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T-complex protein 1 subunit theta [Jatropha curcas]
Protein Classification
TCP-1/cpn60 chaperonin family protein ( domain architecture ID 16 )
TCP-1/cpn60 chaperonin family protein similar to mycobacterial 60 kDa chaperonin (GroEL) that together with its co-chaperonin GroES, plays an essential role in assisting protein folding
List of domain hits
Name
Accession
Description
Interval
E-value
chaperonin_like super family
cl02777 chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
9-535
0e+00
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.
TIGR02346 :Pssm-ID: 351886 [Multi-domain]
Cd Length: 531
Bit Score: 841.68
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 9 GI QAM LKEG HK H L SGL D EAV L KNI D ACK Q LS T ITRTSLGPNGMNKMVINHL D KLFVTNDAATI VN ELEVQHPAAK I LV L A 88
Cdd:TIGR02346 1 GI ASL LKEG YR H F SGL E EAV I KNI E ACK E LS Q ITRTSLGPNGMNKMVINHL E KLFVTNDAATI LR ELEVQHPAAK L LV M A 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 89 GKA Q QE EIGDG A NL TISF AGELL QN AEELIRMGLHPSEII S GY NK A IT KA I EIL D ELV E ke S E TM D V R N K EHV I TRMR A A 168
Cdd:TIGR02346 81 SEM Q EN EIGDG T NL VLVL AGELL NK AEELIRMGLHPSEII K GY EM A LK KA M EIL E ELV V -- W E VK D L R D K DEL I KALK A S 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 169 I A SKQ F G Q E EV L CK L I A D AC IQ V C PKNP A NFNVDN V RV A K LV GG G L HDCTIVR GMV LKTD A V G TI K R V EK AKVAVF AGGV 248
Cdd:TIGR02346 159 I S SKQ Y G N E DF L AQ L V A Q AC ST V L PKNP Q NFNVDN I RV C K IL GG S L SNSEVLK GMV FNRE A E G SV K S V KN AKVAVF SCPL 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 249 DT SA TETKGTVLIH S A DQ L E NY A K T EE AKV E EL IKA V ADSG AK VIV S G AA VG E MALH FCER Y KL MVLKI S SKFELRR F C R 328
Cdd:TIGR02346 239 DT AT TETKGTVLIH N A EE L L NY S K G EE NQI E AM IKA I ADSG VN VIV T G GS VG D MALH YLNK Y NI MVLKI P SKFELRR L C K 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 329 T T G SVAILK L SQ P N P DDL GY A DS IS V E EIGG VR VTV V K N E E G GNSVC T VV LRGSTD SI L E D L ERA V DDGVNT Y KA MCR D S 408
Cdd:TIGR02346 319 T V G ATPLPR L GA P T P EEI GY V DS VY V S EIGG DK VTV F K Q E N G DSKIS T II LRGSTD NL L D D I ERA I DDGVNT V KA LVK D G 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 R IV PGA A ATEIELA R RL KEFSF K ET GLDQYAI A KFAE S FE MV P K TL S ENAGLNA M E I I SS LYA E H AS GN SKV GID L E EGI 488
Cdd:TIGR02346 399 R LL PGA G ATEIELA S RL TKYGE K LP GLDQYAI K KFAE A FE II P R TL A ENAGLNA N E V I PK LYA A H KK GN KSK GID I E AES 478
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 802585508 489 C -- KD VATMN I W D LYV TK FF A L K Y A AD AA C TVLRVDQIIMAKPAGGP N P 535
Cdd:TIGR02346 479 D gv KD ASEAG I Y D MLA TK KW A I K L A TE AA V TVLRVDQIIMAKPAGGP K P 527
Name
Accession
Description
Interval
E-value
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
9-535
0e+00
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: 841.68
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 9 GI QAM LKEG HK H L SGL D EAV L KNI D ACK Q LS T ITRTSLGPNGMNKMVINHL D KLFVTNDAATI VN ELEVQHPAAK I LV L A 88
Cdd:TIGR02346 1 GI ASL LKEG YR H F SGL E EAV I KNI E ACK E LS Q ITRTSLGPNGMNKMVINHL E KLFVTNDAATI LR ELEVQHPAAK L LV M A 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 89 GKA Q QE EIGDG A NL TISF AGELL QN AEELIRMGLHPSEII S GY NK A IT KA I EIL D ELV E ke S E TM D V R N K EHV I TRMR A A 168
Cdd:TIGR02346 81 SEM Q EN EIGDG T NL VLVL AGELL NK AEELIRMGLHPSEII K GY EM A LK KA M EIL E ELV V -- W E VK D L R D K DEL I KALK A S 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 169 I A SKQ F G Q E EV L CK L I A D AC IQ V C PKNP A NFNVDN V RV A K LV GG G L HDCTIVR GMV LKTD A V G TI K R V EK AKVAVF AGGV 248
Cdd:TIGR02346 159 I S SKQ Y G N E DF L AQ L V A Q AC ST V L PKNP Q NFNVDN I RV C K IL GG S L SNSEVLK GMV FNRE A E G SV K S V KN AKVAVF SCPL 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 249 DT SA TETKGTVLIH S A DQ L E NY A K T EE AKV E EL IKA V ADSG AK VIV S G AA VG E MALH FCER Y KL MVLKI S SKFELRR F C R 328
Cdd:TIGR02346 239 DT AT TETKGTVLIH N A EE L L NY S K G EE NQI E AM IKA I ADSG VN VIV T G GS VG D MALH YLNK Y NI MVLKI P SKFELRR L C K 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 329 T T G SVAILK L SQ P N P DDL GY A DS IS V E EIGG VR VTV V K N E E G GNSVC T VV LRGSTD SI L E D L ERA V DDGVNT Y KA MCR D S 408
Cdd:TIGR02346 319 T V G ATPLPR L GA P T P EEI GY V DS VY V S EIGG DK VTV F K Q E N G DSKIS T II LRGSTD NL L D D I ERA I DDGVNT V KA LVK D G 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 R IV PGA A ATEIELA R RL KEFSF K ET GLDQYAI A KFAE S FE MV P K TL S ENAGLNA M E I I SS LYA E H AS GN SKV GID L E EGI 488
Cdd:TIGR02346 399 R LL PGA G ATEIELA S RL TKYGE K LP GLDQYAI K KFAE A FE II P R TL A ENAGLNA N E V I PK LYA A H KK GN KSK GID I E AES 478
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 802585508 489 C -- KD VATMN I W D LYV TK FF A L K Y A AD AA C TVLRVDQIIMAKPAGGP N P 535
Cdd:TIGR02346 479 D gv KD ASEAG I Y D MLA TK KW A I K L A TE AA V TVLRVDQIIMAKPAGGP K P 527
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
19-528
0e+00
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: 754.06
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 19 K H L SGL D EAVL K NI D ACK Q LS T ITRTS L GPNGMNKMVINHL D KLFVT N DAATI VN ELEVQHPAAK I LV L A GKA Q Q EEIGD 98
Cdd:cd03341 1 R H Y SGL E EAVL R NI E ACK E LS Q ITRTS Y GPNGMNKMVINHL E KLFVT S DAATI LR ELEVQHPAAK L LV M A SQM Q E EEIGD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 99 G A NL TISF AGELL QN AEEL I RMGLHPSEII S GY N KA IT KA I EIL D ELV EKES E tm D V RNKE H V ITRMRA AIASKQ F G Q E E 178
Cdd:cd03341 81 G T NL VVVL AGELL EK AEEL L RMGLHPSEII E GY E KA LK KA L EIL E ELV VYKI E -- D L RNKE E V SKALKT AIASKQ Y G N E D 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 179 V L CK L I A D ACI Q V C P K N PA NFNVDN V RV A K LV GG G L H D CTI VRGMV L K TDAV G TI KRV E KAKVAVF AGGV D T satetkgt 258
Cdd:cd03341 159 F L SP L V A E ACI S V L P E N IG NFNVDN I RV V K IL GG S L E D SKV VRGMV F K REPE G SV KRV K KAKVAVF SCPF D I -------- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 259 vlihsadqlenyakteeakveelikavads G AK VIV S G AA VG EM ALH F C ER Y KL MV L KI S SKFELRR F CRT T G SVAILK L 338
Cdd:cd03341 231 ------------------------------ G VN VIV A G GS VG DL ALH Y C NK Y GI MV I KI N SKFELRR L CRT V G ATPLPR L 280
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 339 SQ P N P DDL GY A DS IS VEEIG GVR V T V VKNEEGGNSVC T V VLRG S T DS IL E D L ERA V DDGVN TY K AMCR D S R I VPGA A ATE 418
Cdd:cd03341 281 GA P T P EEI GY C DS VY VEEIG DTK V V V FRQNKEDSKIA T I VLRG A T QN IL D D V ERA I DDGVN VF K SLTK D G R F VPGA G ATE 360
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 419 IELA RR LKE FSF K ET GL D QYAI A KFAE S FE M VP K TL S ENAGL N A M E II S S LYA E H AS GN SKV G I D L E E G I -- C KD VATMN 496
Cdd:cd03341 361 IELA KK LKE YGE K TP GL E QYAI K KFAE A FE V VP R TL A ENAGL D A T E VL S E LYA A H QK GN KSA G V D I E S G D eg T KD AKEAG 440
490 500 510
....*....|....*....|....*....|..
gi 802585508 497 I W D LYV TK FF A L K Y A AD AA C TVLRVDQIIMAK 528
Cdd:cd03341 441 I F D HLA TK KW A I K L A TE AA V TVLRVDQIIMAK 472
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
38-528
0e+00
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain]
Cd Length: 489
Bit Score: 545.65
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 38 L ST I T RTSLGP N GM N KM VI N HLDKLF VTND A ATI VN ELE V QHPAAK I LV L A G KAQ Q EE I GDG ANLTISF AGELL QN AE E L 117
Cdd:pfam00118 1 L AD I V RTSLGP K GM D KM LV N SGGDVT VTND G ATI LK ELE I QHPAAK L LV E A A KAQ D EE V GDG TTTVVVL AGELL EE AE K L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 118 IRM G L HP SE II S GY N KA IT KA I EILD ELVEKES E TM D vrn K E HVITRM R AAIA SK QFGQ E - EV L C KL IA DA C i QVC PKN P 196
Cdd:pfam00118 81 LAA G V HP TT II E GY E KA LE KA L EILD SIISIPV E DV D --- R E DLLKVA R TSLS SK IISR E s DF L A KL VV DA V - LAI PKN D 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 197 AN F NVD N VR V A K LV GG G L H D CTI V R G M VL KTDAVGT -- I KR V E K AKV AVFAGGVDTSA TETK G TV LIHS A D QLE NYA K T E 274
Cdd:pfam00118 157 GS F DLG N IG V V K IL GG S L E D SEL V D G V VL DKGPLHP dm P KR L E N AKV LLLNCSLEYEK TETK A TV VLSD A E QLE RFL K A E 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 275 E AKVE E LIKAVA DSG AK V I V SGAAVGEM ALHF CERYKL M V L KISS K FE L R R FCRT TG SV A ILK L SQPN PDDLG Y A DSISV 354
Cdd:pfam00118 237 E EQIL E IVEKII DSG VN V V V CQKGIDDL ALHF LAKNGI M A L RRVK K RD L E R LAKA TG AR A VSS L DDLT PDDLG T A GKVEE 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 355 E E IG GVRV T VVKNEEGGNS v C T VV LRG S TD SI L EDL ER AVD D GVNTY K AMCR D S R I VPG AA A T E I ELAR R L K E FSFKET G 434
Cdd:pfam00118 317 E K IG DEKY T FIEGCKSPKA - A T IL LRG A TD HV L DEI ER SIH D ALCVV K NAIE D P R V VPG GG A V E M ELAR A L R E YAKSVS G 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 435 LD Q Y AI AK FAE SF E MV PKTL S ENAGL NAM E IISS L Y A E HASG NSKV GID L E E G ICK D VATMNIW D LYVT K FF ALK Y A AD A 514
Cdd:pfam00118 396 KE Q L AI EA FAE AL E VI PKTL A ENAGL DPI E VLAE L R A A HASG EKHA GID V E T G EII D MKEAGVV D PLKV K RQ ALK S A TE A 475
490
....*....|....
gi 802585508 515 A C T V LR V D Q II M AK 528
Cdd:pfam00118 476 A S T I LR I D D II K AK 489
thermosome_alpha
NF041082 thermosome subunit alpha;
14-528
9.85e-123
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 370.37
E-value: 9.85e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 14 LKEG HKHL SG L D e A VLK NI D A C K QLSTIT RT S LGP N GM N KM VINH L DKLFV TND AA TI VN E LEVQ HPAAK IL V LAG K A Q Q 93
Cdd:NF041082 6 LKEG TQRT SG R D - A QRN NI M A A K AVAEAV RT T LGP K GM D KM LVDS L GDVVI TND GV TI LK E MDIE HPAAK MI V EVA K T Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 94 E E I GDG ANLTISF AGELL QN AEEL IRMGL HP SE I IS GY NK A IT KA I EILDE LVE K eset M D VRN KE HVITRMRA A IAS K Q 173
Cdd:NF041082 85 D E V GDG TTTAVVL AGELL KK AEEL LDQDI HP TI I AE GY RL A AE KA L EILDE IAI K ---- V D PDD KE TLKKIAAT A MTG K G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 174 FGQ - EEV L CK L IA DA CIQ V C - PKNPA N FNV DN VR V A K L VGG GLH D CTI V R G M V LKTDA V -- G TI KRVE K AK V A VFAGGVD 249
Cdd:NF041082 161 AEA a KDK L AD L VV DA VKA V A e KDGGY N VDL DN IK V E K K VGG SIE D SEL V E G V V IDKER V hp G MP KRVE N AK I A LLDAPLE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 250 TSA TE TKGTVL I HSA DQL ENYAKT EE AKVE E LIKAV ADSGA K V IVSGAAVGEM A L H FCERYKLMVLKISS K FELRRFCRT 329
Cdd:NF041082 241 VKK TE IDAKIS I TDP DQL QAFLDQ EE KMLK E MVDKI ADSGA N V VFCQKGIDDL A Q H YLAKEGILAVRRVK K SDMEKLAKA 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 330 TG SVAILKLSQPN P D DLGYA DSISVEEI GG VRVTV V KNEEGGNS V c T VV LRG S T DSILEDL ERA VD D GVNTYKAMCR D SR 409
Cdd:NF041082 321 TG ARIVTSIDDLS P E DLGYA GLVEERKV GG DKMIF V EGCKNPKA V - T IL LRG G T EHVVDEV ERA LE D ALRVVRVVLE D GK 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 410 I V P G AA A T E I ELA R RL K E FSFKET G LD Q Y AI AK FAE SF E MV P K TL S ENAGL NAMEIISS L YAE H AS GN SKV G I D LEE G IC 489
Cdd:NF041082 400 V V A G GG A P E V ELA L RL R E YAASVG G RE Q L AI EA FAE AL E II P R TL A ENAGL DPIDALVE L RSA H EK GN KTA G L D VYT G KV 479
490 500 510
....*....|....*....|....*....|....*....
gi 802585508 490 K D VATMNIWDLYVT K FF A L K Y A AD AA CTV LR V D QI I M A K 528
Cdd:NF041082 480 V D MLEIGVVEPLRV K TQ A I K S A TE AA VMI LR I D DV I A A A 518
thermosome_beta
NF041083 thermosome subunit beta;
14-528
4.37e-116
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 353.49
E-value: 4.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 14 LKEG HKHLS G L D e A VLK NI D A C K QLSTIT RT S LGP N GM N KM VINH L DKLFV TND A ATI VN E LE VQHPAAK I LV LAG K A Q Q 93
Cdd:NF041083 6 LKEG TQRTK G R D - A QRN NI M A A K AVAEAV RT T LGP K GM D KM LVDS L GDIVI TND G ATI LK E MD VQHPAAK M LV EVA K T Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 94 E E I GDG ANLTISF AGELL QN AEEL IRMGL HP SE I IS GY NK A IT KAIEILDE LV EK eset M D VRNK E HVITRMRAAIA SK Q 173
Cdd:NF041083 85 D E V GDG TTTAVVL AGELL KK AEEL LDQNI HP TI I AN GY RL A AE KAIEILDE IA EK ---- V D PDDR E TLKKIAETSLT SK G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 174 FGQE - EV L CKLIAD A CI QV CP K NPANFN VD -- N VRVA K LV GG GLH D CTIVR G M V LKTDA V -- G TI KRVE K AK V A VFAGGV 248
Cdd:NF041083 161 VEEA r DY L AEIAVK A VK QV AE K RDGKYY VD ld N IQIE K KH GG SIE D TQLIY G I V IDKEV V hp G MP KRVE N AK I A LLDAPL 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 249 DTSA TE TKGTVL I HSA DQL ENYAKT EE AKVE E LIKAVADS GA K V IVSGAAVGEM A L H FCERYKLMVLKISS K FELRRFCR 328
Cdd:NF041083 241 EVKK TE IDAEIR I TDP DQL QKFLDQ EE KMLK E MVDKIKAT GA N V VFCQKGIDDL A Q H YLAKAGILAVRRVK K SDMEKLAK 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 329 T TG SVAILKLSQPN P D DLGYA DSISVEEI G GVRVTV V KNEEGGNS V c T VVL RG S T DSILEDL ERA VD D GVNTYKAMCR D S 408
Cdd:NF041083 321 A TG ARIVTNIDDLT P E DLGYA ELVEERKV G DDKMVF V EGCKNPKA V - T ILI RG G T EHVVDEA ERA LE D ALSVVADAVE D G 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 R IV P G AA A T E I ELA R RL K E FSFKET G LD Q Y A IAK FAE SF E MV P K TL S ENAGL NAME I ISS L YAE H AS G NSKV GI DLEE G I 488
Cdd:NF041083 400 K IV A G GG A P E V ELA K RL R E YAATVG G RE Q L A VEA FAE AL E II P R TL A ENAGL DPID I LVK L RSA H EK G KKWA GI NVFT G E 479
490 500 510 520
....*....|....*....|....*....|....*....|
gi 802585508 489 CK D VATMNIWDLYVT K FF A L K Y A AD AA CTV LR V D QI I M AK 528
Cdd:NF041083 480 VV D MWELGVIEPLRV K TQ A I K S A TE AA TMI LR I D DV I A AK 519
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
10-529
4.24e-67
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 226.06
E-value: 4.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 10 IQAM LK E G HKHLS G l DE A V L KNIDACKQLSTITR T S LGP N GM N K MVI ----- NHLDKLF VTND A ATI VNELEVQH PAAKI 84
Cdd:PTZ00212 7 PPQV LK Q G AQEEK G - ET A R L QSFVGAIAVADLVK T T LGP K GM D K ILQ pmseg PRSGNVT VTND G ATI LKSVWLDN PAAKI 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 85 LV LAG K A Q Q EE I GDG ANLTISF AGELL QN AE E L IRMGL HP SE II S G YNK A ITK A IEI L D E LVEKESETMDVR n KE HVITR 164
Cdd:PTZ00212 86 LV DIS K T Q D EE V GDG TTSVVVL AGELL RE AE K L LDQKI HP QT II E G WRM A LDV A RKA L E E IAFDHGSDEEKF - KE DLLNI 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 165 M R AAIA SK QFGQ E - EVLC KL IA DA CIQV cpkn PANF N V D NVRVA K LV GG G L H D CTIVR G MV L - K TDA VG TI KR V E KA K VA 242
Cdd:PTZ00212 165 A R TTLS SK LLTV E k DHFA KL AV DA VLRL ---- KGSG N L D YIQII K KP GG T L R D SYLED G FI L e K KIG VG QP KR L E NC K IL 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 243 V FAGGV DT SATETK G T - V LIH S ADQLENYAKT E EA K VEELIKAVADS G AK V IVSGAAVGEMALHFCERYKL M VLK i SSK F 321
Cdd:PTZ00212 241 V ANTPM DT DKIKIY G A k V KVD S MEKVAEIEAA E KE K MKNKVDKILAH G CN V FINRQLIYNYPEQLFAEAGI M AIE - HAD F 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 322 E - LR R FCRTT G SVAILKLSQ P NPDD LG YA D S I SVEE IG GVRVT ---- VV K N E eggns V CT V VLRG STDS IL EDL ER AVD D 396
Cdd:PTZ00212 320 D g ME R LAAAL G AEIVSTFDT P EKVK LG HC D L I EEIM IG EDKLI rfsg CA K G E ----- A CT I VLRG ASTH IL DEA ER SLH D 394
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 397 GVNTYKAMCR D S R I V P G AAAT E IEL A RRLK E FSF K ET G LDQY AI AK FA ESFEMV P KTLSE N A G LNAM E II S S L Y AEH AS G 476
Cdd:PTZ00212 395 ALCVLSQTVK D T R V V L G GGCS E MLM A NAVE E LAK K VE G KKSL AI EA FA KALRQI P TIIAD N G G YDSA E LV S K L R AEH YK G 474
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 802585508 477 N SKV GID L E E G ICK D VATMN I WDL Y VT K FFA L KY A AD AA CTV LRVD Q II MAK P 529
Cdd:PTZ00212 475 N KTA GID M E K G TVG D MKELG I TES Y KV K LSQ L CS A TE AA EMI LRVD D II RCA P 527
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
25-535
5.23e-65
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 219.56
E-value: 5.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 25 DE A VLK NI DAC K Q L STITRTS LGP N G M N K M vinh L D K L F ---- V TND AA TI VN E L E VQH P ---- A A KILVLAGKAQQE E I 96
Cdd:COG0459 9 ED A RRA NI RGV K A L ADAVKVT LGP K G R N V M ---- L V K S F gdpt I TND GV TI AK E I E LED P fenm G A QLVKEVASKTND E A 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 97 GDG ANLTISF AG E LL QNAEE L IRM G LH P SE I IS G YN KA IT KA I E I L DEL vekese TMD V RN KE HV itrmr A AI A SKQFGQ 176
Cdd:COG0459 85 GDG TTTATVL AG A LL KEGLK L VAA G AN P TD I KR G ID KA VE KA V E E L KKI ------ AKP V DD KE EL ----- A QV A TISANG 153
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 177 E E VLCK LIA D A CIQ V CPK npanfnv DNVR V AK lv G G GL H - DCTI V R GM VL --------- K TD AVGTIKRV E K A KVAV fag 246
Cdd:COG0459 154 D E EIGE LIA E A MEK V GKD ------- GVIT V EE -- G K GL E t ELEV V E GM QF dkgylspyf V TD PEKMPAEL E N A YILL --- 221
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 247 gvdtsa T ET K gtvl I H S ADQ L enyakteeakv EE L IKA VA D SG AKVIVSGAAVGEM AL HFCERYKLM - VL KISS ------ 319
Cdd:COG0459 222 ------ T DK K ---- I S S IQD L ----------- LP L LEK VA Q SG KPLLIIAEDIDGE AL ATLVVNGIR g VL RVVA vkapgf 280
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 320 ---- K FE L RRFCRT TG SVA I ----- LKL SQPNP DDLG Y A DSI sve E IGGVRV T V V KNEEGGNSV c TVVLRGS T DSILEDL 390
Cdd:COG0459 281 gdrr K AM L EDIAIL TG GRV I sedlg LKL EDVTL DDLG R A KRV --- E VDKDNT T I V EGAGNPKAI - VILVGAA T EVEVKER 356
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 391 E R A V D D GVNTYK A MCRD s R IVPG AA A TEIEL AR R L K E FSF K ET G LD Q YA I AKF A ESF E MVPKTLS ENAGL NAMEIISSL y 470
Cdd:COG0459 357 K R R V E D ALHATR A AVEE - G IVPG GG A ALLRA AR A L R E LAA K LE G DE Q LG I EIV A RAL E APLRQIA ENAGL DGSVVVEKV - 434
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802585508 471 AEHASGN sk V G I D LEE G ICK D VATMNIW D - LY V TK f F AL KY AA DA A CTV L RVDQI I MA KP AGGPNP 535
Cdd:COG0459 435 RAAKDKG -- F G F D AAT G EYV D MLEAGVI D p AK V KR - S AL QN AA SV A GLI L TTEAV I AD KP EKEEAA 497
Name
Accession
Description
Interval
E-value
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
9-535
0e+00
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: 841.68
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 9 GI QAM LKEG HK H L SGL D EAV L KNI D ACK Q LS T ITRTSLGPNGMNKMVINHL D KLFVTNDAATI VN ELEVQHPAAK I LV L A 88
Cdd:TIGR02346 1 GI ASL LKEG YR H F SGL E EAV I KNI E ACK E LS Q ITRTSLGPNGMNKMVINHL E KLFVTNDAATI LR ELEVQHPAAK L LV M A 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 89 GKA Q QE EIGDG A NL TISF AGELL QN AEELIRMGLHPSEII S GY NK A IT KA I EIL D ELV E ke S E TM D V R N K EHV I TRMR A A 168
Cdd:TIGR02346 81 SEM Q EN EIGDG T NL VLVL AGELL NK AEELIRMGLHPSEII K GY EM A LK KA M EIL E ELV V -- W E VK D L R D K DEL I KALK A S 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 169 I A SKQ F G Q E EV L CK L I A D AC IQ V C PKNP A NFNVDN V RV A K LV GG G L HDCTIVR GMV LKTD A V G TI K R V EK AKVAVF AGGV 248
Cdd:TIGR02346 159 I S SKQ Y G N E DF L AQ L V A Q AC ST V L PKNP Q NFNVDN I RV C K IL GG S L SNSEVLK GMV FNRE A E G SV K S V KN AKVAVF SCPL 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 249 DT SA TETKGTVLIH S A DQ L E NY A K T EE AKV E EL IKA V ADSG AK VIV S G AA VG E MALH FCER Y KL MVLKI S SKFELRR F C R 328
Cdd:TIGR02346 239 DT AT TETKGTVLIH N A EE L L NY S K G EE NQI E AM IKA I ADSG VN VIV T G GS VG D MALH YLNK Y NI MVLKI P SKFELRR L C K 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 329 T T G SVAILK L SQ P N P DDL GY A DS IS V E EIGG VR VTV V K N E E G GNSVC T VV LRGSTD SI L E D L ERA V DDGVNT Y KA MCR D S 408
Cdd:TIGR02346 319 T V G ATPLPR L GA P T P EEI GY V DS VY V S EIGG DK VTV F K Q E N G DSKIS T II LRGSTD NL L D D I ERA I DDGVNT V KA LVK D G 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 R IV PGA A ATEIELA R RL KEFSF K ET GLDQYAI A KFAE S FE MV P K TL S ENAGLNA M E I I SS LYA E H AS GN SKV GID L E EGI 488
Cdd:TIGR02346 399 R LL PGA G ATEIELA S RL TKYGE K LP GLDQYAI K KFAE A FE II P R TL A ENAGLNA N E V I PK LYA A H KK GN KSK GID I E AES 478
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 802585508 489 C -- KD VATMN I W D LYV TK FF A L K Y A AD AA C TVLRVDQIIMAKPAGGP N P 535
Cdd:TIGR02346 479 D gv KD ASEAG I Y D MLA TK KW A I K L A TE AA V TVLRVDQIIMAKPAGGP K P 527
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
19-528
0e+00
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: 754.06
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 19 K H L SGL D EAVL K NI D ACK Q LS T ITRTS L GPNGMNKMVINHL D KLFVT N DAATI VN ELEVQHPAAK I LV L A GKA Q Q EEIGD 98
Cdd:cd03341 1 R H Y SGL E EAVL R NI E ACK E LS Q ITRTS Y GPNGMNKMVINHL E KLFVT S DAATI LR ELEVQHPAAK L LV M A SQM Q E EEIGD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 99 G A NL TISF AGELL QN AEEL I RMGLHPSEII S GY N KA IT KA I EIL D ELV EKES E tm D V RNKE H V ITRMRA AIASKQ F G Q E E 178
Cdd:cd03341 81 G T NL VVVL AGELL EK AEEL L RMGLHPSEII E GY E KA LK KA L EIL E ELV VYKI E -- D L RNKE E V SKALKT AIASKQ Y G N E D 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 179 V L CK L I A D ACI Q V C P K N PA NFNVDN V RV A K LV GG G L H D CTI VRGMV L K TDAV G TI KRV E KAKVAVF AGGV D T satetkgt 258
Cdd:cd03341 159 F L SP L V A E ACI S V L P E N IG NFNVDN I RV V K IL GG S L E D SKV VRGMV F K REPE G SV KRV K KAKVAVF SCPF D I -------- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 259 vlihsadqlenyakteeakveelikavads G AK VIV S G AA VG EM ALH F C ER Y KL MV L KI S SKFELRR F CRT T G SVAILK L 338
Cdd:cd03341 231 ------------------------------ G VN VIV A G GS VG DL ALH Y C NK Y GI MV I KI N SKFELRR L CRT V G ATPLPR L 280
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 339 SQ P N P DDL GY A DS IS VEEIG GVR V T V VKNEEGGNSVC T V VLRG S T DS IL E D L ERA V DDGVN TY K AMCR D S R I VPGA A ATE 418
Cdd:cd03341 281 GA P T P EEI GY C DS VY VEEIG DTK V V V FRQNKEDSKIA T I VLRG A T QN IL D D V ERA I DDGVN VF K SLTK D G R F VPGA G ATE 360
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 419 IELA RR LKE FSF K ET GL D QYAI A KFAE S FE M VP K TL S ENAGL N A M E II S S LYA E H AS GN SKV G I D L E E G I -- C KD VATMN 496
Cdd:cd03341 361 IELA KK LKE YGE K TP GL E QYAI K KFAE A FE V VP R TL A ENAGL D A T E VL S E LYA A H QK GN KSA G V D I E S G D eg T KD AKEAG 440
490 500 510
....*....|....*....|....*....|..
gi 802585508 497 I W D LYV TK FF A L K Y A AD AA C TVLRVDQIIMAK 528
Cdd:cd03341 441 I F D HLA TK KW A I K L A TE AA V TVLRVDQIIMAK 472
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
38-528
0e+00
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain]
Cd Length: 489
Bit Score: 545.65
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 38 L ST I T RTSLGP N GM N KM VI N HLDKLF VTND A ATI VN ELE V QHPAAK I LV L A G KAQ Q EE I GDG ANLTISF AGELL QN AE E L 117
Cdd:pfam00118 1 L AD I V RTSLGP K GM D KM LV N SGGDVT VTND G ATI LK ELE I QHPAAK L LV E A A KAQ D EE V GDG TTTVVVL AGELL EE AE K L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 118 IRM G L HP SE II S GY N KA IT KA I EILD ELVEKES E TM D vrn K E HVITRM R AAIA SK QFGQ E - EV L C KL IA DA C i QVC PKN P 196
Cdd:pfam00118 81 LAA G V HP TT II E GY E KA LE KA L EILD SIISIPV E DV D --- R E DLLKVA R TSLS SK IISR E s DF L A KL VV DA V - LAI PKN D 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 197 AN F NVD N VR V A K LV GG G L H D CTI V R G M VL KTDAVGT -- I KR V E K AKV AVFAGGVDTSA TETK G TV LIHS A D QLE NYA K T E 274
Cdd:pfam00118 157 GS F DLG N IG V V K IL GG S L E D SEL V D G V VL DKGPLHP dm P KR L E N AKV LLLNCSLEYEK TETK A TV VLSD A E QLE RFL K A E 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 275 E AKVE E LIKAVA DSG AK V I V SGAAVGEM ALHF CERYKL M V L KISS K FE L R R FCRT TG SV A ILK L SQPN PDDLG Y A DSISV 354
Cdd:pfam00118 237 E EQIL E IVEKII DSG VN V V V CQKGIDDL ALHF LAKNGI M A L RRVK K RD L E R LAKA TG AR A VSS L DDLT PDDLG T A GKVEE 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 355 E E IG GVRV T VVKNEEGGNS v C T VV LRG S TD SI L EDL ER AVD D GVNTY K AMCR D S R I VPG AA A T E I ELAR R L K E FSFKET G 434
Cdd:pfam00118 317 E K IG DEKY T FIEGCKSPKA - A T IL LRG A TD HV L DEI ER SIH D ALCVV K NAIE D P R V VPG GG A V E M ELAR A L R E YAKSVS G 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 435 LD Q Y AI AK FAE SF E MV PKTL S ENAGL NAM E IISS L Y A E HASG NSKV GID L E E G ICK D VATMNIW D LYVT K FF ALK Y A AD A 514
Cdd:pfam00118 396 KE Q L AI EA FAE AL E VI PKTL A ENAGL DPI E VLAE L R A A HASG EKHA GID V E T G EII D MKEAGVV D PLKV K RQ ALK S A TE A 475
490
....*....|....
gi 802585508 515 A C T V LR V D Q II M AK 528
Cdd:pfam00118 476 A S T I LR I D D II K AK 489
chaperonin_type_I_II
cd00309 chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
19-526
9.01e-166
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: 478.46
E-value: 9.01e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 19 K HLSGLD EA V L K NI D A C K Q L STITR T S LGP N GM N KM VINH L DKLFV TND A ATI VN E L EV Q HPAAK I LV LAG K A Q QE E I GD 98
Cdd:cd00309 1 K EREFGE EA R L S NI N A A K A L ADAVK T T LGP K GM D KM LVDS L GDPTI TND G ATI LK E I EV E HPAAK L LV EVA K S Q DD E V GD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 99 G ANLTISF AGELL QN AE E L IRM G L HP S EII S GY N KA IT KA I EIL D E L veke SETM DV RNK E HVITRMRAAIA SK QFGQ - E 177
Cdd:cd00309 81 G TTTVVVL AGELL KE AE K L LAA G I HP T EII R GY E KA VE KA L EIL K E I ---- AVPI DV EDR E ELLKVATTSLN SK LVSG g D 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 178 EV L CK L IA DA CIQ V CPK N P a NFNVDNV RV A K LV GG G L H D CTI V R GMV LKTDAVGTI -- KR V E K AK VAVFAGGVDT satet 255
Cdd:cd00309 157 DF L GE L VV DA VLK V GKE N G - DVDLGVI RV E K KK GG S L E D SEL V V GMV FDKGYLSPY mp KR L E N AK ILLLDCKLEY ----- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 256 kgtvlihsadqlenyakteeakveelikavadsgak V IVSGAAVGEM ALH FCERYKL M VLKISS K FE L R R FCRT TG SVAI 335
Cdd:cd00309 231 ------------------------------------ V VIAEKGIDDE ALH YLAKLGI M AVRRVR K ED L E R IAKA TG ATIV 274
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 336 LK L SQPN P D DLG Y A DSISVEE IG GVRV T VVKNEE GG n S V C T VV LRG S T DSI L EDL ER AVD D GVNTYK A MCR D SR IVPG AA 415
Cdd:cd00309 275 SR L EDLT P E DLG T A GLVEETK IG DEKY T FIEGCK GG - K V A T IL LRG A T EVE L DEA ER SLH D ALCAVR A AVE D GG IVPG GG 353
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 416 A T EIEL ARR L K E FSFKET G LD Q YA I AK FA ESF E MV P K TL S ENAGL NAM E IISS L Y A E HA S G NSKV G I D L E E G ICK D VATM 495
Cdd:cd00309 354 A A EIEL SKA L E E LAKTLP G KE Q LG I EA FA DAL E VI P R TL A ENAGL DPI E VVTK L R A K HA E G GGNA G G D V E T G EIV D MKEA 433
490 500 510
....*....|....*....|....*....|.
gi 802585508 496 N I W D LYVT K FF ALK Y A AD AA CTV L RV D Q II M 526
Cdd:cd00309 434 G I I D PLKV K RQ ALK S A TE AA SLI L TI D D II V 464
cpn60
cd03343 cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
14-528
7.17e-126
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: 378.53
E-value: 7.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 14 LKEG HKHL SG L D e A VLK NI D A C K QLSTIT RT S LGP N GM N KM VINH L DKLFV TND A ATI VN E LEVQ HPAAK I LV LAG K A Q Q 93
Cdd:cd03343 4 LKEG TQRT SG R D - A QRM NI A A A K AVAEAV RT T LGP K GM D KM LVDS L GDVTI TND G ATI LK E MDIE HPAAK M LV EVA K T Q D 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 94 EE I GDG ANLTISF AGELL QN AE E L IRMGL HP SE II S GY NK A IT KA I E I LDE LVE K eset M D VRN K EHVITRMRAAIAS K Q 173
Cdd:cd03343 83 EE V GDG TTTAVVL AGELL EK AE D L LDQNI HP TV II E GY RL A AE KA L E L LDE IAI K ---- V D PDD K DTLRKIAKTSLTG K G 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 174 FGQE - EV L CK L IA DA CI QV CP K NPANFN VD -- N VRVA K LV GG GLH D CTIV RG M V LKTDA V -- G TI KRVE K AK V A VFAGGV 248
Cdd:cd03343 159 AEAA k DK L AD L VV DA VL QV AE K RDGKYV VD ld N IKIE K KT GG SVD D TELI RG I V IDKEV V hp G MP KRVE N AK I A LLDAPL 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 249 DTSA TE TKGTVL I H S A DQL ENYAKT EEA KVE E LIKAV AD S GA K V IVSGAAVGEM A L H FCERYKLMVLKISS K FELRRFC R 328
Cdd:cd03343 239 EVKK TE IDAKIR I T S P DQL QAFLEQ EEA MLK E MVDKI AD T GA N V VFCQKGIDDL A Q H YLAKAGILAVRRVK K SDMEKLA R 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 329 T TG SVAILKLSQPN P D DLG Y A DSISVEEI G GVRVTV V KNEEGGNS V c T VV LRG S T DSILED LERA VD D GVNTYKAMCR D S 408
Cdd:cd03343 319 A TG AKIVTNIDDLT P E DLG E A ELVEERKV G DDKMVF V EGCKNPKA V - T IL LRG G T EHVVDE LERA LE D ALRVVADALE D G 397
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 RI V P G AA A T EIELA R RL K E FSFKET G LD Q Y A IAK FA ESF E MV P K TL S ENAGL NAMEIISS L Y A E H AS GN SKV G I D LEE G I 488
Cdd:cd03343 398 KV V A G GG A V EIELA K RL R E YARSVG G RE Q L A VEA FA DAL E EI P R TL A ENAGL DPIDTLVE L R A A H EK GN KNA G L D VYT G E 477
490 500 510 520
....*....|....*....|....*....|....*....|
gi 802585508 489 CK D VATMNIWDLYVT K FF A L K Y A AD AA CTV LR V D QI I M AK 528
Cdd:cd03343 478 VV D MLEKGVIEPLRV K KQ A I K S A TE AA TMI LR I D DV I A AK 517
thermosome_alpha
NF041082 thermosome subunit alpha;
14-528
9.85e-123
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 370.37
E-value: 9.85e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 14 LKEG HKHL SG L D e A VLK NI D A C K QLSTIT RT S LGP N GM N KM VINH L DKLFV TND AA TI VN E LEVQ HPAAK IL V LAG K A Q Q 93
Cdd:NF041082 6 LKEG TQRT SG R D - A QRN NI M A A K AVAEAV RT T LGP K GM D KM LVDS L GDVVI TND GV TI LK E MDIE HPAAK MI V EVA K T Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 94 E E I GDG ANLTISF AGELL QN AEEL IRMGL HP SE I IS GY NK A IT KA I EILDE LVE K eset M D VRN KE HVITRMRA A IAS K Q 173
Cdd:NF041082 85 D E V GDG TTTAVVL AGELL KK AEEL LDQDI HP TI I AE GY RL A AE KA L EILDE IAI K ---- V D PDD KE TLKKIAAT A MTG K G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 174 FGQ - EEV L CK L IA DA CIQ V C - PKNPA N FNV DN VR V A K L VGG GLH D CTI V R G M V LKTDA V -- G TI KRVE K AK V A VFAGGVD 249
Cdd:NF041082 161 AEA a KDK L AD L VV DA VKA V A e KDGGY N VDL DN IK V E K K VGG SIE D SEL V E G V V IDKER V hp G MP KRVE N AK I A LLDAPLE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 250 TSA TE TKGTVL I HSA DQL ENYAKT EE AKVE E LIKAV ADSGA K V IVSGAAVGEM A L H FCERYKLMVLKISS K FELRRFCRT 329
Cdd:NF041082 241 VKK TE IDAKIS I TDP DQL QAFLDQ EE KMLK E MVDKI ADSGA N V VFCQKGIDDL A Q H YLAKEGILAVRRVK K SDMEKLAKA 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 330 TG SVAILKLSQPN P D DLGYA DSISVEEI GG VRVTV V KNEEGGNS V c T VV LRG S T DSILEDL ERA VD D GVNTYKAMCR D SR 409
Cdd:NF041082 321 TG ARIVTSIDDLS P E DLGYA GLVEERKV GG DKMIF V EGCKNPKA V - T IL LRG G T EHVVDEV ERA LE D ALRVVRVVLE D GK 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 410 I V P G AA A T E I ELA R RL K E FSFKET G LD Q Y AI AK FAE SF E MV P K TL S ENAGL NAMEIISS L YAE H AS GN SKV G I D LEE G IC 489
Cdd:NF041082 400 V V A G GG A P E V ELA L RL R E YAASVG G RE Q L AI EA FAE AL E II P R TL A ENAGL DPIDALVE L RSA H EK GN KTA G L D VYT G KV 479
490 500 510
....*....|....*....|....*....|....*....
gi 802585508 490 K D VATMNIWDLYVT K FF A L K Y A AD AA CTV LR V D QI I M A K 528
Cdd:NF041082 480 V D MLEIGVVEPLRV K TQ A I K S A TE AA VMI LR I D DV I A A A 518
thermosome_arch
TIGR02339 thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
13-527
2.43e-121
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274080
Cd Length: 519
Bit Score: 367.09
E-value: 2.43e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 13 M LKEG HKHL SG L D e A VLK NI D A C K QLSTITRTS LGP N GM N KM VINH L DKLFV TND A ATI VN E LEVQ HPAAK I LV LAG K A Q 92
Cdd:TIGR02339 4 I LKEG TQRT SG R D - A QRN NI A A A K AVAEAVKST LGP R GM D KM LVDS L GDVTI TND G ATI LK E MDIE HPAAK M LV EVA K T Q 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 93 Q EE I GDG ANLTISF AGELL QN AE E L IRMGL HP SE II S GY N KA IT KA I EI L DE LVE K eset MDVRNKEHVITRMRAAIA SK 172
Cdd:TIGR02339 83 D EE V GDG TTTAVVL AGELL EK AE D L LEQDI HP TV II E GY R KA AE KA L EI I DE IAT K ---- ISPEDRDLLKKIAYTSLT SK 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 173 QFGQE -- EV L CK L IAD A CI QV CPKNP --- ANFNV DN VRVA K LV GG GLH D CTI V R G M V LKTDA V -- G TI KRVE K AK V A VFA 245
Cdd:TIGR02339 159 ASAEV ak DK L AD L VVE A VK QV AELRG dgk YYVDL DN IKIV K KK GG SIE D TEL V E G I V VDKEV V hp G MP KRVE N AK I A LLD 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 246 GGVDTSA TE TKGTVL I HSA DQ LENYAKT EEA KVE E LIKAV A DS GA K V IVSGAAVGEM A L H FCERYKLMVLKISS K FELRR 325
Cdd:TIGR02339 239 APLEVEK TE IDAKIR I TDP DQ IKKFLDQ EEA MLK E MVDKI A SA GA N V VICQKGIDDV A Q H YLAKAGILAVRRVK K SDIEK 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 326 FC R T TG SVAILKLSQPNPD DLGYA DSISVEEI G GVRVTV V KNEEGGNS V c T VV LRG S T DSILED LER AVD D GVNTYKAMC 405
Cdd:TIGR02339 319 LA R A TG ARIVSSIDEITES DLGYA ELVEERKV G EDKMVF V EGCKNPKA V - T IL LRG G T EHVVDE LER SIQ D ALHVVANAL 397
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 406 R D SR IV P G AA A T EIELA R RL KEFSFKET G LD Q Y AI AK FA ESF E MV P KT L S ENAGL NAMEIISS L Y A E H AS GN SKV GI DLE 485
Cdd:TIGR02339 398 E D GK IV A G GG A V EIELA L RL RSYARSVG G RE Q L AI EA FA DAL E EI P RI L A ENAGL DPIDALVD L R A K H EK GN KNA GI NVF 477
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 802585508 486 E G ICK D VATMNIWDLYVT K FF A L K Y A AD AA CTV LR V D QI I M A 527
Cdd:TIGR02339 478 T G EIE D MLELGVIEPLRV K EQ A I K S A TE AA TMI LR I D DV I A A 519
thermosome_beta
NF041083 thermosome subunit beta;
14-528
4.37e-116
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 353.49
E-value: 4.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 14 LKEG HKHLS G L D e A VLK NI D A C K QLSTIT RT S LGP N GM N KM VINH L DKLFV TND A ATI VN E LE VQHPAAK I LV LAG K A Q Q 93
Cdd:NF041083 6 LKEG TQRTK G R D - A QRN NI M A A K AVAEAV RT T LGP K GM D KM LVDS L GDIVI TND G ATI LK E MD VQHPAAK M LV EVA K T Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 94 E E I GDG ANLTISF AGELL QN AEEL IRMGL HP SE I IS GY NK A IT KAIEILDE LV EK eset M D VRNK E HVITRMRAAIA SK Q 173
Cdd:NF041083 85 D E V GDG TTTAVVL AGELL KK AEEL LDQNI HP TI I AN GY RL A AE KAIEILDE IA EK ---- V D PDDR E TLKKIAETSLT SK G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 174 FGQE - EV L CKLIAD A CI QV CP K NPANFN VD -- N VRVA K LV GG GLH D CTIVR G M V LKTDA V -- G TI KRVE K AK V A VFAGGV 248
Cdd:NF041083 161 VEEA r DY L AEIAVK A VK QV AE K RDGKYY VD ld N IQIE K KH GG SIE D TQLIY G I V IDKEV V hp G MP KRVE N AK I A LLDAPL 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 249 DTSA TE TKGTVL I HSA DQL ENYAKT EE AKVE E LIKAVADS GA K V IVSGAAVGEM A L H FCERYKLMVLKISS K FELRRFCR 328
Cdd:NF041083 241 EVKK TE IDAEIR I TDP DQL QKFLDQ EE KMLK E MVDKIKAT GA N V VFCQKGIDDL A Q H YLAKAGILAVRRVK K SDMEKLAK 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 329 T TG SVAILKLSQPN P D DLGYA DSISVEEI G GVRVTV V KNEEGGNS V c T VVL RG S T DSILEDL ERA VD D GVNTYKAMCR D S 408
Cdd:NF041083 321 A TG ARIVTNIDDLT P E DLGYA ELVEERKV G DDKMVF V EGCKNPKA V - T ILI RG G T EHVVDEA ERA LE D ALSVVADAVE D G 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 R IV P G AA A T E I ELA R RL K E FSFKET G LD Q Y A IAK FAE SF E MV P K TL S ENAGL NAME I ISS L YAE H AS G NSKV GI DLEE G I 488
Cdd:NF041083 400 K IV A G GG A P E V ELA K RL R E YAATVG G RE Q L A VEA FAE AL E II P R TL A ENAGL DPID I LVK L RSA H EK G KKWA GI NVFT G E 479
490 500 510 520
....*....|....*....|....*....|....*....|
gi 802585508 489 CK D VATMNIWDLYVT K FF A L K Y A AD AA CTV LR V D QI I M AK 528
Cdd:NF041083 480 VV D MWELGVIEPLRV K TQ A I K S A TE AA TMI LR I D DV I A AK 519
TCP1_delta
cd03338 TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
29-527
6.04e-101
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: 314.22
E-value: 6.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 29 L K NI D A C K QLSTIT RTSLGP N GM N KM VINHLDKLFV TND A ATI VNELE V Q HPAAK I LV LAG KAQ QE E I GDG ANLTISF AG 108
Cdd:cd03338 11 L S NI Q A A K AVADAI RTSLGP R GM D KM IQTGKGEVII TND G ATI LKQMS V L HPAAK M LV ELS KAQ DI E A GDG TTSVVVL AG 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 109 E LL QNA E E L IRM G L HP SE I ISGYNK A IT KA I EILD EL veke S ETM D VRNK E HV I TRMRAAIA SK QFG Q - EEV L CKLIA DA 187
Cdd:cd03338 91 A LL SAC E S L LKK G I HP TV I SESFQI A AK KA V EILD SM ---- S IPV D LNDR E SL I KSATTSLN SK VVS Q y SSL L APIAV DA 166
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 188 CIQ V C - P KNPA N FNVDNV R VA K LV GG GLH D CTI V R G M V LKTD A V --- G TIK R V EKAK VAVFAGGVDTSA T ETKGTVLIHS 263
Cdd:cd03338 167 VLK V I d P ATAT N VDLKDI R IV K KL GG TIE D TEL V D G L V FTQK A S kka G GPT R I EKAK IGLIQFCLSPPK T DMDNNIVVND 246
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 264 AD Q LENYAKT E EAKVEELI K AVAD SG AK V IVSGA ----- AV GEM ALHF CERY K L MV L K ISSKF E LRRF C R T T G SVAILKL 338
Cdd:cd03338 247 YA Q MDRILRE E RKYILNMC K KIKK SG CN V LLIQK silrd AV SDL ALHF LAKL K I MV V K DIERE E IEFI C K T I G CKPVASI 326
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 339 SQPNP D D LG Y AD SISVEEI G G --- V RV T V VKN EEGG nsv C T VVL RGS TDSI L EDL ER AVD D GVNTYKAMCRDSRIV PG AA 415
Cdd:cd03338 327 DHFTE D K LG S AD LVEEVSL G D gki V KI T G VKN PGKT --- V T ILV RGS NKLV L DEA ER SLH D ALCVIRCLVKKRALI PG GG 403
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 416 A T EIE L A RR L K E FSFKE TG LD QY AIAK FA ESF E MV P K TL S ENAGLN AME I ISS L YAE HA S G NSKV GI DLEE G ICKDVATM 495
Cdd:cd03338 404 A P EIE I A LQ L S E WARTL TG VE QY CVRA FA DAL E VI P Y TL A ENAGLN PIS I VTE L RNR HA Q G EKNA GI NVRK G AITNILEE 483
490 500 510
....*....|....*....|....*....|..
gi 802585508 496 N IWDLYVTKFF A LKY A ADAACTV L RV D Q I IM A 527
Cdd:cd03338 484 N VVQPLLVSTS A ITL A TETVRMI L KI D D I VL A 515
chap_CCT_delta
TIGR02342 T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
31-528
1.23e-91
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: 290.15
E-value: 1.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 31 NI D A C K QLSTIT RTSLGP N GM N KM VINHLDKLFV TND A ATI VNELE V Q HPAAK I LV LAG KAQ QE E I GDG ANLTISF AG E L 110
Cdd:TIGR02342 14 NI V A A K AVADAI RTSLGP K GM D KM IQDGKGEVII TND G ATI LKQMA V L HPAAK M LV ELS KAQ DI E A GDG TTSVVIL AG A L 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 111 L QNA E E L IRM G L HP SE I ISGYNK A ITK AI E ILDE L veke S ETM D VRNK E HVITRMRAAIA SK QFG Q - EEV L CK L IA DA CI 189
Cdd:TIGR02342 94 L GAC E R L LNK G I HP TI I SESFQS A ADE AI K ILDE M ---- S IPV D LSDR E QLLKSATTSLS SK VVS Q y SSL L AP L AV DA VL 169
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 190 Q V C - P K N PA N FNVDNVR V A K LV GG GLH D CTIVR G M V LKTD A V --- G TIK R V EKAK VAVFAGGVDTSA T ETKGTVLIHSAD 265
Cdd:TIGR02342 170 K V I d P E N AK N VDLNDIK V V K KL GG TID D TELIE G L V FTQK A S ksa G GPT R I EKAK IGLIQFQISPPK T DMENQIIVNDYA 249
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 266 Q LENYA K T E E A KVEELI K AVADS G AK V I ----- VSGA AV GEM ALHF CERY K L MV L K ISSKF E LRRF C R T T G SVA I LKLSQ 340
Cdd:TIGR02342 250 Q MDRVL K E E R A YILNIV K KIKKT G CN V L liqks ILRD AV NDL ALHF LAKM K I MV V K DIERE E IEFI C K T I G CKP I ASIDH 329
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 341 PNP D D LG Y A D si S VEE IGG ----- VRV T VVK N E eg G NS V c TVV L RGS TDSILEDL ER AVD D GVNTYKAMCRDSRIVP G AA 415
Cdd:TIGR02342 330 FTA D K LG S A E -- L VEE VDS dggki IKI T GIQ N A -- G KT V - TVV V RGS NKLVIDEA ER SLH D ALCVIRCLVKKRGLIA G GG 404
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 416 A T EIE L ARRL KEFSFKET G LDQ Y AIAK FA ESF E MV P K TL S ENAGLN AMEIISS L YAE HA S G NSKV GI DLEE G ICKDVATM 495
Cdd:TIGR02342 405 A P EIE I ARRL SKYARTMK G VES Y CVRA FA DAL E VI P Y TL A ENAGLN PIKVVTE L RNR HA N G EKTA GI SVRK G GITNMLEE 484
490 500 510
....*....|....*....|....*....|...
gi 802585508 496 NIWDLYVTKFF A LKY A ADAACTV L RV D Q I IMAK 528
Cdd:TIGR02342 485 HVLQPLLVTTS A ITL A SETVRSI L KI D D I VFTR 517
chap_CCT_alpha
TIGR02340 T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
25-529
2.74e-83
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: 268.90
E-value: 2.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 25 DEAVLK N ID A CKQLST I TR TSLGP N G MN KM VINHLDKLFV TND A ATI VNE LEV Q HPAAKILV LAGKA Q QE E I GDG ANLTI 104
Cdd:TIGR02340 11 QDVRTQ N VT A AMAIAN I VK TSLGP V G LD KM LVDDIGDVTI TND G ATI LKL LEV E HPAAKILV ELAQL Q DR E V GDG TTSVV 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 105 SF A G ELL QN A E EL IRMGL HP SEI ISGY NK A ITK A IEILD E LVEKESETM dvr NK E HV I TRMRAAIA SK QF G QE - EVLCKL 183
Cdd:TIGR02340 91 II A A ELL KR A D EL VKNKI HP TSV ISGY RL A CKE A VKYIK E NLSVSVDEL --- GR E AL I NVAKTSMS SK II G LD s DFFSNI 167
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 184 IA DA -- CIQVCPK N PAN - FNVDNVRVA K LV G GGLHDCTI V R G MV L KTDAV -- GTI KR VEK AK V A V fagg V D TSATET K -- 256
Cdd:TIGR02340 168 VV DA vl AVKTTNE N GET k YPIKAINIL K AH G KSARESML V K G YA L NCTVA sq QMP KR IKN AK I A C ---- L D FNLQKA K ma 243
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 257 - G T - VLIHSADQ LE NYAKT E EAKVE E L IK AVA D S GA K V IVSGAAVGE M A L HFCERYKL M VLKISS K FE L R R FCRT TG SVA 334
Cdd:TIGR02340 244 l G V q IVVDDPEK LE QIRQR E ADITK E R IK KIL D A GA N V VLTTGGIDD M C L KYFVEAGA M GVRRCK K ED L K R IAKA TG ATL 323
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 335 ILK L SQPNPDD ------ LG Y AD SISV E E I GGVRVTVV K NEEGGN S V c TVV LRG ST D SI L EDL ER AVD D GVNTY K AMCRDS 408
Cdd:TIGR02340 324 VST L ADLEGEE tfeasy LG F AD EVVQ E R I ADDECILI K GTKKRK S A - SII LRG AN D FM L DEM ER SLH D ALCVV K RTLESN 402
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 409 RI VPG AA A T E IE L ARR L KE F SFKETGLD Q Y AIA K FA ESFEMV PKTL SE NA GLNAM E IISS L Y A E HA SGNS K -------- V 480
Cdd:TIGR02340 403 SV VPG GG A V E AA L SIY L EN F ATTLGSRE Q L AIA E FA RALLII PKTL AV NA AKDST E LVAK L R A Y HA AAQL K pekkhlkw Y 482
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 802585508 481 G I DL EE G ICK D VATMNIWDLY V T K FFA LK Y A AD AA C T V LR V D QI I MAK P 529
Cdd:TIGR02340 483 G L DL VN G KIR D NKEAGVLEPT V S K VKS LK F A TE AA I T I LR I D DL I KLN P 531
TCP1_alpha
cd03335 TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
22-529
5.31e-83
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: 268.00
E-value: 5.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 22 SG L D e AVLK N ID A CKQLST I TRT SLGP N G MN KM VINHLDKLFV TND A ATI VNE LEV Q HPAAKILV LAGKA Q QE E I GDG AN 101
Cdd:cd03335 5 SG Q D - VRTQ N VT A AMAIAN I VKS SLGP V G LD KM LVDDIGDVTI TND G ATI LKL LEV E HPAAKILV ELAQL Q DK E V GDG TT 83
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 102 LTISF A G ELL QN A E EL IRMGL HP SE IISGY NK A ITK A IEILD E LVEKESETMD vrn KE HV I TRMRAAIA SK QF G QE - EVL 180
Cdd:cd03335 84 SVVII A A ELL KR A N EL VKQKI HP TT IISGY RL A CKE A VKYIK E HLSISVDNLG --- KE SL I NVAKTSMS SK II G AD s DFF 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 181 CKLIA DA CIQ V --- CP K NPANFNVDN V RVA K LV G GGLHDCTI V R G MV L KTD -- AV G TIK RV EK AK V A V fagg V D TSATE T 255
Cdd:cd03335 161 ANMVV DA ILA V ktt NE K GKTKYPIKA V NIL K AH G KSAKESYL V N G YA L NCT ra SQ G MPT RV KN AK I A C ---- L D FNLQK T 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 256 K --- G T - V LIHSADQ LE NYAKT E EAKVE E L IK AVADS GA K V IVSGAAVGE M A L HFCERYKL M VLKISS K FE LRR FCRT TG 331
Cdd:cd03335 237 K mkl G V q V VVTDPEK LE KIRQR E SDITK E R IK KILAA GA N V VLTTGGIDD M C L KYFVEAGA M AVRRVK K ED LRR IAKA TG 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 332 SVAILK L SQPN ------ P DD LG Y A DSISV E E IG GVRVTVV K NEEGGN S v CTVV LRG ST D SI L EDL ER AVD D GVNTY K AMC 405
Cdd:cd03335 317 ATLVST L ANLE geetfd P SY LG E A EEVVQ E R IG DDELILI K GTKKRS S - ASII LRG AN D FM L DEM ER SLH D ALCVV K RTL 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 406 RDSRI VPG AA A T E IE L ARR L KE F SFKETGLD Q Y AIA K FAE SFEMV PKTL SE NA GLN A M E IISS L Y A E HA SGNS K ------ 479
Cdd:cd03335 396 ESNSV VPG GG A V E TA L SIY L EN F ATTLGSRE Q L AIA E FAE ALLVI PKTL AV NA AKD A T E LVAK L R A Y HA AAQV K pdkkhl 475
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 802585508 480 -- V G I DL EE G ICK D VATMNIWDLY V T K FFA LK Y A AD AA C T V LR V D QI I MAK P 529
Cdd:cd03335 476 kw Y G L DL IN G KVR D NLEAGVLEPT V S K IKS LK F A TE AA I T I LR I D DL I KLN P 527
TCP1_gamma
cd03337 TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
26-525
7.86e-83
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: 266.08
E-value: 7.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 26 E A V L K NI D A C K QLSTIT RT S LGP NG M N KM VINHLDKLFV TND AAT I VN E LE V Q HPAAK ILVLAGKA Q Q EE I GDG ANLT I S 105
Cdd:cd03337 16 K A Q L G NI Q A A K TVADVI RT C LGP RA M L KM LLDPMGGIVL TND GNA I LR E ID V A HPAAK SMIELSRT Q D EE V GDG TTSV I I 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 106 F AGE L L QN AE ELIRM G L HP SE II SG Y N KA ITK A IE IL D E L veke S ETM DV RNKEHVITRMRAA I AS K QFGQEEV L - C K L I 184
Cdd:cd03337 96 L AGE I L AV AE PFLER G I HP TV II KA Y R KA LED A LK IL E E I ---- S IPV DV NDRAQMLKIIKSC I GT K FVSRWSD L m C N L A 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 185 A DA -- CIQ V C p K N PANFNV D --- NVR V A K LV GG GLH D CTIVR G MV L KT D AV -- GTIK R V E KAKV avfaggvdtsatetkg 257
Cdd:cd03337 172 L DA vk TVA V E - E N GRKKEI D ikr YAK V E K IP GG EIE D SRVLD G VM L NK D VT hp KMRR R I E NPRI ---------------- 234
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 258 t VL IHSA dq LE NYAK TE eakveeli K A V A D sgakvivsgaavge M A L H FCERYKLMV L KISS K FELR R FC R TT G SVAILK 337
Cdd:cd03337 235 - VL LDCP -- LE YLVI TE -------- K G V S D -------------- L A Q H YLVKAGITA L RRVR K TDNN R IA R AC G ATIVNR 289
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 338 LSQPNPD D L G - Y A DSIS V EE IG GVRV T VVKNEEGG n SV CT VV LRG STDSI L EDL ER AVD D GVNTYKAMCRDSRI VPG AA A 416
Cdd:cd03337 290 PEELTES D V G t G A GLFE V KK IG DEYF T FITECKDP - KA CT IL LRG ASKDV L NEV ER NLQ D AMAVARNIILNPKL VPG GG A 368
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 417 TE IELARR L K E FSFKET G LD Q YAIAKF A ESF E MV P K TL SE N A G L N AMEIISS L Y A E HA S - G NS KV GID L E E G ICK D VATM 495
Cdd:cd03337 369 TE MAVSHA L S E KAKSIE G VE Q WPYKAV A SAL E VI P R TL AQ N C G A N VIRTLTE L R A K HA Q g E NS TW GID G E T G DIV D MKEL 448
490 500 510
....*....|....*....|....*....|
gi 802585508 496 N IWD LYVT K FFAL K Y A AD AAC TV LR V D Q I I 525
Cdd:cd03337 449 G IWD PLAV K AQTY K T A IE AAC ML LR I D D I V 478
TCP1_eta
cd03340 TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
13-530
1.88e-78
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: 256.06
E-value: 1.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 13 M LKEG HKHLS G LDE a VLK NI D AC KQLSTIT RT S LGP N GM N K MVINHLD K LFVT ND A ATI VNE L EVQ HPAAK I LV LAG K A Q 92
Cdd:cd03340 4 L LKEG TDTSQ G KGQ - LIS NI N AC QAIADAV RT T LGP R GM D K LIVDGRG K VTIS ND G ATI LKL L DIV HPAAK T LV DIA K S Q 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 93 QE E I GDG ANLTISF AGE L L QN A EEL I RM G L HP SE II S GY N KA ITK AIE ILD E LVEKESETMDVRNK E HVITRMRA A IA SK 172
Cdd:cd03340 83 DA E V GDG TTSVVVL AGE F L KE A KPF I ED G V HP QI II R GY R KA LQL AIE KIK E IAVNIDKEDKEEQR E LLEKCAAT A LN SK 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 173 QFGQ E - E VLC K LIA DA CIQV cpkn PANFNV D NVRVA K LV GG G L H D CTI V R G MVL K T davg T I --------- K RVEKA K VA 242
Cdd:cd03340 163 LIAS E k E FFA K MVV DA VLSL ---- DDDLDL D MIGIK K VP GG S L E D SQL V N G VAF K K ---- T F syagfeqqp K KFKNP K IL 234
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 243 VFAGGVDTS A TETKGT V LIHSADQLENYAKT E EAKVEELIKAVAD SGA K V IV S GAAV G EM A LHFCERYKLMVLKISSKFE 322
Cdd:cd03340 235 LLNVELELK A EKDNAE V RVEDPEEYQAIVDA E WKIIYDKLEKIVK SGA N V VL S KLPI G DL A TQYFADRDIFCAGRVPEED 314
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 323 L R R FCRT TG SVAILKL S QPNP D D LG YADSISVEEI GG V R VTVVKNEEGGNS v CT VV LRG STDSIL E DL ER AVD D GVNTYK 402
Cdd:cd03340 315 L K R VAQA TG GSIQTTV S NITD D V LG TCGLFEERQV GG E R YNIFTGCPKAKT - CT II LRG GAEQFI E EA ER SLH D AIMIVR 393
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 403 AMCRDSRI V P G AA A T E I EL ARR L KEF S FKET G LD Q YA I AK FA ESF E MV P KT L SE NAG LN A ME I ISS L YAE HA S G NS K - V G 481
Cdd:cd03340 394 RAIKNDSV V A G GG A I E M EL SKY L RDY S RTIA G KQ Q LV I NA FA KAL E II P RQ L CD NAG FD A TD I LNK L RQK HA Q G GG K w Y G 473
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 802585508 482 I D L - E EGI CKDVATM n I W DLYVT K FF AL KY A AD AAC TV L R VD QI I MAKPA 530
Cdd:cd03340 474 V D I n N EGI ADNFEAF - V W EPSLV K IN AL TA A TE AAC LI L S VD ET I KNPKS 522
chap_CCT_epsi
TIGR02343 T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
19-525
3.39e-77
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: 252.80
E-value: 3.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 19 K H L S GL D e A VLK NI D A C K QLST I T RTSLGP N GM N KM V I NHLDKLF VTND A ATI VNELE V QHPA AK IL V LAG K A Q QE EIGD 98
Cdd:TIGR02343 21 K R L K GL E - A KKS NI A A A K SVAS I L RTSLGP K GM D KM L I SPDGDIT VTND G ATI LSQMD V DNQI AK LM V ELS K S Q DD EIGD 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 99 G ANLTISF AG E LL QN AEEL IRM G L HP SE I IS G YNK A ITK A I E I L D E LVEKE S et M D VR N K E HV I TRMRAAIA SK QFGQ - E 177
Cdd:TIGR02343 100 G TTGVVVL AG A LL EQ AEEL LDK G I HP IK I AD G FEE A ARI A V E H L E E ISDEI S -- A D NN N R E PL I QAAKTSLG SK IVSK c H 177
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 178 EVLCKLIA DA CIQ V CPKNPANFNV D NVR V AKL VGG G L H D CTIVR G MVLKT D AV -- GTI K R VE K AK V A VFAGGVDTSATE T 255
Cdd:TIGR02343 178 RRFAEIAV DA VLN V ADMERRDVDF D LIK V EGK VGG S L E D TKLIK G IIIDK D FS hp QMP K E VE D AK I A ILTCPFEPPKPK T 257
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 256 K GTVL I H S ADQLENYA K T E EA K VE E L I KAVAD SGA KVIVSGAAVGEM A L H FCERYK L MVLKISSKF EL RRFCRT TG SVAI 335
Cdd:TIGR02343 258 K HKLD I S S VEEYKKLQ K Y E QQ K FK E M I DDIKK SGA NLVICQWGFDDE A N H LLLQND L PAVRWVGGQ EL ELIAIA TG GRIV 337
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 336 LKLSQPNP D D LG Y A DSISVEEI G GV -- R VT V VKNEEGGNS V c T VVL RG STDS I L E DLE R AVD D GVNTYKAMCR DSRIV P G 413
Cdd:TIGR02343 338 PRFQELSK D K LG K A GLVREISF G TT kd R ML V IEQCKNSKA V - T IFI RG GNKM I I E EAK R SIH D ALCVVRNLIK DSRIV Y G 416
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 414 AA A T EI ELARRLKEFSF K ET G LD QYAI AK FA ESF E MV P KT L S EN A GL NAMEII S S L YAEH - ASG N SKV G I D LEEGICK D V 492
Cdd:TIGR02343 417 GG A A EI SCSLAVSQEAD K YP G VE QYAI RA FA DAL E TI P MA L A EN S GL DPIGTL S T L KSLQ l KEK N PNL G V D CLGYGTN D M 496
490 500 510
....*....|....*....|....*....|...
gi 802585508 493 ATMNIWDLYVT K FFALKY A ADAACTV L RV D QI I 525
Cdd:TIGR02343 497 KEQFVFETLIG K KQQILL A TQLVRMI L KI D DV I 529
chap_CCT_gamma
TIGR02344 T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
26-525
1.27e-76
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: 251.20
E-value: 1.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 26 E A V L K NI D A C K QLST I T RT S LGP NG M N KM VINHLDKLFV TND AAT I VN E LE V Q HPAAK ILVLAGKA Q Q EE I GDG ANLT I S 105
Cdd:TIGR02344 16 K A Q L S NI Q A A K AVAD I I RT C LGP RS M L KM LLDPMGGIVM TND GNA I LR E ID V A HPAAK SMIELSRT Q D EE V GDG TTSV I I 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 106 F AGE L L QN AE ELIRMGL HP SE II SG Y N KA ITK A IEI L D E L veke S ETM DV RNKEHVITRMRAA I AS K QFGQ - EEVL C K L I 184
Cdd:TIGR02344 96 L AGE M L SV AE PFLEQNI HP TV II RA Y R KA LDD A LSV L E E I ---- S IPV DV NDDAAMLKLIQSC I GT K FVSR w SDLM C D L A 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 185 A DA CIQ V CPKNPANFNV D --- NVR V A K LV GG GLH D CTIVR G MVLKT D AVGTI -- KRV E KAKVAVFAGGVDTSAT E TKGTV 259
Cdd:TIGR02344 172 L DA VRT V QRDENGRKEI D ikr YAK V E K IP GG DIE D SCVLK G VMINK D VTHPK mr RYI E NPRIVLLDCPLEYKKG E SQTNI 251
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 260 L I HSADQLENYAKT EE AK V EELIKAVADSGAKVIVSGAA V GEM A L H FCERYKLMVLKISS K FELR R FC R TT G SVAILKLS 339
Cdd:TIGR02344 252 E I TKEEDWNRILQM EE EY V QLMCEDIIAVKPDLVITEKG V SDL A Q H YLLKANITAIRRVR K TDNN R IA R AC G ATIVNRPE 331
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 340 QPNPD D L G Y - ADSIS V EE IG GVRV T VVKNEEGGNS v CT VV LRG STDS IL EDL ER AVD D GVNTYKAMCR D SRI VPG AA ATE 418
Cdd:TIGR02344 332 ELRES D V G T g CGLFE V KK IG DEYF T FITECKDPKA - CT IL LRG ASKD IL NEV ER NLQ D AMAVARNVLL D PKL VPG GG ATE 410
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 419 IELARR L K E F S F K ET G LD Q YAIAKF A ESF E MV P K TL SE N A G L N AMEIISS L Y A E HA SG N SK - V GID L E E G ICK D VATMN I 497
Cdd:TIGR02344 411 MAVSVA L T E K S K K LE G VE Q WPYRAV A DAL E II P R TL AQ N C G A N VIRTLTE L R A K HA QE N NC t W GID G E T G KIV D MKEKG I 490
490 500
....*....|....*....|....*...
gi 802585508 498 W DLYVT K FFAL K Y A ADA AC TV LR V D Q I I 525
Cdd:TIGR02344 491 W EPLAV K LQTY K T A IES AC LL LR I D D I V 518
chap_CCT_eta
TIGR02345 T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
13-528
1.46e-75
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: 248.52
E-value: 1.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 13 M LKEG HKHLS G LDE a VLK NI D AC KQLSTITR T S LGP N GM N K MVINHLD K LFVT ND A ATI VNE L EVQ HPAAK I LV LAG K A Q 92
Cdd:TIGR02345 6 L LKEG TDTSQ G KGQ - LIS NI N AC VAIAEALK T T LGP R GM D K LIVGSNG K ATIS ND G ATI LKL L DIV HPAAK T LV DIA K S Q 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 93 QE E I GDG ANLTISF AGELL QN A EEL I RM G L HP SE II SG Y NK A ITK A I E ILD E L - V EKES E TMDV R nk E HVITRMRA A IA S 171
Cdd:TIGR02345 85 DA E V GDG TTSVTIL AGELL KE A KPF I EE G V HP QL II RC Y RE A LSL A V E KIK E I a V TIDE E KGEQ R -- E LLEKCAAT A LS S 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 172 K QFGQE - E VLC K L I A DA CIQV cpk NPANFNVDNVRVA K LV GG G L H D CTI V R G MVL K T davg T I --------- K RVEKA K V 241
Cdd:TIGR02345 163 K LISHN k E FFS K M I V DA VLSL --- DRDDLDLKLIGIK K VQ GG A L E D SQL V N G VAF K K ---- T F syagfeqqp K KFANP K I 235
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 242 AVFAGGVDTS A TETKGTVLIHSADQLENYAKT E E A KVEELIKAVAD SGA K V IV S GAAV G EM A LHFCERYKLMVLKIS S KF 321
Cdd:TIGR02345 236 LLLNVELELK A EKDNAEIRVEDVEDYQAIVDA E W A IIFRKLEKIVE SGA N V VL S KLPI G DL A TQYFADRDIFCAGRV S AE 315
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 322 E L R R FCRTT G SVAILKL S QPNP D D LG YADSISVEE IG GV R VTVVKNEEGGNS v CT VV LRG STDSIL E DL ER AVD D GVNTY 401
Cdd:TIGR02345 316 D L K R VIKAC G GSIQSTT S DLEA D V LG TCALFEERQ IG SE R YNYFTGCPHAKT - CT II LRG GAEQFI E EA ER SLH D AIMIV 394
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 402 KAMCRDSR IV P G AA A T E I EL ARR L KEF S FKET G LD Q YA I AK FA ESF E MV P KT L S ENAG LNAM EI ISS L YAE HA S G NSKV G 481
Cdd:TIGR02345 395 RRALKNKK IV A G GG A I E M EL SKC L RDY S KTID G KQ Q LI I NA FA KAL E II P RQ L C ENAG FDSI EI LNK L RSR HA K G GKWY G 474
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 802585508 482 I D LEEGICK D VATMNI W DLYVT K FF ALK Y A AD AACT V L R VD QI I MAK 528
Cdd:TIGR02345 475 V D INTEDIG D NFEAFV W EPALV K IN ALK A A FE AACT I L S VD ET I TNP 521
TCP1_epsilon
cd03339 TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
16-525
9.91e-75
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: 246.06
E-value: 9.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 16 E GH K H L S GL d EA VLKN I D A C K QLST I T RTSLGP N GM N K MVINHLDKLF VTND A ATI VNELE V Q H PA AK I LV LAG K A Q QE E 95
Cdd:cd03339 14 E KK K R L K GL - EA HKSH I L A A K SVAN I L RTSLGP R GM D K ILVSPDGEVT VTND G ATI LEKMD V D H QI AK L LV ELS K S Q DD E 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 96 IGDG ANLTISF AG E LL QN AE E L IRM G L HP SE I IS GY NK A ITK A I E I L D E LVE K ES et MDVR NKE HV I TRMRAAIA SK QFG 175
Cdd:cd03339 93 IGDG TTGVVVL AG A LL EQ AE K L LDR G I HP IR I AD GY EQ A CKI A V E H L E E IAD K IE -- FSPD NKE PL I QTAMTSLG SK IVS 170
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 176 - QEEVLCKLIA DA CIQ V CPKNPANF N VDNVR V AKL VGG G L H D CTI V R G M V LKT D AV -- GTI K R V EK AK V A VFAGGVDTSA 252
Cdd:cd03339 171 r CHRQFAEIAV DA VLS V ADLERKDV N FELIK V EGK VGG R L E D TKL V K G I V IDK D FS hp QMP K E V KD AK I A ILTCPFEPPK 250
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 253 TE TK GTVL I H S ADQLENYAKT E EAKVE E LIKA V A D S GA KVIVSGAAVGEM A L H FCERYK L MVLKISSKF E LRRFCRT TG S 332
Cdd:cd03339 251 PK TK HKLD I T S VEDYKKLQEY E QKYFR E MVEQ V K D A GA NLVICQWGFDDE A N H LLLQNG L PAVRWVGGV E IELIAIA TG G 330
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 333 VAILKLSQPN P DD LG Y A DSISVEEI G GVRVTVVKN E EGG NS - VC T VVL RG STDS I L E DLE R AVD D GVNTYKAMC RD S RIV 411
Cdd:cd03339 331 RIVPRFEDLS P EK LG K A GLVREISF G TTKDKMLVI E GCP NS k AV T IFI RG GNKM I I E EAK R SLH D ALCVVRNLI RD N RIV 410
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 412 P G AA A T EI ELARRLKEFSF K ET G LD QYA IAK FA ESF E MV P KT L S EN A GLN AM E II S SLY A EH - ASG N SKV GID - L EE G I c 489
Cdd:cd03339 411 Y G GG A A EI SCSLAVEKAAD K CS G IE QYA MRA FA DAL E SI P LA L A EN S GLN PI E TL S EVK A RQ v KEK N PHL GID c L GR G T - 489
490 500 510
....*....|....*....|....*....|....*.
gi 802585508 490 K D VATMNIWDLYVT K FFALKY A ADAACTV L RV D QI I 525
Cdd:cd03339 490 N D MKEQKVFETLIS K KQQILL A TQVVKMI L KI D DV I 525
TCP1_beta
cd03336 TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
41-529
1.50e-68
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: 229.52
E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 41 ITR T S LGP N GM N K MVI -- NHLDKLF VTND A ATI VNELE V QH PAAK I LV LAG K A Q QE E I GDG ANLTISF A G ELL QN AE E L I 118
Cdd:cd03336 28 LVK T T LGP K GM D K ILQ sv GRSGGVT VTND G ATI LKSIG V DN PAAK V LV DIS K V Q DD E V GDG TTSVTVL A A ELL RE AE K L V 107
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 119 RMGL HP SE II S GY NK A ITK A I E I L DELVEKE S ET m DVRNK E HVITRM R AAIA SK QFG Q E - E VLCK L IA DA CIQV cpkn PA 197
Cdd:cd03336 108 AQKI HP QT II E GY RM A TAA A R E A L LSSAVDH S SD - EEAFR E DLLNIA R TTLS SK ILT Q D k E HFAE L AV DA VLRL ---- KG 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 198 NF N V D NVRVA K LV GG G L H D CTIVR G MV L - K TDA V GTI KR V E K AK VAVFAGGV DT SATETK G T - V LIH S ADQLENYAKT E E 275
Cdd:cd03336 183 SG N L D AIQII K KL GG S L K D SYLDE G FL L d K KIG V NQP KR I E N AK ILIANTPM DT DKIKIF G A k V RVD S TAKVAEIEEA E K 262
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 276 A K VEELIKAVADS G AKVIVSGAAVGEMALHFCERYKL M VLK i SSK F E - LR R FCRT TG SVAILKLSQ P NPDD LG YADS I SV 354
Cdd:cd03336 263 E K MKNKVEKILKH G INCFINRQLIYNYPEQLFADAGI M AIE - HAD F D g VE R LALV TG GEIASTFDH P ELVK LG TCKL I EE 341
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 355 EE IG GVRVT ---- V VKN E eggns V CT V VLRG STDS IL EDL ER AVD D GVNTYKAMCR D S R I V P G AAAT E IEL A RRLK E FSF 430
Cdd:cd03336 342 IM IG EDKLI rfsg V AAG E ----- A CT I VLRG ASQQ IL DEA ER SLH D ALCVLAQTVK D T R V V L G GGCS E MLM A KAVE E LAK 416
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 431 K ET G LDQY AI AK FA ESFEMV P KTLSE NAG LNAM E IISS L Y A E H AS GN SKV G I D LEE G ICK D VATMN I WDLYVT K FFA L KY 510
Cdd:cd03336 417 K TP G KKSL AI EA FA KALRQL P TIIAD NAG YDSA E LVAQ L R A A H YN GN TTA G L D MRK G TVG D MKELG I TESFKV K RQV L LS 496
490
....*....|....*....
gi 802585508 511 A AD AA CTV LRVD Q II MAK P 529
Cdd:cd03336 497 A SE AA EMI LRVD D II KCA P 515
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
10-529
4.24e-67
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 226.06
E-value: 4.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 10 IQAM LK E G HKHLS G l DE A V L KNIDACKQLSTITR T S LGP N GM N K MVI ----- NHLDKLF VTND A ATI VNELEVQH PAAKI 84
Cdd:PTZ00212 7 PPQV LK Q G AQEEK G - ET A R L QSFVGAIAVADLVK T T LGP K GM D K ILQ pmseg PRSGNVT VTND G ATI LKSVWLDN PAAKI 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 85 LV LAG K A Q Q EE I GDG ANLTISF AGELL QN AE E L IRMGL HP SE II S G YNK A ITK A IEI L D E LVEKESETMDVR n KE HVITR 164
Cdd:PTZ00212 86 LV DIS K T Q D EE V GDG TTSVVVL AGELL RE AE K L LDQKI HP QT II E G WRM A LDV A RKA L E E IAFDHGSDEEKF - KE DLLNI 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 165 M R AAIA SK QFGQ E - EVLC KL IA DA CIQV cpkn PANF N V D NVRVA K LV GG G L H D CTIVR G MV L - K TDA VG TI KR V E KA K VA 242
Cdd:PTZ00212 165 A R TTLS SK LLTV E k DHFA KL AV DA VLRL ---- KGSG N L D YIQII K KP GG T L R D SYLED G FI L e K KIG VG QP KR L E NC K IL 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 243 V FAGGV DT SATETK G T - V LIH S ADQLENYAKT E EA K VEELIKAVADS G AK V IVSGAAVGEMALHFCERYKL M VLK i SSK F 321
Cdd:PTZ00212 241 V ANTPM DT DKIKIY G A k V KVD S MEKVAEIEAA E KE K MKNKVDKILAH G CN V FINRQLIYNYPEQLFAEAGI M AIE - HAD F 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 322 E - LR R FCRTT G SVAILKLSQ P NPDD LG YA D S I SVEE IG GVRVT ---- VV K N E eggns V CT V VLRG STDS IL EDL ER AVD D 396
Cdd:PTZ00212 320 D g ME R LAAAL G AEIVSTFDT P EKVK LG HC D L I EEIM IG EDKLI rfsg CA K G E ----- A CT I VLRG ASTH IL DEA ER SLH D 394
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 397 GVNTYKAMCR D S R I V P G AAAT E IEL A RRLK E FSF K ET G LDQY AI AK FA ESFEMV P KTLSE N A G LNAM E II S S L Y AEH AS G 476
Cdd:PTZ00212 395 ALCVLSQTVK D T R V V L G GGCS E MLM A NAVE E LAK K VE G KKSL AI EA FA KALRQI P TIIAD N G G YDSA E LV S K L R AEH YK G 474
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 802585508 477 N SKV GID L E E G ICK D VATMN I WDL Y VT K FFA L KY A AD AA CTV LRVD Q II MAK P 529
Cdd:PTZ00212 475 N KTA GID M E K G TVG D MKELG I TES Y KV K LSQ L CS A TE AA EMI LRVD D II RCA P 527
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
25-535
5.23e-65
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 219.56
E-value: 5.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 25 DE A VLK NI DAC K Q L STITRTS LGP N G M N K M vinh L D K L F ---- V TND AA TI VN E L E VQH P ---- A A KILVLAGKAQQE E I 96
Cdd:COG0459 9 ED A RRA NI RGV K A L ADAVKVT LGP K G R N V M ---- L V K S F gdpt I TND GV TI AK E I E LED P fenm G A QLVKEVASKTND E A 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 97 GDG ANLTISF AG E LL QNAEE L IRM G LH P SE I IS G YN KA IT KA I E I L DEL vekese TMD V RN KE HV itrmr A AI A SKQFGQ 176
Cdd:COG0459 85 GDG TTTATVL AG A LL KEGLK L VAA G AN P TD I KR G ID KA VE KA V E E L KKI ------ AKP V DD KE EL ----- A QV A TISANG 153
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 177 E E VLCK LIA D A CIQ V CPK npanfnv DNVR V AK lv G G GL H - DCTI V R GM VL --------- K TD AVGTIKRV E K A KVAV fag 246
Cdd:COG0459 154 D E EIGE LIA E A MEK V GKD ------- GVIT V EE -- G K GL E t ELEV V E GM QF dkgylspyf V TD PEKMPAEL E N A YILL --- 221
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 247 gvdtsa T ET K gtvl I H S ADQ L enyakteeakv EE L IKA VA D SG AKVIVSGAAVGEM AL HFCERYKLM - VL KISS ------ 319
Cdd:COG0459 222 ------ T DK K ---- I S S IQD L ----------- LP L LEK VA Q SG KPLLIIAEDIDGE AL ATLVVNGIR g VL RVVA vkapgf 280
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 320 ---- K FE L RRFCRT TG SVA I ----- LKL SQPNP DDLG Y A DSI sve E IGGVRV T V V KNEEGGNSV c TVVLRGS T DSILEDL 390
Cdd:COG0459 281 gdrr K AM L EDIAIL TG GRV I sedlg LKL EDVTL DDLG R A KRV --- E VDKDNT T I V EGAGNPKAI - VILVGAA T EVEVKER 356
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 391 E R A V D D GVNTYK A MCRD s R IVPG AA A TEIEL AR R L K E FSF K ET G LD Q YA I AKF A ESF E MVPKTLS ENAGL NAMEIISSL y 470
Cdd:COG0459 357 K R R V E D ALHATR A AVEE - G IVPG GG A ALLRA AR A L R E LAA K LE G DE Q LG I EIV A RAL E APLRQIA ENAGL DGSVVVEKV - 434
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802585508 471 AEHASGN sk V G I D LEE G ICK D VATMNIW D - LY V TK f F AL KY AA DA A CTV L RVDQI I MA KP AGGPNP 535
Cdd:COG0459 435 RAAKDKG -- F G F D AAT G EYV D MLEAGVI D p AK V KR - S AL QN AA SV A GLI L TTEAV I AD KP EKEEAA 497
chap_CCT_zeta
TIGR02347 T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
25-527
1.95e-62
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: 213.83
E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 25 D E A VLK NI D A CKQ L STITR T S LGP N G MN KM VINHLDKLFV T N D AATIV NE LEV QHP A A KILVL A GK AQ QEEI GDG ANL T I 104
Cdd:TIGR02347 15 D A A LMM NI N A ARG L QDVLK T N LGP K G TL KM LVSGAGDIKL T K D GNVLL NE MQI QHP T A SMIAR A AT AQ DDIT GDG TTS T V 94
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 105 SFA GELL QN AE EL I RM G L HP SE I IS G YNK A ITK A IEI LD ELVE K ESETM D vrn K E HVITRM R AAIAS K - QFGQEEV L CKL 183
Cdd:TIGR02347 95 LLI GELL KQ AE RY I LE G V HP RI I TE G FEI A RKE A LQF LD KFKV K KEDEV D --- R E FLLNVA R TSLRT K l PADLADQ L TEI 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 184 IA DA c IQVCP K NPANFNVDN V RVAKLVGGGLH D C T IV RG M VL KTD A -- VGTIK RV EK A KVAVFAGGVDTSA TE TKGTVLI 261
Cdd:TIGR02347 172 VV DA - VLAIK K DGEDIDLFM V EIMEMKHKSAT D T T LI RG L VL DHG A rh PDMPR RV KN A YILTCNVSLEYEK TE VNSGFFY 250
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 262 H SA D Q L E NYA K T E ---- EAK V EEL I ---- K AVAD S GA K -- V IVSGAAVGEMA L HFCERYKL M V L KISSKFELR R FCRTT G 331
Cdd:TIGR02347 251 S SA E Q R E KLV K A E rkfv DDR V KKI I elkk K VCGK S PD K gf V VINQKGIDPPS L DLLAKEGI M A L RRAKRRNME R LTLAC G 330
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 332 SV A ILKLSQPN P DD LG Y A DSISVEE IG GVRV T VVKNEEGGN S v CT VVLR G ST D SILEDLER AV D DG VNTY K AMCR D SRI V 411
Cdd:TIGR02347 331 GE A LNSVEDLT P EC LG W A GLVYETT IG EEKY T FIEECKNPK S - CT ILIK G PN D HTIAQIKD AV R DG LRAV K NAIE D KCV V 409
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 412 PGA A A T EI ELA R R LKE FSFKET G LDQYAIAK FA ESFEMV PKTL S EN A G LN A MEIISS L YA EH AS G NSK VG I DL EE G ICK D 491
Cdd:TIGR02347 410 PGA G A F EI AAY R H LKE YKKSVK G KAKLGVEA FA NALLVI PKTL A EN S G FD A QDTLVK L ED EH DE G GEV VG V DL NT G EPI D 489
490 500 510
....*....|....*....|....*....|....*.
gi 802585508 492 VATMN IWD L Y VT K FFALKY A ADA A CTV L R VD QIIM A 527
Cdd:TIGR02347 490 PEIKG IWD N Y RV K KQLIQS A TVI A SQL L L VD EVMR A 525
chap_CCT_beta
TIGR02341 T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
41-529
9.88e-62
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: 211.64
E-value: 9.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 41 ITRTS LGP N GM N K MVI -- NHLDKLF VTND A ATI VNELE V QH PAAK I LV LAG K A Q QE E I GDG ANLTISF A G ELL QN AE E LI 118
Cdd:TIGR02341 29 LVKST LGP K GM D K ILQ ss SSDASIM VTND G ATI LKSIG V DN PAAK V LV DMS K V Q DD E V GDG TTSVTVL A A ELL RE AE K LI 108
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 119 RMGL HP SE II S GY NK A ITK A IEI L - DEL V EKE S ETMDV R nk EHVITRM R AAIA SK QFG Q - EEVLCK L IA DA CIQV cpkn P 196
Cdd:TIGR02341 109 NQKI HP QT II A GY RE A TKA A RDA L l KSA V DNG S DEVKF R -- QDLMNIA R TTLS SK ILS Q h KDHFAQ L AV DA VLRL ---- K 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 197 ANF N VDNVRVA K LV GG G L H D CTIVR G MV L - K TDA V GTI KR V E K AK VAVFAG G V DT SATETK G T - V LIH S ADQLENYAKT E 274
Cdd:TIGR02341 183 GSG N LEAIQII K KL GG S L A D SYLDE G FL L d K KIG V NQP KR I E N AK ILIANT G M DT DKVKIF G S r V RVD S TAKVAELEHA E 262
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 275 EA K VE E LIKAVADS G AKVIVSGAAVGEMALHFCERYKL M VLKISSKFELR R FCRT TG SVAILKLSQ P NPDD LG YA D S I SV 354
Cdd:TIGR02341 263 KE K MK E KVEKILKH G INCFINRQLIYNYPEQLFADAGV M AIEHADFEGVE R LALV TG GEIVSTFDH P ELVK LG SC D L I EE 342
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 355 EE IG GVRVTVVKNEEG G NS v CT V VLRG S T DS IL EDL ER AVD D GVNTYKAMCRD SR I V P G AAAT E IELARRLKEFSFKET G 434
Cdd:TIGR02341 343 IM IG EDKLLKFSGVKL G EA - CT I VLRG A T QQ IL DEA ER SLH D ALCVLSQTVKE SR T V L G GGCS E MLMSKAVTQEAQRTP G 421
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 435 LDQY A IAK FA ESFEMV P KTLSE NAG LNAM E IISS L Y A E H AS GN SKV G I D LE EG ICK D VATMN I WDL Y VT K FFALKY AA D A 514
Cdd:TIGR02341 422 KEAL A VEA FA RALRQL P TIIAD NAG FDSA E LVAQ L R A A H YN GN TTM G L D MN EG TIA D MRQLG I TES Y KV K RAVVSS AA E A 501
490
....*....|....*
gi 802585508 515 A CTV LRVD Q II M A K P 529
Cdd:TIGR02341 502 A EVI LRVD N II K A A P 516
TCP1_zeta
cd03342 TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
25-527
5.54e-60
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: 205.95
E-value: 5.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 25 DE A VLK NI D A C K Q L STITR T S LGP N G MN KM VINHLDKLFV T N D AATIVN E LEV QHP A A KILVL A GK AQ QEEI GDG ANLTI 104
Cdd:cd03342 11 GQ A LAV NI S A A K G L QDVLK T N LGP K G TL KM LVSGAGDIKL T K D GNVLLS E MQI QHP T A SMIAR A AT AQ DDIT GDG TTSNV 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 105 SFA GELL QN AE EL I RM G L HP SE I IS G YNK A IT KA IEI L DEL ve K ESETM D V r NK E HVITRM R AAIAS K QFGQ - EEV L CKL 183
Cdd:cd03342 91 LLI GELL KQ AE RY I QE G V HP RI I TE G FEL A KN KA LKF L ESF -- K VPVEI D T - DR E LLLSVA R TSLRT K LHAD l ADQ L TEI 167
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 184 IA DA c IQVCP K NPANFNVDN V RVAKLVGGGLH D CTIV RG M VL KTD A -- VGTI KRVE K A KVAV fagg VDT S atetkgtvli 261
Cdd:cd03342 168 VV DA - VLAIY K PDEPIDLHM V EIMQMQHKSDS D TKLI RG L VL DHG A rh PDMP KRVE N A YILT ---- CNV S ---------- 232
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 262 hsadq LE n Y A KTE eakveelikav AD SG -- AK V IVSGAAVGEMA L HFCERYKLMV L KISSKFELR R FCRTT G S VA ILKLS 339
Cdd:cd03342 233 ----- LE - Y E KTE ----------- VN SG ff YS V VINQKGIDPPS L DMLAKEGILA L RRAKRRNME R LTLAC G G VA MNSVD 295
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 340 QPN P DD LGYA DSISVEEI G GVRV T VVKNEEGGN S v CT VVLR G ST D SILEDLER A VD DG VNTY K AMCR D SRI VPGA A A T E I 419
Cdd:cd03342 296 DLS P EC LGYA GLVYERTL G EEKY T FIEGVKNPK S - CT ILIK G PN D HTITQIKD A IR DG LRAV K NAIE D KCV VPGA G A F E V 374
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 420 E L ARR LKEF SFKET G LDQYAIAK FA ESFEMV PKTL S EN A GL NAM E IISS L YA E H A S G NSKV G I DL EE G ICK D VATMN IWD 499
Cdd:cd03342 375 A L YAH LKEF KKSVK G KAKLGVQA FA DALLVI PKTL A EN S GL DVQ E TLVK L QD E Y A E G GQVG G V DL DT G EPM D PESEG IWD 454
490 500
....*....|....*....|....*...
gi 802585508 500 L Y VT K FFA L KY A ADA A CTV L R VD Q II M A 527
Cdd:cd03342 455 N Y SV K RQI L HS A TVI A SQL L L VD E II R A 482
chaperonin_like
cd03333 chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
166-407
1.04e-47
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: 164.95
E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 166 RAAIA SK QFGQEEV L C KL IA DA CIQ V C P K N P a NFNVDNVR V A K LV GG G L H D CTI V R G M V LKTDAVGTI -- KR V E K AK VAV 243
Cdd:cd03333 9 TTSLN SK LSSWDDF L G KL VV DA VLK V G P D N R - MDDLGVIK V E K IP GG S L E D SEL V V G V V FDKGYASPY mp KR L E N AK ILL 87
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 244 FAGGVDT satetkgtvlihsadqlenyakteeakveelikavadsgak V IVSGAAVGEM ALH FCERYKL M VLKISS K FE L 323
Cdd:cd03333 88 LDCPLEY ----------------------------------------- V VIAEKGIDDL ALH YLAKAGI M AVRRVK K ED L 126
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 324 R R FC R T TG SVAILK L SQPN P D DLG Y A DSISVEE IG GVRV T VVKNEE GG n SVC T VV LRG S T DSI L EDLE R AVD D GVNTYK A 403
Cdd:cd03333 127 E R IA R A TG ATIVSS L EDLT P E DLG T A ELVEETK IG EEKL T FIEGCK GG - KAA T IL LRG A T EVE L DEVK R SLH D ALCAVR A 205
....
gi 802585508 404 MCRD 407
Cdd:cd03333 206 AVEE 209
groEL
PRK12849 chaperonin GroEL; Reviewed
26-187
2.44e-04
chaperonin GroEL; Reviewed
Pssm-ID: 237230
Cd Length: 542
Bit Score: 43.64
E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 26 E A VLKNIDA ckq L STITRTS LGP N G M N km V I nh L DK L F ---- V T N D AAT I VN E L E VQH P ---- A A KILVLAGKAQQEEI G 97
Cdd:PRK12849 13 R A LERGVNK --- L ADAVKVT LGP K G R N -- V V -- I DK S F gapt I T K D GVS I AK E I E LED P fenl G A QLVKEVASKTNDVA G 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 98 DG ANLTISF A GE L L Q NAEELIRM G LH P SEIIS G YN KA ITKAI E I L DE L VEKE S ETMDVR nke H V itrmr A A I AS kqf GQE 177
Cdd:PRK12849 86 DG TTTATVL A QA L V Q EGLKNVAA G AN P MDLKR G ID KA VEAVV E E L KA L ARPV S GSEEIA --- Q V ----- A T I SA --- NGD 154
170
....*....|
gi 802585508 178 E VLCK LIA D A 187
Cdd:PRK12849 155 E EIGE LIA E A 164
Fab1_TCP
cd03334 TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
178-395
3.99e-04
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: 42.21
E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 178 EV L CK L IAD A CIQ V C P KNP A NFNV D N --- V RVA K LV GG GLH D CTI V R G M V LKTDA vg TI KR ---- VEKAKVAVFA G GVDT 250
Cdd:cd03334 21 DI L LP L VWK A ASN V K P DVR A GDDM D I rqy V KIK K IP GG SPS D SEV V D G V V FTKNV -- AH KR mpsk IKNPRILLLQ G PLEY 98
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802585508 251 SAT E T K GT vlihsad Q L ENYAKT E EAKVEE L IKAVADSGAK VI VSGAA V GEM A LHFCERYKLMV --- L K I S S kfe L R R FC 327
Cdd:cd03334 99 QRV E N K LL ------- S L DPVILQ E KEYLKN L VSRIVALRPD VI LVEKS V SRI A QDLLLEAGITL vln V K P S V --- L E R IS 168
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802585508 328 R T TG S - VAILKLSQPNPDD LG YAD S IS V E --- E IG G VRV T VV ----- KN E E G gnsv CT VV LRG STDSI L EDLE R A V D 395
Cdd:cd03334 169 R C TG A d IISSMDDLLTSPK LG TCE S FR V R tyv E EH G RSK T LM ffegc PK E L G ---- CT IL LRG GDLEE L KKVK R V V E 241
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
