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T-complex protein 1 subunit zeta isoform b [Homo sapiens]
Protein Classification
List of domain hits
Name
Accession
Description
Interval
E-value
chap_CCT_zeta super family
cl28957
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485
0e+00
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
The actual alignment was detected with superfamily member TIGR02347 :Pssm-ID: 274088 [Multi-domain]
Cd Length: 531
Bit Score: 857.50
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 3 A VK T LNPKAE VA R AQ AAL AV NI S AARGLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL H EM --------------- 67
Cdd:TIGR02347 1 S VK L LNPKAE SL R RD AAL MM NI N AARGLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL N EM qiqhptasmiaraat 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------------------ G L HPRIITEGFE A A KEK ALQFL EEV KV SR E -- M DRE T L ID VARTSLRTK V 115
Cdd:TIGR02347 81 aqdditgdgttstvlligellkqaeryile G V HPRIITEGFE I A RKE ALQFL DKF KV KK E de V DRE F L LN VARTSLRTK L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 H A E LAD V LTE A VVD SI LAIKK QD E P IDLFM I EIMEMKHKS E TDT S LIRGLVLDHGARHPDM KK RV ED AYILTCNVSLEYE 195
Cdd:TIGR02347 161 P A D LAD Q LTE I VVD AV LAIKK DG E D IDLFM V EIMEMKHKS A TDT T LIRGLVLDHGARHPDM PR RV KN AYILTCNVSLEYE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 196 KTEVNSGFFY K SAE E REKLVKAERKF IE DRVKKIIELK R KVCG D S - DKGFVVINQKGIDP F SLD A L S KEGI V ALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFY S SAE Q REKLVKAERKF VD DRVKKIIELK K KVCG K S p DKGFVVINQKGIDP P SLD L L A KEGI M ALRRAKRR 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 275 NMERLTLACGG V ALNS FD DL S P D CLG H AGLVYE Y T L GEEK F TFIE K C N NP R S V T L LIKGPN K HT LT QIKDAVRDGLRAVK 354
Cdd:TIGR02347 321 NMERLTLACGG E ALNS VE DL T P E CLG W AGLVYE T T I GEEK Y TFIE E C K NP K S C T I LIKGPN D HT IA QIKDAVRDGLRAVK 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 355 NAI D D G CVVPGAGA V E V A MAEA L IKH K P SVKG R A Q LGV Q AFA D ALL I IPK V LA Q NSGFD L Q E TLVK IQA EH S E S G QL VGV 434
Cdd:TIGR02347 401 NAI E D K CVVPGAGA F E I A AYRH L KEY K K SVKG K A K LGV E AFA N ALL V IPK T LA E NSGFD A Q D TLVK LED EH D E G G EV VGV 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58331171 435 DLNTGEP MVAAEV G V WDNY C VKKQL LH S C TVIA TNI LLVDE I MRAG M S S LK 485
Cdd:TIGR02347 481 DLNTGEP IDPEIK G I WDNY R VKKQL IQ S A TVIA SQL LLVDE V MRAG R S M LK 531
Name
Accession
Description
Interval
E-value
chap_CCT_zeta
TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485
0e+00
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain]
Cd Length: 531
Bit Score: 857.50
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 3 A VK T LNPKAE VA R AQ AAL AV NI S AARGLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL H EM --------------- 67
Cdd:TIGR02347 1 S VK L LNPKAE SL R RD AAL MM NI N AARGLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL N EM qiqhptasmiaraat 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------------------ G L HPRIITEGFE A A KEK ALQFL EEV KV SR E -- M DRE T L ID VARTSLRTK V 115
Cdd:TIGR02347 81 aqdditgdgttstvlligellkqaeryile G V HPRIITEGFE I A RKE ALQFL DKF KV KK E de V DRE F L LN VARTSLRTK L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 H A E LAD V LTE A VVD SI LAIKK QD E P IDLFM I EIMEMKHKS E TDT S LIRGLVLDHGARHPDM KK RV ED AYILTCNVSLEYE 195
Cdd:TIGR02347 161 P A D LAD Q LTE I VVD AV LAIKK DG E D IDLFM V EIMEMKHKS A TDT T LIRGLVLDHGARHPDM PR RV KN AYILTCNVSLEYE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 196 KTEVNSGFFY K SAE E REKLVKAERKF IE DRVKKIIELK R KVCG D S - DKGFVVINQKGIDP F SLD A L S KEGI V ALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFY S SAE Q REKLVKAERKF VD DRVKKIIELK K KVCG K S p DKGFVVINQKGIDP P SLD L L A KEGI M ALRRAKRR 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 275 NMERLTLACGG V ALNS FD DL S P D CLG H AGLVYE Y T L GEEK F TFIE K C N NP R S V T L LIKGPN K HT LT QIKDAVRDGLRAVK 354
Cdd:TIGR02347 321 NMERLTLACGG E ALNS VE DL T P E CLG W AGLVYE T T I GEEK Y TFIE E C K NP K S C T I LIKGPN D HT IA QIKDAVRDGLRAVK 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 355 NAI D D G CVVPGAGA V E V A MAEA L IKH K P SVKG R A Q LGV Q AFA D ALL I IPK V LA Q NSGFD L Q E TLVK IQA EH S E S G QL VGV 434
Cdd:TIGR02347 401 NAI E D K CVVPGAGA F E I A AYRH L KEY K K SVKG K A K LGV E AFA N ALL V IPK T LA E NSGFD A Q D TLVK LED EH D E G G EV VGV 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58331171 435 DLNTGEP MVAAEV G V WDNY C VKKQL LH S C TVIA TNI LLVDE I MRAG M S S LK 485
Cdd:TIGR02347 481 DLNTGEP IDPEIK G I WDNY R VKKQL IQ S A TVIA SQL LLVDE V MRAG R S M LK 531
TCP1_zeta
cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
7-481
0e+00
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain]
Cd Length: 484
Bit Score: 819.58
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 7 LNPKAEV A R AQA ALAVNISAA R GLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL H EM ------------------- 67
Cdd:cd03342 1 LNPKAEV L R RGQ ALAVNISAA K GLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL S EM qiqhptasmiaraataqdd 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------------------- G L HPRIITEGFE A AK E KAL Q FLE EV KV SR E M -- DRE T L ID VARTSLRTK V HA E L 119
Cdd:cd03342 81 itgdgttsnvlligellkqaeryiqe G V HPRIITEGFE L AK N KAL K FLE SF KV PV E I dt DRE L L LS VARTSLRTK L HA D L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 120 AD V LTE A VVD SI LAI K K Q DEPIDL F M I EIM E M K HKS ET DT S LIRGLVLDHGARHPDM K KRVE D AYILTCNVSLEYEKTEV 199
Cdd:cd03342 161 AD Q LTE I VVD AV LAI Y K P DEPIDL H M V EIM Q M Q HKS DS DT K LIRGLVLDHGARHPDM P KRVE N AYILTCNVSLEYEKTEV 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 NSGFFY K saeereklvkaerkfiedrvkkiielkrkvcgdsdkgf VVINQKGIDP F SLD A L S KEGI V ALRRAKRRNMERL 279
Cdd:cd03342 241 NSGFFY S -------------------------------------- VVINQKGIDP P SLD M L A KEGI L ALRRAKRRNMERL 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 280 TLACGGVA L NS F DDLSP D CLG H AGLVYE Y TLGEEK F TFIE KCN NP R S V T L LIKGPN K HT L TQIKDA V RDGLRAVKNAI D D 359
Cdd:cd03342 283 TLACGGVA M NS V DDLSP E CLG Y AGLVYE R TLGEEK Y TFIE GVK NP K S C T I LIKGPN D HT I TQIKDA I RDGLRAVKNAI E D 362
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 360 G CVVPGAGA V EVA MAEA L IKH K P SVKG R A Q LGVQAFADALL I IPK V LA Q NSG F D L QETLVK I Q A E HS E S GQ LV GVDL N TG 439
Cdd:cd03342 363 K CVVPGAGA F EVA LYAH L KEF K K SVKG K A K LGVQAFADALL V IPK T LA E NSG L D V QETLVK L Q D E YA E G GQ VG GVDL D TG 442
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 58331171 440 EPM VAAEV G V WDNY C VK K Q L LHS C TVIA TNI LLVDEI M RAG M 481
Cdd:cd03342 443 EPM DPESE G I WDNY S VK R Q I LHS A TVIA SQL LLVDEI I RAG R 484
Cpn60_TCP1
pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-480
2.29e-178
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: 509.05
E-value: 2.29e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 30 L Q D VL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L H E M ------------------------------------------ 67
Cdd:pfam00118 1 L A D IV RT S LGPKG MD KMLV NSG GD VTV T N DG ATI L K E L eiqhpaakllveaakaqdeevgdgtttvvvlagelleeaekl 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 --- G L HP RI I T EG F E A A K EKAL QF L EEVKV -- SREM DRE T L ID VARTSL RT K VHAELA D V L TEA VVD SI LAI K K Q D EPI D 142
Cdd:pfam00118 81 laa G V HP TT I I EG Y E K A L EKAL EI L DSIIS ip VEDV DRE D L LK VARTSL SS K IISRES D F L AKL VVD AV LAI P K N D GSF D 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 143 L FM I EIMEMKHK S ET D TS L IR G L VLD H G AR HPDM K KR V E D A YI L TC N V SLEYEKTE VNSGFFYKS AE ER E KLV KAE RKF I 222
Cdd:pfam00118 161 L GN I GVVKILGG S LE D SE L VD G V VLD K G PL HPDM P KR L E N A KV L LL N C SLEYEKTE TKATVVLSD AE QL E RFL KAE EEQ I 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 223 EDR V K KII ELKRK V cgdsdkgfv V IN QKGID PFS L DA L S K E GI V ALRR A K R R NM ERL TL A C G GV A LN S F DDL S PD C LG H A 302
Cdd:pfam00118 241 LEI V E KII DSGVN V --------- V VC QKGID DLA L HF L A K N GI M ALRR V K K R DL ERL AK A T G AR A VS S L DDL T PD D LG T A 311
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 303 G L V Y E YTL G E EK F TFIE K C NN P RSV T L L IK G PNK H T L TQ I KDAVR D G L RA VKNAI D D GC VVPG A GAVE VAM A E AL IKHKP 382
Cdd:pfam00118 312 G K V E E EKI G D EK Y TFIE G C KS P KAA T I L LR G ATD H V L DE I ERSIH D A L CV VKNAI E D PR VVPG G GAVE MEL A R AL REYAK 391
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 383 SV K G RA QL GVQ AFA D AL LI IPK V LA Q N S G F D LQ E T L VKIQ A E H SESGQLV G V D LN TGE PMVAA E V GV W D NYC VK K Q L L H S 462
Cdd:pfam00118 392 SV S G KE QL AIE AFA E AL EV IPK T LA E N A G L D PI E V L AELR A A H ASGEKHA G I D VE TGE IIDMK E A GV V D PLK VK R Q A L K S 471
490
....*....|....*...
gi 58331171 463 C T VI A TN IL LV D E I MR A G 480
Cdd:pfam00118 472 A T EA A ST IL RI D D I IK A K 489
thermosome_alpha
NF041082
thermosome subunit alpha;
19-480
6.37e-114
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 345.72
E-value: 6.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI S AA RGLQDVL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L H EM ------------------------------- 67
Cdd:NF041082 18 A QRN NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GD VVI T N DG VTI L K EM diehpaakmivevaktqddevgdgtttavvl 97
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------- GL HP R II T EG FEA A K EKAL QF L E E VKVS - REM D R ETL IDV A R T SLRT K VHAELA D V L TEA VVD SIL 132
Cdd:NF041082 98 agellkkaeelldq DI HP T II A EG YRL A A EKAL EI L D E IAIK v DPD D K ETL KKI A A T AMTG K GAEAAK D K L ADL VVD AVK 177
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 133 A I -- K KQDEPI DL FM I EIMEMKHK S ET D TS L IR G L V L D HGAR HP D M K KRVE D A Y I LTCNVS LE YE KTE VNSGFFYKSAEE 210
Cdd:NF041082 178 A V ae K DGGYNV DL DN I KVEKKVGG S IE D SE L VE G V V I D KERV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAKISITDPDQ 257
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 211 REKLVKA E R K FIEDR V K KI IELKRK vcgdsdkgf VV IN QKGID PFSLDA L S KEGI V A L RR A K RRN ME R L TL A C G GVALN S 290
Cdd:NF041082 258 LQAFLDQ E E K MLKEM V D KI ADSGAN --------- VV FC QKGID DLAQHY L A KEGI L A V RR V K KSD ME K L AK A T G ARIVT S 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 291 F DDLSP DC LG H AGLV Y E YTL G EE K FT F I E K C N NP RS VT L L IK G PNK H TLTQIKD A VR D G LR A V KNAID DG C VV P G A GA V E 370
Cdd:NF041082 329 I DDLSP ED LG Y AGLV E E RKV G GD K MI F V E G C K NP KA VT I L LR G GTE H VVDEVER A LE D A LR V V RVVLE DG K VV A G G GA P E 408
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 371 V AM A EA L IKHKP SV K GR A QL GVQ AFA D AL L IIP KV LA Q N S G F D LQET LV KIQAE H SESGQLV G V D LN TG EPMVAA E V GV W 450
Cdd:NF041082 409 V EL A LR L REYAA SV G GR E QL AIE AFA E AL E IIP RT LA E N A G L D PIDA LV ELRSA H EKGNKTA G L D VY TG KVVDML E I GV V 488
490 500 510
....*....|....*....|....*....|
gi 58331171 451 DNYC VK K Q LLH S C T VI A TN IL LV D EIMR A G 480
Cdd:NF041082 489 EPLR VK T Q AIK S A T EA A VM IL RI D DVIA A A 518
thermosome_beta
NF041083
thermosome subunit beta;
19-480
7.96e-114
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 345.40
E-value: 7.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI S AA RGLQDVL RT N LGPKG TM KMLV SGA GDI KL T K DG NVL L H EM ------------------------------- 67
Cdd:NF041083 18 A QRN NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GDI VI T N DG ATI L K EM dvqhpaakmlvevaktqddevgdgtttavvl 97
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------- GL HP R II TE G FEA A K EKA LQF L E E V -- KV SRE m DRETL IDV A R TSL RT K VHA E LA D V L T E AV V DSI 131
Cdd:NF041083 98 agellkkaeelldq NI HP T II AN G YRL A A EKA IEI L D E I ae KV DPD - DRETL KKI A E TSL TS K GVE E AR D Y L A E IA V KAV 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 132 LAIKKQDEP --- I DL FM I E I MEMKHK S ET DT S LI R G L V L D HGAR HP D M K KRVE D A Y I LTCNVS LE YE KTE VNSGFFYKSA 208
Cdd:NF041083 177 KQVAEKRDG kyy V DL DN I Q I EKKHGG S IE DT Q LI Y G I V I D KEVV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAEIRITDP 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 EERE K LVKA E R K FIEDR V K KI IELKRK vcgdsdkgf VV IN QKGID PFSLDA L S K E GI V A L RR A K RRN ME R L TL A C G GVAL 288
Cdd:NF041083 257 DQLQ K FLDQ E E K MLKEM V D KI KATGAN --------- VV FC QKGID DLAQHY L A K A GI L A V RR V K KSD ME K L AK A T G ARIV 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSF DDL S P DC LG H A G LV Y E YTL G EE K FT F I E K C N NP RS VT L LI K G PNK H TLTQIKD A VR D G L RA V KN A ID DG CV V P G A GA 368
Cdd:NF041083 328 TNI DDL T P ED LG Y A E LV E E RKV G DD K MV F V E G C K NP KA VT I LI R G GTE H VVDEAER A LE D A L SV V AD A VE DG KI V A G G GA 407
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 369 V EV AM A EA L IKHKPS V K GR A QL G V Q AFA D AL L IIP KV LA Q N S G F D LQET LVK IQAE H SESGQLV G VDLN TGE PMVAA E V G 448
Cdd:NF041083 408 P EV EL A KR L REYAAT V G GR E QL A V E AFA E AL E IIP RT LA E N A G L D PIDI LVK LRSA H EKGKKWA G INVF TGE VVDMW E L G 487
490 500 510
....*....|....*....|....*....|..
gi 58331171 449 V WDNYC VK K Q LLH S C T VI AT N IL LV D EIMR A G 480
Cdd:NF041083 488 V IEPLR VK T Q AIK S A T EA AT M IL RI D DVIA A K 519
GroEL
COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-479
5.44e-62
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 209.93
E-value: 5.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI SAARG L Q D VLRTN LGPKG TMK MLV SGA GD IKL T K DG NVLLH E M ------------------------------- 67
Cdd:COG0459 11 A RRA NI RGVKA L A D AVKVT LGPKG RNV MLV KSF GD PTI T N DG VTIAK E I eledpfenmgaqlvkevasktndeagdgttt 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------ G LH P RI I TE G FEA A K EKA LQF L EE -- VK V S rem D R E T L ID VA RT S LRTK vh A E LADVLT EA V 127
Cdd:COG0459 91 atvlagallkeglklvaa G AN P TD I KR G IDK A V EKA VEE L KK ia KP V D --- D K E E L AQ VA TI S ANGD -- E E IGELIA EA M 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 128 vdsi LAIK K QDE pidl FMI E imem KH K S - ET DTSLIR G LVL D H G ARH P D ------- M KKRV E D AYIL TCNVSLE yektev 199
Cdd:COG0459 166 ---- EKVG K DGV ---- ITV E ---- EG K G l ET ELEVVE G MQF D K G YLS P Y fvtdpek M PAEL E N AYIL LTDKKIS ------ 227
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 nsgffyk S AEEREK L vkaerkfiedr VK K IIELKRK vcgdsdkgf VV I NQKG ID PFS L DA L SKE GI VALR R A -------- 271
Cdd:COG0459 228 ------- S IQDLLP L ----------- LE K VAQSGKP --------- LL I IAED ID GEA L AT L VVN GI RGVL R V vavkapgf 280
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 272 - K RR N -- M E RLTLAC GG VALN ----- SFD D LSP D C LG H A GL V YE ytl GEEKF T FI E KCN NP RSVTL L IKGPNKHTLTQI K 343
Cdd:COG0459 281 g D RR K am L E DIAILT GG RVIS edlgl KLE D VTL D D LG R A KR V EV --- DKDNT T IV E GAG NP KAIVI L VGAATEVEVKER K 357
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 344 DA V R D G L R A VKN A IDD G c V VPG A GA VEVAM A E AL IKHKPSVK G RA QLG VQAF A D AL LIIPKVL A Q N S G F D LQETLV K IQ A 423
Cdd:COG0459 358 RR V E D A L H A TRA A VEE G - I VPG G GA ALLRA A R AL RELAAKLE G DE QLG IEIV A R AL EAPLRQI A E N A G L D GSVVVE K VR A 436
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 58331171 424 EHSES gql V G V D LN TGE P -- M VA A ev GV W D NYC VK KQL L HSCTVI A TN IL LVDEIMRA 479
Cdd:COG0459 437 AKDKG --- F G F D AA TGE Y vd M LE A -- GV I D PAK VK RSA L QNAASV A GL IL TTEAVIAD 489
PTZ00212
PTZ00212
T-complex protein 1 subunit beta; Provisional
10-479
2.87e-57
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 198.33
E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 10 K A E V AR A Q aalav NISA A RGLQ D VLR T N LGPKG TM K M L VS ----- GA G DIKL T K DG NVL L HEMG L --------------- 69
Cdd:PTZ00212 19 K G E T AR L Q ----- SFVG A IAVA D LVK T T LGPKG MD K I L QP msegp RS G NVTV T N DG ATI L KSVW L dnpaakilvdisktq 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 70 ------------------------------ HP RI I T EG FEA A KEK A LQF LEE VKVSREM D ---- R E T L IDV ART S L RT K V 115
Cdd:PTZ00212 94 deevgdgttsvvvlagellreaeklldqki HP QT I I EG WRM A LDV A RKA LEE IAFDHGS D eekf K E D L LNI ART T L SS K L 173
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 HAELA D VLTEAV VD SI L AI K KQ dep ID L FM I E I MEMKHKSET D TS L IR G LV L DH -- G ARH P dmk KR V E DAY IL TC N VSLE 193
Cdd:PTZ00212 174 LTVEK D HFAKLA VD AV L RL K GS --- GN L DY I Q I IKKPGGTLR D SY L ED G FI L EK ki G VGQ P --- KR L E NCK IL VA N TPMD 247
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 194 YE K ----- TE V NSGFFY K S AE erek LVK AE RKFIEDR V K KI IELK rkv C G dsdkgf V V IN QKG I DPFSLDALSKE GI V A L 268
Cdd:PTZ00212 248 TD K ikiyg AK V KVDSME K V AE ---- IEA AE KEKMKNK V D KI LAHG --- C N ------ V F IN RQL I YNYPEQLFAEA GI M A I 314
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 269 RR A KRRN MERL TL A C G GVALNS FD DLSPDC LGH AG L VY E YTL GE E K FTFIEK C NNPRSV T LLIK G PNK H T L TQIKDAVR D 348
Cdd:PTZ00212 315 EH A DFDG MERL AA A L G AEIVST FD TPEKVK LGH CD L IE E IMI GE D K LIRFSG C AKGEAC T IVLR G AST H I L DEAERSLH D 394
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 349 G L RAVKNAID D GC VV P G A G AV E VA MA E A LIKHKPS V K G RAQ L GVQ AFA D AL LI IP KVL A Q N S G F D LQ E TLV K IQ AEH SES 428
Cdd:PTZ00212 395 A L CVLSQTVK D TR VV L G G G CS E ML MA N A VEELAKK V E G KKS L AIE AFA K AL RQ IP TII A D N G G Y D SA E LVS K LR AEH YKG 474
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58331171 429 GQLV G V D LNT G EPMVAA E V G VWDN Y C VK KQL L H S C T VI A TN IL L VD E I M R A 479
Cdd:PTZ00212 475 NKTA G I D MEK G TVGDMK E L G ITES Y K VK LSQ L C S A T EA A EM IL R VD D I I R C 525
Name
Accession
Description
Interval
E-value
chap_CCT_zeta
TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485
0e+00
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain]
Cd Length: 531
Bit Score: 857.50
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 3 A VK T LNPKAE VA R AQ AAL AV NI S AARGLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL H EM --------------- 67
Cdd:TIGR02347 1 S VK L LNPKAE SL R RD AAL MM NI N AARGLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL N EM qiqhptasmiaraat 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------------------ G L HPRIITEGFE A A KEK ALQFL EEV KV SR E -- M DRE T L ID VARTSLRTK V 115
Cdd:TIGR02347 81 aqdditgdgttstvlligellkqaeryile G V HPRIITEGFE I A RKE ALQFL DKF KV KK E de V DRE F L LN VARTSLRTK L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 H A E LAD V LTE A VVD SI LAIKK QD E P IDLFM I EIMEMKHKS E TDT S LIRGLVLDHGARHPDM KK RV ED AYILTCNVSLEYE 195
Cdd:TIGR02347 161 P A D LAD Q LTE I VVD AV LAIKK DG E D IDLFM V EIMEMKHKS A TDT T LIRGLVLDHGARHPDM PR RV KN AYILTCNVSLEYE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 196 KTEVNSGFFY K SAE E REKLVKAERKF IE DRVKKIIELK R KVCG D S - DKGFVVINQKGIDP F SLD A L S KEGI V ALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFY S SAE Q REKLVKAERKF VD DRVKKIIELK K KVCG K S p DKGFVVINQKGIDP P SLD L L A KEGI M ALRRAKRR 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 275 NMERLTLACGG V ALNS FD DL S P D CLG H AGLVYE Y T L GEEK F TFIE K C N NP R S V T L LIKGPN K HT LT QIKDAVRDGLRAVK 354
Cdd:TIGR02347 321 NMERLTLACGG E ALNS VE DL T P E CLG W AGLVYE T T I GEEK Y TFIE E C K NP K S C T I LIKGPN D HT IA QIKDAVRDGLRAVK 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 355 NAI D D G CVVPGAGA V E V A MAEA L IKH K P SVKG R A Q LGV Q AFA D ALL I IPK V LA Q NSGFD L Q E TLVK IQA EH S E S G QL VGV 434
Cdd:TIGR02347 401 NAI E D K CVVPGAGA F E I A AYRH L KEY K K SVKG K A K LGV E AFA N ALL V IPK T LA E NSGFD A Q D TLVK LED EH D E G G EV VGV 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58331171 435 DLNTGEP MVAAEV G V WDNY C VKKQL LH S C TVIA TNI LLVDE I MRAG M S S LK 485
Cdd:TIGR02347 481 DLNTGEP IDPEIK G I WDNY R VKKQL IQ S A TVIA SQL LLVDE V MRAG R S M LK 531
TCP1_zeta
cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
7-481
0e+00
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain]
Cd Length: 484
Bit Score: 819.58
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 7 LNPKAEV A R AQA ALAVNISAA R GLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL H EM ------------------- 67
Cdd:cd03342 1 LNPKAEV L R RGQ ALAVNISAA K GLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL S EM qiqhptasmiaraataqdd 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------------------- G L HPRIITEGFE A AK E KAL Q FLE EV KV SR E M -- DRE T L ID VARTSLRTK V HA E L 119
Cdd:cd03342 81 itgdgttsnvlligellkqaeryiqe G V HPRIITEGFE L AK N KAL K FLE SF KV PV E I dt DRE L L LS VARTSLRTK L HA D L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 120 AD V LTE A VVD SI LAI K K Q DEPIDL F M I EIM E M K HKS ET DT S LIRGLVLDHGARHPDM K KRVE D AYILTCNVSLEYEKTEV 199
Cdd:cd03342 161 AD Q LTE I VVD AV LAI Y K P DEPIDL H M V EIM Q M Q HKS DS DT K LIRGLVLDHGARHPDM P KRVE N AYILTCNVSLEYEKTEV 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 NSGFFY K saeereklvkaerkfiedrvkkiielkrkvcgdsdkgf VVINQKGIDP F SLD A L S KEGI V ALRRAKRRNMERL 279
Cdd:cd03342 241 NSGFFY S -------------------------------------- VVINQKGIDP P SLD M L A KEGI L ALRRAKRRNMERL 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 280 TLACGGVA L NS F DDLSP D CLG H AGLVYE Y TLGEEK F TFIE KCN NP R S V T L LIKGPN K HT L TQIKDA V RDGLRAVKNAI D D 359
Cdd:cd03342 283 TLACGGVA M NS V DDLSP E CLG Y AGLVYE R TLGEEK Y TFIE GVK NP K S C T I LIKGPN D HT I TQIKDA I RDGLRAVKNAI E D 362
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 360 G CVVPGAGA V EVA MAEA L IKH K P SVKG R A Q LGVQAFADALL I IPK V LA Q NSG F D L QETLVK I Q A E HS E S GQ LV GVDL N TG 439
Cdd:cd03342 363 K CVVPGAGA F EVA LYAH L KEF K K SVKG K A K LGVQAFADALL V IPK T LA E NSG L D V QETLVK L Q D E YA E G GQ VG GVDL D TG 442
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 58331171 440 EPM VAAEV G V WDNY C VK K Q L LHS C TVIA TNI LLVDEI M RAG M 481
Cdd:cd03342 443 EPM DPESE G I WDNY S VK R Q I LHS A TVIA SQL LLVDEI I RAG R 484
Cpn60_TCP1
pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-480
2.29e-178
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: 509.05
E-value: 2.29e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 30 L Q D VL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L H E M ------------------------------------------ 67
Cdd:pfam00118 1 L A D IV RT S LGPKG MD KMLV NSG GD VTV T N DG ATI L K E L eiqhpaakllveaakaqdeevgdgtttvvvlagelleeaekl 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 --- G L HP RI I T EG F E A A K EKAL QF L EEVKV -- SREM DRE T L ID VARTSL RT K VHAELA D V L TEA VVD SI LAI K K Q D EPI D 142
Cdd:pfam00118 81 laa G V HP TT I I EG Y E K A L EKAL EI L DSIIS ip VEDV DRE D L LK VARTSL SS K IISRES D F L AKL VVD AV LAI P K N D GSF D 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 143 L FM I EIMEMKHK S ET D TS L IR G L VLD H G AR HPDM K KR V E D A YI L TC N V SLEYEKTE VNSGFFYKS AE ER E KLV KAE RKF I 222
Cdd:pfam00118 161 L GN I GVVKILGG S LE D SE L VD G V VLD K G PL HPDM P KR L E N A KV L LL N C SLEYEKTE TKATVVLSD AE QL E RFL KAE EEQ I 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 223 EDR V K KII ELKRK V cgdsdkgfv V IN QKGID PFS L DA L S K E GI V ALRR A K R R NM ERL TL A C G GV A LN S F DDL S PD C LG H A 302
Cdd:pfam00118 241 LEI V E KII DSGVN V --------- V VC QKGID DLA L HF L A K N GI M ALRR V K K R DL ERL AK A T G AR A VS S L DDL T PD D LG T A 311
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 303 G L V Y E YTL G E EK F TFIE K C NN P RSV T L L IK G PNK H T L TQ I KDAVR D G L RA VKNAI D D GC VVPG A GAVE VAM A E AL IKHKP 382
Cdd:pfam00118 312 G K V E E EKI G D EK Y TFIE G C KS P KAA T I L LR G ATD H V L DE I ERSIH D A L CV VKNAI E D PR VVPG G GAVE MEL A R AL REYAK 391
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 383 SV K G RA QL GVQ AFA D AL LI IPK V LA Q N S G F D LQ E T L VKIQ A E H SESGQLV G V D LN TGE PMVAA E V GV W D NYC VK K Q L L H S 462
Cdd:pfam00118 392 SV S G KE QL AIE AFA E AL EV IPK T LA E N A G L D PI E V L AELR A A H ASGEKHA G I D VE TGE IIDMK E A GV V D PLK VK R Q A L K S 471
490
....*....|....*...
gi 58331171 463 C T VI A TN IL LV D E I MR A G 480
Cdd:pfam00118 472 A T EA A ST IL RI D D I IK A K 489
chaperonin_type_I_II
cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
11-478
2.64e-167
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: 480.00
E-value: 2.64e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 11 A E VARAQA A LAV NI S AA RG L Q D VLR T N LGPKG TM KMLV SGA GD IKL T K DG NVL L H E M ----------------------- 67
Cdd:cd00309 1 K E REFGEE A RLS NI N AA KA L A D AVK T T LGPKG MD KMLV DSL GD PTI T N DG ATI L K E I evehpaakllvevaksqddevgd 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ---------------------- G L HP RI I TE G F E A A K EKAL QF L E E VK V S - REM DRE T L ID VA R TSL RT K VHAELA D V L T 124
Cdd:cd00309 81 gtttvvvlagellkeaekllaa G I HP TE I IR G Y E K A V EKAL EI L K E IA V P i DVE DRE E L LK VA T TSL NS K LVSGGD D F L G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 125 E A VVD SI L AIK K QDEPI DL FM I EIMEM K HK S ET D TS L IR G L V L D H G ARH P D M K KR V E D A Y IL TCNVS LEY ektevnsgff 204
Cdd:cd00309 161 E L VVD AV L KVG K ENGDV DL GV I RVEKK K GG S LE D SE L VV G M V F D K G YLS P Y M P KR L E N A K IL LLDCK LEY ---------- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 205 yksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgf VVI NQ KGID PFS L DA L S K E GI V A L RR AKRRNM ER LTL A C G 284
Cdd:cd00309 231 ---------------------------------------- VVI AE KGID DEA L HY L A K L GI M A V RR VRKEDL ER IAK A T G 270
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 285 GVALNSFD DL S P DC LG H AGLV Y E YTL G E EK F TFIE K C NNPRSV T L L IK G PNKHT L TQIKDAVR D G L R AV KN A ID DG CV VP 364
Cdd:cd00309 271 ATIVSRLE DL T P ED LG T AGLV E E TKI G D EK Y TFIE G C KGGKVA T I L LR G ATEVE L DEAERSLH D A L C AV RA A VE DG GI VP 350
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 365 G A GA V E VAMAE AL IKHKPSVK G RA QLG VQ AFADAL LI IP KV LA Q N S G F D LQ E TLV K IQ A E H S E S G QLV G V D LN TGE PMVA 444
Cdd:cd00309 351 G G GA A E IELSK AL EELAKTLP G KE QLG IE AFADAL EV IP RT LA E N A G L D PI E VVT K LR A K H A E G G GNA G G D VE TGE IVDM 430
490 500 510
....*....|....*....|....*....|....
gi 58331171 445 A E V G VW D NYC VK K Q L L H S C T VI A TN IL LV D E I MR 478
Cdd:cd00309 431 K E A G II D PLK VK R Q A L K S A T EA A SL IL TI D D I IV 464
cpn60
cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
19-480
5.73e-115
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: 348.48
E-value: 5.73e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI S AA RGLQDVL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L H EM ------------------------------- 67
Cdd:cd03343 16 A QRM NI A AA KAVAEAV RT T LGPKG MD KMLV DSL GD VTI T N DG ATI L K EM diehpaakmlvevaktqdeevgdgtttavvl 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------- GL HP RI I T EG FEA A K EKAL QF L E E -- V KV SRE m D RE TL IDV A R TSL RT K VHAELA D V L TEA VVD SI 131
Cdd:cd03343 96 agellekaedlldq NI HP TV I I EG YRL A A EKAL EL L D E ia I KV DPD - D KD TL RKI A K TSL TG K GAEAAK D K L ADL VVD AV 174
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 132 L AIKKQDEP --- I DL FM I E I MEMKHK S ET DT S LIRG L V L D HGAR HP D M K KRVE D A Y I LTCNVS LE YE KTE VNSGFFYK S A 208
Cdd:cd03343 175 L QVAEKRDG kyv V DL DN I K I EKKTGG S VD DT E LIRG I V I D KEVV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAKIRIT S P 254
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 EEREKLVKA E RKFIEDR V K KI IELKRK V cgdsdkgfv V IN QKGID PFSLDA L S K E GI V A L RR A K RRN ME R L TL A C G GVAL 288
Cdd:cd03343 255 DQLQAFLEQ E EAMLKEM V D KI ADTGAN V --------- V FC QKGID DLAQHY L A K A GI L A V RR V K KSD ME K L AR A T G AKIV 325
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSF DDL S P DC LG H A G LV Y E YTL G EE K FT F I E K C N NP RS VT L L IK G PNK H TLTQIKD A VR D G LR A V KN A ID DG C VV P G A GA 368
Cdd:cd03343 326 TNI DDL T P ED LG E A E LV E E RKV G DD K MV F V E G C K NP KA VT I L LR G GTE H VVDELER A LE D A LR V V AD A LE DG K VV A G G GA 405
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 369 VE VAM A EA L IKHKP SV K GR A QL G V Q AFADAL LI IP KV LA Q N S G F D LQE TLV KIQ A E H SESGQLV G V D LN TGE PMVAA E V G 448
Cdd:cd03343 406 VE IEL A KR L REYAR SV G GR E QL A V E AFADAL EE IP RT LA E N A G L D PID TLV ELR A A H EKGNKNA G L D VY TGE VVDML E K G 485
490 500 510
....*....|....*....|....*....|..
gi 58331171 449 V WDNYC VKKQ LLH S C T VI AT N IL LV D EIMR A G 480
Cdd:cd03343 486 V IEPLR VKKQ AIK S A T EA AT M IL RI D DVIA A K 517
thermosome_alpha
NF041082
thermosome subunit alpha;
19-480
6.37e-114
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 345.72
E-value: 6.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI S AA RGLQDVL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L H EM ------------------------------- 67
Cdd:NF041082 18 A QRN NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GD VVI T N DG VTI L K EM diehpaakmivevaktqddevgdgtttavvl 97
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------- GL HP R II T EG FEA A K EKAL QF L E E VKVS - REM D R ETL IDV A R T SLRT K VHAELA D V L TEA VVD SIL 132
Cdd:NF041082 98 agellkkaeelldq DI HP T II A EG YRL A A EKAL EI L D E IAIK v DPD D K ETL KKI A A T AMTG K GAEAAK D K L ADL VVD AVK 177
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 133 A I -- K KQDEPI DL FM I EIMEMKHK S ET D TS L IR G L V L D HGAR HP D M K KRVE D A Y I LTCNVS LE YE KTE VNSGFFYKSAEE 210
Cdd:NF041082 178 A V ae K DGGYNV DL DN I KVEKKVGG S IE D SE L VE G V V I D KERV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAKISITDPDQ 257
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 211 REKLVKA E R K FIEDR V K KI IELKRK vcgdsdkgf VV IN QKGID PFSLDA L S KEGI V A L RR A K RRN ME R L TL A C G GVALN S 290
Cdd:NF041082 258 LQAFLDQ E E K MLKEM V D KI ADSGAN --------- VV FC QKGID DLAQHY L A KEGI L A V RR V K KSD ME K L AK A T G ARIVT S 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 291 F DDLSP DC LG H AGLV Y E YTL G EE K FT F I E K C N NP RS VT L L IK G PNK H TLTQIKD A VR D G LR A V KNAID DG C VV P G A GA V E 370
Cdd:NF041082 329 I DDLSP ED LG Y AGLV E E RKV G GD K MI F V E G C K NP KA VT I L LR G GTE H VVDEVER A LE D A LR V V RVVLE DG K VV A G G GA P E 408
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 371 V AM A EA L IKHKP SV K GR A QL GVQ AFA D AL L IIP KV LA Q N S G F D LQET LV KIQAE H SESGQLV G V D LN TG EPMVAA E V GV W 450
Cdd:NF041082 409 V EL A LR L REYAA SV G GR E QL AIE AFA E AL E IIP RT LA E N A G L D PIDA LV ELRSA H EKGNKTA G L D VY TG KVVDML E I GV V 488
490 500 510
....*....|....*....|....*....|
gi 58331171 451 DNYC VK K Q LLH S C T VI A TN IL LV D EIMR A G 480
Cdd:NF041082 489 EPLR VK T Q AIK S A T EA A VM IL RI D DVIA A A 518
thermosome_beta
NF041083
thermosome subunit beta;
19-480
7.96e-114
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 345.40
E-value: 7.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI S AA RGLQDVL RT N LGPKG TM KMLV SGA GDI KL T K DG NVL L H EM ------------------------------- 67
Cdd:NF041083 18 A QRN NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GDI VI T N DG ATI L K EM dvqhpaakmlvevaktqddevgdgtttavvl 97
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 -------------- GL HP R II TE G FEA A K EKA LQF L E E V -- KV SRE m DRETL IDV A R TSL RT K VHA E LA D V L T E AV V DSI 131
Cdd:NF041083 98 agellkkaeelldq NI HP T II AN G YRL A A EKA IEI L D E I ae KV DPD - DRETL KKI A E TSL TS K GVE E AR D Y L A E IA V KAV 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 132 LAIKKQDEP --- I DL FM I E I MEMKHK S ET DT S LI R G L V L D HGAR HP D M K KRVE D A Y I LTCNVS LE YE KTE VNSGFFYKSA 208
Cdd:NF041083 177 KQVAEKRDG kyy V DL DN I Q I EKKHGG S IE DT Q LI Y G I V I D KEVV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAEIRITDP 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 EERE K LVKA E R K FIEDR V K KI IELKRK vcgdsdkgf VV IN QKGID PFSLDA L S K E GI V A L RR A K RRN ME R L TL A C G GVAL 288
Cdd:NF041083 257 DQLQ K FLDQ E E K MLKEM V D KI KATGAN --------- VV FC QKGID DLAQHY L A K A GI L A V RR V K KSD ME K L AK A T G ARIV 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSF DDL S P DC LG H A G LV Y E YTL G EE K FT F I E K C N NP RS VT L LI K G PNK H TLTQIKD A VR D G L RA V KN A ID DG CV V P G A GA 368
Cdd:NF041083 328 TNI DDL T P ED LG Y A E LV E E RKV G DD K MV F V E G C K NP KA VT I LI R G GTE H VVDEAER A LE D A L SV V AD A VE DG KI V A G G GA 407
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 369 V EV AM A EA L IKHKPS V K GR A QL G V Q AFA D AL L IIP KV LA Q N S G F D LQET LVK IQAE H SESGQLV G VDLN TGE PMVAA E V G 448
Cdd:NF041083 408 P EV EL A KR L REYAAT V G GR E QL A V E AFA E AL E IIP RT LA E N A G L D PIDI LVK LRSA H EKGKKWA G INVF TGE VVDMW E L G 487
490 500 510
....*....|....*....|....*....|..
gi 58331171 449 V WDNYC VK K Q LLH S C T VI AT N IL LV D EIMR A G 480
Cdd:NF041083 488 V IEPLR VK T Q AIK S A T EA AT M IL RI D DVIA A K 519
TCP1_epsilon
cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
14-476
1.32e-74
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: 244.13
E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 14 ARAQA A LAVN I S AA RGLQDV LRT N LGP K G TM K M LVS GA G DIKL T K DG NVL L HE M -------------------------- 67
Cdd:cd03339 19 LKGLE A HKSH I L AA KSVANI LRT S LGP R G MD K I LVS PD G EVTV T N DG ATI L EK M dvdhqiakllvelsksqddeigdgtt 98
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------- G L HP RI I TE G F E A A KEK A LQF LEE VKVS --- REMDR E T LI DV A R TSL RT K VHAELADVLT E 125
Cdd:cd03339 99 gvvvlagalleqaeklldr G I HP IR I AD G Y E Q A CKI A VEH LEE IADK ief SPDNK E P LI QT A M TSL GS K IVSRCHRQFA E 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 126 AV VD SI L A --- IKKQ D ep IDLFM I EIMEMKHKSET DT S L IR G L V L D HGAR HP D M K K R V E DA Y I -- LTC nv SL E YE K TEVN 200
Cdd:cd03339 179 IA VD AV L S vad LERK D -- VNFEL I KVEGKVGGRLE DT K L VK G I V I D KDFS HP Q M P K E V K DA K I ai LTC -- PF E PP K PKTK 254
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 201 SGFFYK S A E ERE KL VKA E R K FIEDR V KKI ielkr K VC G DS dkgf V VI N Q K G I D PFSLDA L SKE G IV A L R RAKRRNM E RLT 280
Cdd:cd03339 255 HKLDIT S V E DYK KL QEY E Q K YFREM V EQV ----- K DA G AN ---- L VI C Q W G F D DEANHL L LQN G LP A V R WVGGVEI E LIA 325
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 281 L A C GG VALNS F D DLSP DC LG H AGLV Y E YTL G -- EE K FTF IE K C N N PRS VT LL I K G P NK HTLTQI K DAVR D G L RA V K N A I D 358
Cdd:cd03339 326 I A T GG RIVPR F E DLSP EK LG K AGLV R E ISF G tt KD K MLV IE G C P N SKA VT IF I R G G NK MIIEEA K RSLH D A L CV V R N L I R 405
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 359 D GCV V P G A GA V E VAMAE A LI K HKPSVK G RA Q LGVQ AFADAL LI IP KV LA Q NSG FDLQ ETL VKIQ A EH - S E SGQLV G V D LN 437
Cdd:cd03339 406 D NRI V Y G G GA A E ISCSL A VE K AADKCS G IE Q YAMR AFADAL ES IP LA LA E NSG LNPI ETL SEVK A RQ v K E KNPHL G I D CL 485
490 500 510
....*....|....*....|....*....|....*....
gi 58331171 438 TGEPMVAA E VG V WDNYCV KKQ LLHSC T VIATN IL LV D EI 476
Cdd:cd03339 486 GRGTNDMK E QK V FETLIS KKQ QILLA T QVVKM IL KI D DV 524
chaperonin_like
cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
100-359
1.67e-72
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain]
Cd Length: 209
Bit Score: 228.12
E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 100 RE T L ID VA R TSL RT K V h AELA D V L TEA VVD SI L AIKKQDEPI DL FM I EIMEMKHK S ET D TS L IR G L V L D H G ARH P D M K KR 179
Cdd:cd03333 1 RE L L LQ VA T TSL NS K L - SSWD D F L GKL VVD AV L KVGPDNRMD DL GV I KVEKIPGG S LE D SE L VV G V V F D K G YAS P Y M P KR 79
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 180 V E D A Y IL TCNVS LEY ektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgf VVI NQ KGID PFS L DA 259
Cdd:cd03333 80 L E N A K IL LLDCP LEY -------------------------------------------------- VVI AE KGID DLA L HY 109
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 260 L S K E GI V A L RR A K RRNM ER LTL A C G GVALN S FD DL S P DC LG H A G LV Y E YTL GEEK F TFIE K C NNPRSV T L L IK G PNKHT L 339
Cdd:cd03333 110 L A K A GI M A V RR V K KEDL ER IAR A T G ATIVS S LE DL T P ED LG T A E LV E E TKI GEEK L TFIE G C KGGKAA T I L LR G ATEVE L 189
250 260
....*....|....*....|
gi 58331171 340 TQI K DAVR D G L R AV KN A IDD 359
Cdd:cd03333 190 DEV K RSLH D A L C AV RA A VEE 209
chap_CCT_epsi
TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
15-480
1.41e-69
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: 231.23
E-value: 1.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 15 RAQA A LAV NI S AA RGLQDV LRT N LGPKG TM KML V S GA GDI KL T K DG NVL L HE M --------------------------- 67
Cdd:TIGR02343 24 KGLE A KKS NI A AA KSVASI LRT S LGPKG MD KML I S PD GDI TV T N DG ATI L SQ M dvdnqiaklmvelsksqddeigdgttg 103
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------ G L HP RI I TE GFE A A KEK A LQF LEE V -- KV S REMD - RE T LI DV A R TSL RT K VHAELADVLT E A 126
Cdd:TIGR02343 104 vvvlagalleqaeelldk G I HP IK I AD GFE E A ARI A VEH LEE I sd EI S ADNN n RE P LI QA A K TSL GS K IVSKCHRRFA E I 183
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 127 V VD SI L AI - KKQDEPI D LFM I EIMEMKHK S ET DT S LI R G LVL D HGAR HP D M K K R VEDA Y -- ILTC nv SL E YE K TEVNSGF 203
Cdd:TIGR02343 184 A VD AV L NV a DMERRDV D FDL I KVEGKVGG S LE DT K LI K G III D KDFS HP Q M P K E VEDA K ia ILTC -- PF E PP K PKTKHKL 261
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 204 FYK S A EE RE KL V K A E RKFIEDRVKK I ielk R K VCGD sdkgf V VI N Q K G I D PFSLDA L SKEGIV A L R RAKRRNM E RLTL A C 283
Cdd:TIGR02343 262 DIS S V EE YK KL Q K Y E QQKFKEMIDD I ---- K K SGAN ----- L VI C Q W G F D DEANHL L LQNDLP A V R WVGGQEL E LIAI A T 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 284 GG VALNS F DD LS P D C LG H AGLV Y E YTL G -- EEKFTF IE K C N N PRS VT LL I K G P NK HTLTQI K DAVR D G L RA V K N A I D D GC 361
Cdd:TIGR02343 333 GG RIVPR F QE LS K D K LG K AGLV R E ISF G tt KDRMLV IE Q C K N SKA VT IF I R G G NK MIIEEA K RSIH D A L CV V R N L I K D SR 412
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 362 V V P G A GA V E VAMAE A LIKHKPSVK G RA Q LGVQ AFADAL LI IP KV LA Q NSG F D LQE TL VKIQAEH - S E SGQLV GVD LNTGE 440
Cdd:TIGR02343 413 I V Y G G GA A E ISCSL A VSQEADKYP G VE Q YAIR AFADAL ET IP MA LA E NSG L D PIG TL STLKSLQ l K E KNPNL GVD CLGYG 492
490 500 510 520
....*....|....*....|....*....|....*....|
gi 58331171 441 PMVAA E VG V WDNYCV KKQ LLHSC T VIATN IL LV D EIMRA G 480
Cdd:TIGR02343 493 TNDMK E QF V FETLIG KKQ QILLA T QLVRM IL KI D DVISP G 532
chap_CCT_gamma
TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
8-476
1.87e-69
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: 230.39
E-value: 1.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 8 N P K A E VA R a Q A A L A v NI S AA RGLQ D VL RT N LGP KGTM KML VSGA G D I KL T K DGN VL L H E MGL ------------------ 69
Cdd:TIGR02344 8 N T K R E SG R - K A Q L S - NI Q AA KAVA D II RT C LGP RSML KML LDPM G G I VM T N DGN AI L R E IDV ahpaaksmielsrtqdee 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 70 --------------------------- HP RI I TEGFEA A KEK AL QF LEE VKVSREM - D RETLIDVARTSLR TK VHAELA D 121
Cdd:TIGR02344 86 vgdgttsviilagemlsvaepfleqni HP TV I IRAYRK A LDD AL SV LEE ISIPVDV n D DAAMLKLIQSCIG TK FVSRWS D 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 122 VLTEAVV D SILAIKKQDEPI dl FM I E I MEMK h K S E ------- T D TSLIR G LVLDHGAR HP D M KKRV E DAY I LTCNVS LEY 194
Cdd:TIGR02344 166 LMCDLAL D AVRTVQRDENGR -- KE I D I KRYA - K V E kipggdi E D SCVLK G VMINKDVT HP K M RRYI E NPR I VLLDCP LEY 242
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 195 E K T E VNSGFFYKSA E EREKLVKA E RKFIEDRVKK II EL K RKV cgdsdkgfv VI NQ KG IDPFSLDA L S K EG I V A L RR AKRR 274
Cdd:TIGR02344 243 K K G E SQTNIEITKE E DWNRILQM E EEYVQLMCED II AV K PDL --------- VI TE KG VSDLAQHY L L K AN I T A I RR VRKT 313
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 275 NME R LTL ACG GVAL N SFDD L SPDCL G - HA GL VYEYTL G E E K FTFI EK C NN P RSV T L L IK G PN K HT L TQIKDAVR D GLRAV 353
Cdd:TIGR02344 314 DNN R IAR ACG ATIV N RPEE L RESDV G t GC GL FEVKKI G D E Y FTFI TE C KD P KAC T I L LR G AS K DI L NEVERNLQ D AMAVA 393
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 354 K N AID D GCV VPG A GA V E V A MAE AL IKHKPSVK G RA Q LGVQ A F ADAL L IIP KV LAQN S G FDLQE TL VKIQ A E H S - E SGQLV 432
Cdd:TIGR02344 394 R N VLL D PKL VPG G GA T E M A VSV AL TEKSKKLE G VE Q WPYR A V ADAL E IIP RT LAQN C G ANVIR TL TELR A K H A q E NNCTW 473
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 58331171 433 G V D LN TG EPMVAA E V G V W DNYC VK K Q LLHSCTVI A TNI L LV D E I 476
Cdd:TIGR02344 474 G I D GE TG KIVDMK E K G I W EPLA VK L Q TYKTAIES A CLL L RI D D I 517
TCP1_alpha
cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
23-478
5.66e-69
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: 229.48
E-value: 5.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 23 N IS AA RGLQDVLRTN LGP K G TM KMLV SGA GD IKL T K DG NVL L --------------------- H E M G ------------- 68
Cdd:cd03335 13 N VT AA MAIANIVKSS LGP V G LD KMLV DDI GD VTI T N DG ATI L kllevehpaakilvelaqlqd K E V G dgttsvviiaael 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 69 ----------- L HP RI I TE G FEA A KEK A LQFLE E --- VK V S r EMDR E T LI D VA R TS LRT K VHAELA D VLTEA VVD S ILA I 134
Cdd:cd03335 93 lkranelvkqk I HP TT I IS G YRL A CKE A VKYIK E hls IS V D - NLGK E S LI N VA K TS MSS K IIGADS D FFANM VVD A ILA V 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 135 K KQD E ------ PI D lf MIE I MEMKH KS ETDTS L IR G LV L DHGARHPD M KK RV ED A Y I LTCNVS L EYE K TEVNSGFFYKSA 208
Cdd:cd03335 172 K TTN E kgktky PI K -- AVN I LKAHG KS AKESY L VN G YA L NCTRASQG M PT RV KN A K I ACLDFN L QKT K MKLGVQVVVTDP 249
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 E ER EK LVKA E RKFIED R V KKI IE lkrkv C G DS dkgf VV INQK GID PFS L DALSKE G IV A L RR A K RRNME R LTL A C G GVAL 288
Cdd:cd03335 250 E KL EK IRQR E SDITKE R I KKI LA ----- A G AN ---- VV LTTG GID DMC L KYFVEA G AM A V RR V K KEDLR R IAK A T G ATLV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSFDD L ------ S P DC LG H A GL V YEYTL G EEKFTF I EKCNNPR S VTLLIK G P N KHT L TQIKDAVR D G L RA VK NAIDDGC V 362
Cdd:cd03335 321 STLAN L egeetf D P SY LG E A EE V VQERI G DDELIL I KGTKKRS S ASIILR G A N DFM L DEMERSLH D A L CV VK RTLESNS V 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 363 VPG A GAVE V A MAEA L IKHKPSVKG R A QL GVQA FA D ALL I IPK V LA Q N SGF D LQ E TLV K IQ A E H SES g Q L --------- V G 433
Cdd:cd03335 401 VPG G GAVE T A LSIY L ENFATTLGS R E QL AIAE FA E ALL V IPK T LA V N AAK D AT E LVA K LR A Y H AAA - Q V kpdkkhlkw Y G 479
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 58331171 434 V DL NT G EPMVAA E V GV WDNYCV K KQL L HSC T VI A TN IL LV D EIMR 478
Cdd:cd03335 480 L DL IN G KVRDNL E A GV LEPTVS K IKS L KFA T EA A IT IL RI D DLIK 524
TCP1_gamma
cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
4-476
8.20e-69
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: 227.56
E-value: 8.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 4 V KTL N P K A E VA R a Q A A L A v NI S AA RGLQ DV L RT N LGP KGTM KML VSGA G D I K LT K DGN VL L H E M ---------------- 67
Cdd:cd03337 4 V LNQ N T K R E SG R - K A Q L G - NI Q AA KTVA DV I RT C LGP RAML KML LDPM G G I V LT N DGN AI L R E I dvahpaaksmielsrt 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ----------------------------- G L HP RI I TEGFEA A K E K AL QF LEE VKVS - REM DR ETLIDVARTSLR TK VHA 117
Cdd:cd03337 82 qdeevgdgttsviilageilavaepfler G I HP TV I IKAYRK A L E D AL KI LEE ISIP v DVN DR AQMLKIIKSCIG TK FVS 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 118 ELA D VLTEAVV D SILAIKKQDE ---- P ID L - FMIEIMEMKHKSET D TSLIR G LV L DHGAR HP D M KK R V E DAY I LTCNVS L 192
Cdd:cd03337 162 RWS D LMCNLAL D AVKTVAVEEN grkk E ID I k RYAKVEKIPGGEIE D SRVLD G VM L NKDVT HP K M RR R I E NPR I VLLDCP L 241
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 193 EY ektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgf V VI NQ KG IDPFSLDA L S K E GI V ALRR AK 272
Cdd:cd03337 242 EY -------------------------------------------------- L VI TE KG VSDLAQHY L V K A GI T ALRR VR 271
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 273 RRNME R LTL ACG GVAL N SFDD L SPDCL G HAGLVY E YTL - G E E K FTFI EK C NN P RSV T L L IK G PN K HT L TQIKDAVR D GLR 351
Cdd:cd03337 272 KTDNN R IAR ACG ATIV N RPEE L TESDV G TGAGLF E VKK i G D E Y FTFI TE C KD P KAC T I L LR G AS K DV L NEVERNLQ D AMA 351
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 352 AVK N A I DDGCV VPG A GA V E V A MAE AL IKHKP S VK G RA Q LGVQ A F A D AL LI IP KV LAQN S G FDLQE TL VKIQ A E H SESGQL 431
Cdd:cd03337 352 VAR N I I LNPKL VPG G GA T E M A VSH AL SEKAK S IE G VE Q WPYK A V A S AL EV IP RT LAQN C G ANVIR TL TELR A K H AQGENS 431
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 58331171 432 V - G V D LN TG EPMVAA E V G V WD NYC VK K Q LLHSCTVI A TNI L LV D E I 476
Cdd:cd03337 432 T w G I D GE TG DIVDMK E L G I WD PLA VK A Q TYKTAIEA A CML L RI D D I 477
chap_CCT_alpha
TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
23-478
8.97e-68
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: 226.53
E-value: 8.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 23 N IS AA RGLQDVLR T N LGP K G TM KMLV SGA GD IKL T K DG NVL L --------------------- H E M G ------------- 68
Cdd:TIGR02340 17 N VT AA MAIANIVK T S LGP V G LD KMLV DDI GD VTI T N DG ATI L kllevehpaakilvelaqlqd R E V G dgttsvviiaael 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 69 ----------- L HP RIITE G FEA A KEK A LQFLE E -- VKVSR E MD RE T LI D VA R TS LRT K VHAELA D VLTEA VVD SI LA I K 135
Cdd:TIGR02340 97 lkradelvknk I HP TSVIS G YRL A CKE A VKYIK E nl SVSVD E LG RE A LI N VA K TS MSS K IIGLDS D FFSNI VVD AV LA V K 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 136 KQD E ------ PI D lf M I E I MEMKH KS ETDTS L IR G LV L DHGARHPD M K KR VED A Y I LTCNVS L EYE K TEVNSGFFYKSA E 209
Cdd:TIGR02340 177 TTN E ngetky PI K -- A I N I LKAHG KS ARESM L VK G YA L NCTVASQQ M P KR IKN A K I ACLDFN L QKA K MALGVQIVVDDP E 254
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 210 ER E KLVKA E RKFIED R V KKI IELKRK V cgdsdkgfv V INQK GID PFS L DALSKE G IVAL RR A K RRNME R LTL A C G GVALN 289
Cdd:TIGR02340 255 KL E QIRQR E ADITKE R I KKI LDAGAN V --------- V LTTG GID DMC L KYFVEA G AMGV RR C K KEDLK R IAK A T G ATLVS 325
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 290 SFD DL S ------ PDC LG H A GL V YEYTLGEEKFTF I EKCNNPR S VTLLIK G P N KHT L TQIKDAVR D G L RA VK NAIDDGC VV 363
Cdd:TIGR02340 326 TLA DL E geetfe ASY LG F A DE V VQERIADDECIL I KGTKKRK S ASIILR G A N DFM L DEMERSLH D A L CV VK RTLESNS VV 405
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 364 PG A GAVE V A MAEA L IKHKPSVKG R A QL GVQA FA D ALLIIPK V LA Q N SGF D LQ E TLV K IQ A E H SES g QL --------- V G V 434
Cdd:TIGR02340 406 PG G GAVE A A LSIY L ENFATTLGS R E QL AIAE FA R ALLIIPK T LA V N AAK D ST E LVA K LR A Y H AAA - QL kpekkhlkw Y G L 484
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 58331171 435 DL NT G EPMVAA E V GV WDNYCV K KQL L HSC T VI A TN IL LV D EIMR 478
Cdd:TIGR02340 485 DL VN G KIRDNK E A GV LEPTVS K VKS L KFA T EA A IT IL RI D DLIK 528
chap_CCT_eta
TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
23-479
1.61e-63
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: 214.62
E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 23 NI S A ARGLQDV L R T N LGP K G TM K ML V SGA G DIKLTK DG NVL L HEM ----------------------------------- 67
Cdd:TIGR02345 23 NI N A CVAIAEA L K T T LGP R G MD K LI V GSN G KATISN DG ATI L KLL divhpaaktlvdiaksqdaevgdgttsvtilagel 102
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ---------- G L HP RI I TEGFEA A KEK A LQFLE E VK V SREMD ---- RE T L IDV A R T S L RT K VHAELADVLTEAV VD SI L A 133
Cdd:TIGR02345 103 lkeakpfiee G V HP QL I IRCYRE A LSL A VEKIK E IA V TIDEE kgeq RE L L EKC A A T A L SS K LISHNKEFFSKMI VD AV L S 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 134 IKKQ D ep I DL FM I E I MEMKHKSET D TS L IR G LVLDHG --- A RHPDMK K RVEDAY IL TC NV S LE YEKTEV N SGFFYKSA E E 210
Cdd:TIGR02345 183 LDRD D -- L DL KL I G I KKVQGGALE D SQ L VN G VAFKKT fsy A GFEQQP K KFANPK IL LL NV E LE LKAEKD N AEIRVEDV E D 260
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 211 REKL V K AE RKF I EDRVK KI I E LKRK V cgdsdkgfv V INQKG I DPFSLDALSKEG I VALR R AKRRNME R LTL ACGG VALNS 290
Cdd:TIGR02345 261 YQAI V D AE WAI I FRKLE KI V E SGAN V --------- V LSKLP I GDLATQYFADRD I FCAG R VSAEDLK R VIK ACGG SIQST 331
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 291 FD DL SP D C LG HAG L VY E YTL G E E KFTFIEK C NNPRSV T LLIK G PNKHTLTQIKDAVR D GLRA V KN A IDDGCV V P G A GA V E 370
Cdd:TIGR02345 332 TS DL EA D V LG TCA L FE E RQI G S E RYNYFTG C PHAKTC T IILR G GAEQFIEEAERSLH D AIMI V RR A LKNKKI V A G G GA I E 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 371 VAMAEA L IKHKPSVK G RA QL GVQ AFA D AL L IIP KV L AQ N S GFD LQ E T L V K IQAE H SES G QLV GVD L NT GEPMVAA E VG VW 450
Cdd:TIGR02345 412 MELSKC L RDYSKTID G KQ QL IIN AFA K AL E IIP RQ L CE N A GFD SI E I L N K LRSR H AKG G KWY GVD I NT EDIGDNF E AF VW 491
490 500
....*....|....*....|....*....
gi 58331171 451 DNYC VK KQL L HSCTVI A TN IL L VDE IMRA 479
Cdd:TIGR02345 492 EPAL VK INA L KAAFEA A CT IL S VDE TITN 520
TCP1_delta
cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
23-441
1.94e-62
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: 211.76
E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 23 NI S AA RGLQ D VL RT N LGP K G TM KM LVS G A G DIKL T K DG NVL L HE M ----------------------------------- 67
Cdd:cd03338 13 NI Q AA KAVA D AI RT S LGP R G MD KM IQT G K G EVII T N DG ATI L KQ M svlhpaakmlvelskaqdieagdgttsvvvlagal 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ---------- G L HP RI I T E G F EA A KE KA LQF L EEVKVSREM - DRE T LI DV A R TSL RT KV HAELADV L TEAV VD SI L AI -- 134
Cdd:cd03338 93 lsacesllkk G I HP TV I S E S F QI A AK KA VEI L DSMSIPVDL n DRE S LI KS A T TSL NS KV VSQYSSL L APIA VD AV L KV id 172
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 135 KKQDEPI DL FM I E I MEMKHKSET DT S L IR GLV LDHG A RH - PDMKK R V E D A Y I LTCNVS L EYE KT EVNSGFFYKSAEEREK 213
Cdd:cd03338 173 PATATNV DL KD I R I VKKLGGTIE DT E L VD GLV FTQK A SK k AGGPT R I E K A K I GLIQFC L SPP KT DMDNNIVVNDYAQMDR 252
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 214 LVKA ERK F I EDRV KKI iel K RKV C G dsdkgf V VIN QK G I ----- DPFS L DA L S K EG I VALRRAK R RNM E RLTLAC G GVAL 288
Cdd:cd03338 253 ILRE ERK Y I LNMC KKI --- K KSG C N ------ V LLI QK S I lrdav SDLA L HF L A K LK I MVVKDIE R EEI E FICKTI G CKPV 323
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 N S F D DLSP D C LG H A G LV Y E YT LG EE K FTF I EKCN NP - RS VT L L IK G P NK HT L TQIKDAVR D G L RAVKNAIDDGCVV PG A G 367
Cdd:cd03338 324 A S I D HFTE D K LG S A D LV E E VS LG DG K IVK I TGVK NP g KT VT I L VR G S NK LV L DEAERSLH D A L CVIRCLVKKRALI PG G G 403
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58331171 368 A V E VAM A EA L IKHKPSVK G RA Q LG V Q AFADAL LI IP KV LA Q N S G FDLQETLVKIQAE H SESGQLV G VDLNT G EP 441
Cdd:cd03338 404 A P E IEI A LQ L SEWARTLT G VE Q YC V R AFADAL EV IP YT LA E N A G LNPISIVTELRNR H AQGEKNA G INVRK G AI 477
GroEL
COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-479
5.44e-62
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 209.93
E-value: 5.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 19 A LAV NI SAARG L Q D VLRTN LGPKG TMK MLV SGA GD IKL T K DG NVLLH E M ------------------------------- 67
Cdd:COG0459 11 A RRA NI RGVKA L A D AVKVT LGPKG RNV MLV KSF GD PTI T N DG VTIAK E I eledpfenmgaqlvkevasktndeagdgttt 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 68 ------------------ G LH P RI I TE G FEA A K EKA LQF L EE -- VK V S rem D R E T L ID VA RT S LRTK vh A E LADVLT EA V 127
Cdd:COG0459 91 atvlagallkeglklvaa G AN P TD I KR G IDK A V EKA VEE L KK ia KP V D --- D K E E L AQ VA TI S ANGD -- E E IGELIA EA M 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 128 vdsi LAIK K QDE pidl FMI E imem KH K S - ET DTSLIR G LVL D H G ARH P D ------- M KKRV E D AYIL TCNVSLE yektev 199
Cdd:COG0459 166 ---- EKVG K DGV ---- ITV E ---- EG K G l ET ELEVVE G MQF D K G YLS P Y fvtdpek M PAEL E N AYIL LTDKKIS ------ 227
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 nsgffyk S AEEREK L vkaerkfiedr VK K IIELKRK vcgdsdkgf VV I NQKG ID PFS L DA L SKE GI VALR R A -------- 271
Cdd:COG0459 228 ------- S IQDLLP L ----------- LE K VAQSGKP --------- LL I IAED ID GEA L AT L VVN GI RGVL R V vavkapgf 280
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 272 - K RR N -- M E RLTLAC GG VALN ----- SFD D LSP D C LG H A GL V YE ytl GEEKF T FI E KCN NP RSVTL L IKGPNKHTLTQI K 343
Cdd:COG0459 281 g D RR K am L E DIAILT GG RVIS edlgl KLE D VTL D D LG R A KR V EV --- DKDNT T IV E GAG NP KAIVI L VGAATEVEVKER K 357
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 344 DA V R D G L R A VKN A IDD G c V VPG A GA VEVAM A E AL IKHKPSVK G RA QLG VQAF A D AL LIIPKVL A Q N S G F D LQETLV K IQ A 423
Cdd:COG0459 358 RR V E D A L H A TRA A VEE G - I VPG G GA ALLRA A R AL RELAAKLE G DE QLG IEIV A R AL EAPLRQI A E N A G L D GSVVVE K VR A 436
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 58331171 424 EHSES gql V G V D LN TGE P -- M VA A ev GV W D NYC VK KQL L HSCTVI A TN IL LVDEIMRA 479
Cdd:COG0459 437 AKDKG --- F G F D AA TGE Y vd M LE A -- GV I D PAK VK RSA L QNAASV A GL IL TTEAVIAD 489
TCP1_beta
cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
10-479
2.50e-59
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: 203.33
E-value: 2.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 10 K A E V AR AQA --- A L A VN isaarglq D VLR T N LGPKG TM K M L V S G -- A G DIKL T K DG NVL L -------------------- 64
Cdd:cd03336 10 K G E T AR LSS fvg A I A IG -------- D LVK T T LGPKG MD K I L Q S V gr S G GVTV T N DG ATI L ksigvdnpaakvlvdiskvq 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 65 - H E M G ------------------------ L HP RI I T EG FEA A KEK A LQF L EE ---- VKVSR E MD RE T L IDV ART S L RT K V 115
Cdd:cd03336 82 d D E V G dgttsvtvlaaellreaeklvaqk I HP QT I I EG YRM A TAA A REA L LS savd HSSDE E AF RE D L LNI ART T L SS K I 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 HAELADVLT E AV VD SI L AI K KQD epi D L FM I E I MEMKHK S ET D TS L IR G LV LD H -- G ARH P dmk KR V E D A Y IL TC N VSLE 193
Cdd:cd03336 162 LTQDKEHFA E LA VD AV L RL K GSG --- N L DA I Q I IKKLGG S LK D SY L DE G FL LD K ki G VNQ P --- KR I E N A K IL IA N TPMD 235
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 194 YE K TEV - NSGFFYK S AEEREKLVK AE RKFIEDR V K KI IELKRKV cgdsdkgfv V IN QKG I DPFSLDALSKE GI V A LRR A K 272
Cdd:cd03336 236 TD K IKI f GAKVRVD S TAKVAEIEE AE KEKMKNK V E KI LKHGINC --------- F IN RQL I YNYPEQLFADA GI M A IEH A D 306
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 273 RRNM ERL T L AC GG VALNS FD DLSPDC LG HAG L VY E YTL GE E K FTFIEKCNNPRSV T LLIK G PNKHT L TQIKDAVR D G L RA 352
Cdd:cd03336 307 FDGV ERL A L VT GG EIAST FD HPELVK LG TCK L IE E IMI GE D K LIRFSGVAAGEAC T IVLR G ASQQI L DEAERSLH D A L CV 386
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 353 VKNAID D GC VV P G A G AV E VA MA E A LIKHKPSVK G RAQ L GVQ AFA D AL LII P KVL A Q N S G F D LQ E TLVKIQ A E H SESGQLV 432
Cdd:cd03336 387 LAQTVK D TR VV L G G G CS E ML MA K A VEELAKKTP G KKS L AIE AFA K AL RQL P TII A D N A G Y D SA E LVAQLR A A H YNGNTTA 466
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 58331171 433 G V D LNT G EPMVAA E V G VWDNYC VK K Q L L H S CTVI A TN IL L VD E I MRA 479
Cdd:cd03336 467 G L D MRK G TVGDMK E L G ITESFK VK R Q V L L S ASEA A EM IL R VD D I IKC 513
TCP1_eta
cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
23-479
1.16e-58
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: 201.75
E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 23 NI S A ARGLQ D VL RT N LGP K G TM K ML V S G A G DIKLTK DG NVL L ------ H ------------------------------- 65
Cdd:cd03340 21 NI N A CQAIA D AV RT T LGP R G MD K LI V D G R G KVTISN DG ATI L klldiv H paaktlvdiaksqdaevgdgttsvvvlagef 100
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 66 -------- E M G L HP R II TE G FEA A KEK A LQFLE E VK V ----- SR E MD RE T L IDV A R T S L RT K VH A ELADVLTEA VVD SI L 132
Cdd:cd03340 101 lkeakpfi E D G V HP Q II IR G YRK A LQL A IEKIK E IA V nidke DK E EQ RE L L EKC A A T A L NS K LI A SEKEFFAKM VVD AV L 180
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 133 AI kkq D EPI DL F MI E I MEMKHK S ET D TS L IR G LVLDHG --- A RHPDMK K RVEDAY IL TC NV S LE YEKTEV N SGFFYKSA E 209
Cdd:cd03340 181 SL --- D DDL DL D MI G I KKVPGG S LE D SQ L VN G VAFKKT fsy A GFEQQP K KFKNPK IL LL NV E LE LKAEKD N AEVRVEDP E 257
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 210 E REKL V K AE R K F I E D RVK KI IELKRK V cgdsdkgfv V INQKG I DPFSLDALSKEG I VALR R AKRRNME R LTL A C GG VALN 289
Cdd:cd03340 258 E YQAI V D AE W K I I Y D KLE KI VKSGAN V --------- V LSKLP I GDLATQYFADRD I FCAG R VPEEDLK R VAQ A T GG SIQT 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 290 SFDDLSP D C LG HA GL VY E YTL G E E KFTFIEK C NNPRSV T LLIK G PNKHTLTQIKDAVR D GLRA V KN AI DDGC VV P G A GA V 369
Cdd:cd03340 329 TVSNITD D V LG TC GL FE E RQV G G E RYNIFTG C PKAKTC T IILR G GAEQFIEEAERSLH D AIMI V RR AI KNDS VV A G G GA I 408
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 370 E VAMAEA L IKHKPSVK G RA QL GVQ AFA D AL L IIP KV L AQ N S GFD LQET L V K IQAE H SES G QL - V GVD L N TGEPMVAA E VG 448
Cdd:cd03340 409 E MELSKY L RDYSRTIA G KQ QL VIN AFA K AL E IIP RQ L CD N A GFD ATDI L N K LRQK H AQG G GK w Y GVD I N NEGIADNF E AF 488
490 500 510
....*....|....*....|....*....|.
gi 58331171 449 VW DNYC VK KQL L HSC T VI A TN IL L VDE IMRA 479
Cdd:cd03340 489 VW EPSL VK INA L TAA T EA A CL IL S VDE TIKN 519
PTZ00212
PTZ00212
T-complex protein 1 subunit beta; Provisional
10-479
2.87e-57
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 198.33
E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 10 K A E V AR A Q aalav NISA A RGLQ D VLR T N LGPKG TM K M L VS ----- GA G DIKL T K DG NVL L HEMG L --------------- 69
Cdd:PTZ00212 19 K G E T AR L Q ----- SFVG A IAVA D LVK T T LGPKG MD K I L QP msegp RS G NVTV T N DG ATI L KSVW L dnpaakilvdisktq 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 70 ------------------------------ HP RI I T EG FEA A KEK A LQF LEE VKVSREM D ---- R E T L IDV ART S L RT K V 115
Cdd:PTZ00212 94 deevgdgttsvvvlagellreaeklldqki HP QT I I EG WRM A LDV A RKA LEE IAFDHGS D eekf K E D L LNI ART T L SS K L 173
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 HAELA D VLTEAV VD SI L AI K KQ dep ID L FM I E I MEMKHKSET D TS L IR G LV L DH -- G ARH P dmk KR V E DAY IL TC N VSLE 193
Cdd:PTZ00212 174 LTVEK D HFAKLA VD AV L RL K GS --- GN L DY I Q I IKKPGGTLR D SY L ED G FI L EK ki G VGQ P --- KR L E NCK IL VA N TPMD 247
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 194 YE K ----- TE V NSGFFY K S AE erek LVK AE RKFIEDR V K KI IELK rkv C G dsdkgf V V IN QKG I DPFSLDALSKE GI V A L 268
Cdd:PTZ00212 248 TD K ikiyg AK V KVDSME K V AE ---- IEA AE KEKMKNK V D KI LAHG --- C N ------ V F IN RQL I YNYPEQLFAEA GI M A I 314
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 269 RR A KRRN MERL TL A C G GVALNS FD DLSPDC LGH AG L VY E YTL GE E K FTFIEK C NNPRSV T LLIK G PNK H T L TQIKDAVR D 348
Cdd:PTZ00212 315 EH A DFDG MERL AA A L G AEIVST FD TPEKVK LGH CD L IE E IMI GE D K LIRFSG C AKGEAC T IVLR G AST H I L DEAERSLH D 394
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 349 G L RAVKNAID D GC VV P G A G AV E VA MA E A LIKHKPS V K G RAQ L GVQ AFA D AL LI IP KVL A Q N S G F D LQ E TLV K IQ AEH SES 428
Cdd:PTZ00212 395 A L CVLSQTVK D TR VV L G G G CS E ML MA N A VEELAKK V E G KKS L AIE AFA K AL RQ IP TII A D N G G Y D SA E LVS K LR AEH YKG 474
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58331171 429 GQLV G V D LNT G EPMVAA E V G VWDN Y C VK KQL L H S C T VI A TN IL L VD E I M R A 479
Cdd:PTZ00212 475 NKTA G I D MEK G TVGDMK E L G ITES Y K VK LSQ L C S A T EA A EM IL R VD D I I R C 525
chap_CCT_theta
TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
16-479
1.87e-56
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: 196.09
E-value: 1.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 16 AQA A LAV NI S A ARG L QDVL RT N LGP K G TM KM LVSGAGDIKL T K D GNVL L H E ----------------------------- 66
Cdd:TIGR02346 16 LEE A VIK NI E A CKE L SQIT RT S LGP N G MN KM VINHLEKLFV T N D AATI L R E levqhpaakllvmasemqeneigdgtnlv 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 67 ---------------- MGLHP RI I TE G F E A A KE KA LQF LEE VK V SREM D --- RET LI DVART S LRT K VHAE l A D V L TEA V 127
Cdd:TIGR02346 96 lvlagellnkaeelir MGLHP SE I IK G Y E M A LK KA MEI LEE LV V WEVK D lrd KDE LI KALKA S ISS K QYGN - E D F L AQL V 174
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 128 VDSILAIK - K QDEPIDLFM I EIMEMKHK S ETDTSLIR G L V L dhg A R HPDMK - K R V ED A YILTCNVS L EYEK TE VNSGFFY 205
Cdd:TIGR02346 175 AQACSTVL p K NPQNFNVDN I RVCKILGG S LSNSEVLK G M V F --- N R EAEGS v K S V KN A KVAVFSCP L DTAT TE TKGTVLI 251
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 206 KS AEE REKLV K A E RKF IE DRV K K I IELKRK V cgdsdkgfv VINQKGIDPFS L DA L S K EG I VA L RRAKRRNME RL TLAC G G 285
Cdd:TIGR02346 252 HN AEE LLNYS K G E ENQ IE AMI K A I ADSGVN V --------- IVTGGSVGDMA L HY L N K YN I MV L KIPSKFELR RL CKTV G A 322
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 286 VA L NSFDDLS P DCL G HAGL VY EYTL G EE K F T FIEKC N NPRSV - T LLIK G PNKHT L TQ I KD A VR DG LRA VK NAID DG CVV P 364
Cdd:TIGR02346 323 TP L PRLGAPT P EEI G YVDS VY VSEI G GD K V T VFKQE N GDSKI s T IILR G STDNL L DD I ER A ID DG VNT VK ALVK DG RLL P 402
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 365 GAGA V E VAM A EA L I K HKPSVK G RA Q LGVQA FA D A LL IIP KV LA Q N S G FDLQ E TLV K IQ A E H SESGQLV G V D LNTGEPM V - 443
Cdd:TIGR02346 403 GAGA T E IEL A SR L T K YGEKLP G LD Q YAIKK FA E A FE IIP RT LA E N A G LNAN E VIP K LY A A H KKGNKSK G I D IEAESDG V k 482
490 500 510
....*....|....*....|....*....|....*..
gi 58331171 444 - A A E V G VW D NYCV KK QLLHSC T VI A TNI L L VD E I MR A 479
Cdd:TIGR02346 483 d A S E A G IY D MLAT KK WAIKLA T EA A VTV L R VD Q I IM A 519
TCP1_theta
cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
23-479
1.83e-48
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: 173.18
E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 23 NI S A ARG L QDVL RT NL GP K G TM KM LVSGAGDIKL T K D GNVL L H E ------------------------------------ 66
Cdd:cd03341 13 NI E A CKE L SQIT RT SY GP N G MN KM VINHLEKLFV T S D AATI L R E levqhpaakllvmasqmqeeeigdgtnlvvvlagel 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 67 --------- MGLHP RI I T EG F E A A KE KAL QF LEE V --- K VSREMDR E TLIDVAR T SLRT K V h AELA D V L TEA V VDSILAI 134
Cdd:cd03341 93 lekaeellr MGLHP SE I I EG Y E K A LK KAL EI LEE L vvy K IEDLRNK E EVSKALK T AIAS K Q - YGNE D F L SPL V AEACISV 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 135 KKQD ep I DL F MIE --- IMEMKHK S ET D TSLI RG L V L dhg A R H P DMK - KRV ED A YI -- LT C NVS leyek TE VN sgffyksa 208
Cdd:cd03341 172 LPEN -- I GN F NVD nir VVKILGG S LE D SKVV RG M V F --- K R E P EGS v KRV KK A KV av FS C PFD ----- IG VN -------- 233
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 eereklvkaerkfiedrvkkiielkrkvcgdsdkgf V VINQKGIDPFS L DALS K E GI VALRRAKRRNME RL TLAC G GVA L 288
Cdd:cd03341 234 ------------------------------------ V IVAGGSVGDLA L HYCN K Y GI MVIKINSKFELR RL CRTV G ATP L 277
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSFDDLS P DCL G HAGL VY EYTL G EE K FTFIEKCNNPRSV - T LLIK G PNKHT L TQIKD A VR DG LRAV K NAID DG CV VPGAG 367
Cdd:cd03341 278 PRLGAPT P EEI G YCDS VY VEEI G DT K VVVFRQNKEDSKI a T IVLR G ATQNI L DDVER A ID DG VNVF K SLTK DG RF VPGAG 357
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 368 A V E VAM A EA L IKHKPSVK G RA Q LGVQA FA D A LLII P KV LA Q N S G F D LQ E T L VKIQ A E H SESGQLV GVD LNT G EPMV -- A A 445
Cdd:cd03341 358 A T E IEL A KK L KEYGEKTP G LE Q YAIKK FA E A FEVV P RT LA E N A G L D AT E V L SELY A A H QKGNKSA GVD IES G DEGT kd A K 437
490 500 510
....*....|....*....|....*....|....
gi 58331171 446 E V G VW D NYCV KK QLLHSC T VI A TNI L L VD E I MR A 479
Cdd:cd03341 438 E A G IF D HLAT KK WAIKLA T EA A VTV L R VD Q I IM A 471
chap_CCT_beta
TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
7-479
2.22e-46
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: 168.50
E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 7 LNPK A EVA RA QA A LAVNISA A RGLQ D VLRTN LGPKG TM K M L V S GA -- GD I KL T K DG NVL L -------------------- 64
Cdd:TIGR02341 3 FKDG A DEE RA EN A RLSSFVG A IAIG D LVKST LGPKG MD K I L Q S SS sd AS I MV T N DG ATI L ksigvdnpaakvlvdmskvq 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 65 - H E M G ------------------------ L HP RI I TE G FEA A KEK A LQF L EEVK V SREM D ---- R ET L IDV ART S L RT K V 115
Cdd:TIGR02341 83 d D E V G dgttsvtvlaaellreaeklinqk I HP QT I IA G YRE A TKA A RDA L LKSA V DNGS D evkf R QD L MNI ART T L SS K I 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 HAELA D VLTEAV VD SI L AI K KQD epi D L FM I E I MEMKHK S ET D TS L IR G LV LD H -- G ARH P dmk KR V E D A Y IL TC N VSLE 193
Cdd:TIGR02341 163 LSQHK D HFAQLA VD AV L RL K GSG --- N L EA I Q I IKKLGG S LA D SY L DE G FL LD K ki G VNQ P --- KR I E N A K IL IA N TGMD 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 194 YE K TEV - N S GFFYK S AEEREK L VK AE RKFIEDR V K KI IELKRKV cgdsdkgfv V IN QKG I DPFSLDALSKE G IV A LRR A K 272
Cdd:TIGR02341 237 TD K VKI f G S RVRVD S TAKVAE L EH AE KEKMKEK V E KI LKHGINC --------- F IN RQL I YNYPEQLFADA G VM A IEH A D 307
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 273 RRNM ERL T L AC GG VALNS FD DLSPDC LG HAG L VY E YTL GE E K FTFIEKCNNPRSV T LLIK G PNKHT L TQIKDAVR D G L RA 352
Cdd:TIGR02341 308 FEGV ERL A L VT GG EIVST FD HPELVK LG SCD L IE E IMI GE D K LLKFSGVKLGEAC T IVLR G ATQQI L DEAERSLH D A L CV 387
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 353 VKNAIDDGCV V P G A G AV E VA M AE A LIKHKPSVK G RAQ L G V Q AFA D AL LII P KVL A Q N S GFD LQ E TLVKIQ A E H SESGQLV 432
Cdd:TIGR02341 388 LSQTVKESRT V L G G G CS E ML M SK A VTQEAQRTP G KEA L A V E AFA R AL RQL P TII A D N A GFD SA E LVAQLR A A H YNGNTTM 467
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 58331171 433 G V D L N T G EPMVAAEV G VWDN Y C VK KQLLH S CTVI A TN IL L VD E I MR A 479
Cdd:TIGR02341 468 G L D M N E G TIADMRQL G ITES Y K VK RAVVS S AAEA A EV IL R VD N I IK A 514
Fab1_TCP
cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
158-346
1.95e-13
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain]
Cd Length: 261
Bit Score: 70.33
E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 158 D TSLIR G L V LDHGAR H PD M KKRVEDAY IL TCNVS LEY EK te V NSGFFY ksaee REKLVKA E RKFIEDR V KK I IE L KRK V c 237
Cdd:cd03334 62 D SEVVD G V V FTKNVA H KR M PSKIKNPR IL LLQGP LEY QR -- V ENKLLS ----- LDPVILQ E KEYLKNL V SR I VA L RPD V - 133
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 238 gdsdkgfv VINQ K GIDPFSL D A L SKE GI VALRRA K RRNM ER LTLAC G GVALN S F DDL S - PDC LG HAGLVYEY T LG EE K -- 314
Cdd:cd03334 134 -------- ILVE K SVSRIAQ D L L LEA GI TLVLNV K PSVL ER ISRCT G ADIIS S M DDL L t SPK LG TCESFRVR T YV EE H gr 205
170 180 190
....*....|....*....|....*....|....*
gi 58331171 315 --- FT F I E K C NNPRSV T L L IK G PNKHT L TQI K DA V 346
Cdd:cd03334 206 skt LM F F E G C PKELGC T I L LR G GDLEE L KKV K RV V 240
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