDDVAQHYLAKA G ILAVRRVKKSD I EK L ARAT G ARIVSS I de 333
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 346 LPPLEP G KCHK V YRMEF GE SALIMF E w EREIAPFLSVV LRG P T IQGLRGA E QAVYYGIDAFSQLCQ D PRLLP G A GA T E MA 425
Cdd:TIGR02339 334 ITESDL G YAEL V EERKV GE DKMVFV E - GCKNPKAVTIL LRG G T EHVVDEL E RSIQDALHVVANALE D GKIVA G G GA V E IE 412
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 426 LA RM L VDKGSRLD G PNG LA FQ AFA Q AL SSL P KT LAENAGL AAQSV L AEMSGY H QA GN FVI G -- V G T DGLVNVAQE G IWDI 503
Cdd:TIGR02339 413 LA LR L RSYARSVG G REQ LA IE AFA D AL EEI P RI LAENAGL DPIDA L VDLRAK H EK GN KNA G in V F T GEIEDMLEL G VIEP 492
490 500
....*....|....*....|....*..
gi 83642818 504 LR T K A Q GLQAV T GLVQQLVTV D QI I V A 530
Cdd:TIGR02339 493 LR V K E Q AIKSA T EAATMILRI D DV I A A 519
cpn60
cd03343 cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
46-531
6.07e-59
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: 204.42
E-value: 6.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 46 AAA QTL A SII R SCY GP Y G LQ K F LV SAQ G ETVC T GHA A A ILK ALEL EHPAA RFVQ E L A Q TQ A E NT GDGT AFV V L L TEA LLE 125
Cdd:cd03343 22 AAA KAV A EAV R TTL GP K G MD K M LV DSL G DVTI T NDG A T ILK EMDI EHPAA KMLV E V A K TQ D E EV GDGT TTA V V L AGE LLE 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 126 Q A QY LL WAGLT P AQLR E AFVT A TAEV L TA L PSL AI c SLG P LEDP --- SW A LY S VMSTHTLSNAEY L TK LV AQ A CW - ISRE 201
Cdd:cd03343 102 K A ED LL DQNIH P TVII E GYRL A AEKA L EL L DEI AI - KVD P DDKD tlr KI A KT S LTGKGAEAAKDK L AD LV VD A VL q VAEK 180
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 202 PN G SFKPE -- S I VVCILQ GG ILT D SRI I P GI A I cgklcgr KT EV LN -------- D A RV AL FNC P FGPSNPFAP A TL R LS S 271
Cdd:cd03343 181 RD G KYVVD ld N I KIEKKT GG SVD D TEL I R GI V I ------- DK EV VH pgmpkrve N A KI AL LDA P LEVKKTEID A KI R IT S 253
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 272 P EE L IR F RK Q T E QVEM E IAE - L A MM G I NV AVV lgevn ERSV D Q ------ A DY c G VMVIQVKSRKEIVY L SDKL G VPLLNR 344
Cdd:cd03343 254 P DQ L QA F LE Q E E AMLK E MVD k I A DT G A NV VFC ----- QKGI D D laqhyl A KA - G ILAVRRVKKSDMEK L ARAT G AKIVTN 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 345 I -- L P P LEP G KCHK V YRMEF G ESALIMF E WERE i APFLSVV LRG P T IQGLRGA E Q A VYYGIDAFSQLCQ D PRLLP G A GA T 422
Cdd:cd03343 328 I dd L T P EDL G EAEL V EERKV G DDKMVFV E GCKN - PKAVTIL LRG G T EHVVDEL E R A LEDALRVVADALE D GKVVA G G GA V 406
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 423 E MA LA RM L VDKGSRLD G PNG LA FQ AFA Q AL SSL P K TLAENAGL AAQSV L A E MSGY H QA GN FVI G -- V G T DGL V NVAQE G I 500
Cdd:cd03343 407 E IE LA KR L REYARSVG G REQ LA VE AFA D AL EEI P R TLAENAGL DPIDT L V E LRAA H EK GN KNA G ld V Y T GEV V DMLEK G V 486
490 500 510
....*....|....*....|....*....|.
gi 83642818 501 WDI LR T K A Q GLQAV T GLVQQLVTV D QI I V A R 531
Cdd:cd03343 487 IEP LR V K K Q AIKSA T EAATMILRI D DV I A A K 517
thermosome_alpha
NF041082 thermosome subunit alpha;
47-530
1.02e-51
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 184.70
E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A SII R SCY GP Y G LQ K F LV SAQ G ET V C T GHAAA ILK ALEL EHPAA RFVQ E L A Q TQ AENT GDGT AFV V L L TEA LL EQ 126
Cdd:NF041082 25 AA KAV A EAV R TTL GP K G MD K M LV DSL G DV V I T NDGVT ILK EMDI EHPAA KMIV E V A K TQ DDEV GDGT TTA V V L AGE LL KK 104
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QY LL WAGLT P AQLR E AFVT A TAEV L TA L PSL AI c SLG P LEDP --- SW A LYSVMSTHTLSNAEY L TK LV AQ A CWISR E PN 203
Cdd:NF041082 105 A EE LL DQDIH P TIIA E GYRL A AEKA L EI L DEI AI - KVD P DDKE tlk KI A ATAMTGKGAEAAKDK L AD LV VD A VKAVA E KD 183
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 204 G SFK -- PES I V V CILQ GG ILT DS RIIP G IA I cgklcgr KT E VLN -------- D A RV AL FNC P FGPSNPFAP A TLRLSS P E 273
Cdd:NF041082 184 G GYN vd LDN I K V EKKV GG SIE DS ELVE G VV I ------- DK E RVH pgmpkrve N A KI AL LDA P LEVKKTEID A KISITD P D 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 274 E L IR F RK Q T E QVEM E IAE - L A MM G I NV AVVLGEVN ersv D Q A DY ---- C G VMVIQVKSRKEIVY L SDKL G VPLLNR I -- L 346
Cdd:NF041082 257 Q L QA F LD Q E E KMLK E MVD k I A DS G A NV VFCQKGID ---- D L A QH ylak E G ILAVRRVKKSDMEK L AKAT G ARIVTS I dd L 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 347 P P LEP G KCHK V YRMEF G ESAL I MF E w EREIAPFLSVV LRG P T IQGLRGA E Q A VYYGIDAFSQLCQ D PRLLP G A GA T E MA L 426
Cdd:NF041082 333 S P EDL G YAGL V EERKV G GDKM I FV E - GCKNPKAVTIL LRG G T EHVVDEV E R A LEDALRVVRVVLE D GKVVA G G GA P E VE L 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 427 A RM L VDKGSRLD G PNG LA FQ AFA Q AL SSL P K TLAENAGL AAQSV L A E MSGY H QA GN FVI G VG -- T DGL V NVAQE G IWDI L 504
Cdd:NF041082 412 A LR L REYAASVG G REQ LA IE AFA E AL EII P R TLAENAGL DPIDA L V E LRSA H EK GN KTA G LD vy T GKV V DMLEI G VVEP L 491
490 500
....*....|....*....|....*.
gi 83642818 505 R T K A Q GLQAV T GLVQQLVTV D QI I V A 530
Cdd:NF041082 492 R V K T Q AIKSA T EAAVMILRI D DV I A A 517
thermosome_beta
NF041083 thermosome subunit beta;
47-531
2.53e-48
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 175.52
E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A SII R SCY GP Y G LQ K F LV SAQ G ET V C T GHA A A ILK ALELE HPAA RFVQ E L A Q TQ AENT GDGT AFV V L L TEA LL EQ 126
Cdd:NF041083 25 AA KAV A EAV R TTL GP K G MD K M LV DSL G DI V I T NDG A T ILK EMDVQ HPAA KMLV E V A K TQ DDEV GDGT TTA V V L AGE LL KK 104
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QY LL WAGLT P AQLREAFVT A TAEVLTA L PSL A I c SLG P l E D PSW ---- A LY S VM S THTLSNAE YL TKLVAQ A C - WISRE 201
Cdd:NF041083 105 A EE LL DQNIH P TIIANGYRL A AEKAIEI L DEI A E - KVD P - D D RET lkki A ET S LT S KGVEEARD YL AEIAVK A V k QVAEK 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 202 PN G SFK -- PES I VVCILQ GG ILT D SRI I P GI A I CG - KLCGRKTEVLND A RV AL FNC P FGPSNPFAP A TL R LSS P EE L IR F 278
Cdd:NF041083 183 RD G KYY vd LDN I QIEKKH GG SIE D TQL I Y GI V I DK e VVHPGMPKRVEN A KI AL LDA P LEVKKTEID A EI R ITD P DQ L QK F 262
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 279 RK Q T E QVEM E IAE - LAMM G I NV AVV lgevn ERSV D Q - A DY ---- C G VM - V IQ VK s RKEIVY L SDKL G VPLLNR I -- L P P L 349
Cdd:NF041083 263 LD Q E E KMLK E MVD k IKAT G A NV VFC ----- QKGI D D l A QH ylak A G IL a V RR VK - KSDMEK L AKAT G ARIVTN I dd L T P E 336
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 350 EP G KCHK V YRMEF G ESALIMF E WERE i APFLSVVL RG P T IQGLRG AE Q A VYYGIDAFSQLCQ D PRLLP G A GA T E MA LA RM 429
Cdd:NF041083 337 DL G YAEL V EERKV G DDKMVFV E GCKN - PKAVTILI RG G T EHVVDE AE R A LEDALSVVADAVE D GKIVA G G GA P E VE LA KR 415
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 430 L VDKGSRLD G PNG LA FQ AFA Q AL SSL P K TLAENAGL AAQSV L AEMSGY H QA G NFVI G -- V G T DGL V NVAQE G IWDI LR T K 507
Cdd:NF041083 416 L REYAATVG G REQ LA VE AFA E AL EII P R TLAENAGL DPIDI L VKLRSA H EK G KKWA G in V F T GEV V DMWEL G VIEP LR V K 495
490 500
....*....|....*....|....
gi 83642818 508 A Q GLQAV T GLVQQLVTV D QI I V A R 531
Cdd:NF041083 496 T Q AIKSA T EAATMILRI D DV I A A K 519
chap_CCT_epsi
TIGR02343 T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
40-528
6.95e-46
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: 169.21
E-value: 6.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 40 CILRAT AAA QTL ASI I R SCY GP Y G LQ K F L V S AQ G ETVC T GHA A A IL KALELEHPA A RFVQ EL AQT Q AENT GDGT AF VV L L 119
Cdd:TIGR02343 28 AKKSNI AAA KSV ASI L R TSL GP K G MD K M L I S PD G DITV T NDG A T IL SQMDVDNQI A KLMV EL SKS Q DDEI GDGT TG VV V L 107
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 120 TE ALLEQA QY LL WA G LT P AQLREA F VT A TAEVLTA L PSLA -- I CSLGPLED P ----- SWA L Y S - VM S THTLSN AE YLTKL 191
Cdd:TIGR02343 108 AG ALLEQA EE LL DK G IH P IKIADG F EE A ARIAVEH L EEIS de I SADNNNRE P liqaa KTS L G S k IV S KCHRRF AE IAVDA 187
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 192 V AQACWIS R E p NGS F --- K P E SI V vcilq GG I L T D SRI I P GI A I CGKLC -- GRKT EV L n DA RV A LFN CPF G P SN P FAPAT 266
Cdd:TIGR02343 188 V LNVADME R R - DVD F dli K V E GK V ----- GG S L E D TKL I K GI I I DKDFS hp QMPK EV E - DA KI A ILT CPF E P PK P KTKHK 260
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 267 L RL SS P EE LIRFR K QTE Q -- V EM e I AELAMM G I N VAVVL ---- G E V N ERSV d Q A D YCG V MVI qvk SRK E IVYLSDKL G vp 340
Cdd:TIGR02343 261 L DI SS V EE YKKLQ K YEQ Q kf K EM - I DDIKKS G A N LVICQ wgfd D E A N HLLL - Q N D LPA V RWV --- GGQ E LELIAIAT G -- 333
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 341 ll N RI L P PLEP ------ GK CHK V YRME FG ESA -- LIMF E WERE i APFLSVVL RG PTIQGLRG A EQAVYYGIDAFSQ L CQ D 412
Cdd:TIGR02343 334 -- G RI V P RFQE lskdkl GK AGL V REIS FG TTK dr MLVI E QCKN - SKAVTIFI RG GNKMIIEE A KRSIHDALCVVRN L IK D 410
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 413 P R LLP G A GA T E MALARMLVDKGSRLD G PNGL A FQ AFA Q AL SSL P KT LAEN A GL AAQSV L AEMSGYH - QAG N FVI GV GT -- 489
Cdd:TIGR02343 411 S R IVY G G GA A E ISCSLAVSQEADKYP G VEQY A IR AFA D AL ETI P MA LAEN S GL DPIGT L STLKSLQ l KEK N PNL GV DC lg 490
490 500 510
....*....|....*....|....*....|....*....
gi 83642818 490 D G LVNVAQEGIWDI L RT K A Q GLQAV T G LV QQLVTV D QI I 528
Cdd:TIGR02343 491 Y G TNDMKEQFVFET L IG K K Q QILLA T Q LV RMILKI D DV I 529
chap_CCT_delta
TIGR02342 T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
47-531
2.12e-44
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: 164.96
E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A SI IR SCY GP Y G LQ K FLVSAQ GE TVC T GHA A A ILK ALELE HPAA RFVQ EL AQT Q AENT GDGT AF VV L L TE ALL EQ 126
Cdd:TIGR02342 17 AA KAV A DA IR TSL GP K G MD K MIQDGK GE VII T NDG A T ILK QMAVL HPAA KMLV EL SKA Q DIEA GDGT TS VV I L AG ALL GA 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 AQY LL WA G LT P AQLR E A F VT A TA E VLTA L PSLA I cslg P LEDPSWALYSVMS T HT LS naeyl T K L V A Q ACW --------- 197
Cdd:TIGR02342 97 CER LL NK G IH P TIIS E S F QS A AD E AIKI L DEMS I ---- P VDLSDREQLLKSA T TS LS ----- S K V V S Q YSS llaplavda 167
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 198 ---- I SR E PNGSFKPES I V V CILQ GG ILT D SRI I P G IAICG K LC --- G RK T EV l ND A RVA L FNCPFG P SNPFAPATLRLS 270
Cdd:TIGR02342 168 vlkv I DP E NAKNVDLND I K V VKKL GG TID D TEL I E G LVFTQ K AS ksa G GP T RI - EK A KIG L IQFQIS P PKTDMENQIIVN 246
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 271 SPEELI R FR K QTEQVEME I A - ELAMM G I NV ----- AVVLGE VN ERSVDQADYCGV MV IQVKS R K EI VYLSDKL G VPLLNR 344
Cdd:TIGR02342 247 DYAQMD R VL K EERAYILN I V k KIKKT G C NV lliqk SILRDA VN DLALHFLAKMKI MV VKDIE R E EI EFICKTI G CKPIAS 326
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 345 I -- LPPLEP G KCHK V YRMEFGESAL I MFEWEREIAPFLS VV L RG PTIQGLRG AE QAVYYGIDAFSQ L CQDPR L LP G A GA T 422
Cdd:TIGR02342 327 I dh FTADKL G SAEL V EEVDSDGGKI I KITGIQNAGKTVT VV V RG SNKLVIDE AE RSLHDALCVIRC L VKKRG L IA G G GA P 406
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 423 E MAL AR M L VDKGSRLD G PNGLAFQ AFA Q AL SSL P K TLAENAGL AAQS V LA E MSGY H QA G NFVI G VGT -- D G LV N VAQ E GI 500
Cdd:TIGR02342 407 E IEI AR R L SKYARTMK G VESYCVR AFA D AL EVI P Y TLAENAGL NPIK V VT E LRNR H AN G EKTA G ISV rk G G IT N MLE E HV 486
490 500 510
....*....|....*....|....*....|.
gi 83642818 501 WDI L RTKAQGLQAVTGL V QQLVTV D Q I IVA R 531
Cdd:TIGR02342 487 LQP L LVTTSAITLASET V RSILKI D D I VFT R 517
TCP1_delta
cd03338 TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
47-530
1.29e-41
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: 157.06
E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A SI IR SCY GP Y G LQ K FLVSAQ GE TVC T GHA A A ILK ALELE HPAA RFVQ EL AQT Q AENT GDGT AF VV L L TE ALL EQ 126
Cdd:cd03338 16 AA KAV A DA IR TSL GP R G MD K MIQTGK GE VII T NDG A T ILK QMSVL HPAA KMLV EL SKA Q DIEA GDGT TS VV V L AG ALL SA 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 AQY LL WA G LT P AQLR E A F VT A TAEVLTA L P S LA I - CS L GPL E D pswa L YSVMS T h T L S naeyl T K L V A Q acwisrep NG S 205
Cdd:cd03338 96 CES LL KK G IH P TVIS E S F QI A AKKAVEI L D S MS I p VD L NDR E S ---- L IKSAT T - S L N ----- S K V V S Q -------- YS S 157
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 206 FKPESI V VCI L Q --------------------- GG ILT D SRIIP G IAI --- CG K LC G RK T EV l ND A RVA L FNCPFG P SNP 261
Cdd:cd03338 158 LLAPIA V DAV L K vidpatatnvdlkdirivkkl GG TIE D TELVD G LVF tqk AS K KA G GP T RI - EK A KIG L IQFCLS P PKT 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 262 FAPATLRLSSPEELI R FRKQTEQVEMEIA - ELAMM G I NV AVV ---- L GE - V NERSVDQADYCGV MV IQVKS R K EI VYLSD 335
Cdd:cd03338 237 DMDNNIVVNDYAQMD R ILREERKYILNMC k KIKKS G C NV LLI qksi L RD a V SDLALHFLAKLKI MV VKDIE R E EI EFICK 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 336 KL G VPLLNR I -- LPPLEP G KCHK V YRMEF G ESALIMFEWEREIAPFLSVVL RG PTIQG L RG AE QAV yyg I DA fsq LC --- 410
Cdd:cd03338 317 TI G CKPVAS I dh FTEDKL G SADL V EEVSL G DGKIVKITGVKNPGKTVTILV RG SNKLV L DE AE RSL --- H DA --- LC vir 390
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 411 --- QDPR L L PG A GA T E MAL A RM L VDKGSR L D G PNGLAFQ AFA Q AL SSL P K TLAENAGL AAQ S VLA E MSGY H QA G -- N FV I 485
Cdd:cd03338 391 clv KKRA L I PG G GA P E IEI A LQ L SEWART L T G VEQYCVR AFA D AL EVI P Y TLAENAGL NPI S IVT E LRNR H AQ G ek N AG I 470
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 83642818 486 G V GTDGLV N VAQ E GIWDI L RTKAQGLQAV T GL V QQLVTV D Q I IV A 530
Cdd:cd03338 471 N V RKGAIT N ILE E NVVQP L LVSTSAITLA T ET V RMILKI D D I VL A 515
TCP1_gamma
cd03337 TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
46-528
3.20e-41
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: 155.15
E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 46 A AA Q T L A SI IR S C Y GP YGLQ K F L VSAQ G ET V C T GHAA AIL KALELE HPAA RFVQ EL AQ TQ A E NT GDGT AF V VL L TEAL L E 125
Cdd:cd03337 23 Q AA K T V A DV IR T C L GP RAML K M L LDPM G GI V L T NDGN AIL REIDVA HPAA KSMI EL SR TQ D E EV GDGT TS V II L AGEI L A 102
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 126 Q A QYL L WA G LT P AQLRE A FVT A TAEV L TA L PSLA I c SLGPLEDP sw ALYSVMST h TLS naeyl TK L V AQ ---- A C WIS -- 199
Cdd:cd03337 103 V A EPF L ER G IH P TVIIK A YRK A LEDA L KI L EEIS I - PVDVNDRA -- QMLKIIKS - CIG ----- TK F V SR wsdl M C NLA ld 173
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 200 ------ R E P NG SF K PES I ----- V VC I L q GG ILT DSR IIP G IAI c G K -- LCGRKTEVLNDA R VA L FN CP F gpsnpfapat 266
Cdd:cd03337 174 avktva V E E NG RK K EID I kryak V EK I P - GG EIE DSR VLD G VML - N K dv THPKMRRRIENP R IV L LD CP L ---------- 241
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 267 lrlsspe E LIRF rkq TE QVEMEI A ELAMMGINVAVV lgevne R S V DQA D ------ Y CG VMVI qvk S R K E IVYL SD K lgvp 340
Cdd:cd03337 242 ------- E YLVI --- TE KGVSDL A QHYLVKAGITAL ------ R R V RKT D nnriar A CG ATIV --- N R P E ELTE SD V ---- 298
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 341 llnrilpplep G KCHKVYRMEFGESALIM F EW E REIAPFLSVV LRG PTIQG L RGA E QAVYYGIDAFSQLCQD P R L L PG A G 420
Cdd:cd03337 299 ----------- G TGAGLFEVKKIGDEYFT F IT E CKDPKACTIL LRG ASKDV L NEV E RNLQDAMAVARNIILN P K L V PG G G 367
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 421 ATEMA LARM L VD K GSRLD G PNGLAFQ A F A Q AL SSL P K TLA E N A G LAAQSV L A E MSGY H - Q AG N FVI G V - G TD G - L V NVAQ 497
Cdd:cd03337 368 ATEMA VSHA L SE K AKSIE G VEQWPYK A V A S AL EVI P R TLA Q N C G ANVIRT L T E LRAK H a Q GE N STW G I d G ET G d I V DMKE 447
490 500 510
....*....|....*....|....*....|.
gi 83642818 498 E GIWD I L RT KAQ GLQAVTGLVQQ L VTV D Q I I 528
Cdd:cd03337 448 L GIWD P L AV KAQ TYKTAIEAACM L LRI D D I V 478
chap_CCT_zeta
TIGR02347 T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
47-535
4.15e-40
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: 152.97
E-value: 4.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QT L ASIIRSCY GP Y G LQ K F LVS AQ G ETVC T GHAAAI L KALELE HP A A RFVQEL A QT Q AEN TGDGT AFV VLL TEA LL E Q 126
Cdd:TIGR02347 24 AA RG L QDVLKTNL GP K G TL K M LVS GA G DIKL T KDGNVL L NEMQIQ HP T A SMIARA A TA Q DDI TGDGT TST VLL IGE LL K Q 103
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QYLLWA G LT P AQLR E A F VT A TA E V L TA L PSLAICSLGPLEDP sw A L YS V MS T HTLSN ----- A EY LT KL V AQ A CWISRE 201
Cdd:TIGR02347 104 A ERYILE G VH P RIIT E G F EI A RK E A L QF L DKFKVKKEDEVDRE -- F L LN V AR T SLRTK lpadl A DQ LT EI V VD A VLAIKK 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 202 PNGSFKPESIVVCILQGGIL TD SRI I P G -------------------- I AI C G - K L CGR KTEV lndarvalf N CP F GP S N 260
Cdd:TIGR02347 182 DGEDIDLFMVEIMEMKHKSA TD TTL I R G lvldhgarhpdmprrvknay I LT C N v S L EYE KTEV --------- N SG F FY S S 252
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 261 pfap A TL R lssp E E L IRF - RK QTEQVEME I A EL AM ---- MGINVAV V L ge V N ERSV D QADY ----- C G V M VIQVKS R KEI 330
Cdd:TIGR02347 253 ---- A EQ R ---- E K L VKA e RK FVDDRVKK I I EL KK kvcg KSPDKGF V V -- I N QKGI D PPSL dllak E G I M ALRRAK R RNM 322
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 331 VY L SDKL G VPL LN RI -- L P P LEP G KCHK VY RMEF GE SALIMF E w E REIAPFLSVVLR GP TIQGLRGAEQ AV YY G ID A FSQ 408
Cdd:TIGR02347 323 ER L TLAC G GEA LN SV ed L T P ECL G WAGL VY ETTI GE EKYTFI E - E CKNPKSCTILIK GP NDHTIAQIKD AV RD G LR A VKN 401
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 409 LCQ D PRLL PGAGA T E M A LA R M L VDKGSRLD G PNG L AFQ AFA Q AL SSL PKTLAEN A G LA AQ SV L AEMSGY H QA G NF V I GV G 488
Cdd:TIGR02347 402 AIE D KCVV PGAGA F E I A AY R H L KEYKKSVK G KAK L GVE AFA N AL LVI PKTLAEN S G FD AQ DT L VKLEDE H DE G GE V V GV D 481
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 83642818 489 -- T DGLVNVAQE GIWD IL R T K A Q GL Q AV T GLVQ QL VT VD QIIV A RKTPR 535
Cdd:TIGR02347 482 ln T GEPIDPEIK GIWD NY R V K K Q LI Q SA T VIAS QL LL VD EVMR A GRSML 530
TCP1_beta
cd03336 TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
42-535
1.88e-39
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: 150.94
E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 42 L RATAA A QTLASIIRSCY GP Y G LQ K F L V S A -- Q G ETVC T GHA A A ILK ALELEH PAA RFVQELAQT Q AENT GDGT AF V VL L 119
Cdd:cd03336 16 L SSFVG A IAIGDLVKTTL GP K G MD K I L Q S V gr S G GVTV T NDG A T ILK SIGVDN PAA KVLVDISKV Q DDEV GDGT TS V TV L 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 120 TEA LL EQ A QY L LWAGLT P AQLR E AFVT ATA EVLT AL P S L A ICSLGPL E DPSWA L YSVMS T h TLS ------ NA E YLTK L VA 193
Cdd:cd03336 96 AAE LL RE A EK L VAQKIH P QTII E GYRM ATA AARE AL L S S A VDHSSDE E AFRED L LNIAR T - TLS skiltq DK E HFAE L AV 174
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 194 Q A cw IS R E p N GS FKPES I VVCILQ GG I L T DS RIIP G IAICG K LCGRKTEVLND A RVALF N C P -------- FG psnpfap A 265
Cdd:cd03336 175 D A -- VL R L - K GS GNLDA I QIIKKL GG S L K DS YLDE G FLLDK K IGVNQPKRIEN A KILIA N T P mdtdkiki FG ------- A 244
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 266 TL R LS S PEEL irfrkqteq V E M E I AE LAM M ---------- GIN VAV ----------- VLGEVNERSVDQ AD YC GV MVIQV 324
Cdd:cd03336 245 KV R VD S TAKV --------- A E I E E AE KEK M knkvekilkh GIN CFI nrqliynypeq LFADAGIMAIEH AD FD GV ERLAL 315
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 325 KSRK EI VYLS D K lgv P L L NRI lpplep G K C HKVYRMEF GE SA LI M F EWERE i APFLSV VLRG PTI Q G L RG AE QAVYYGID 404
Cdd:cd03336 316 VTGG EI ASTF D H --- P E L VKL ------ G T C KLIEEIMI GE DK LI R F SGVAA - GEACTI VLRG ASQ Q I L DE AE RSLHDALC 385
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 405 AFS Q LCQ D P R LLP G A G AT EM AL A RMLVDKGSRLD G PNG LA FQ AFA Q AL SS LP KTL A E NAG LAAQSVL A EMSGY H QA GN FV 484
Cdd:cd03336 386 VLA Q TVK D T R VVL G G G CS EM LM A KAVEELAKKTP G KKS LA IE AFA K AL RQ LP TII A D NAG YDSAELV A QLRAA H YN GN TT 465
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 83642818 485 I G V ---- GT D G lv NVAQE GI WDILRT K A Q G L QAVTGLVQQLVT VD Q II VAR kt PR 535
Cdd:cd03336 466 A G L dmrk GT V G -- DMKEL GI TESFKV K R Q V L LSASEAAEMILR VD D II KCA -- PR 516
chap_CCT_beta
TIGR02341 T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
42-535
4.16e-38
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: 147.31
E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 42 L RATAA A QTLASIIR S CY GP Y G LQ K F L V S AQGETVC -- T GHA A A ILK ALELEH PAA RFVQELAQT Q AENT GDGT AF V VL L 119
Cdd:TIGR02341 17 L SSFVG A IAIGDLVK S TL GP K G MD K I L Q S SSSDASI mv T NDG A T ILK SIGVDN PAA KVLVDMSKV Q DDEV GDGT TS V TV L 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 120 TEA LL EQ A QY L LWAGLT P AQLREAFVT AT AEVLT AL PSL A ICS ---- LGPLE D PSWALYSVM S THT LS - NAEYLTK L VAQ 194
Cdd:TIGR02341 97 AAE LL RE A EK L INQKIH P QTIIAGYRE AT KAARD AL LKS A VDN gsde VKFRQ D LMNIARTTL S SKI LS q HKDHFAQ L AVD 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 195 A cw IS R E p N GS FKP E S I VVCILQ GG I L T DS RIIP G IAICG K LCGRKTEVLND A RVALF N CP -------- FG psnpfap AT 266
Cdd:TIGR02341 177 A -- VL R L - K GS GNL E A I QIIKKL GG S L A DS YLDE G FLLDK K IGVNQPKRIEN A KILIA N TG mdtdkvki FG ------- SR 246
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 267 L R LS S PEELIRFRK - QT E QVEMEIAELAMM GIN VAV ----------- VLGEVNERSVDQ AD YC GV MVIQVKSRK EIV YLS 334
Cdd:TIGR02341 247 V R VD S TAKVAELEH a EK E KMKEKVEKILKH GIN CFI nrqliynypeq LFADAGVMAIEH AD FE GV ERLALVTGG EIV STF 326
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 335 D K lgv P L L NRI lpplep G K C HKVYRMEF GE SA L IM F E w EREIAPFLSV VLRG P T I Q G L RG AE QAVYYGIDAF SQ LCQDP R 414
Cdd:TIGR02341 327 D H --- P E L VKL ------ G S C DLIEEIMI GE DK L LK F S - GVKLGEACTI VLRG A T Q Q I L DE AE RSLHDALCVL SQ TVKES R 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 415 LLP G A G AT EM ALARMLVDKGS R LD G PNG LA FQ AFA Q AL SS LP KTL A E NAG LAAQSVL A EMSGY H QA GN FVI G VGTDG -- L 492
Cdd:TIGR02341 397 TVL G G G CS EM LMSKAVTQEAQ R TP G KEA LA VE AFA R AL RQ LP TII A D NAG FDSAELV A QLRAA H YN GN TTM G LDMNE gt I 476
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 83642818 493 VNVA Q E GI WDILRT K AQGLQAVTGLVQQLVT VD Q II V A RKTP R 535
Cdd:TIGR02341 477 ADMR Q L GI TESYKV K RAVVSSAAEAAEVILR VD N II K A APRK R 519
chap_CCT_eta
TIGR02345 T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
47-533
6.48e-38
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: 146.83
E-value: 6.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 A AQTL A SIIRSCY GP Y G LQ K FL V SAQ G ETVCTGHA A A ILK A L ELE HPAA RFVQEL A QT Q AENT GDGT AF V VL L TEA LL EQ 126
Cdd:TIGR02345 26 A CVAI A EALKTTL GP R G MD K LI V GSN G KATISNDG A T ILK L L DIV HPAA KTLVDI A KS Q DAEV GDGT TS V TI L AGE LL KE 105
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QYLLWA G LT P AQLREAFVT A TAEVLTALPSL A ICSLGPLEDPSWA L YSVMS T HTL S ----- N A E YLT K LVAQ A cw ISRE 201
Cdd:TIGR02345 106 A KPFIEE G VH P QLIIRCYRE A LSLAVEKIKEI A VTIDEEKGEQREL L EKCAA T ALS S klish N K E FFS K MIVD A -- VLSL 183
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 202 PNGSFKPES I VVCIL QGG I L T DS RIIP G I A I -- CGKLC G -- RKTEVLNDARVA L F N CPFGPSNPFAP A TL R LSSP E EL -- 275
Cdd:TIGR02345 184 DRDDLDLKL I GIKKV QGG A L E DS QLVN G V A F kk TFSYA G fe QQPKKFANPKIL L L N VELELKAEKDN A EI R VEDV E DY qa 263
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 276 ------- I R FRK QTEQ VE --------- ME I AE LA MM ----- G I NV A vvl G E V NERSVDQ - ADY CG VMVIQVK S rkeiv Y L 333
Cdd:TIGR02345 264 ivdaewa I I FRK LEKI VE sganvvlsk LP I GD LA TQ yfadr D I FC A --- G R V SAEDLKR v IKA CG GSIQSTT S ----- D L 335
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 334 SDKL gvpllnrilpple P G K C HKVYRMEF G ESALIM F E w EREI A PFLSVV LRG PTI Q GLRG AE QAVYYG I DAFSQLCQDP 413
Cdd:TIGR02345 336 EADV ------------- L G T C ALFEERQI G SERYNY F T - GCPH A KTCTII LRG GAE Q FIEE AE RSLHDA I MIVRRALKNK 401
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 414 RLLP G A GA T EM A L ARM L V D KGSRL DG PNG L AFQ AFA Q AL SSL P KT L A ENAG LAAQSV L AEMSGY H QA G -- NFVIGVG T DG 491
Cdd:TIGR02345 402 KIVA G G GA I EM E L SKC L R D YSKTI DG KQQ L IIN AFA K AL EII P RQ L C ENAG FDSIEI L NKLRSR H AK G gk WYGVDIN T ED 481
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 83642818 492 LVNVAQEGI W DILRT K AQG L Q A VTGLVQQLVT VD QI I VAR K T 533
Cdd:TIGR02345 482 IGDNFEAFV W EPALV K INA L K A AFEAACTILS VD ET I TNP K S 523
TCP1_epsilon
cd03339 TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
46-529
4.30e-37
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: 144.36
E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 46 A AA QTL A S I I R SCY GP Y G LQ K F LVS AQ GE TVC T GHA A A IL KALELE H PA A RFVQ EL AQT Q AENT GDGT AF VV L L TE ALLE 125
Cdd:cd03339 30 L AA KSV A N I L R TSL GP R G MD K I LVS PD GE VTV T NDG A T IL EKMDVD H QI A KLLV EL SKS Q DDEI GDGT TG VV V L AG ALLE 109
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 126 QA QY LL WA G LT P AQLREAFVT A TAEVLTA L PSL A ICSLGPLEDPSWALYSV M S th T L SN ---------- AE YLTKL V AQA 195
Cdd:cd03339 110 QA EK LL DR G IH P IRIADGYEQ A CKIAVEH L EEI A DKIEFSPDNKEPLIQTA M T -- S L GS kivsrchrqf AE IAVDA V LSV 187
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 196 CWIS R E p NGS F --- K P E SI V vcilq GG I L T D SRIIP GI A I cgklcg R K T ------- EVLN DA RV A LFN CPF G P SN P FAPA 265
Cdd:cd03339 188 ADLE R K - DVN F eli K V E GK V ----- GG R L E D TKLVK GI V I ------ D K D fshpqmp KEVK DA KI A ILT CPF E P PK P KTKH 255
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 266 T L RLS S P E ELIRFRKQTEQ -- V EM e IAELAMM G I N VAVVLGEVN ersv D Q A DYC ---- G VMVIQVKSRK EI vyls DKLGV 339
Cdd:cd03339 256 K L DIT S V E DYKKLQEYEQK yf R EM - VEQVKDA G A N LVICQWGFD ---- D E A NHL llqn G LPAVRWVGGV EI ---- ELIAI 326
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 340 PLLN RI L P PL E P ------ GK CHK V YRME FG ESA -- LIMF E WERE i APFLSVVL RG PTIQGLRG A EQAVYYGIDAFSQ L CQ 411
Cdd:cd03339 327 ATGG RI V P RF E D lspekl GK AGL V REIS FG TTK dk MLVI E GCPN - SKAVTIFI RG GNKMIIEE A KRSLHDALCVVRN L IR 405
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 412 D P R LLP G A GA T E MALARMLVDKGSRLD G PNGL A FQ AFA Q AL S S L P KT LAEN A GL AAQSV L A E MSGYH - QAG N FVI G VGT - 489
Cdd:cd03339 406 D N R IVY G G GA A E ISCSLAVEKAADKCS G IEQY A MR AFA D AL E S I P LA LAEN S GL NPIET L S E VKARQ v KEK N PHL G IDC l 485
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 83642818 490 - D G LVNVAQEGIWDI L RT K A Q GLQAV T GL V QQLVTV D QI IV 529
Cdd:cd03339 486 g R G TNDMKEQKVFET L IS K K Q QILLA T QV V KMILKI D DV IV 526
chap_CCT_gamma
TIGR02344 T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
47-528
6.58e-37
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: 143.72
E-value: 6.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A S IIR S C Y GP YGLQ K F L VSAQ G ET V C T GHAA AIL KALELE HPAA RFVQ EL AQ TQ A E NT GDGT AF V VL L TEAL L EQ 126
Cdd:TIGR02344 24 AA KAV A D IIR T C L GP RSML K M L LDPM G GI V M T NDGN AIL REIDVA HPAA KSMI EL SR TQ D E EV GDGT TS V II L AGEM L SV 103
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QYL L WAGLT P AQLRE A FVT A TAEV L TA L PSLA I cslg P L ----- EDPSWALY S VMS T HTL S N - AEYLTK L VAQ A C - WIS 199
Cdd:TIGR02344 104 A EPF L EQNIH P TVIIR A YRK A LDDA L SV L EEIS I ---- P V dvndd AAMLKLIQ S CIG T KFV S R w SDLMCD L ALD A V r TVQ 179
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 200 R EP NG SF -------- K P E S I vvcil Q GG ILT DS RIIP G IA I CGKLCGR K TE - VLNDA R VA L FN CP F ---- G P S NPFA pat 266
Cdd:TIGR02344 180 R DE NG RK eidikrya K V E K I ----- P GG DIE DS CVLK G VM I NKDVTHP K MR r YIENP R IV L LD CP L eykk G E S QTNI --- 251
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 267 lrlsspe E LIRFRKQTEQVE ME IAELAM M GINVAV V LGEV -- N E RS V - D Q A DY ---- CGVMV I QVKSRKEIVYLSDKL G V 339
Cdd:TIGR02344 252 ------- E ITKEEDWNRILQ ME EEYVQL M CEDIIA V KPDL vi T E KG V s D L A QH yllk ANITA I RRVRKTDNNRIARAC G A 324
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 340 PLL NR ILPPL E PG --- K C HKVYRMEF G ESALIMFE w E REIAPFLSVV LRG PTIQG L RGA E QAVYYGIDAFSQLCQ DP R L L 416
Cdd:TIGR02344 325 TIV NR PEELR E SD vgt G C GLFEVKKI G DEYFTFIT - E CKDPKACTIL LRG ASKDI L NEV E RNLQDAMAVARNVLL DP K L V 403
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 417 PG A GATEMA LARM L VD K GSR L D G PNGLAFQ A F A Q AL SSL P K TLA E N A G LAAQSV L A E MSGY H - Q AG N FVI G V - G TD G - L V 493
Cdd:TIGR02344 404 PG G GATEMA VSVA L TE K SKK L E G VEQWPYR A V A D AL EII P R TLA Q N C G ANVIRT L T E LRAK H a Q EN N CTW G I d G ET G k I V 483
490 500 510
....*....|....*....|....*....|....*
gi 83642818 494 NVAQE GIW DI L RT K A Q GLQAVTGLVQQ L VTV D Q I I 528
Cdd:TIGR02344 484 DMKEK GIW EP L AV K L Q TYKTAIESACL L LRI D D I V 518
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
14-537
7.77e-37
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 143.63
E-value: 7.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 14 QSDLEL PQ R LK L G LE knp E SQ GE ep LCI L RATAA A QTL A SIIRSCY GP Y G LQ K F L VSAQ ----- G ETVC T GHA A A ILK AL 88
Cdd:PTZ00212 2 IMANVP PQ V LK Q G AQ --- E EK GE -- TAR L QSFVG A IAV A DLVKTTL GP K G MD K I L QPMS egprs G NVTV T NDG A T ILK SV 76
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 89 E L EH PAA RFVQELAQ TQ A E NT GDGT AF VV L L TEA LL EQ A QY LL WAGLT P AQLR E AFVT A TAEVLT AL PSL A ICSLGPL E D 168
Cdd:PTZ00212 77 W L DN PAA KILVDISK TQ D E EV GDGT TS VV V L AGE LL RE A EK LL DQKIH P QTII E GWRM A LDVARK AL EEI A FDHGSDE E K 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 169 PSWA L YSVMS T h TLS N ------ AEYLT KL VAQ A cw IS R E p N GS FKPES I VVCILQ GG I L T DS RIIP G ------ I AIC gkl 236
Cdd:PTZ00212 157 FKED L LNIAR T - TLS S klltve KDHFA KL AVD A -- VL R L - K GS GNLDY I QIIKKP GG T L R DS YLED G filekk I GVG --- 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 237 CGRKT E vln DARVALF N C P -------- F G psnpfap A TLRLS S P E EL irfrkqteq V E M E I AE LAM M ---------- G I N 298
Cdd:PTZ00212 230 QPKRL E --- NCKILVA N T P mdtdkiki Y G ------- A KVKVD S M E KV --------- A E I E A AE KEK M knkvdkilah G C N 290
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 299 V AV ----------- VLG E VNERSVDQ AD YC G VMVIQVKSRK EIV YLS D K lgv P LLNRI lpplep G K C HKVYRMEF GE SA L 367
Cdd:PTZ00212 291 V FI nrqliynypeq LFA E AGIMAIEH AD FD G MERLAAALGA EIV STF D T --- P EKVKL ------ G H C DLIEEIMI GE DK L 361
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 368 I M F E - WEREI A pf LSV VLRG PTIQG L RG AE QAVYYGIDAF SQ LCQ D P R LLP G A G AT EM AL A RMLVDKGSRLD G PNG LA FQ 446
Cdd:PTZ00212 362 I R F S g CAKGE A -- CTI VLRG ASTHI L DE AE RSLHDALCVL SQ TVK D T R VVL G G G CS EM LM A NAVEELAKKVE G KKS LA IE 439
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 447 AFA Q AL SSL P KTL A E N A G LAAQSVLAEMSGY H QA GN FVI G VG - TD G L V - NVAQE GI WDILRT K AQG L QAV T GLVQQLVT V 524
Cdd:PTZ00212 440 AFA K AL RQI P TII A D N G G YDSAELVSKLRAE H YK GN KTA G ID m EK G T V g DMKEL GI TESYKV K LSQ L CSA T EAAEMILR V 519
570
....*....|...
gi 83642818 525 D Q II va R KT PR Y R 537
Cdd:PTZ00212 520 D D II -- R CA PR Q R 530
chap_CCT_alpha
TIGR02340 T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
47-480
5.56e-36
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: 141.40
E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A S I IRSCY GP Y GL Q K F LV SAQ G ETVC T GHA A A ILK A LE L EHPAA RFVQ ELAQ T Q AENT GDGT AF VV LLTEA LL EQ 126
Cdd:TIGR02340 20 AA MAI A N I VKTSL GP V GL D K M LV DDI G DVTI T NDG A T ILK L LE V EHPAA KILV ELAQ L Q DREV GDGT TS VV IIAAE LL KR 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QY L LWAGLT P AQLREAFVT A TA E VLTAL - PS L AICS lgp L E DPSW AL YS V ---- MS THTLS - NAEYLTKL V AQ A CWISR 200
Cdd:TIGR02340 100 A DE L VKNKIH P TSVISGYRL A CK E AVKYI k EN L SVSV --- D E LGRE AL IN V akts MS SKIIG l DSDFFSNI V VD A VLAVK 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 201 EP N GSFKP ---- ES I VVCILQ G GILTD S RIIP G I A ICGKLC -- GRKTEVL N d A RV A L -- FN C ----- PF G PS - NPFA P AT 266
Cdd:TIGR02340 177 TT N ENGET kypi KA I NILKAH G KSARE S MLVK G Y A LNCTVA sq QMPKRIK N - A KI A C ld FN L qkakm AL G VQ i VVDD P EK 255
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 267 L rlsspe E L IR F R k QTEQVEME I AELAMM G I NV AVVL G EVNERSVDQADYC G V M VIQVKSRKEIVYLSDKL G VP L LNRI - 345
Cdd:TIGR02340 256 L ------ E Q IR Q R - EADITKER I KKILDA G A NV VLTT G GIDDMCLKYFVEA G A M GVRRCKKEDLKRIAKAT G AT L VSTL a 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 346 ------- LPPLEP G KCHK V YRMEFGESAL I MFEWERE i APFL S VV LRG PTIQG L RGA E QAVYYGIDAFSQLCQDPRLL PG 418
Cdd:TIGR02340 329 dlegeet FEASYL G FADE V VQERIADDEC I LIKGTKK - RKSA S II LRG ANDFM L DEM E RSLHDALCVVKRTLESNSVV PG 407
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83642818 419 A GA T E M AL ARM L VDKGSR L DGPNG LA FQA FA Q AL SSL PKTLA E NA GLAAQSVL A EMSG YH Q A 480
Cdd:TIGR02340 408 G GA V E A AL SIY L ENFATT L GSREQ LA IAE FA R AL LII PKTLA V NA AKDSTELV A KLRA YH A A 469
TCP1_alpha
cd03335 TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
47-480
9.13e-36
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: 140.50
E-value: 9.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 AA QTL A S I IR S CY GP Y GL Q K F LV SAQ G ETVC T GHA A A ILK A LE L EHPAA RFVQ ELAQ T Q AENT GDGT AF VV LLTEA LL EQ 126
Cdd:cd03335 16 AA MAI A N I VK S SL GP V GL D K M LV DDI G DVTI T NDG A T ILK L LE V EHPAA KILV ELAQ L Q DKEV GDGT TS VV IIAAE LL KR 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QY L LWAGLT P AQ -------- LR EA f V TATA E V L talp S LAICS LG -- P L ED psw ALYSV MS THTLS - NAEYLTKL V AQ A 195
Cdd:cd03335 96 A NE L VKQKIH P TT iisgyrla CK EA - V KYIK E H L ---- S ISVDN LG ke S L IN --- VAKTS MS SKIIG a DSDFFANM V VD A 167
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 196 -- CWISREPN G SF K - P - ESIVVCILQ G GILTD S RIIP G I A I - C GKL - C G RK T E V L N d A RV A LFN cp F gpsn PFAPATLR L 269
Cdd:cd03335 168 il AVKTTNEK G KT K y P i KAVNILKAH G KSAKE S YLVN G Y A L n C TRA s Q G MP T R V K N - A KI A CLD -- F ---- NLQKTKMK L 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 270 ------ SS PE E L IRF R KQ ----- T E QVEMEI A E lamm G I NV AVVL G EVNERSVDQADYC G V M VIQVKSRKEIVYLSDKL G 338
Cdd:cd03335 241 gvqvvv TD PE K L EKI R QR esdit K E RIKKIL A A ---- G A NV VLTT G GIDDMCLKYFVEA G A M AVRRVKKEDLRRIAKAT G 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 339 VP L LNRI -------- LP P LEP G KCHK V YRMEF G ESA LI MFEWERE i APFL S VV LRG PTIQG L RGA E QAVYYGIDAFSQLC 410
Cdd:cd03335 317 AT L VSTL anlegeet FD P SYL G EAEE V VQERI G DDE LI LIKGTKK - RSSA S II LRG ANDFM L DEM E RSLHDALCVVKRTL 395
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 411 QDPRLL PG A GA T E M AL ARM L VDKGSR L DGPNG LA FQA FA Q AL SSL PKTLA E NA GLA A QSVL A EMSG YH Q A 480
Cdd:cd03335 396 ESNSVV PG G GA V E T AL SIY L ENFATT L GSREQ LA IAE FA E AL LVI PKTLA V NA AKD A TELV A KLRA YH A A 465
TCP1_zeta
cd03342 TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
40-532
1.60e-32
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: 130.46
E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 40 CILRATA AA QT L ASIIRSCY GP Y G LQ K F LVS AQ G ETVC T GHAAAI L KALELE HP A A RFVQEL A QT Q AEN TGDGT AFV VLL 119
Cdd:cd03342 13 ALAVNIS AA KG L QDVLKTNL GP K G TL K M LVS GA G DIKL T KDGNVL L SEMQIQ HP T A SMIARA A TA Q DDI TGDGT TSN VLL 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 120 TEA LL E QA QYLLWA G LT P AQLR E A F VT A TAEV L TA L P S LAI cslg P L E - D PSWA - L Y SV MS T HTLSN ----- A EY LT KL V 192
Cdd:cd03342 93 IGE LL K QA ERYIQE G VH P RIIT E G F EL A KNKA L KF L E S FKV ---- P V E i D TDRE l L L SV AR T SLRTK lhadl A DQ LT EI V 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 193 AQ A CWISRE P NGSFKPESIVVCIL Q GGILT D SRI I P G I aicgklcgrkte VL ND arvalfncpf G PSN P FA P atlrlssp 272
Cdd:cd03342 169 VD A VLAIYK P DEPIDLHMVEIMQM Q HKSDS D TKL I R G L ------------ VL DH ---------- G ARH P DM P -------- 218
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 273 eelirfr K QT E QV --------- E M E IA E lammg I N VA ---- VV lge V N ERSV D Q ad YC ------- G VMVIQVKS R KEIVY 332
Cdd:cd03342 219 ------- K RV E NA yiltcnvsl E Y E KT E ----- V N SG ffys VV --- I N QKGI D P -- PS ldmlake G ILALRRAK R RNMER 281
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 333 L SDKL G VPLL N RI -- L P P LEP G KCHK VY RMEF GE S ali MFEWEREI - A P FLSVV L - R GP --- TI Q ---- GL R GAEQ AV YY 401
Cdd:cd03342 282 L TLAC G GVAM N SV dd L S P ECL G YAGL VY ERTL GE E --- KYTFIEGV k N P KSCTI L i K GP ndh TI T qikd AI R DGLR AV KN 358
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 402 G I D afsqlcq D PRLL PGAGA T E M AL ARM L VDKGSRLD G PNG L AF QAFA Q AL SSL PKTLAEN A GL AA Q SV L AEMSGYHQA G 481
Cdd:cd03342 359 A I E ------- D KCVV PGAGA F E V AL YAH L KEFKKSVK G KAK L GV QAFA D AL LVI PKTLAEN S GL DV Q ET L VKLQDEYAE G 431
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 83642818 482 NF V I GV G -- T DGLVNVAQ EGIWD ILRT K A Q G L QAV T GLVQ QL VT VD Q II V A RK 532
Cdd:cd03342 432 GQ V G GV D ld T GEPMDPES EGIWD NYSV K R Q I L HSA T VIAS QL LL VD E II R A GR 484
TCP1_eta
cd03340 TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
47-533
2.18e-29
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: 122.01
E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 47 A A Q TL A SII R SCY GP Y G LQ K FL V SAQ G ETVCTGHA A A ILK A L ELE HPAA RFVQEL A QT Q AENT GDGT AF VV L L TEAL L EQ 126
Cdd:cd03340 24 A C Q AI A DAV R TTL GP R G MD K LI V DGR G KVTISNDG A T ILK L L DIV HPAA KTLVDI A KS Q DAEV GDGT TS VV V L AGEF L KE 103
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 127 A QYLLWA G LT P AQLREAFVT A TAEVLTALPSL A I - CSLGPL E DPSWA L YSVMS T h T L S ------ NA E YLT K L V AQ A C w I S 199
Cdd:cd03340 104 A KPFIED G VH P QIIIRGYRK A LQLAIEKIKEI A V n IDKEDK E EQREL L EKCAA T - A L N sklias EK E FFA K M V VD A V - L S 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 200 REPNGSFK pe S I VVCILQ GG I L T DS RIIP G I A I cgklcg R KT ---------- EVLNDARVA L F N CPFGPSNPFAP A TL R L 269
Cdd:cd03340 182 LDDDLDLD -- M I GIKKVP GG S L E DS QLVN G V A F ------ K KT fsyagfeqqp KKFKNPKIL L L N VELELKAEKDN A EV R V 253
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 270 SS PEE L --------- I RFR K QTEQ V E --------- ME I AE LA MM ----- G I NV A vvl G E V N E --- RS V D QA dy C G VMVIQ 323
Cdd:cd03340 254 ED PEE Y qaivdaewk I IYD K LEKI V K sganvvlsk LP I GD LA TQ yfadr D I FC A --- G R V P E edl KR V A QA -- T G GSIQT 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 324 VK S R keiv YLS D K L gvpllnrilpplep G K C HKVYRMEF G ESALIM F E w EREI A PFLSVV LRG PTI Q GLRG AE QAVYYG I 403
Cdd:cd03340 329 TV S N ---- ITD D V L -------------- G T C GLFEERQV G GERYNI F T - GCPK A KTCTII LRG GAE Q FIEE AE RSLHDA I 389
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 404 DAFSQLCQDPRLLP G A GA T EM A L ARM L V D KGSRLD G PNG L AFQ AFA Q AL SSL P KT L AE NAG LA A QSV L AEMSGY H QA G NF 483
Cdd:cd03340 390 MIVRRAIKNDSVVA G G GA I EM E L SKY L R D YSRTIA G KQQ L VIN AFA K AL EII P RQ L CD NAG FD A TDI L NKLRQK H AQ G GG 469
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 83642818 484 V - I GV -- GTD G LVNVAQEGI W DILRT K AQG L Q A V T GLVQQLVT VD QI I VAR K T 533
Cdd:cd03340 470 K w Y GV di NNE G IADNFEAFV W EPSLV K INA L T A A T EAACLILS VD ET I KNP K S 522
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
46-534
4.43e-29
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 120.57
E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 46 AAAQT LA SIIRSCY GP Y G LQKF LV SAQ G ETVC T GHAAA I L K AL ELE H P ---- A A RF V Q E L A QTQAENT GDGT AFVVL L TE 121
Cdd:COG0459 17 RGVKA LA DAVKVTL GP K G RNVM LV KSF G DPTI T NDGVT I A K EI ELE D P fenm G A QL V K E V A SKTNDEA GDGT TTATV L AG 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 122 ALL EQAQY L LW AG LT P AQLREAFVT A TAEVLTA L PSL A I cslg P LE D PSW a L YS V MST h TLSNA E YLTK L V A Q A cw ISR - 200
Cdd:COG0459 97 ALL KEGLK L VA AG AN P TDIKRGIDK A VEKAVEE L KKI A K ---- P VD D KEE - L AQ V ATI - SANGD E EIGE L I A E A -- MEK v 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 201 EPN G SFKP E SI vvcilq G G IL T DSRIIP G IAI -------- CGKLCGRKTEV L ND A RVA L FNCP fgpsnpfapatlr L SS P 272
Cdd:COG0459 169 GKD G VITV E EG ------ K G LE T ELEVVE G MQF dkgylspy FVTDPEKMPAE L EN A YIL L TDKK ------------- I SS I 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 273 EE L IRFRKQT ----------- E QVEM E I - A E L A --- MM G I - N V AV V -- L G EVNE R S --- V D Q A DYC G VM VI qvksrkeiv 331
Cdd:COG0459 230 QD L LPLLEKV aqsgkplliia E DIDG E A l A T L V vng IR G V l R V VA V ka P G FGDR R K aml E D I A ILT G GR VI --------- 300
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 332 yl S DK LG VP L LNRI L PP L ep G KCHK V yrm E FGESALIMF E w EREIAPFLSVVLRGP T ---------- IQ - G L RGAEQ AV Y 400
Cdd:COG0459 301 -- S ED LG LK L EDVT L DD L -- G RAKR V --- E VDKDNTTIV E - GAGNPKAIVILVGAA T evevkerkrr VE d A L HATRA AV E 372
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 401 Y GI dafsqlcqdprl L PG A GA TEMAL AR M L VDKGSR L D G PNG L AFQAF A Q AL SSLPKTL AENAGL AAQS V LAEMSG y HQA 480
Cdd:COG0459 373 E GI ------------ V PG G GA ALLRA AR A L RELAAK L E G DEQ L GIEIV A R AL EAPLRQI AENAGL DGSV V VEKVRA - AKD 439
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 83642818 481 GN F VIGVG T DGL V NVAQE G IW D ILRT K AQG LQ A --- V T GL vqq LV T VDQI I VARKTP 534
Cdd:COG0459 440 KG F GFDAA T GEY V DMLEA G VI D PAKV K RSA LQ N aas V A GL --- IL T TEAV I ADKPEK 493
PRK14104
PRK14104 chaperonin GroEL; Provisional
43-155
4.72e-05
chaperonin GroEL; Provisional
Pssm-ID: 172594
Cd Length: 546
Bit Score: 46.18
E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83642818 43 R ATAAAQT LA SIIRSCY GP Y G LQKF L VSAQ G ETVC T GHAAAIL K AL EL ---- E HPA A RF V Q E L A QTQ A ENT GDGT AFVVL 118
Cdd:PRK14104 15 R MLRGVDI LA NAVKVTL GP K G RNVV L DKSF G APRI T KDGVTVA K EI EL edkf E NMG A QM V R E V A SKS A DAA GDGT TTATV 94
90 100 110
....*....|....*....|....*....|....*..
gi 83642818 119 L TE A LLEQAQYLLW AG LT P AQ L REAFVT A TAE V LTA L 155
Cdd:PRK14104 95 L AQ A IVREGAKSVA AG MN P MD L KRGIDL A VEA V VAD L 131
Blast search parameters
Data Source:
Precalculated data, version = cdd.v.3.21
Preset Options: Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
