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T-complex protein 1 subunit zeta-2 isoform 3 [Homo sapiens]
Protein Classification
T-complex protein 1 subunit zeta ( domain architecture ID 1003097 )
T-complex protein 1 subunit zeta is a component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis
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: 780.46
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 3 AI K AV N S KAE VA R AR AAL AV NI C AARGLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL D EM --------------- 67
Cdd:TIGR02347 1 SV K LL N P KAE 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 302058292 68 ------------------------------ G L HPRII A EGFE A A KIK AL EV L EEV KV T KE -- MK R KI LL D VARTSL Q TK V 115
Cdd:TIGR02347 81 aqdditgdgttstvlligellkqaeryile G V HPRII T EGFE I A RKE AL QF L DKF KV K KE de VD R EF LL N VARTSL R TK L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 116 H A E LAD V LTE V VVD S VLA VRRP G YP IDLFMVEIMEMKHK LG TDT K LI Q GLVLDHGARHPDM KK RV ED A F IL I CNVSLEYE 195
Cdd:TIGR02347 161 P A D LAD Q LTE I VVD A VLA IKKD G ED IDLFMVEIMEMKHK SA TDT T LI R GLVLDHGARHPDM PR RV KN A Y IL T CNVSLEYE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 196 KTEVNSGFFY KT AE EK EKLVKAERKF IE DRV Q KII D LK D KVC AQ S - N KGFVVINQKGIDP F SLD S LAK H GI V ALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFY SS AE QR EKLVKAERKF VD DRV K KII E LK K KVC GK S p D KGFVVINQKGIDP P SLD L LAK E GI M ALRRAKRR 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 NMERL S LACGG M A V NS F EDLT VD CLG H AGLVYE Y T L GEEK F TFIEEC V NP C S V T L L V KGPN K HT LT Q V KDA I RDGLRA I K 354
Cdd:TIGR02347 321 NMERL T LACGG E A L NS V EDLT PE CLG W AGLVYE T T I GEEK Y TFIEEC K NP K S C T I L I KGPN D HT IA Q I KDA V RDGLRA V K 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 355 NAIED G C M VPGAGA I E V A MAEA L VT YK N S I KG R A R LGV Q AFA D ALL I IPK V LA Q N A G Y D P Q E TLVK VQA EH V E SKQL VGV 434
Cdd:TIGR02347 401 NAIED K C V VPGAGA F E I A AYRH L KE YK K S V KG K A K LGV E AFA N ALL V IPK T LA E N S G F D A Q D TLVK LED EH D E GGEV VGV 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 302058292 435 DLNTGEP MVAADA 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: 780.46
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 3 AI K AV N S KAE VA R AR AAL AV NI C AARGLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL D EM --------------- 67
Cdd:TIGR02347 1 SV K LL N P KAE 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 302058292 68 ------------------------------ G L HPRII A EGFE A A KIK AL EV L EEV KV T KE -- MK R KI LL D VARTSL Q TK V 115
Cdd:TIGR02347 81 aqdditgdgttstvlligellkqaeryile G V HPRII T EGFE I A RKE AL QF L DKF KV K KE de VD R EF LL N VARTSL R TK L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 116 H A E LAD V LTE V VVD S VLA VRRP G YP IDLFMVEIMEMKHK LG TDT K LI Q GLVLDHGARHPDM KK RV ED A F IL I CNVSLEYE 195
Cdd:TIGR02347 161 P A D LAD Q LTE I VVD A VLA IKKD G ED IDLFMVEIMEMKHK SA TDT T LI R GLVLDHGARHPDM PR RV KN A Y IL T CNVSLEYE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 196 KTEVNSGFFY KT AE EK EKLVKAERKF IE DRV Q KII D LK D KVC AQ S - N KGFVVINQKGIDP F SLD S LAK H GI V ALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFY SS AE QR EKLVKAERKF VD DRV K KII E LK K KVC GK S p D KGFVVINQKGIDP P SLD L LAK E GI M ALRRAKRR 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 NMERL S LACGG M A V NS F EDLT VD CLG H AGLVYE Y T L GEEK F TFIEEC V NP C S V T L L V KGPN K HT LT Q V KDA I RDGLRA I K 354
Cdd:TIGR02347 321 NMERL T LACGG E A L NS V EDLT PE CLG W AGLVYE T T I GEEK Y TFIEEC K NP K S C T I L I KGPN D HT IA Q I KDA V RDGLRA V K 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 355 NAIED G C M VPGAGA I E V A MAEA L VT YK N S I KG R A R LGV Q AFA D ALL I IPK V LA Q N A G Y D P Q E TLVK VQA EH V E SKQL VGV 434
Cdd:TIGR02347 401 NAIED K C V VPGAGA F E I A AYRH L KE YK K S V KG K A K LGV E AFA N ALL V IPK T LA E N S G F D A Q D TLVK LED EH D E GGEV VGV 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 302058292 435 DLNTGEP MVAADA 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 ...
23-481
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: 756.41
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA R GLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL D EM ----------------------------------- 67
Cdd:cd03342 17 NI S AA K GLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL S EM qiqhptasmiaraataqdditgdgttsnvlligel 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HPRII A EGFE A AK I KAL EV LE EV KV TK E MK -- R KI LL D VARTSL Q TK V HA E LAD V LTE V VVD S VLA VR 135
Cdd:cd03342 97 lkqaeryiqe G V HPRII T EGFE L AK N KAL KF LE SF KV PV E ID td R EL LL S VARTSL R TK L HA D LAD Q LTE I VVD A VLA IY 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 R P GY PIDL F MVEIM E M K HK LGT DTKLI Q GLVLDHGARHPDM K KRVE D A F IL I CNVSLEYEKTEVNSGFFY K taeekeklv 215
Cdd:cd03342 177 K P DE PIDL H MVEIM Q M Q HK SDS DTKLI R GLVLDHGARHPDM P KRVE N A Y IL T CNVSLEYEKTEVNSGFFY S --------- 247
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 216 kaerkfiedrvqkiidlkdkvcaqsnkgf VVINQKGIDP F SLD S LAK H GI V ALRRAKRRNMERL S LACGG M A V NS FE DL T 295
Cdd:cd03342 248 ----------------------------- VVINQKGIDP P SLD M LAK E GI L ALRRAKRRNMERL T LACGG V A M NS VD DL S 298
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 296 VD CLG H AGLVYE Y TLGEEK F TFIE ECV NP C S V T L L V KGPN K HT L TQ V KDAIRDGLRA I KNAIED G C M VPGAGA I EVA MAE 375
Cdd:cd03342 299 PE CLG Y AGLVYE R TLGEEK Y TFIE GVK NP K S C T I L I KGPN D HT I TQ I KDAIRDGLRA V KNAIED K C V VPGAGA F EVA LYA 378
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 376 A L VTY K N S I KG R A R LGVQAFADALL I IPK V LA Q N A G Y D P QETLVK V Q A E HV E SK Q LV GVDL N TGEPM VAADA G V WDNY C V 455
Cdd:cd03342 379 H L KEF K K S V KG K A K LGVQAFADALL V IPK T LA E N S G L D V QETLVK L Q D E YA E GG Q VG GVDL D TGEPM DPESE G I WDNY S V 458
490 500
....*....|....*....|....*.
gi 302058292 456 K K Q L LHS C TVIA TNI LLVDEI M RAG M 481
Cdd:cd03342 459 K 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
6.84e-172
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: 492.49
E-value: 6.84e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 30 L Q D VL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L D 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 302058292 68 --- G L HP RI I A EG F E A A KI KALE V L EEVKV -- TKEMK R KI LL D VARTSL QT K VHAELA D V L TEV VVD S VLA VRRPGYPI D 142
Cdd:pfam00118 81 laa G V HP TT I I EG Y E K A LE KALE I L DSIIS ip VEDVD R ED LL K VARTSL SS K IISRES D F L AKL VVD A VLA IPKNDGSF D 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 143 L FMVEIMEMKHKLGT D TK L IQ G L VLD H G AR HPDM K KR V E D A FI L IC N V SLEYEKTE VNSGFFYKT AE EK E KLV KAE RKF I 222
Cdd:pfam00118 161 L GNIGVVKILGGSLE 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 302058292 223 EDR V Q KIID LKDK V caqsnkgfv V IN QKGID PFS L DS LAK H GI V ALRR A K R R NM ERL SL A C G GM AV N S FE DLT V D C LG H A 302
Cdd:pfam00118 241 LEI V E KIID SGVN V --------- V VC QKGID DLA L HF LAK N GI M ALRR V K K R DL ERL AK A T G AR AV S S LD DLT P D D LG T A 311
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 303 G L V Y E YTL G E EK F TFIE E C VN P CSV T L L VK G PNK H T L TQVKDA I R D G L RAI KNAIED GCM VPG A GA I E VAM A E AL VT Y KN 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 DEIERS I H D A L CVV KNAIED PRV VPG G GA V E MEL A R AL RE Y AK 391
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 383 S IK G RAR L GVQ AFA D AL LI IPK V LA Q NAG Y DP Q E T L VKVQ A E H VESKQLV G V D LN TGE PMVAAD AGV W D NYC VK K Q L L H S 462
Cdd:pfam00118 392 S VS G KEQ L AIE AFA E AL EV IPK T LA E NAG L DP I E V L AELR A A H ASGEKHA G I D VE TGE IIDMKE AGV V D PLK VK R Q A L K S 471
490
....*....|....*...
gi 302058292 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;
23-480
8.17e-114
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 345.33
E-value: 8.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQDVL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L D EM ----------------------------------- 67
Cdd:NF041082 22 NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GD VVI T N DG VTI L K EM diehpaakmivevaktqddevgdgtttavvlagel 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- GL HP R IIAEG FEA A KI KALE V L E E VKVT - KEMKRKI L LDV A R T SLQT K VHAELA D V L TEV VVD S V L AV RR 136
Cdd:NF041082 102 lkkaeelldq DI HP T IIAEG YRL A AE KALE I L D E IAIK v DPDDKET L KKI A A T AMTG K GAEAAK D K L ADL VVD A V K AV AE 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P -- GY PI DL FMVEI me M K HKL G T -- D TK L IQ G L V L D HGAR HP D M K KRVE D A F I LICNVS LE YE KTE VNSGFFYKTAEEKE 212
Cdd:NF041082 182 K dg GY NV DL DNIKV -- E K KVG G 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 IDAKISITDPDQLQ 259
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 213 KLVKA E R K FIEDR V Q KI I D lkdkvc AQS N kgf VV IN QKGID PFSLDS LAK H GI V A L RR A K RRN ME R L SL A C G GMA V N S FE 292
Cdd:NF041082 260 AFLDQ E E K MLKEM V D KI A D ------ SGA N --- VV FC QKGID DLAQHY LAK E GI L A V RR V K KSD ME K L AK A T G ARI V T S ID 330
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 293 DL TVDC LG H AGLV Y E YTL G EE K FT F I E E C V NP CS VT L L VK G PNK H TLTQ V KD A IR D G LR AIKNAI EDG CM V P G A GA I EV A 372
Cdd:NF041082 331 DL SPED 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 VVDE V ER A LE D A LR VVRVVL EDG KV V A G G GA P EV E 410
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 373 M A EA L VT Y KN S IK GR AR L GVQ AFA D AL L IIP KV LA Q NAG Y DP QET LV KVQAE H VESKQLV G V D LN TG EPMVAADA GV WDN 452
Cdd:NF041082 411 L A LR L RE Y AA S VG GR EQ L AIE AFA E AL E IIP RT LA E NAG L DP IDA LV ELRSA H EKGNKTA G L D VY TG KVVDMLEI GV VEP 490
490 500
....*....|....*....|....*...
gi 302058292 453 YC VK K Q LLH S C T VI A TN IL LV D EIMR A G 480
Cdd:NF041082 491 LR VK T Q AIK S A T EA A VM IL RI D DVIA A A 518
thermosome_beta
NF041083
thermosome subunit beta;
23-480
1.46e-112
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 342.31
E-value: 1.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQDVL RT N LGPKG TM KMLV SGA GDI KL T K DG NVL L D EM ----------------------------------- 67
Cdd:NF041083 22 NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GDI VI T N DG ATI L K EM dvqhpaakmlvevaktqddevgdgtttavvlagel 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- GL HP R IIA E G FEA A KI KA L E V L E E VKVT - KEMK R KI L LDV A R TSL QT K VHA E LA D V L T E VV V DS V LA V -- 134
Cdd:NF041083 102 lkkaeelldq NI HP T IIA N G YRL A AE KA I E I L D E IAEK v DPDD R ET L KKI A E TSL TS K GVE E AR D Y L A E IA V KA V KQ V ae 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 - R RPG Y PI DL FMVE I MEMKHKLGT DT K LI Q G L V L D HGAR HP D M K KRVE D A F I LICNVS LE YE KTE VNSGFFYKTAEEKE K 213
Cdd:NF041083 182 k R DGK Y YV DL DNIQ I EKKHGGSIE DT Q LI Y G I V I D KEVV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAEIRITDPDQLQ K 261
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 214 LVKA E R K FIEDR V Q KI ID lkdkvc AQS N kgf VV IN QKGID PFSLDS LAK H GI V A L RR A K RRN ME R L SL A C G GMA V NSFE D 293
Cdd:NF041083 262 FLDQ E E K MLKEM V D KI KA ------ TGA N --- VV FC QKGID DLAQHY LAK A GI L A V RR V K KSD ME K L AK A T G ARI V TNID D 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 294 LT VDC LG H A G LV Y E YTL G EE K FT F I E E C V NP CS VT L L VK G PNK H TLTQVKD A IR D G L RAIKN A I EDG CM V P G A GA I EV AM 373
Cdd:NF041083 333 LT PED LG Y A E LV E E RKV G DD K MV F V E G C K NP KA VT I L IR G GTE H VVDEAER A LE D A L SVVAD A V EDG KI V A G G GA P EV EL 412
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 374 A EA L VT Y KNSIK GR AR L G V Q AFA D AL L IIP KV LA Q NAG Y DP QET LVK VQAE H VES K QLV G VDLN TGE PMVAADA GV WDNY 453
Cdd:NF041083 413 A KR L RE Y AATVG GR EQ L A V E AFA E AL E IIP RT LA E NAG L DP IDI LVK LRSA H EKG K KWA G INVF TGE VVDMWEL GV IEPL 492
490 500
....*....|....*....|....*..
gi 302058292 454 C VK K Q LLH S C T VI AT N IL LV D EIMR A G 480
Cdd:NF041083 493 R 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]; ...
23-479
3.68e-65
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 218.41
E-value: 3.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI CAARG L Q D VLRTN LGPKG TMK MLV SGA GD IKL T K DG NVLLD E M ----------------------------------- 67
Cdd:COG0459 15 NI RGVKA L A D AVKVT LGPKG RNV MLV KSF GD PTI T N DG VTIAK E I eledpfenmgaqlvkevasktndeagdgtttatvl 94
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 -------------- G LH P RI I AE G FEA A KI KA L E V L EE -- VK V TK emk RKI L LD VA RT S LQTK vhaela DVLT E VVVDSV 131
Cdd:COG0459 95 agallkeglklvaa G AN P TD I KR G IDK A VE KA V E E L KK ia KP V DD --- KEE L AQ VA TI S ANGD ------ EEIG E LIAEAM 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 132 LA V RRP G Y pidl FM VE imem KH K - L G T DTKLIQ G LVL D H G ARH P D ------- M KKRV E D A F IL ICNVSLE yektevnsgf 203
Cdd:COG0459 166 EK V GKD G V ---- IT VE ---- EG K g L E T ELEVVE G MQF D K G YLS P Y fvtdpek M PAEL E N A Y IL LTDKKIS ---------- 227
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 204 fyktaeekeklvkaerkfied RV Q KIID L KD KV c AQS N K G f VV I NQKG ID PFS L DS L AKH GI VALR R A --------- K RR 274
Cdd:COG0459 228 --------------------- SI Q DLLP L LE KV - AQS G K P - LL I IAED ID GEA L AT L VVN GI RGVL R V vavkapgfg D RR 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 N -- M E RLSLAC GG MAVN ----- SF ED L T V D C LG H A GL V YE ytl GEEKF T FI E ECV NP CSVTL LV KGPNKHTLTQV K DAIR 347
Cdd:COG0459 285 K am L E DIAILT GG RVIS edlgl KL ED V T L D D LG R A KR V EV --- DKDNT T IV E GAG NP KAIVI LV GAATEVEVKER K RRVE 361
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 348 D G L R A IKN A I E D G C m VPG A GA IEVAM A E AL VTYKNSIK G RAR LG VQAF A D AL LIIPKVL A Q NAG Y D PQETLV KV Q A E hve 427
Cdd:COG0459 362 D A L H A TRA A V E E G I - VPG G GA ALLRA A R AL RELAAKLE G DEQ LG IEIV A R AL EAPLRQI A E NAG L D GSVVVE KV R A A --- 437
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 302058292 428 SKQLV G V D LN TGE PMVAAD AGV W D NYC VK KQL L HSCTVI A TN IL LVDEIMRA 479
Cdd:COG0459 438 KDKGF G F D AA TGE YVDMLE AGV I D PAK VK RSA L QNAASV A GL IL TTEAVIAD 489
PTZ00212
PTZ00212
T-complex protein 1 subunit beta; Provisional
23-479
2.29e-55
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 193.32
E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NICA A RGLQ D VLR T N LGPKG TM K M L VS ----- GA G DIKL T K DG NVL L --------------------- D E M G -------- 68
Cdd:PTZ00212 27 SFVG A IAVA D LVK T T LGPKG MD K I L QP msegp RS G NVTV T N DG ATI L ksvwldnpaakilvdisktqd E E V G dgttsvvv 106
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 69 ---------------- L HP RI I A EG FEA A KIK A LEV LEE VKVT ---- K E MKRKI LL DV ART S L QT K VHAELA D VLTEVV V 128
Cdd:PTZ00212 107 lagellreaeklldqk I HP QT I I EG WRM A LDV A RKA LEE IAFD hgsd E E KFKED LL NI ART T L SS K LLTVEK D HFAKLA V 186
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 129 D S VL AVRRP G ypi D L FMVE I ME mkh K L G --- T D TK L IQ G LV L DH -- G ARH P dmk KR V E DAF IL IC N VSLEYE K ----- TE 198
Cdd:PTZ00212 187 D A VL RLKGS G --- N L DYIQ I IK --- K P G gtl R D SY L ED G FI L EK ki G VGQ P --- KR L E NCK IL VA N TPMDTD K ikiyg AK 257
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 199 V NSGFFY K T AE ekek LVK AE RKFIEDR V Q KI ID lkdkvc AQS N kgf V V IN QKG I DPFSLDSL A KH GI V A LRR A KRRN MER 278
Cdd:PTZ00212 258 V KVDSME K V AE ---- IEA AE KEKMKNK V D KI LA ------ HGC N --- V F IN RQL I YNYPEQLF A EA GI M A IEH A DFDG MER 324
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 279 L SL A C G GMA V NS F EDLTVDC LGH AG L VY E YTL GE E K FTFIEE C VNPCSV T LLVK G PNK H T L TQVKDAIR D G L RAIKNAIE 358
Cdd:PTZ00212 325 L AA A L G AEI V ST F DTPEKVK LGH CD L IE E IMI GE D K LIRFSG C AKGEAC T IVLR G AST H I L DEAERSLH D A L CVLSQTVK 404
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 359 D GCM V P G A G AI E VA MA E A LVTYKNSIK G RAR L GVQ AFA D AL LI IP KVL A Q N A GYD PQ E TLV K VQ AEH VESKQLV G V D LNT 438
Cdd:PTZ00212 405 D TRV V L G G G CS E ML MA N A VEELAKKVE G KKS L AIE AFA K AL RQ IP TII A D N G GYD SA E LVS K LR AEH YKGNKTA G I D MEK 484
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 302058292 439 G EPMVAADA 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 485 G TVGDMKEL 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: 780.46
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 3 AI K AV N S KAE VA R AR AAL AV NI C AARGLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL D EM --------------- 67
Cdd:TIGR02347 1 SV K LL N P KAE 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 302058292 68 ------------------------------ G L HPRII A EGFE A A KIK AL EV L EEV KV T KE -- MK R KI LL D VARTSL Q TK V 115
Cdd:TIGR02347 81 aqdditgdgttstvlligellkqaeryile G V HPRII T EGFE I A RKE AL QF L DKF KV K KE de VD R EF LL N VARTSL R TK L 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 116 H A E LAD V LTE V VVD S VLA VRRP G YP IDLFMVEIMEMKHK LG TDT K LI Q GLVLDHGARHPDM KK RV ED A F IL I CNVSLEYE 195
Cdd:TIGR02347 161 P A D LAD Q LTE I VVD A VLA IKKD G ED IDLFMVEIMEMKHK SA TDT T LI R GLVLDHGARHPDM PR RV KN A Y IL T CNVSLEYE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 196 KTEVNSGFFY KT AE EK EKLVKAERKF IE DRV Q KII D LK D KVC AQ S - N KGFVVINQKGIDP F SLD S LAK H GI V ALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFY SS AE QR EKLVKAERKF VD DRV K KII E LK K KVC GK S p D KGFVVINQKGIDP P SLD L LAK E GI M ALRRAKRR 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 NMERL S LACGG M A V NS F EDLT VD CLG H AGLVYE Y T L GEEK F TFIEEC V NP C S V T L L V KGPN K HT LT Q V KDA I RDGLRA I K 354
Cdd:TIGR02347 321 NMERL T LACGG E A L NS V EDLT PE CLG W AGLVYE T T I GEEK Y TFIEEC K NP K S C T I L I KGPN D HT IA Q I KDA V RDGLRA V K 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 355 NAIED G C M VPGAGA I E V A MAEA L VT YK N S I KG R A R LGV Q AFA D ALL I IPK V LA Q N A G Y D P Q E TLVK VQA EH V E SKQL VGV 434
Cdd:TIGR02347 401 NAIED K C V VPGAGA F E I A AYRH L KE YK K S V KG K A K LGV E AFA N ALL V IPK T LA E N S G F D A Q D TLVK LED EH D E GGEV VGV 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 302058292 435 DLNTGEP MVAADA 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 ...
23-481
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: 756.41
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA R GLQDVL R TNLGPKGT M KMLVSGAGDIKLTKDGNVLL D EM ----------------------------------- 67
Cdd:cd03342 17 NI S AA K GLQDVL K TNLGPKGT L KMLVSGAGDIKLTKDGNVLL S EM qiqhptasmiaraataqdditgdgttsnvlligel 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HPRII A EGFE A AK I KAL EV LE EV KV TK E MK -- R KI LL D VARTSL Q TK V HA E LAD V LTE V VVD S VLA VR 135
Cdd:cd03342 97 lkqaeryiqe G V HPRII T EGFE L AK N KAL KF LE SF KV PV E ID td R EL LL S VARTSL R TK L HA D LAD Q LTE I VVD A VLA IY 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 R P GY PIDL F MVEIM E M K HK LGT DTKLI Q GLVLDHGARHPDM K KRVE D A F IL I CNVSLEYEKTEVNSGFFY K taeekeklv 215
Cdd:cd03342 177 K P DE PIDL H MVEIM Q M Q HK SDS DTKLI R GLVLDHGARHPDM P KRVE N A Y IL T CNVSLEYEKTEVNSGFFY S --------- 247
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 216 kaerkfiedrvqkiidlkdkvcaqsnkgf VVINQKGIDP F SLD S LAK H GI V ALRRAKRRNMERL S LACGG M A V NS FE DL T 295
Cdd:cd03342 248 ----------------------------- VVINQKGIDP P SLD M LAK E GI L ALRRAKRRNMERL T LACGG V A M NS VD DL S 298
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 296 VD CLG H AGLVYE Y TLGEEK F TFIE ECV NP C S V T L L V KGPN K HT L TQ V KDAIRDGLRA I KNAIED G C M VPGAGA I EVA MAE 375
Cdd:cd03342 299 PE CLG Y AGLVYE R TLGEEK Y TFIE GVK NP K S C T I L I KGPN D HT I TQ I KDAIRDGLRA V KNAIED K C V VPGAGA F EVA LYA 378
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 376 A L VTY K N S I KG R A R LGVQAFADALL I IPK V LA Q N A G Y D P QETLVK V Q A E HV E SK Q LV GVDL N TGEPM VAADA G V WDNY C V 455
Cdd:cd03342 379 H L KEF K K S V KG K A K LGVQAFADALL V IPK T LA E N S G L D V QETLVK L Q D E YA E GG Q VG GVDL D TGEPM DPESE G I WDNY S V 458
490 500
....*....|....*....|....*.
gi 302058292 456 K K Q L LHS C TVIA TNI LLVDEI M RAG M 481
Cdd:cd03342 459 K 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
6.84e-172
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: 492.49
E-value: 6.84e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 30 L Q D VL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L D 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 302058292 68 --- G L HP RI I A EG F E A A KI KALE V L EEVKV -- TKEMK R KI LL D VARTSL QT K VHAELA D V L TEV VVD S VLA VRRPGYPI D 142
Cdd:pfam00118 81 laa G V HP TT I I EG Y E K A LE KALE I L DSIIS ip VEDVD R ED LL K VARTSL SS K IISRES D F L AKL VVD A VLA IPKNDGSF D 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 143 L FMVEIMEMKHKLGT D TK L IQ G L VLD H G AR HPDM K KR V E D A FI L IC N V SLEYEKTE VNSGFFYKT AE EK E KLV KAE RKF I 222
Cdd:pfam00118 161 L GNIGVVKILGGSLE 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 302058292 223 EDR V Q KIID LKDK V caqsnkgfv V IN QKGID PFS L DS LAK H GI V ALRR A K R R NM ERL SL A C G GM AV N S FE DLT V D C LG H A 302
Cdd:pfam00118 241 LEI V E KIID SGVN V --------- V VC QKGID DLA L HF LAK N GI M ALRR V K K R DL ERL AK A T G AR AV S S LD DLT P D D LG T A 311
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 303 G L V Y E YTL G E EK F TFIE E C VN P CSV T L L VK G PNK H T L TQVKDA I R D G L RAI KNAIED GCM VPG A GA I E VAM A E AL VT Y KN 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 DEIERS I H D A L CVV KNAIED PRV VPG G GA V E MEL A R AL RE Y AK 391
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 383 S IK G RAR L GVQ AFA D AL LI IPK V LA Q NAG Y DP Q E T L VKVQ A E H VESKQLV G V D LN TGE PMVAAD AGV W D NYC VK K Q L L H S 462
Cdd:pfam00118 392 S VS G KEQ L AIE AFA E AL EV IPK T LA E NAG L DP I E V L AELR A A H ASGEKHA G I D VE TGE IIDMKE AGV V D PLK VK R Q A L K S 471
490
....*....|....*...
gi 302058292 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 ...
23-478
1.47e-158
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: 457.66
E-value: 1.47e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RG L Q D VLR T N LGPKG TM KMLV SGA GD IKL T K DG NVL L D E M ----------------------------------- 67
Cdd:cd00309 13 NI N AA KA L A D AVK T T LGPKG MD KMLV DSL GD PTI T N DG ATI L K E I evehpaakllvevaksqddevgdgtttvvvlagel 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HP RI I AE G F E A A KI KALE V L E E VK V TKEMK - R KI LL D VA R TSL QT K VHAELA D V L T E V VVD S VL A V RR 136
Cdd:cd00309 93 lkeaekllaa G I HP TE I IR G Y E K A VE KALE I L K E IA V PIDVE d R EE LL K VA T TSL NS K LVSGGD D F L G E L VVD A VL K V GK 172
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 PGYPI DL FMVEIMEM K HKLGT D TK L IQ G L V L D H G ARH P D M K KR V E D A F IL ICNVS LEY ektevnsgffyktaeekeklvk 216
Cdd:cd00309 173 ENGDV DL GVIRVEKK K GGSLE 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 302058292 217 aerkfiedrvqkiidlkdkvcaqsnkgf VVI NQ KGID PFS L DS LAK H GI V A L RR AKRRNM ER LSL A C G GMA V NSF EDLT V 296
Cdd:cd00309 231 ---------------------------- VVI AE KGID DEA L HY LAK L GI M A V RR VRKEDL ER IAK A T G ATI V SRL EDLT P 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 297 DC LG H AGLV Y E YTL G E EK F TFIE E C VNPCSV T L L VK G PNKHT L TQVKDAIR D G L R A IKN A I EDG CM VPG A GA I E VAMAE A 376
Cdd:cd00309 283 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 A VRA A V EDG GI VPG G GA A E IELSK A 362
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 377 L VTYKNSIK G RAR LG VQ AFADAL LI IP KV LA Q NAG Y DP Q E TLV K VQ A E H V E SKQLV G V D LN TGE PMVAAD AG VW D NYC VK 456
Cdd:cd00309 363 L EELAKTLP G KEQ LG IE AFADAL EV IP RT LA E NAG L DP I E VVT K LR A K H A E GGGNA G G D VE TGE IVDMKE AG II D PLK VK 442
490 500
....*....|....*....|..
gi 302058292 457 K Q L L H S C T VI A TN IL LV D E I MR 478
Cdd:cd00309 443 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 ...
23-480
7.71e-114
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: 345.40
E-value: 7.71e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQDVL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L D EM ----------------------------------- 67
Cdd:cd03343 20 NI A AA KAVAEAV RT T LGPKG MD KMLV DSL GD VTI T N DG ATI L K EM diehpaakmlvevaktqdeevgdgtttavvlagel 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- GL HP RI I A EG FEA A KI KALE V L E E -- V KV TKE m KRKI L LDV A R TSL QT K VHAELA D V L TEV VVD S VL A V - 134
Cdd:cd03343 100 lekaedlldq NI HP TV I I EG YRL A AE KALE L L D E ia I KV DPD - DKDT L RKI A K TSL TG K GAEAAK D K L ADL VVD A VL Q V a 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 -- R RPG Y PI DL FMVE I M em K HKL G T -- DT K LI Q G L V L D HGAR HP D M K KRVE D A F I LICNVS LE YE KTE VNSGFFYKTAEE 210
Cdd:cd03343 179 ek R DGK Y VV DL DNIK I E -- K KTG G S vd DT E LI R G I V I D KEVV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAKIRITSPDQ 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 KEKLVKA E RKFIEDR V Q KI I D lkdkvc AQS N kgf VV IN QKGID PFSLDS LAK H GI V A L RR A K RRN ME R L SL A C G GMA V NS 290
Cdd:cd03343 257 LQAFLEQ E EAMLKEM V D KI A D ------ TGA N --- VV FC QKGID DLAQHY LAK A GI L A V RR V K KSD ME K L AR A T G AKI V TN 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 FE DLT VDC LG H A G LV Y E YTL G EE K FT F I E E C V NP CS VT L L VK G PNK H TLTQVKD A IR D G LR AIKN A I EDG CM V P G A GA I E 370
Cdd:cd03343 328 ID DLT PED 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 VVAD A L EDG KV V A G G GA V E 407
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 371 VAM A EA L VT Y KN S IK GR AR L G V Q AFADAL LI IP KV LA Q NAG Y DP QE TLV KVQ A E H VESKQLV G V D LN TGE PMVAADA GV W 450
Cdd:cd03343 408 IEL A KR L RE Y AR S VG GR EQ L A V E AFADAL EE IP RT LA E NAG L DP ID TLV ELR A A H EKGNKNA G L D VY TGE VVDMLEK GV I 487
490 500 510
....*....|....*....|....*....|
gi 302058292 451 DNYC VKKQ LLH S C T VI AT N IL LV D EIMR A G 480
Cdd:cd03343 488 EPLR VKKQ AIK S A T EA AT M IL RI D DVIA A K 517
thermosome_alpha
NF041082
thermosome subunit alpha;
23-480
8.17e-114
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 345.33
E-value: 8.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQDVL RT N LGPKG TM KMLV SGA GD IKL T K DG NVL L D EM ----------------------------------- 67
Cdd:NF041082 22 NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GD VVI T N DG VTI L K EM diehpaakmivevaktqddevgdgtttavvlagel 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- GL HP R IIAEG FEA A KI KALE V L E E VKVT - KEMKRKI L LDV A R T SLQT K VHAELA D V L TEV VVD S V L AV RR 136
Cdd:NF041082 102 lkkaeelldq DI HP T IIAEG YRL A AE KALE I L D E IAIK v DPDDKET L KKI A A T AMTG K GAEAAK D K L ADL VVD A V K AV AE 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P -- GY PI DL FMVEI me M K HKL G T -- D TK L IQ G L V L D HGAR HP D M K KRVE D A F I LICNVS LE YE KTE VNSGFFYKTAEEKE 212
Cdd:NF041082 182 K dg GY NV DL DNIKV -- E K KVG G 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 IDAKISITDPDQLQ 259
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 213 KLVKA E R K FIEDR V Q KI I D lkdkvc AQS N kgf VV IN QKGID PFSLDS LAK H GI V A L RR A K RRN ME R L SL A C G GMA V N S FE 292
Cdd:NF041082 260 AFLDQ E E K MLKEM V D KI A D ------ SGA N --- VV FC QKGID DLAQHY LAK E GI L A V RR V K KSD ME K L AK A T G ARI V T S ID 330
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 293 DL TVDC LG H AGLV Y E YTL G EE K FT F I E E C V NP CS VT L L VK G PNK H TLTQ V KD A IR D G LR AIKNAI EDG CM V P G A GA I EV A 372
Cdd:NF041082 331 DL SPED 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 VVDE V ER A LE D A LR VVRVVL EDG KV V A G G GA P EV E 410
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 373 M A EA L VT Y KN S IK GR AR L GVQ AFA D AL L IIP KV LA Q NAG Y DP QET LV KVQAE H VESKQLV G V D LN TG EPMVAADA GV WDN 452
Cdd:NF041082 411 L A LR L RE Y AA S VG GR EQ L AIE AFA E AL E IIP RT LA E NAG L DP IDA LV ELRSA H EKGNKTA G L D VY TG KVVDMLEI GV VEP 490
490 500
....*....|....*....|....*...
gi 302058292 453 YC VK K Q LLH S C T VI A TN IL LV D EIMR A G 480
Cdd:NF041082 491 LR VK T Q AIK S A T EA A VM IL RI D DVIA A A 518
thermosome_beta
NF041083
thermosome subunit beta;
23-480
1.46e-112
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 342.31
E-value: 1.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQDVL RT N LGPKG TM KMLV SGA GDI KL T K DG NVL L D EM ----------------------------------- 67
Cdd:NF041083 22 NI M AA KAVAEAV RT T LGPKG MD KMLV DSL GDI VI T N DG ATI L K EM dvqhpaakmlvevaktqddevgdgtttavvlagel 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- GL HP R IIA E G FEA A KI KA L E V L E E VKVT - KEMK R KI L LDV A R TSL QT K VHA E LA D V L T E VV V DS V LA V -- 134
Cdd:NF041083 102 lkkaeelldq NI HP T IIA N G YRL A AE KA I E I L D E IAEK v DPDD R ET L KKI A E TSL TS K GVE E AR D Y L A E IA V KA V KQ V ae 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 - R RPG Y PI DL FMVE I MEMKHKLGT DT K LI Q G L V L D HGAR HP D M K KRVE D A F I LICNVS LE YE KTE VNSGFFYKTAEEKE K 213
Cdd:NF041083 182 k R DGK Y YV DL DNIQ I EKKHGGSIE DT Q LI Y G I V I D KEVV HP G M P KRVE N A K I ALLDAP LE VK KTE IDAEIRITDPDQLQ K 261
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 214 LVKA E R K FIEDR V Q KI ID lkdkvc AQS N kgf VV IN QKGID PFSLDS LAK H GI V A L RR A K RRN ME R L SL A C G GMA V NSFE D 293
Cdd:NF041083 262 FLDQ E E K MLKEM V D KI KA ------ TGA N --- VV FC QKGID DLAQHY LAK A GI L A V RR V K KSD ME K L AK A T G ARI V TNID D 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 294 LT VDC LG H A G LV Y E YTL G EE K FT F I E E C V NP CS VT L L VK G PNK H TLTQVKD A IR D G L RAIKN A I EDG CM V P G A GA I EV AM 373
Cdd:NF041083 333 LT PED LG Y A E LV E E RKV G DD K MV F V E G C K NP KA VT I L IR G GTE H VVDEAER A LE D A L SVVAD A V EDG KI V A G G GA P EV EL 412
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 374 A EA L VT Y KNSIK GR AR L G V Q AFA D AL L IIP KV LA Q NAG Y DP QET LVK VQAE H VES K QLV G VDLN TGE PMVAADA GV WDNY 453
Cdd:NF041083 413 A KR L RE Y AATVG GR EQ L A V E AFA E AL E IIP RT LA E NAG L DP IDI LVK LRSA H EKG K KWA G INVF TGE VVDMWEL GV IEPL 492
490 500
....*....|....*....|....*..
gi 302058292 454 C VK K Q LLH S C T VI AT N IL LV D EIMR A G 480
Cdd:NF041083 493 R 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 ...
23-476
1.72e-76
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: 249.14
E-value: 1.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 N I C AA RGLQDV LRT N LGP K G TM K M LVS GA G DIKL T K DG NVL L DE M ----------------------------------- 67
Cdd:cd03339 28 H I L AA KSVANI LRT S LGP R G MD K I LVS PD G EVTV T N DG ATI L EK M dvdhqiakllvelsksqddeigdgttgvvvlagal 107
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HP RI IA E G F E A A KIK A L E V LEE VKVTK E --- MKRKI L LDV A R TSL QT K VHAELADVLT E VV VD S VL A V 134
Cdd:cd03339 108 leqaeklldr G I HP IR IA D G Y E Q A CKI A V E H LEE IADKI E fsp DNKEP L IQT A M TSL GS K IVSRCHRQFA E IA VD A VL S V 187
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 ---- R RP gyp IDL fmv E IMEMKH K L G --- T DTKL IQ G L V L D HGAR HP D M K K R V E DA F I L I CNVSL E YE K TEVNSGFFYKT 207
Cdd:cd03339 188 adle R KD --- VNF --- E LIKVEG K V G grl E DTKL VK G I V I D KDFS HP Q M P K E V K DA K I A I LTCPF E PP K PKTKHKLDITS 261
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 208 A E EKE KL VKA E R K FIEDR V QKII D lkdkvc A QS N kgf V VI N Q K G I D PFSLDS L AKH G IV A L R RAKRRNM E RLSL A C GG MA 287
Cdd:cd03339 262 V E DYK KL QEY E Q K YFREM V EQVK D ------ A GA N --- L VI C Q W G F D DEANHL L LQN G LP A V R WVGGVEI E LIAI A T GG RI 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 288 V NS FEDL TVDC LG H AGLV Y E YTL G -- EE K FTF IE E C V N PCS VT LLVK G P NK HTLTQV K DAIR D G L RAIK N A I E D GCM V P G 365
Cdd:cd03339 333 V PR FEDL SPEK LG K AGLV R E ISF G tt KD K MLV IE G C P N SKA VT IFIR G G NK MIIEEA K RSLH D A L CVVR N L I R D NRI V Y G 412
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 366 A GA I E VAMAE A LVTYKNSIK G RARLGVQ AFADAL LI IP KV LA Q N A G YD P Q ETL VK V Q A EH V ES K Q - LV G V D LNTGEPMVA 444
Cdd:cd03339 413 G GA A E ISCSL A VEKAADKCS G IEQYAMR AFADAL ES IP LA LA E N S G LN P I ETL SE V K A RQ V KE K N p HL G I D CLGRGTNDM 492
490 500 510
....*....|....*....|....*....|..
gi 302058292 445 ADAG V WDNYCV KKQ LLHSC T VIATN IL LV D EI 476
Cdd:cd03339 493 KEQK V FETLIS KKQ QILLA T QVVKM IL KI D DV 524
chap_CCT_epsi
TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
23-480
8.75e-70
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: 231.62
E-value: 8.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQDV LRT N LGPKG TM KML V S GA GDI KL T K DG NVL L DE M ----------------------------------- 67
Cdd:TIGR02343 32 NI A AA KSVASI LRT S LGPKG MD KML I S PD GDI TV T N DG ATI L SQ M dvdnqiaklmvelsksqddeigdgttgvvvlagal 111
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HP RI IA E GFE A A KIK A L E V LEE V -- KVTKEMK - R KI L LDV A R TSL QT K VHAELADVLT E VV VD S VL A V 134
Cdd:TIGR02343 112 leqaeelldk G I HP IK IA D GFE E A ARI A V E H LEE I sd EISADNN n R EP L IQA A K TSL GS K IVSKCHRRFA E IA VD A VL N V 191
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 ---- RR P gyp I D L fmv EIMEMKH K L G --- T DTKLI Q G LVL D HGAR HP D M K K R VEDA F I L I CNVSL E YE K TEVNSGFFYKT 207
Cdd:TIGR02343 192 adme RR D --- V D F --- DLIKVEG K V G gsl E DTKLI K G III D KDFS HP Q M P K E VEDA K I A I LTCPF E PP K PKTKHKLDISS 265
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 208 A EE KE KL V K A E RKFIEDRVQK I ID lkdkvc AQS N kgf V VI N Q K G I D PFSLDS L AKHGIV A L R RAKRRNM E RLSL A C GG MA 287
Cdd:TIGR02343 266 V EE YK KL Q K Y E QQKFKEMIDD I KK ------ SGA N --- L VI C Q W G F D DEANHL L LQNDLP A V R WVGGQEL E LIAI A T GG RI 336
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 288 V NS F ED L TV D C LG H AGLV Y E YTL G -- EEKFTF IE E C V N PCS VT LLVK G P NK HTLTQV K DA I R D G L RAIK N A I E D GCM V P G 365
Cdd:TIGR02343 337 V PR F QE L SK D K LG K AGLV R E ISF G tt KDRMLV IE Q C K N SKA VT IFIR G G NK MIIEEA K RS I H D A L CVVR N L I K D SRI V Y G 416
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 366 A GA I E VAMAE A LVTYKNSIK G RARLGVQ AFADAL LI IP KV LA Q N A G Y DP QE TL VKVQAEHVES K Q - LV GVD LNTGEPMVA 444
Cdd:TIGR02343 417 G GA A E ISCSL A VSQEADKYP G VEQYAIR AFADAL ET IP MA LA E N S G L DP IG TL STLKSLQLKE K N p NL GVD CLGYGTNDM 496
490 500 510
....*....|....*....|....*....|....*.
gi 302058292 445 ADAG V WDNYCV KKQ LLHSC T VIATN IL LV D EIMRA G 480
Cdd:TIGR02343 497 KEQF V FETLIG KKQ QILLA T QLVRM IL KI D DVISP G 532
chaperonin_like
cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
100-359
7.63e-69
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: 218.87
E-value: 7.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 100 R KI LL D VA R TSL QT K V h AELA D V L TEV VVD S VL A V RRPGYPI DL FMVEIMEMKHKLGT D TK L IQ G L V L D H G ARH P D M K KR 179
Cdd:cd03333 1 R EL LL Q VA T TSL NS K L - SSWD D F L GKL VVD A VL K V GPDNRMD DL GVIKVEKIPGGSLE 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 302058292 180 V E D A F IL ICNVS LEY ektevnsgffyktaeekeklvkaerkfiedrvqkiidlkdkvcaqsnkgf VVI NQ KGID PFS L DS 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 302058292 260 LAK H GI V A L RR A K RRNM ER LSL A C G GMA V N S F EDLT VDC LG H A G LV Y E YTL GEEK F TFIE E C VNPCSV T L L VK G PNKHT L 339
Cdd:cd03333 110 LAK A GI M A V RR V K KEDL ER IAR A T G ATI V S S L EDLT PED 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 302058292 340 TQ VK DAIR D G L R A IKN A I E D 359
Cdd:cd03333 190 DE VK RSLH D A L C A VRA A V E E 209
chap_CCT_gamma
TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
23-476
6.29e-67
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: 223.85
E-value: 6.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQ D VL RT N LGP KGTM KML VSGA G D I KL T K DGN VL L D E MGL --------------------------------- 69
Cdd:TIGR02344 21 NI Q AA KAVA D II RT C LGP RSML KML LDPM G G I VM T N DGN AI L R E IDV ahpaaksmielsrtqdeevgdgttsviilagem 100
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 70 ------------ HP RI I AEGFEA A KIK AL E VLEE VKVTKEMK - RKIL L DVARTSLQ TK VHAELA D VLTEVVV D S V LA V R R 136
Cdd:TIGR02344 101 lsvaepfleqni HP TV I IRAYRK A LDD AL S VLEE ISIPVDVN d DAAM L KLIQSCIG TK FVSRWS D LMCDLAL D A V RT V Q R 180
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 PGYPI dl FMVE I MEM ---- K HKL G -- T D TKLIQ G LVLDHGAR HP D M KKRV E DAF I LICNVS LEY E K T E VNSGFFYKTA E E 210
Cdd:TIGR02344 181 DENGR -- KEID I KRY akve K IPG G di E D SCVLK G VMINKDVT HP K M RRYI E NPR I VLLDCP LEY K K G E SQTNIEITKE E D 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 KEKLVKA E RKFIEDRVQK II DL K DKV caqsnkgfv VI NQ KG IDPFSLDS L A K HG I V A L RR AKRRNME R LSL ACG GMA VN S 290
Cdd:TIGR02344 259 WNRILQM E EEYVQLMCED II AV K PDL --------- VI TE KG VSDLAQHY L L K AN I T A I RR VRKTDNN R IAR ACG ATI VN R 329
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 F E D L TVDCL G - HA GL VYEYTL G E E K FTFI E EC VN P CSV T L L VK G PN K HT L TQ V KDAIR D GLRAIK N AIE D GCM VPG A GA I 369
Cdd:TIGR02344 330 P E E L RESDV G t GC GL FEVKKI G D E Y FTFI T EC KD P KAC T I L LR G AS K DI L NE V ERNLQ D AMAVAR N VLL D PKL VPG G GA T 409
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 370 E V A MAE AL VTYKNSIK G RARLGVQ A F ADAL L IIP KV LAQN A G YDPQE TL VKVQ A E H V - E SKQLV G V D LN TG EPMVAADA G 448
Cdd:TIGR02344 410 E M A VSV AL TEKSKKLE G VEQWPYR A V ADAL E IIP RT LAQN C G ANVIR TL TELR A K H A q E NNCTW G I D GE TG KIVDMKEK G 489
490 500
....*....|....*....|....*...
gi 302058292 449 V W DNYC VK K Q LLHSCTVI A TNI L LV D E I 476
Cdd:TIGR02344 490 I W EPLA VK L Q TYKTAIES A CLL L RI D D I 517
TCP1_gamma
cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
23-476
2.51e-65
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: 218.32
E-value: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQ DV L RT N LGP KGTM KML VSGA G D I K LT K DGN VL L D E M ----------------------------------- 67
Cdd:cd03337 21 NI Q AA KTVA DV I RT C LGP RAML KML LDPM G G I V LT N DGN AI L R E I dvahpaaksmielsrtqdeevgdgttsviilagei 100
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HP RI I AEGFEA A KIK AL EV LEE VKVT - KEMK R KIL L DVARTSLQ TK VHAELA D VLTEVVV D S V LA V RR 136
Cdd:cd03337 101 lavaepfler G I HP TV I IKAYRK A LED AL KI LEE ISIP v DVND R AQM L KIIKSCIG TK FVSRWS D LMCNLAL D A V KT V AV 180
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P ---- GYP ID L -- FM - VE imem K HKL G T -- D TKLIQ G LV L DHGAR HP D M KK R V E DAF I LICNVS LEY ektevnsgffykt 207
Cdd:cd03337 181 E engr KKE ID I kr YA k VE ---- K IPG G E ie D SRVLD G VM L NKDVT HP K M RR R I E NPR I VLLDCP LEY ------------- 243
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 208 aeekeklvkaerkfiedrvqkiidlkdkvcaqsnkgf V VI NQ KG IDPFSLDS L A K H GI V ALRR AKRRNME R LSL ACG GMA 287
Cdd:cd03337 244 ------------------------------------- L VI TE KG VSDLAQHY L V K A GI T ALRR VRKTDNN R IAR ACG ATI 286
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 288 VN SF E D LT VDCL G HAGLVY E YTL - G E E K FTFI E EC VN P CSV T L L VK G PN K HT L TQ V KDAIR D GLRAIK N A I EDGCM VPG A 366
Cdd:cd03337 287 VN RP E E LT ESDV G TGAGLF E VKK i G D E Y FTFI T EC KD P KAC T I L LR G AS K DV L NE V ERNLQ D AMAVAR N I I LNPKL VPG G 366
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 367 GA I E V A MAE AL VTYKN SI K G RARLGVQ A F A D AL LI IP KV LAQN A G YDPQE TL VKVQ A E H VES - KQLV G V D LN TG EPMVAA 445
Cdd:cd03337 367 GA T E M A VSH AL SEKAK SI E G VEQWPYK A V A S AL EV IP RT LAQN C G ANVIR TL TELR A K H AQG e NSTW G I D GE TG DIVDMK 446
490 500 510
....*....|....*....|....*....|.
gi 302058292 446 DA G V WD NYC VK K Q LLHSCTVI A TNI L LV D E I 476
Cdd:cd03337 447 EL G I WD PLA VK A Q TYKTAIEA A CML L RI D D I 477
GroEL
COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
23-479
3.68e-65
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 218.41
E-value: 3.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI CAARG L Q D VLRTN LGPKG TMK MLV SGA GD IKL T K DG NVLLD E M ----------------------------------- 67
Cdd:COG0459 15 NI RGVKA L A D AVKVT LGPKG RNV MLV KSF GD PTI T N DG VTIAK E I eledpfenmgaqlvkevasktndeagdgtttatvl 94
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 -------------- G LH P RI I AE G FEA A KI KA L E V L EE -- VK V TK emk RKI L LD VA RT S LQTK vhaela DVLT E VVVDSV 131
Cdd:COG0459 95 agallkeglklvaa G AN P TD I KR G IDK A VE KA V E E L KK ia KP V DD --- KEE L AQ VA TI S ANGD ------ EEIG E LIAEAM 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 132 LA V RRP G Y pidl FM VE imem KH K - L G T DTKLIQ G LVL D H G ARH P D ------- M KKRV E D A F IL ICNVSLE yektevnsgf 203
Cdd:COG0459 166 EK V GKD G V ---- IT VE ---- EG K g L E T ELEVVE G MQF D K G YLS P Y fvtdpek M PAEL E N A Y IL LTDKKIS ---------- 227
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 204 fyktaeekeklvkaerkfied RV Q KIID L KD KV c AQS N K G f VV I NQKG ID PFS L DS L AKH GI VALR R A --------- K RR 274
Cdd:COG0459 228 --------------------- SI Q DLLP L LE KV - AQS G K P - LL I IAED ID GEA L AT L VVN GI RGVL R V vavkapgfg D RR 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 N -- M E RLSLAC GG MAVN ----- SF ED L T V D C LG H A GL V YE ytl GEEKF T FI E ECV NP CSVTL LV KGPNKHTLTQV K DAIR 347
Cdd:COG0459 285 K am L E DIAILT GG RVIS edlgl KL ED V T L D D LG R A KR V EV --- DKDNT T IV E GAG NP KAIVI LV GAATEVEVKER K RRVE 361
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 348 D G L R A IKN A I E D G C m VPG A GA IEVAM A E AL VTYKNSIK G RAR LG VQAF A D AL LIIPKVL A Q NAG Y D PQETLV KV Q A E hve 427
Cdd:COG0459 362 D A L H A TRA A V E E G I - VPG G GA ALLRA A R AL RELAAKLE G DEQ LG IEIV A R AL EAPLRQI A E NAG L D GSVVVE KV R A A --- 437
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 302058292 428 SKQLV G V D LN TGE PMVAAD AGV W D NYC VK KQL L HSCTVI A TN IL LVDEIMRA 479
Cdd:COG0459 438 KDKGF G F D AA TGE YVDMLE AGV I D PAK VK RSA L QNAASV A GL IL TTEAVIAD 489
TCP1_alpha
cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
23-478
9.48e-63
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: 212.91
E-value: 9.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 N IC AA RGLQDVLRTN LGP K G TM KMLV SGA GD IKL T K DG NVL L -------------------------------------- 64
Cdd:cd03335 13 N VT AA MAIANIVKSS LGP V G LD KMLV DDI GD VTI T N DG ATI L kllevehpaakilvelaqlqdkevgdgttsvviiaael 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 65 ---- D E --- MGL HP RI I AE G FEA A KIK A LEVLE E VKVTK -- EMKRKI L LD VA R TS LQT K VHAELA D VLTEV VVD SV LAV R 135
Cdd:cd03335 93 lkra N E lvk QKI HP TT I IS G YRL A CKE A VKYIK E HLSIS vd NLGKES L IN VA K TS MSS K IIGADS D FFANM VVD AI LAV K 172
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 R ------ PG YPI D lf M V E I MEMKH K LGTDTK L IQ G LV L DHGARHPD M KK RV ED A F I LICNVS L EYE K TEVNSGFFYKTA E 209
Cdd:cd03335 173 T tnekgk TK YPI K -- A V N I LKAHG K SAKESY L VN G YA L NCTRASQG M PT RV KN A K I ACLDFN L QKT K MKLGVQVVVTDP E 250
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 210 EK EK LVKA E RKFIED R VQ KI ID lkdkvc A QS N kgf VV INQK GID PFS L DSLAKH G IV A L RR A K RRNME R LSL A C G GMA V N 289
Cdd:cd03335 251 KL EK IRQR E SDITKE R IK KI LA ------ A GA N --- VV LTTG GID DMC L KYFVEA G AM A V RR V K KEDLR R IAK A T G ATL V S 321
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 290 SFED L TVD ------ C LG H A GL V YEYTL G EEKFTF I EECVNPC S VTLLVK G P N KHT L TQVKDAIR D G L RAI K NAI E DGCM V 363
Cdd:cd03335 322 TLAN L EGE etfdps Y LG E A EE V VQERI G DDELIL I KGTKKRS S ASIILR G A N DFM L DEMERSLH D A L CVV K RTL E SNSV V 401
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 364 PG A GA I E V A MAEA L VTYKNSIKG R AR L GVQA FA D ALL I IPK V LA Q NA GY D PQ E TLV K VQ A E H VESKQL -------- V G V D 435
Cdd:cd03335 402 PG G GA V E T A LSIY L ENFATTLGS R EQ L AIAE FA E ALL V IPK T LA V NA AK D AT E LVA K LR A Y H AAAQVK pdkkhlkw Y G L D 481
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 302058292 436 L NT G EPMVAAD AGV WDNYCV K KQL L HSC T VI A TN IL LV D EIMR 478
Cdd:cd03335 482 L IN G KVRDNLE AGV LEPTVS K IKS L KFA T EA A IT IL RI D DLIK 524
TCP1_delta
cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
23-441
9.57e-63
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: 212.53
E-value: 9.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQ D VL RT N LGP K G TM KM LVS G A G DIKL T K DG NVL L DE 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 302058292 68 ---------- G L HP RI I A E G F EA A KI KA L E V L EEVKVTKEMK - R KI L LDV A R TSL QT KV HAELADV L TEVV VD S VL A V RR 136
Cdd:cd03338 93 lsacesllkk G I HP TV I S E S F QI A AK KA V E I L DSMSIPVDLN d R ES L IKS A T TSL NS KV VSQYSSL L APIA VD A VL K V ID 172
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P GYP -- I DL FMVE I ME mkh KLG --- T DT K L IQ GLV LDHG A RH - PDMKK R V E D A F I LICNVS L EYE KT EVNSGFFYKTAEE 210
Cdd:cd03338 173 P ATA tn V DL KDIR I VK --- KLG gti E DT E L VD GLV FTQK A SK k AGGPT R I E K A K I GLIQFC L SPP KT DMDNNIVVNDYAQ 249
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 KEKLVKA ERK F I EDRVQ KI idl K DKV C A qsnkgf V VIN QK G I ----- DPFS L DS LAK HG I VALRRAK R RNM E RLSLAC G G 285
Cdd:cd03338 250 MDRILRE ERK Y I LNMCK KI --- K KSG C N ------ V LLI QK S I lrdav SDLA L HF LAK LK I MVVKDIE R EEI E FICKTI G C 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 286 MA V N S FEDL T V D C LG H A G LV Y E YT LG EE K FTF I EECV NP C - S VT L LV K G P NK HT L TQVKDAIR D G L RA I KNAIEDGCMV P 364
Cdd:cd03338 321 KP V A S IDHF T E D K LG S A D LV E E VS LG DG K IVK I TGVK NP G k T VT I LV R G S NK LV L DEAERSLH D A L CV I RCLVKKRALI P 400
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302058292 365 G A GA I E VAM A EA L VTYKNSIK G RARLG V Q AFADAL LI IP KV LA Q NAG YD P QETLVKVQAE H VESKQLV G VDLNT G EP 441
Cdd:cd03338 401 G G GA P E IEI A LQ L SEWARTLT G VEQYC V R AFADAL EV IP YT LA E NAG LN P ISIVTELRNR H AQGEKNA G INVRK G AI 477
chap_CCT_alpha
TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
23-478
9.67e-63
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: 213.04
E-value: 9.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 N IC AA RGLQDVLR T N LGP K G TM KMLV SGA GD IKL T K DG NVL L DEM ----------------------------------- 67
Cdd:TIGR02340 17 N VT AA MAIANIVK T S LGP V G LD KMLV DDI GD VTI T N DG ATI L KLL evehpaakilvelaqlqdrevgdgttsvviiaael 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- GL HP RIIAE G FEA A KIK A LEVLE E VKVTK -- E MK R KI L LD VA R TS LQT K VHAELA D VLTEV VVD S VLAV R 135
Cdd:TIGR02340 97 lkradelvkn KI HP TSVIS G YRL A CKE A VKYIK E NLSVS vd E LG R EA L IN VA K TS MSS K IIGLDS D FFSNI VVD A VLAV K 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 ------ RPG YPI D lf MVE I MEMKH K LGTDTK L IQ G LV L DHGARHPD M K KR VED A F I LICNVS L EYE K TEVNSGFFYKTA E 209
Cdd:TIGR02340 177 ttneng ETK YPI K -- AIN I LKAHG K SARESM 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 302058292 210 EK E KLVKA E RKFIED R VQ KI I D lkdkvc A QS N kgf VV INQK GID PFS L DSLAKH G IVAL RR A K RRNME R LSL A C G GMA V N 289
Cdd:TIGR02340 255 KL E QIRQR E ADITKE R IK KI L D ------ A GA N --- VV LTTG GID DMC L KYFVEA G AMGV RR C K KEDLK R IAK A T G ATL V S 325
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 290 SFE DL TVD ------ C LG H A GL V YEYTLGEEKFTF I EECVNPC S VTLLVK G P N KHT L TQVKDAIR D G L RAI K NAI E DGCM V 363
Cdd:TIGR02340 326 TLA DL EGE etfeas Y LG F A DE V VQERIADDECIL I KGTKKRK S ASIILR G A N DFM L DEMERSLH D A L CVV K RTL E SNSV V 405
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 364 PG A GA I E V A MAEA L VTYKNSIKG R AR L GVQA FA D ALLIIPK V LA Q NA GY D PQ E TLV K VQ A E H VES ------ K Q L -- V G V D 435
Cdd:TIGR02340 406 PG G GA V E A A LSIY L ENFATTLGS R EQ L AIAE FA R ALLIIPK T LA V NA AK D ST E LVA K LR A Y H AAA qlkpek K H L kw Y G L D 485
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 302058292 436 L NT G EPMVAAD AGV WDNYCV K KQL L HSC T VI A TN IL LV D EIMR 478
Cdd:TIGR02340 486 L VN G KIRDNKE AGV LEPTVS K VKS L KFA T EA A IT IL RI D DLIK 528
TCP1_beta
cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
32-479
7.39e-60
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: 204.87
E-value: 7.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 32 D VLR T N LGPKG TM K M L V S G -- A G DIKL T K DG NVL L --------------------- DE M G -------------------- 68
Cdd:cd03336 27 D LVK T T LGPKG MD K I L Q S V gr S G GVTV T N DG ATI L ksigvdnpaakvlvdiskvqd DE V G dgttsvtvlaaellreaekl 106
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 69 ---- L HP RI I A EG FEA A KIK A L E V L EE ---- VKVTK E MK R KI LL DV ART S L QT K VHAELADVLT E VV VD S VL AVRRP G yp 140
Cdd:cd03336 107 vaqk I HP QT I I EG YRM A TAA A R E A L LS savd HSSDE E AF R ED LL NI ART T L SS K ILTQDKEHFA E LA VD A VL RLKGS G -- 184
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 141 i D L FMVE I ME mkh KLG --- T D TK L IQ G LV LD H -- G ARH P dmk KR V E D A F ILI C N VSLEYE K ----- TE V NSGFFY K T AE e 210
Cdd:cd03336 185 - N L DAIQ I IK --- KLG gsl K D SY L DE G FL LD K ki G VNQ P --- KR I E N A K ILI A N TPMDTD K ikifg AK V RVDSTA K V AE - 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 kek LVK AE RKFIEDR V Q KI I dlkdkvcaq SNKGFVV IN QKG I DPFSLDSL A KH GI V A LRR A KRRNM ERL S L AC GG MAVNS 290
Cdd:cd03336 257 --- IEE AE KEKMKNK V E KI L --------- KHGINCF IN RQL I YNYPEQLF A DA GI M A IEH A DFDGV ERL A L VT GG EIAST 324
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 F EDLTVDC LG HAG L VY E YTL GE E K FTFIEECVNPCSV T LLVK G PNKHT L TQVKDAIR D G L RAIKNAIE D GCM V P G A G AI E 370
Cdd:cd03336 325 F DHPELVK LG TCK L IE E IMI GE D K LIRFSGVAAGEAC T IVLR G ASQQI L DEAERSLH D A L CVLAQTVK D TRV V L G G G CS E 404
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 371 VA MA E A LVTYKNSIK G RAR L GVQ AFA D AL LII P KVL A Q NAGYD PQ E TLVKVQ A E H VESKQLV G V D LNT G EPMVAADA G VW 450
Cdd:cd03336 405 ML MA K A VEELAKKTP G KKS L AIE AFA K AL RQL P TII A D NAGYD SA E LVAQLR A A H YNGNTTA G L D MRK G TVGDMKEL G IT 484
490 500
....*....|....*....|....*....
gi 302058292 451 DNYC VK K Q L L H S CTVI A TN IL L VD E I MRA 479
Cdd:cd03336 485 ESFK VK R Q V L L S ASEA A EM IL R VD D I IKC 513
chap_CCT_delta
TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
23-477
1.40e-59
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274083
Cd Length: 517
Bit Score: 204.25
E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C AA RGLQ D VL RT N LGPKG TM KM LVS G A G DIKL T K DG NVL L DE M ----------------------------------- 67
Cdd:TIGR02342 14 NI V AA KAVA D AI RT S LGPKG MD KM IQD G K G EVII T N DG ATI L KQ M avlhpaakmlvelskaqdieagdgttsvvilagal 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 68 ---------- G L HP R II A E G F EA A KIK A LEV L E E VKVTKEMK - R KI LL DV A R TSL QT KV HAELADV L TEVV VD S VL A V RR 136
Cdd:TIGR02342 94 lgacerllnk G I HP T II S E S F QS A ADE A IKI L D E MSIPVDLS d R EQ LL KS A T TSL SS KV VSQYSSL L APLA VD A VL K V ID 173
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P GYPIDLFMVE I MEM K HKL GT -- DT K LI Q GLV LDHG A RHPD - MKK R V E D A F I LICNVSLEYE KT EVNSGFFYKTAEEKEK 213
Cdd:TIGR02342 174 P ENAKNVDLND I KVV K KLG GT id DT E LI E GLV FTQK A SKSA g GPT R I E K A K I GLIQFQISPP KT DMENQIIVNDYAQMDR 253
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 214 LV K A ER KF I EDR V Q KI idlkdkvca QSNKGF V VIN QK G I ----- DPFS L DS LAK HG I VALRRAK R RNM E RLSLAC G GMAV 288
Cdd:TIGR02342 254 VL K E ER AY I LNI V K KI --------- KKTGCN V LLI QK S I lrdav NDLA L HF LAK MK I MVVKDIE R EEI E FICKTI G CKPI 324
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 289 N S FEDL T V D C LG H A G LV Y E YTLGEE K FTF I EECV N PC - S VT LL V K G P NK HTLTQVKDAIR D G L RA I KNAIEDGCMVP G A G 367
Cdd:TIGR02342 325 A S IDHF T A D K LG S A E LV E E VDSDGG K IIK I TGIQ N AG k T VT VV V R G S NK LVIDEAERSLH D A L CV I RCLVKKRGLIA G G G 404
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 368 A I E VAM A EA L VT Y KNSI KG RARLG V Q AFADAL LI IP KV LA Q NAG YD P QETLVKVQAE H VESKQLV G VDLNT G EPMVAADA 447
Cdd:TIGR02342 405 A P E IEI A RR L SK Y ARTM KG VESYC V R AFADAL EV IP YT LA E NAG LN P IKVVTELRNR H ANGEKTA G ISVRK G GITNMLEE 484
490 500 510
....*....|....*....|....*....|
gi 302058292 448 G V WDNYC V KKQLLHSCTVIATN IL LV D E I M 477
Cdd:TIGR02342 485 H V LQPLL V TTSAITLASETVRS IL KI D D I V 514
chap_CCT_eta
TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
23-479
1.23e-56
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: 196.52
E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C A ARGLQDV L R T N LGP K G TM K ML V SGA G DIKLTK DG NVL L DEM ----------------------------------- 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 302058292 68 ---------- G L HP RI I AEGFEA A KIK A L E VLE E VK VT ---- K EMK R KI L LDV A R T S L QT K VHAELADVLTEVV VD S VL A 133
Cdd:TIGR02345 103 lkeakpfiee G V HP QL I IRCYRE A LSL A V E KIK E IA VT idee K GEQ R EL L EKC A A T A L SS K LISHNKEFFSKMI VD A VL S 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 134 VR R PG yp I DL FMVE I MEMKHKLGT D TK L IQ G LVLDHG --- A RHPDMK K RVEDAF IL IC NV S LE YEKTEV N SGFFYKTA E E 210
Cdd:TIGR02345 183 LD R DD -- L DL KLIG 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 302058292 211 KEKL V K AE RKF I EDRVQ KI I dlkdkvcaq SNKGF VV INQKG I DPFSLDSL A KHG I VALR R AKRRNME R LSL ACGG MAVNS 290
Cdd:TIGR02345 261 YQAI V D AE WAI I FRKLE KI V --------- ESGAN VV LSKLP I GDLATQYF A DRD I FCAG R VSAEDLK R VIK ACGG SIQST 331
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 FE DL TV D C LG HAG L VY E YTL G E E KFTFIEE C VNPCSV T LLVK G PNKHTLTQVKDAIR D GLRAIKN A IEDGCM V P G A GAIE 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 AIMIVRR A LKNKKI V A G G GAIE 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 371 VAMAEA L VT Y KNS I K G RAR L GVQ AFA D AL L IIP KV L AQ NAG Y D PQ E T L V K VQAE H VESKQLV GVD L NT GEPMVAAD A G VW 450
Cdd:TIGR02345 412 MELSKC L RD Y SKT I D G KQQ L IIN AFA K AL E IIP RQ L CE NAG F D SI E I L N K LRSR H AKGGKWY GVD I NT EDIGDNFE A F VW 491
490 500
....*....|....*....|....*....
gi 302058292 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_eta
cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
23-479
8.81e-56
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: 194.04
E-value: 8.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C A ARGLQ D VL RT N LGP K G TM K ML V S G A G DIKLTK DG NV --- LLD ---------------------------------- 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 AT ilk LLD ivhpaaktlvdiaksqdaevgdgttsvvvlagef 100
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 66 -------- E M G L HP R II AE G FEA A KIK A L E VLE E VK V T ----- KE MK R KI L LDV A R T S L QT K VH A ELADVLTEV VVD S VL 132
Cdd:cd03340 101 lkeakpfi E D G V HP Q II IR G YRK A LQL A I E KIK E IA V N idked KE EQ R EL L EKC A A T A L NS K LI A SEKEFFAKM VVD A VL 180
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 133 AVRRP gyp I DL F M VE I MEMKHKLGT D TK L IQ G LVLDHG --- A RHPDMK K RVEDAF IL IC NV S LE YEKTEV N SGFFYKTA E 209
Cdd:cd03340 181 SLDDD --- L DL D M IG I KKVPGGSLE 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 302058292 210 E KEKL V K AE R K F I E D RVQ KI IDLKDK V caqsnkgfv V INQKG I DPFSLDSL A KHG I VALR R AKRRNME R LSL A C GG MAVN 289
Cdd:cd03340 258 E YQAI V D AE W K I I Y D KLE KI VKSGAN V --------- V LSKLP I GDLATQYF A DRD I FCAG R VPEEDLK R VAQ A T GG SIQT 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 290 SFEDL T V D C LG HA GL VY E YTL G E E KFTFIEE C VNPCSV T LLVK G PNKHTLTQVKDAIR D GLRAIKN AI EDGCM V P G A GAI 369
Cdd:cd03340 329 TVSNI T D D V LG TC GL FE E RQV G G E RYNIFTG C PKAKTC T IILR G GAEQFIEEAERSLH D AIMIVRR AI KNDSV V A G G GAI 408
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 370 E VAMAEA L VT Y KNS I K G RAR L GVQ AFA D AL L IIP KV L AQ NAG Y D PQET L V K VQAE H VESKQL - V GVD L N TGEPMVAAD A G 448
Cdd:cd03340 409 E MELSKY L RD Y SRT I A G KQQ L VIN AFA K AL E IIP RQ L CD NAG F D ATDI L N K LRQK H AQGGGK w Y GVD I N NEGIADNFE A F 488
490 500 510
....*....|....*....|....*....|.
gi 302058292 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
23-479
2.29e-55
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 193.32
E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NICA A RGLQ D VLR T N LGPKG TM K M L VS ----- GA G DIKL T K DG NVL L --------------------- D E M G -------- 68
Cdd:PTZ00212 27 SFVG A IAVA D LVK T T LGPKG MD K I L QP msegp RS G NVTV T N DG ATI L ksvwldnpaakilvdisktqd E E V G dgttsvvv 106
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 69 ---------------- L HP RI I A EG FEA A KIK A LEV LEE VKVT ---- K E MKRKI LL DV ART S L QT K VHAELA D VLTEVV V 128
Cdd:PTZ00212 107 lagellreaeklldqk I HP QT I I EG WRM A LDV A RKA LEE IAFD hgsd E E KFKED LL NI ART T L SS K LLTVEK D HFAKLA V 186
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 129 D S VL AVRRP G ypi D L FMVE I ME mkh K L G --- T D TK L IQ G LV L DH -- G ARH P dmk KR V E DAF IL IC N VSLEYE K ----- TE 198
Cdd:PTZ00212 187 D A VL RLKGS G --- N L DYIQ I IK --- K P G gtl R D SY L ED G FI L EK ki G VGQ P --- KR L E NCK IL VA N TPMDTD K ikiyg AK 257
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 199 V NSGFFY K T AE ekek LVK AE RKFIEDR V Q KI ID lkdkvc AQS N kgf V V IN QKG I DPFSLDSL A KH GI V A LRR A KRRN MER 278
Cdd:PTZ00212 258 V KVDSME K V AE ---- IEA AE KEKMKNK V D KI LA ------ HGC N --- V F IN RQL I YNYPEQLF A EA GI M A IEH A DFDG MER 324
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 279 L SL A C G GMA V NS F EDLTVDC LGH AG L VY E YTL GE E K FTFIEE C VNPCSV T LLVK G PNK H T L TQVKDAIR D G L RAIKNAIE 358
Cdd:PTZ00212 325 L AA A L G AEI V ST F DTPEKVK LGH CD L IE E IMI GE D K LIRFSG C AKGEAC T IVLR G AST H I L DEAERSLH D A L CVLSQTVK 404
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 359 D GCM V P G A G AI E VA MA E A LVTYKNSIK G RAR L GVQ AFA D AL LI IP KVL A Q N A GYD PQ E TLV K VQ AEH VESKQLV G V D LNT 438
Cdd:PTZ00212 405 D TRV V L G G G CS E ML MA N A VEELAKKVE G KKS L AIE AFA K AL RQ IP TII A D N G GYD SA E LVS K LR AEH YKGNKTA G I D MEK 484
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 302058292 439 G EPMVAADA 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 485 G TVGDMKEL 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 ...
23-479
1.35e-51
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: 182.99
E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C A ARG L QDVL RT N LGP K G TM KM LVSGAGDIKL T K D GNVL L D E ------------------------------------ 66
Cdd:TIGR02346 23 NI E A CKE L SQIT RT S LGP N G MN KM VINHLEKLFV T N D AATI L R E levqhpaakllvmasemqeneigdgtnlvlvlagel 102
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 67 --------- MGLHP RI I AE G F E A A KI KA L E V LEE VK V TKEM --- KRKI L LDVART S LQT K VHAE l A D V L TEV V VDSVLA V 134
Cdd:TIGR02346 103 lnkaeelir MGLHP SE I IK G Y E M A LK KA M E I LEE LV V WEVK dlr DKDE L IKALKA S ISS K QYGN - E D F L AQL V AQACST V 181
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 R r P GY P ID l F M V EIMEMKHK LG T --- DTKLIQ G L V L dhg A R HPDMK - K R V ED A FILICNVS L EYEK TE VNSGFFYKT AEE 210
Cdd:TIGR02346 182 L - P KN P QN - F N V DNIRVCKI LG G sls NSEVLK G M V F --- N R EAEGS v K S V KN A KVAVFSCP L DTAT TE TKGTVLIHN AEE 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 KEKLV K A E RKF IE DRVQK I I D LKDK V caqsnkgfv VINQKGIDPFS L DS L A K HG I VA L RRAKRRNME RL SLAC G GMAVNS 290
Cdd:TIGR02346 257 LLNYS K G E ENQ IE AMIKA I A D SGVN V --------- IVTGGSVGDMA L HY L N K YN I MV L KIPSKFELR RL CKTV G ATPLPR 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 FEDL T VDCL G HAGL VY EYTL G EE K F T FIEECVNPCSV - T LLVK G PNKHT L TQVKD AI R DG LRAI K NAIE DG CMV PGAGA I 369
Cdd:TIGR02346 328 LGAP T PEEI G YVDS VY VSEI G GD K V T VFKQENGDSKI s T IILR G STDNL L DDIER AI D DG VNTV K ALVK DG RLL PGAGA T 407
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 370 E VAM A EA L VT Y KNSIK G RARLGVQA FA D A LL IIP KV LA Q NAG YDPQ E TLV K VQ A E H VESKQLV G V D LNTGEPM V -- A AD A 447
Cdd:TIGR02346 408 E IEL A SR L TK Y GEKLP G LDQYAIKK FA E A FE IIP RT LA E NAG LNAN E VIP K LY A A H KKGNKSK G I D IEAESDG V kd A SE A 487
490 500 510
....*....|....*....|....*....|..
gi 302058292 448 G VW D NYCV KK QLLHSC T VI A TNI L L VD E I MR A 479
Cdd:TIGR02346 488 G IY D MLAT KK WAIKLA T EA A VTV L R VD Q I IM A 519
chap_CCT_beta
TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
32-479
7.41e-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: 167.34
E-value: 7.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 32 D VLRTN LGPKG TM K M L V S GA -- GD I KL T K DG NVL L --------------------- DE M G -------------------- 68
Cdd:TIGR02341 28 D LVKST LGPKG MD K I L Q S SS sd AS I MV T N DG ATI L ksigvdnpaakvlvdmskvqd DE V G dgttsvtvlaaellreaekl 107
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 69 ---- L HP RI I AE G FEA A KIK A LEV L EEVK V ---- TKEMK R KI L LDV ART S L QT K VHAELA D VLTEVV VD S VL AVRRP G yp 140
Cdd:TIGR02341 108 inqk I HP QT I IA G YRE A TKA A RDA L LKSA V dngs DEVKF R QD L MNI ART T L SS K ILSQHK D HFAQLA VD A VL RLKGS G -- 185
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 141 i D L FMVE I ME mkh KLG --- T D TK L IQ G LV LD H -- G ARH P dmk KR V E D A F ILI C N VSLEYE K TEV - N S GFFYKTAEEKEK L 214
Cdd:TIGR02341 186 - N L EAIQ I IK --- KLG gsl A D SY L DE G FL LD K ki G VNQ P --- KR I E N A K ILI A N TGMDTD K VKI f G S RVRVDSTAKVAE L 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 215 VK AE RKFIEDR V Q KI I dlkdkvcaq SNKGFVV IN QKG I DPFSLDSL A KH G IV A LRR A KRRNM ERL S L AC GG MA V NS F EDL 294
Cdd:TIGR02341 259 EH AE KEKMKEK V E KI L --------- KHGINCF IN RQL I YNYPEQLF A DA G VM A IEH A DFEGV ERL A L VT GG EI V ST F DHP 329
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 295 TVDC LG HAG L VY E YTL GE E K FTFIEECVNPCSV T LLVK G PNKHT L TQVKDAIR D G L RAIKNAIEDGCM V P G A G AI E VA M A 374
Cdd:TIGR02341 330 ELVK LG SCD L IE E IMI GE D K LLKFSGVKLGEAC T IVLR G ATQQI L DEAERSLH D A L CVLSQTVKESRT V L G G G CS E ML M S 409
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 375 E A LVTYKNSIK G RAR L G V Q AFA D AL LII P KVL A Q NAG Y D PQ E TLVKVQ A E H VESKQLV G V D L N T G EPMVAADA G VWDN Y C 454
Cdd:TIGR02341 410 K A VTQEAQRTP G KEA L A V E AFA R AL RQL P TII A D NAG F D SA E LVAQLR A A H YNGNTTM G L D M N E G TIADMRQL G ITES Y K 489
490 500
....*....|....*....|....*
gi 302058292 455 VK KQLLH S CTVI A TN IL L VD E I MR A 479
Cdd:TIGR02341 490 VK RAVVS S AAEA A EV IL R VD N I IK A 514
TCP1_theta
cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
23-479
7.43e-45
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: 163.55
E-value: 7.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 23 NI C A ARG L QDVL RT NL GP K G TM KM LVSGAGDIKL T K D GNVL L D 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 302058292 67 --------- MGLHP RI I A EG F E A A KI KALE V LEE VK V T K EMKRKILLD V A --- R T SLQT K V h AELA D V L TEV V VDSVLA V 134
Cdd:cd03341 93 lekaeellr MGLHP SE I I EG Y E K A LK KALE I LEE LV V Y K IEDLRNKEE V S kal K T AIAS K Q - YGNE D F L SPL V AEACIS V 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 rrpg Y P IDL -- F M V EIMEMKHK LG --- T D T K LIQ G L V L dhg A R H P DMK - KRV ED A FILICNVSLE yek TE VN sgffykta 208
Cdd:cd03341 172 ---- L P ENI gn F N V DNIRVVKI LG gsl E D S K VVR G M V F --- K R E P EGS v KRV KK A KVAVFSCPFD --- IG VN -------- 233
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 209 eekeklvkaerkfiedrvqkiidlkdkvcaqsnkgf V VINQKGIDPFS L DSLA K H GI VALRRAKRRNME RL SLAC G GMAV 288
Cdd:cd03341 234 ------------------------------------ V IVAGGSVGDLA L HYCN K Y GI MVIKINSKFELR RL CRTV G ATPL 277
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 289 NSFEDL T VDCL G HAGL VY EYTL G EE K FTFIEECVNPCSV - T LLVK G PNKHT L TQ V KD AI R DG LRAI K NAIE DG CM VPGAG 367
Cdd:cd03341 278 PRLGAP T PEEI G YCDS VY VEEI G DT K VVVFRQNKEDSKI a T IVLR G ATQNI L DD V ER AI D DG VNVF K SLTK DG RF VPGAG 357
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 368 A I E VAM A EA L VT Y KNSIK G RARLGVQA FA D A LLII P KV LA Q NAG Y D PQ E T L VKVQ A E H VESKQLV GVD LNT G EPMV -- A A 445
Cdd:cd03341 358 A T E IEL A KK L KE Y GEKTP G LEQYAIKK FA E A FEVV P RT LA E NAG L D AT E V L SELY A A H QKGNKSA GVD IES G DEGT kd A K 437
490 500 510
....*....|....*....|....*....|....
gi 302058292 446 D AG VW D NYCV KK QLLHSC T VI A TNI L L VD E I MR A 479
Cdd:cd03341 438 E AG IF D HLAT KK WAIKLA T EA A VTV L R VD Q I IM A 471
Fab1_TCP
cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
158-343
1.53e-12
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: 67.63
E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 158 D TKLIQ G L V LDHGAR H PD M KKRVEDAF IL ICNVS LEY EK te V NSGFFYK taeek EKLVKA E RKFIEDR V QK I ID L KDK V c 237
Cdd:cd03334 62 D SEVVD G V V FTKNVA H KR M PSKIKNPR IL LLQGP LEY QR -- V ENKLLSL ----- DPVILQ E KEYLKNL V SR I VA L RPD V - 133
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 238 aqsnkgfv VINQ K GIDPFSL D S L AKH GI VALRRA K RRNM ER L S LAC G GMAVN S FE DL t VDC -- LG HAGLVYEY T LG EE K - 314
Cdd:cd03334 134 -------- ILVE K SVSRIAQ D L L LEA GI TLVLNV K PSVL ER I S RCT G ADIIS S MD DL - LTS pk LG TCESFRVR T YV EE H g 204
170 180 190
....*....|....*....|....*....|...
gi 302058292 315 ---- FT F I E E C VNPCSV T L L VK G PNKHT L TQ VK 343
Cdd:cd03334 205 rskt LM F F E G C PKELGC T I L LR G GDLEE L KK VK 237
PTZ00114
PTZ00114
Heat shock protein 60; Provisional
343-413
6.94e-04
Heat shock protein 60; Provisional
Pssm-ID: 185455
Cd Length: 555
Bit Score: 42.21
E-value: 6.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302058292 343 KD A I R D G L R A IKN A I E D G c M VPG A G AIEVAMAEA L -- VTYK N SIKGRA R L GV QAFAD AL LIIP K VL A Q NAG YD 413
Cdd:PTZ00114 405 KD R I E D A L N A TRA A V E E G - I VPG G G VALLRASKL L dk LEED N ELTPDQ R T GV KIVRN AL RLPT K QI A E NAG VE 476
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