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TCP-1/cpn60 chaperonin family, putative [Leishmania utingensis]
Protein Classification
T-complex protein 1 subunit theta ( domain architecture ID 10129600 )
T-complex protein 1 subunit theta is a molecular chaperone that assists the folding of proteins upon ATP hydrolysis and is required for correct subcellular localization of pgl-1
List of domain hits
Name
Accession
Description
Interval
E-value
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
19-521
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: 710.91
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 19 VDDP VL K NIEAC R ELS K ITR S S M GPNG LC KMVINHL N KLFVT H DAATILRELEV E HPAAKLLV Q A ANAMQ EE V GDGTN F V 98
Cdd:cd03341 6 LEEA VL R NIEAC K ELS Q ITR T S Y GPNG MN KMVINHL E KLFVT S DAATILRELEV Q HPAAKLLV M A SQMQE EE I GDGTN L V 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 99 V T L C GELL SQ AE S L V RMGLHPSEIIEGY K KA GS K S LE L L DTM V CKSVD D CLR KE Q V MD A IR T S IASKQYG Y EDFL AGV VA 178
Cdd:cd03341 86 V V L A GELL EK AE E L L RMGLHPSEIIEGY E KA LK K A LE I L EEL V VYKIE D LRN KE E V SK A LK T A IASKQYG N EDFL SPL VA 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 179 D ACI N V C P S N VRS FNVDN V RVVK LD G E S ILST K L VRG F V IG R NT E SNL K HL K S AKVAV Y SC AV D V psletkgtalienae 258
Cdd:cd03341 166 E ACI S V L P E N IGN FNVDN I RVVK IL G G S LEDS K V VRG M V FK R EP E GSV K RV K K AKVAV F SC PF D I --------------- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 259 dliqysrkeeeimqeiisnihks G A N L IV SNSTF GDLALH FI N RL G M M AVR I P SKFELRRLC AA VGA RVMT RL D AP SM E D 338
Cdd:cd03341 231 ----------------------- G V N V IV AGGSV GDLALH YC N KY G I M VIK I N SKFELRRLC RT VGA TPLP RL G AP TP E E 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 339 M G A CDSV D V LD IG GKN V TA F V Q DRD DSK LS TIV V RGATQN V LDDVERAIDDGVNVFK A LTKD K R V V A GAGA V E M EL Q K E L 418
Cdd:cd03341 288 I G Y CDSV Y V EE IG DTK V VV F R Q NKE DSK IA TIV L RGATQN I LDDVERAIDDGVNVFK S LTKD G R F V P GAGA T E I EL A K K L 367
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 419 TL Y A E AN PGL D QYA VR K Y A SS FEVV A RTLAE AS G FNG T DMVTQ L E A D H NA G K K YQ G ANLND G -- T T L DA V EAGI VEPHM T 496
Cdd:cd03341 368 KE Y G E KT PGL E QYA IK K F A EA FEVV P RTLAE NA G LDA T EVLSE L Y A A H QK G N K SA G VDIES G de G T K DA K EAGI FDHLA T 447
490 500
....*....|....*....|....*
gi 2752564595 497 K F WAI R LAT DTVL TVL S V N QII V AK 521
Cdd:cd03341 448 K K WAI K LAT EAAV TVL R V D QII M AK 472
Name
Accession
Description
Interval
E-value
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
19-521
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: 710.91
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 19 VDDP VL K NIEAC R ELS K ITR S S M GPNG LC KMVINHL N KLFVT H DAATILRELEV E HPAAKLLV Q A ANAMQ EE V GDGTN F V 98
Cdd:cd03341 6 LEEA VL R NIEAC K ELS Q ITR T S Y GPNG MN KMVINHL E KLFVT S DAATILRELEV Q HPAAKLLV M A SQMQE EE I GDGTN L V 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 99 V T L C GELL SQ AE S L V RMGLHPSEIIEGY K KA GS K S LE L L DTM V CKSVD D CLR KE Q V MD A IR T S IASKQYG Y EDFL AGV VA 178
Cdd:cd03341 86 V V L A GELL EK AE E L L RMGLHPSEIIEGY E KA LK K A LE I L EEL V VYKIE D LRN KE E V SK A LK T A IASKQYG N EDFL SPL VA 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 179 D ACI N V C P S N VRS FNVDN V RVVK LD G E S ILST K L VRG F V IG R NT E SNL K HL K S AKVAV Y SC AV D V psletkgtalienae 258
Cdd:cd03341 166 E ACI S V L P E N IGN FNVDN I RVVK IL G G S LEDS K V VRG M V FK R EP E GSV K RV K K AKVAV F SC PF D I --------------- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 259 dliqysrkeeeimqeiisnihks G A N L IV SNSTF GDLALH FI N RL G M M AVR I P SKFELRRLC AA VGA RVMT RL D AP SM E D 338
Cdd:cd03341 231 ----------------------- G V N V IV AGGSV GDLALH YC N KY G I M VIK I N SKFELRRLC RT VGA TPLP RL G AP TP E E 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 339 M G A CDSV D V LD IG GKN V TA F V Q DRD DSK LS TIV V RGATQN V LDDVERAIDDGVNVFK A LTKD K R V V A GAGA V E M EL Q K E L 418
Cdd:cd03341 288 I G Y CDSV Y V EE IG DTK V VV F R Q NKE DSK IA TIV L RGATQN I LDDVERAIDDGVNVFK S LTKD G R F V P GAGA T E I EL A K K L 367
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 419 TL Y A E AN PGL D QYA VR K Y A SS FEVV A RTLAE AS G FNG T DMVTQ L E A D H NA G K K YQ G ANLND G -- T T L DA V EAGI VEPHM T 496
Cdd:cd03341 368 KE Y G E KT PGL E QYA IK K F A EA FEVV P RTLAE NA G LDA T EVLSE L Y A A H QK G N K SA G VDIES G de G T K DA K EAGI FDHLA T 447
490 500
....*....|....*....|....*
gi 2752564595 497 K F WAI R LAT DTVL TVL S V N QII V AK 521
Cdd:cd03341 448 K K WAI K LAT EAAV TVL R V D QII M AK 472
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
7-532
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: 694.54
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 7 G PQ S M LK D G SAF --- VDDP V L KNIEAC R ELS K ITR S S M GPNG LC KMVINHL N KLFVT H DAATILRELEV E HPAAKLLV Q A 83
Cdd:TIGR02346 1 G IA S L LK E G YRH fsg LEEA V I KNIEAC K ELS Q ITR T S L GPNG MN KMVINHL E KLFVT N DAATILRELEV Q HPAAKLLV M A 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 84 ANAMQE E V GDGTN F V VT L C GELL SQ AE S L V RMGLHPSEII E GY KK A GS K SL E L L DTM V CKS V D D CLR K EQVMD A IRT SI A 163
Cdd:TIGR02346 81 SEMQEN E I GDGTN L V LV L A GELL NK AE E L I RMGLHPSEII K GY EM A LK K AM E I L EEL V VWE V K D LRD K DELIK A LKA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 164 SKQYG Y EDFLA GV VA D AC IN V C P S N VRS FNVDN V RV V K LD G E S ILSTKLVR G F V IG R NT E SNL K HL K S AKVAV Y SC AV D V 243
Cdd:TIGR02346 161 SKQYG N EDFLA QL VA Q AC ST V L P K N PQN FNVDN I RV C K IL G G S LSNSEVLK G M V FN R EA E GSV K SV K N AKVAV F SC PL D T 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 244 PSL ETKGT A LI E NAE D L IQ YS RK EE EIMQEI I SN I HK SG A N L IV SNSTF GD L ALH FI N RLGM M AVR IPSKFELRRLC AA V 323
Cdd:TIGR02346 241 ATT ETKGT V LI H NAE E L LN YS KG EE NQIEAM I KA I AD SG V N V IV TGGSV GD M ALH YL N KYNI M VLK IPSKFELRRLC KT V 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 324 GA RVMT RL D AP SM E DM G AC DSV D V LD IGG KN VT A F V Q DRD DSK L STI VV RG A T Q N V LDD V ERAIDDGVN VF KAL T KD K R V 403
Cdd:TIGR02346 321 GA TPLP RL G AP TP E EI G YV DSV Y V SE IGG DK VT V F K Q ENG DSK I STI IL RG S T D N L LDD I ERAIDDGVN TV KAL V KD G R L 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 404 VA GAGA V E M EL QKE LT L Y A E AN PGLDQYA VR K Y A SS FE VVA RTLAE AS G F N GTDMVTQ L E A D H NA G K K YQ G ANLNDGT -- 481
Cdd:TIGR02346 401 LP GAGA T E I EL ASR LT K Y G E KL PGLDQYA IK K F A EA FE IIP RTLAE NA G L N ANEVIPK L Y A A H KK G N K SK G IDIEAES dg 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2752564595 482 TL DA V EAGI VEPHM TK F WAI R LAT DTVL TVL S V N QII V AK Q AGGPK NRPDQ 532
Cdd:TIGR02346 481 VK DA S EAGI YDMLA TK K WAI K LAT EAAV TVL R V D QII M AK P AGGPK PPQGK 531
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
33-521
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: 542.18
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 33 L SK I T R S S M GP N G LC KM VI N HLNKLF VT H D A ATIL R ELE VE HPAAKLLV Q AA N A MQ EEVGDGT NF VV T L C GELL SQ AE S L 112
Cdd:pfam00118 1 L AD I V R T S L GP K G MD KM LV N SGGDVT VT N D G ATIL K ELE IQ HPAAKLLV E AA K A QD EEVGDGT TT VV V L A GELL EE AE K L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 113 VRM G L HP SE IIEGY K KA GS K S LE L LD TMVCKS V D D CL R k E QVMDAI RTS IA SK QYGY E - DFLA GV V A DA C i NVC P S N VR S 191
Cdd:pfam00118 81 LAA G V HP TT IIEGY E KA LE K A LE I LD SIISIP V E D VD R - E DLLKVA RTS LS SK IISR E s DFLA KL V V DA V - LAI P K N DG S 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 192 F NVD N VR VVK LD G E S ILSTK LV R G F V IGRNTESNL -- K H L KS AKV AVYS C AVDVPSL ETK G T ALIEN AE D L IQYSRK EEE 269
Cdd:pfam00118 159 F DLG N IG VVK IL G G S LEDSE LV D G V V LDKGPLHPD mp K R L EN AKV LLLN C SLEYEKT ETK A T VVLSD AE Q L ERFLKA EEE 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 270 IMQ EI ISN I HK SG A N LI V SNSTFG DLALHF INRL G M MA V R IPS K FE L R RL CA A V GAR VMTR LD APSME D M G ACDS V DVLD 349
Cdd:pfam00118 239 QIL EI VEK I ID SG V N VV V CQKGID DLALHF LAKN G I MA L R RVK K RD L E RL AK A T GAR AVSS LD DLTPD D L G TAGK V EEEK 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 350 IG GKNV T a F VQDRDDS K LS TI VV RGAT QN VLD DV ER A I D D GVN V F K ALTK D K RVV A G A GAVEMEL QKE L TL YA EANP G LD 429
Cdd:pfam00118 319 IG DEKY T - F IEGCKSP K AA TI LL RGAT DH VLD EI ER S I H D ALC V V K NAIE D P RVV P G G GAVEMEL ARA L RE YA KSVS G KE 397
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 430 Q Y A VRKY A SSF EV VAR TLAE AS G FNGTDMVTQ L E A D H NA G K K YQ G ANLND G TTL D AV EAG I V E P HMT K FW A IRL AT DTVL 509
Cdd:pfam00118 398 Q L A IEAF A EAL EV IPK TLAE NA G LDPIEVLAE L R A A H AS G E K HA G IDVET G EII D MK EAG V V D P LKV K RQ A LKS AT EAAS 477
490
....*....|..
gi 2752564595 510 T V L SVNQ II V AK 521
Cdd:pfam00118 478 T I L RIDD II K AK 489
thermosome_alpha
NF041082 thermosome subunit alpha;
26-521
4.11e-120
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 363.44
E-value: 4.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRELSKIT R SSM GP N G LC KM VINH L NKLFV T H D AA TIL R E LEV EHPAAK LL V QA A NAMQE EVGDGT NFV V T L C GEL 105
Cdd:NF041082 22 NI M A AKAVAEAV R TTL GP K G MD KM LVDS L GDVVI T N D GV TIL K E MDI EHPAAK MI V EV A KTQDD EVGDGT TTA V V L A GEL 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L SQ AE S L VRMGL HP SE I I EGY KK A GS K S LE L LD TMVC K - SV DD clr KE QVMDAIR T SIAS K QYG - YE D F LA GV V A DA CIN 183
Cdd:NF041082 102 L KK AE E L LDQDI HP TI I A EGY RL A AE K A LE I LD EIAI K v DP DD --- KE TLKKIAA T AMTG K GAE a AK D K LA DL V V DA VKA 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 184 V C - PSNVRSFNV DN VR V V K LD G E SI LSTK LV R G F VI G -- R NTESNL K HLKS AK V A VYSCAVD V PSL E TKGTAL I ENAED L 260
Cdd:NF041082 179 V A e KDGGYNVDL DN IK V E K KV G G SI EDSE LV E G V VI D ke R VHPGMP K RVEN AK I A LLDAPLE V KKT E IDAKIS I TDPDQ L 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 261 IQYSRK EE EIMQ E IISN I HK SGAN LIVSNSTFG DLA L H FINRL G MM AVR IPS K FELRR L CA A V GAR VM T RL D AP S M ED M G 340
Cdd:NF041082 259 QAFLDQ EE KMLK E MVDK I AD SGAN VVFCQKGID DLA Q H YLAKE G IL AVR RVK K SDMEK L AK A T GAR IV T SI D DL S P ED L G 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 341 ACDS V DVLDI GG KNVT a FV QDRDDS K LS TI VV RG A T QN V L D D VERA ID D GVN V FKALTK D KR VVAG A GA V E M EL QKE L TL 420
Cdd:NF041082 339 YAGL V EERKV GG DKMI - FV EGCKNP K AV TI LL RG G T EH V V D E VERA LE D ALR V VRVVLE D GK VVAG G GA P E V EL ALR L RE 417
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 421 YA EANP G LD Q Y A VRKY A SSF E VVA RTLAE AS G FNGT D MVTQ L EAD H NA G K K YQ G ANLND G TTL D AV E A G I VEP HMT K FW A 500
Cdd:NF041082 418 YA ASVG G RE Q L A IEAF A EAL E IIP RTLAE NA G LDPI D ALVE L RSA H EK G N K TA G LDVYT G KVV D ML E I G V VEP LRV K TQ A 497
490 500
....*....|....*....|.
gi 2752564595 501 I RL AT DTVLTV L SVNQI I V A K 521
Cdd:NF041082 498 I KS AT EAAVMI L RIDDV I A A A 518
thermosome_beta
NF041083 thermosome subunit beta;
26-521
2.59e-117
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 356.18
E-value: 2.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRELSKIT R SSM GP N G LC KM VINH L NKLFV T H D A ATIL R E LE V E HPAAK L LV QA A NAMQE EVGDGT NFV V T L C GEL 105
Cdd:NF041083 22 NI M A AKAVAEAV R TTL GP K G MD KM LVDS L GDIVI T N D G ATIL K E MD V Q HPAAK M LV EV A KTQDD EVGDGT TTA V V L A GEL 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L SQ AE S L VRMGL HP SE I IE GY KK A GS K SL E L LD TMVC K - SV DD clr K E QVMDAIR TS IA SK QYGYE - D F LA GVVAD A CIN 183
Cdd:NF041083 102 L KK AE E L LDQNI HP TI I AN GY RL A AE K AI E I LD EIAE K v DP DD --- R E TLKKIAE TS LT SK GVEEA r D Y LA EIAVK A VKQ 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 184 V CPSNVRSFN VD -- N VRVV K LD G E SI LS T K L VR G F VI GRN - TESNL - K HLKS AK V A VYSCAVD V PSL E TKGTAL I ENAED 259
Cdd:NF041083 179 V AEKRDGKYY VD ld N IQIE K KH G G SI ED T Q L IY G I VI DKE v VHPGM p K RVEN AK I A LLDAPLE V KKT E IDAEIR I TDPDQ 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 260 L IQYSRK EE EIMQ E IISN I HKS GAN LIVSNSTFG DLA L H FINRL G MM AVR IPS K FELRR L CA A V GAR VM T RL D APSM ED M 339
Cdd:NF041083 259 L QKFLDQ EE KMLK E MVDK I KAT GAN VVFCQKGID DLA Q H YLAKA G IL AVR RVK K SDMEK L AK A T GAR IV T NI D DLTP ED L 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 340 G ACDS V DVLDI G GKNVT a FV QDRDDS K LS TI VV RG A T QN V L D DV ERA ID D GVN V FKALTK D KRV VAG A GA V E M EL Q K E L T 419
Cdd:NF041083 339 G YAEL V EERKV G DDKMV - FV EGCKNP K AV TI LI RG G T EH V V D EA ERA LE D ALS V VADAVE D GKI VAG G GA P E V EL A K R L R 417
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 420 L YA EANP G LD Q Y AV RKY A SSF E VVA RTLAE AS G FNGT D MVTQ L EAD H NA GKK YQ G A N LND G TTL D AV E A G IV EP HMT K FW 499
Cdd:NF041083 418 E YA ATVG G RE Q L AV EAF A EAL E IIP RTLAE NA G LDPI D ILVK L RSA H EK GKK WA G I N VFT G EVV D MW E L G VI EP LRV K TQ 497
490 500
....*....|....*....|..
gi 2752564595 500 AI RL AT DTVLTV L SVNQI I V AK 521
Cdd:NF041083 498 AI KS AT EAATMI L RIDDV I A AK 519
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
3-518
6.46e-71
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 236.08
E-value: 6.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 3 F M QTG P QSM LK D G SAFV -- DDPV L KNIEACRELSKITRSSM GP N G LC K MVI ----- NHLNKLF VT H D A ATIL RELEVEH P 75
Cdd:PTZ00212 2 I M ANV P PQV LK Q G AQEE kg ETAR L QSFVGAIAVADLVKTTL GP K G MD K ILQ pmseg PRSGNVT VT N D G ATIL KSVWLDN P 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 76 AAK L LV QAANAMQ EEVGDGT NF VV T L C GELL SQ AE S L VRMGL HP SE IIEG YKK A GSKSLEL L DTM - VCKSV D DCLR KE QV 154
Cdd:PTZ00212 82 AAK I LV DISKTQD EEVGDGT TS VV V L A GELL RE AE K L LDQKI HP QT IIEG WRM A LDVARKA L EEI a FDHGS D EEKF KE DL 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 155 MDAI RT SIA SK QYGY E - D FL A GVVA DA CINV cpsn VR S F N V D NVRVV K LD G ESILSTK L VR GF V ---- IG RNTESN L KHL 229
Cdd:PTZ00212 162 LNIA RT TLS SK LLTV E k D HF A KLAV DA VLRL ---- KG S G N L D YIQII K KP G GTLRDSY L ED GF I lekk IG VGQPKR L ENC 237
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 230 K --------- SA K VAV Y SCA V D V P S L E T kg T A L IE N AE dliqysrke E E I M QEIISN I HKS G A N LIVSNSTFGDLALHFI 300
Cdd:PTZ00212 238 K ilvantpmd TD K IKI Y GAK V K V D S M E K -- V A E IE A AE --------- K E K M KNKVDK I LAH G C N VFINRQLIYNYPEQLF 306
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 301 NRL G M MA VR i PSK F E - LR RL C AA V GA RVMTRL D A P SMEDM G A CD SVDVLD IG GKNVTA F vqdrdd S KLS ----- TIV V RG 374
Cdd:PTZ00212 307 AEA G I MA IE - HAD F D g ME RL A AA L GA EIVSTF D T P EKVKL G H CD LIEEIM IG EDKLIR F ------ S GCA kgeac TIV L RG 379
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 375 A TQNV LD DV ER AID D GVN V FKALT KD K RVV A G A G AV EM ELQKELTLY A EANP G LDQY A VRKY A SSFEVVARTL A EAS G FN 454
Cdd:PTZ00212 380 A STHI LD EA ER SLH D ALC V LSQTV KD T RVV L G G G CS EM LMANAVEEL A KKVE G KKSL A IEAF A KALRQIPTII A DNG G YD 459
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2752564595 455 GTDM V TQ L E A D H NA G K K YQ G ANLND GT TL D AV E A GI V E PHMT K FWAIRL AT DTVLTV L S V NQ II 518
Cdd:PTZ00212 460 SAEL V SK L R A E H YK G N K TA G IDMEK GT VG D MK E L GI T E SYKV K LSQLCS AT EAAEMI L R V DD II 523
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
25-528
6.65e-67
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 224.57
E-value: 6.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 25 K NI EACRE L SKITRSSM GP N G LCK M VINHLNKLFV T H D AA TI LR E L E V E H P ---- A A K L LVQA A NAMQE E V GDGT NFVVT 100
Cdd:COG0459 14 A NI RGVKA L ADAVKVTL GP K G RNV M LVKSFGDPTI T N D GV TI AK E I E L E D P fenm G A Q L VKEV A SKTND E A GDGT TTATV 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 101 L C G E LL SQAES LV RM G LH P SE I IE G YK KA GS K SL E L L DTMV c K S VDD clr KE QVMDAIRT S IASK qygye DFLAGVV A D A 180
Cdd:COG0459 94 L A G A LL KEGLK LV AA G AN P TD I KR G ID KA VE K AV E E L KKIA - K P VDD --- KE ELAQVATI S ANGD ----- EEIGELI A E A 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 181 cinvcpsnvrsfn VDN V --- R V VKLD -- GESILSTKL V R G FVIGR --------- NT E SNLKH L KS A KVAVYSCA vdvpsl 246
Cdd:COG0459 165 ------------- MEK V gkd G V ITVE eg KGLETELEV V E G MQFDK gylspyfvt DP E KMPAE L EN A YILLTDKK ------ 225
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 247 etkgtal I ENAE DL I qysrkeeeimq EIISNIHK SG AN L IVSNSTFGDL AL HFINRL G MM ------ AV RI P S ----- K FE 315
Cdd:COG0459 226 ------- I SSIQ DL L ----------- PLLEKVAQ SG KP L LIIAEDIDGE AL ATLVVN G IR gvlrvv AV KA P G fgdrr K AM 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 316 L RRLCAAV G A RV MTR ----- L DAPSME D M G ACDS V D V ldig G K NV T AF V QDRDDS K LST I V V RG AT QNVLDDVE R AID D G 390
Cdd:COG0459 288 L EDIAILT G G RV ISE dlglk L EDVTLD D L G RAKR V E V ---- D K DN T TI V EGAGNP K AIV I L V GA AT EVEVKERK R RVE D A 363
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 391 VNVFK A LTKDK r V V A G A GA VEMELQKE L TLY A EANP G LD Q YAVRKY A SSF E VVA R TL AE AS G FN G TDM V TQLE A dhn A GK 470
Cdd:COG0459 364 LHATR A AVEEG - I V P G G GA ALLRAARA L REL A AKLE G DE Q LGIEIV A RAL E APL R QI AE NA G LD G SVV V EKVR A --- A KD 439
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2752564595 471 K YQ G ANLND G TTL D AV EAG IVE P HMT K FW A IRL A TDTVLTV L SVNQI I VA K QAGGPKN 528
Cdd:COG0459 440 K GF G FDAAT G EYV D ML EAG VID P AKV K RS A LQN A ASVAGLI L TTEAV I AD K PEKEEAA 497
Name
Accession
Description
Interval
E-value
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
19-521
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: 710.91
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 19 VDDP VL K NIEAC R ELS K ITR S S M GPNG LC KMVINHL N KLFVT H DAATILRELEV E HPAAKLLV Q A ANAMQ EE V GDGTN F V 98
Cdd:cd03341 6 LEEA VL R NIEAC K ELS Q ITR T S Y GPNG MN KMVINHL E KLFVT S DAATILRELEV Q HPAAKLLV M A SQMQE EE I GDGTN L V 85
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 99 V T L C GELL SQ AE S L V RMGLHPSEIIEGY K KA GS K S LE L L DTM V CKSVD D CLR KE Q V MD A IR T S IASKQYG Y EDFL AGV VA 178
Cdd:cd03341 86 V V L A GELL EK AE E L L RMGLHPSEIIEGY E KA LK K A LE I L EEL V VYKIE D LRN KE E V SK A LK T A IASKQYG N EDFL SPL VA 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 179 D ACI N V C P S N VRS FNVDN V RVVK LD G E S ILST K L VRG F V IG R NT E SNL K HL K S AKVAV Y SC AV D V psletkgtalienae 258
Cdd:cd03341 166 E ACI S V L P E N IGN FNVDN I RVVK IL G G S LEDS K V VRG M V FK R EP E GSV K RV K K AKVAV F SC PF D I --------------- 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 259 dliqysrkeeeimqeiisnihks G A N L IV SNSTF GDLALH FI N RL G M M AVR I P SKFELRRLC AA VGA RVMT RL D AP SM E D 338
Cdd:cd03341 231 ----------------------- G V N V IV AGGSV GDLALH YC N KY G I M VIK I N SKFELRRLC RT VGA TPLP RL G AP TP E E 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 339 M G A CDSV D V LD IG GKN V TA F V Q DRD DSK LS TIV V RGATQN V LDDVERAIDDGVNVFK A LTKD K R V V A GAGA V E M EL Q K E L 418
Cdd:cd03341 288 I G Y CDSV Y V EE IG DTK V VV F R Q NKE DSK IA TIV L RGATQN I LDDVERAIDDGVNVFK S LTKD G R F V P GAGA T E I EL A K K L 367
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 419 TL Y A E AN PGL D QYA VR K Y A SS FEVV A RTLAE AS G FNG T DMVTQ L E A D H NA G K K YQ G ANLND G -- T T L DA V EAGI VEPHM T 496
Cdd:cd03341 368 KE Y G E KT PGL E QYA IK K F A EA FEVV P RTLAE NA G LDA T EVLSE L Y A A H QK G N K SA G VDIES G de G T K DA K EAGI FDHLA T 447
490 500
....*....|....*....|....*
gi 2752564595 497 K F WAI R LAT DTVL TVL S V N QII V AK 521
Cdd:cd03341 448 K K WAI K LAT EAAV TVL R V D QII M AK 472
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
7-532
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: 694.54
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 7 G PQ S M LK D G SAF --- VDDP V L KNIEAC R ELS K ITR S S M GPNG LC KMVINHL N KLFVT H DAATILRELEV E HPAAKLLV Q A 83
Cdd:TIGR02346 1 G IA S L LK E G YRH fsg LEEA V I KNIEAC K ELS Q ITR T S L GPNG MN KMVINHL E KLFVT N DAATILRELEV Q HPAAKLLV M A 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 84 ANAMQE E V GDGTN F V VT L C GELL SQ AE S L V RMGLHPSEII E GY KK A GS K SL E L L DTM V CKS V D D CLR K EQVMD A IRT SI A 163
Cdd:TIGR02346 81 SEMQEN E I GDGTN L V LV L A GELL NK AE E L I RMGLHPSEII K GY EM A LK K AM E I L EEL V VWE V K D LRD K DELIK A LKA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 164 SKQYG Y EDFLA GV VA D AC IN V C P S N VRS FNVDN V RV V K LD G E S ILSTKLVR G F V IG R NT E SNL K HL K S AKVAV Y SC AV D V 243
Cdd:TIGR02346 161 SKQYG N EDFLA QL VA Q AC ST V L P K N PQN FNVDN I RV C K IL G G S LSNSEVLK G M V FN R EA E GSV K SV K N AKVAV F SC PL D T 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 244 PSL ETKGT A LI E NAE D L IQ YS RK EE EIMQEI I SN I HK SG A N L IV SNSTF GD L ALH FI N RLGM M AVR IPSKFELRRLC AA V 323
Cdd:TIGR02346 241 ATT ETKGT V LI H NAE E L LN YS KG EE NQIEAM I KA I AD SG V N V IV TGGSV GD M ALH YL N KYNI M VLK IPSKFELRRLC KT V 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 324 GA RVMT RL D AP SM E DM G AC DSV D V LD IGG KN VT A F V Q DRD DSK L STI VV RG A T Q N V LDD V ERAIDDGVN VF KAL T KD K R V 403
Cdd:TIGR02346 321 GA TPLP RL G AP TP E EI G YV DSV Y V SE IGG DK VT V F K Q ENG DSK I STI IL RG S T D N L LDD I ERAIDDGVN TV KAL V KD G R L 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 404 VA GAGA V E M EL QKE LT L Y A E AN PGLDQYA VR K Y A SS FE VVA RTLAE AS G F N GTDMVTQ L E A D H NA G K K YQ G ANLNDGT -- 481
Cdd:TIGR02346 401 LP GAGA T E I EL ASR LT K Y G E KL PGLDQYA IK K F A EA FE IIP RTLAE NA G L N ANEVIPK L Y A A H KK G N K SK G IDIEAES dg 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2752564595 482 TL DA V EAGI VEPHM TK F WAI R LAT DTVL TVL S V N QII V AK Q AGGPK NRPDQ 532
Cdd:TIGR02346 481 VK DA S EAGI YDMLA TK K WAI K LAT EAAV TVL R V D QII M AK P AGGPK PPQGK 531
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
33-521
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: 542.18
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 33 L SK I T R S S M GP N G LC KM VI N HLNKLF VT H D A ATIL R ELE VE HPAAKLLV Q AA N A MQ EEVGDGT NF VV T L C GELL SQ AE S L 112
Cdd:pfam00118 1 L AD I V R T S L GP K G MD KM LV N SGGDVT VT N D G ATIL K ELE IQ HPAAKLLV E AA K A QD EEVGDGT TT VV V L A GELL EE AE K L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 113 VRM G L HP SE IIEGY K KA GS K S LE L LD TMVCKS V D D CL R k E QVMDAI RTS IA SK QYGY E - DFLA GV V A DA C i NVC P S N VR S 191
Cdd:pfam00118 81 LAA G V HP TT IIEGY E KA LE K A LE I LD SIISIP V E D VD R - E DLLKVA RTS LS SK IISR E s DFLA KL V V DA V - LAI P K N DG S 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 192 F NVD N VR VVK LD G E S ILSTK LV R G F V IGRNTESNL -- K H L KS AKV AVYS C AVDVPSL ETK G T ALIEN AE D L IQYSRK EEE 269
Cdd:pfam00118 159 F DLG N IG VVK IL G G S LEDSE LV D G V V LDKGPLHPD mp K R L EN AKV LLLN C SLEYEKT ETK A T VVLSD AE Q L ERFLKA EEE 238
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 270 IMQ EI ISN I HK SG A N LI V SNSTFG DLALHF INRL G M MA V R IPS K FE L R RL CA A V GAR VMTR LD APSME D M G ACDS V DVLD 349
Cdd:pfam00118 239 QIL EI VEK I ID SG V N VV V CQKGID DLALHF LAKN G I MA L R RVK K RD L E RL AK A T GAR AVSS LD DLTPD D L G TAGK V EEEK 318
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 350 IG GKNV T a F VQDRDDS K LS TI VV RGAT QN VLD DV ER A I D D GVN V F K ALTK D K RVV A G A GAVEMEL QKE L TL YA EANP G LD 429
Cdd:pfam00118 319 IG DEKY T - F IEGCKSP K AA TI LL RGAT DH VLD EI ER S I H D ALC V V K NAIE D P RVV P G G GAVEMEL ARA L RE YA KSVS G KE 397
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 430 Q Y A VRKY A SSF EV VAR TLAE AS G FNGTDMVTQ L E A D H NA G K K YQ G ANLND G TTL D AV EAG I V E P HMT K FW A IRL AT DTVL 509
Cdd:pfam00118 398 Q L A IEAF A EAL EV IPK TLAE NA G LDPIEVLAE L R A A H AS G E K HA G IDVET G EII D MK EAG V V D P LKV K RQ A LKS AT EAAS 477
490
....*....|..
gi 2752564595 510 T V L SVNQ II V AK 521
Cdd:pfam00118 478 T I L RIDD II K AK 489
chaperonin_type_I_II
cd00309 chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
20-519
1.75e-165
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: 477.31
E-value: 1.75e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 20 DDPV L K NI E A CRE L SKITRSSM GP N G LC KM VINH L NKLFV T H D A ATIL R E L EVEHPAAKLLV QA A NAMQE EVGDGT NF VV 99
Cdd:cd00309 7 EEAR L S NI N A AKA L ADAVKTTL GP K G MD KM LVDS L GDPTI T N D G ATIL K E I EVEHPAAKLLV EV A KSQDD EVGDGT TT VV 86
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 100 T L C GELL SQ AE S L VRM G L HP S EII E GY K KA GS K S LE L L DTMVCKS vd D CLRK E QVMDAIR TS IA SK Q - Y G YE DFL AGV V A 178
Cdd:cd00309 87 V L A GELL KE AE K L LAA G I HP T EII R GY E KA VE K A LE I L KEIAVPI -- D VEDR E ELLKVAT TS LN SK L v S G GD DFL GEL V V 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 179 DA CIN V CPS N v RSFNVDNV RV V K LD G E S ILSTK LV R G F V IGRNTE S N -- L K H L KS AK VAVYS C AVD vpsletkgtalien 256
Cdd:cd00309 165 DA VLK V GKE N - GDVDLGVI RV E K KK G G S LEDSE LV V G M V FDKGYL S P ym P K R L EN AK ILLLD C KLE -------------- 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 257 aedliqysrkeeeimqeiisnihksga NLIVSNSTFG D L ALH FINR LG M MAVR IPS K FE L R R LCA A V GA RVMT RL DAPSM 336
Cdd:cd00309 230 --------------------------- YVVIAEKGID D E ALH YLAK LG I MAVR RVR K ED L E R IAK A T GA TIVS RL EDLTP 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 337 ED M G ACDS V DVLD IG GKNV T AFVQDRD d S K LS TI VV RGAT QNV LD DV ER AID D GVNVFK A LTK D KRV V A G A GA V E M EL Q K 416
Cdd:cd00309 283 ED L G TAGL V EETK IG DEKY T FIEGCKG - G K VA TI LL RGAT EVE LD EA ER SLH D ALCAVR A AVE D GGI V P G G GA A E I EL S K 361
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 417 E L TLY A EAN PG LD Q YAVRKY A SSF EV VA RTLAE AS G FNGTDM VT Q L E A D H NA G KKYQ G ANLND G TTL D AV EAGI VE P HMT 496
Cdd:cd00309 362 A L EEL A KTL PG KE Q LGIEAF A DAL EV IP RTLAE NA G LDPIEV VT K L R A K H AE G GGNA G GDVET G EIV D MK EAGI ID P LKV 441
490 500
....*....|....*....|...
gi 2752564595 497 K FW A IRL AT DTVLTV L SVNQ IIV 519
Cdd:cd00309 442 K RQ A LKS AT EAASLI L TIDD IIV 464
thermosome_alpha
NF041082 thermosome subunit alpha;
26-521
4.11e-120
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 363.44
E-value: 4.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRELSKIT R SSM GP N G LC KM VINH L NKLFV T H D AA TIL R E LEV EHPAAK LL V QA A NAMQE EVGDGT NFV V T L C GEL 105
Cdd:NF041082 22 NI M A AKAVAEAV R TTL GP K G MD KM LVDS L GDVVI T N D GV TIL K E MDI EHPAAK MI V EV A KTQDD EVGDGT TTA V V L A GEL 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L SQ AE S L VRMGL HP SE I I EGY KK A GS K S LE L LD TMVC K - SV DD clr KE QVMDAIR T SIAS K QYG - YE D F LA GV V A DA CIN 183
Cdd:NF041082 102 L KK AE E L LDQDI HP TI I A EGY RL A AE K A LE I LD EIAI K v DP DD --- KE TLKKIAA T AMTG K GAE a AK D K LA DL V V DA VKA 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 184 V C - PSNVRSFNV DN VR V V K LD G E SI LSTK LV R G F VI G -- R NTESNL K HLKS AK V A VYSCAVD V PSL E TKGTAL I ENAED L 260
Cdd:NF041082 179 V A e KDGGYNVDL DN IK V E K KV G G SI EDSE LV E G V VI D ke R VHPGMP K RVEN AK I A LLDAPLE V KKT E IDAKIS I TDPDQ L 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 261 IQYSRK EE EIMQ E IISN I HK SGAN LIVSNSTFG DLA L H FINRL G MM AVR IPS K FELRR L CA A V GAR VM T RL D AP S M ED M G 340
Cdd:NF041082 259 QAFLDQ EE KMLK E MVDK I AD SGAN VVFCQKGID DLA Q H YLAKE G IL AVR RVK K SDMEK L AK A T GAR IV T SI D DL S P ED L G 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 341 ACDS V DVLDI GG KNVT a FV QDRDDS K LS TI VV RG A T QN V L D D VERA ID D GVN V FKALTK D KR VVAG A GA V E M EL QKE L TL 420
Cdd:NF041082 339 YAGL V EERKV GG DKMI - FV EGCKNP K AV TI LL RG G T EH V V D E VERA LE D ALR V VRVVLE D GK VVAG G GA P E V EL ALR L RE 417
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 421 YA EANP G LD Q Y A VRKY A SSF E VVA RTLAE AS G FNGT D MVTQ L EAD H NA G K K YQ G ANLND G TTL D AV E A G I VEP HMT K FW A 500
Cdd:NF041082 418 YA ASVG G RE Q L A IEAF A EAL E IIP RTLAE NA G LDPI D ALVE L RSA H EK G N K TA G LDVYT G KVV D ML E I G V VEP LRV K TQ A 497
490 500
....*....|....*....|.
gi 2752564595 501 I RL AT DTVLTV L SVNQI I V A K 521
Cdd:NF041082 498 I KS AT EAAVMI L RIDDV I A A A 518
cpn60
cd03343 cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
26-521
9.01e-120
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: 362.35
E-value: 9.01e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRELSKIT R SSM GP N G LC KM VINH L NKLFV T H D A ATIL R E LEV EHPAAK L LV QA A NAMQ EEVGDGT NFV V T L C GEL 105
Cdd:cd03343 20 NI A A AKAVAEAV R TTL GP K G MD KM LVDS L GDVTI T N D G ATIL K E MDI EHPAAK M LV EV A KTQD EEVGDGT TTA V V L A GEL 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L SQ AE S L VRMGL HP SE IIEGY KK A GS K S LELLD TMVC K - SV DD clr K EQVMDAIR TS IAS K QYG - YE D F LA GV V A DA CIN 183
Cdd:cd03343 100 L EK AE D L LDQNI HP TV IIEGY RL A AE K A LELLD EIAI K v DP DD --- K DTLRKIAK TS LTG K GAE a AK D K LA DL V V DA VLQ 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 184 V CPSNVRSFN VD -- N VRVV K LD G E S ILS T K L V RG F VI GRN - TESNL - K HLKS AK V A VYSCAVD V PSL E TKGTAL I ENAED 259
Cdd:cd03343 177 V AEKRDGKYV VD ld N IKIE K KT G G S VDD T E L I RG I VI DKE v VHPGM p K RVEN AK I A LLDAPLE V KKT E IDAKIR I TSPDQ 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 260 L IQYSRK EE EIMQ E IISN I HKS GAN LIVSNSTFG DLA L H FINRL G MM AVR IPS K FELRR L CA A V GA RVM T RL D APSM ED M 339
Cdd:cd03343 257 L QAFLEQ EE AMLK E MVDK I ADT GAN VVFCQKGID DLA Q H YLAKA G IL AVR RVK K SDMEK L AR A T GA KIV T NI D DLTP ED L 336
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 340 G ACDS V DVLDI G GKNVT a FV QDRDDS K LS TI VV RG A T QN V L D DV ERA ID D GVN V FKALTK D KR VVAG A GAVE M EL Q K E L T 419
Cdd:cd03343 337 G EAEL V EERKV G DDKMV - FV EGCKNP K AV TI LL RG G T EH V V D EL ERA LE D ALR V VADALE D GK VVAG G GAVE I EL A K R L R 415
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 420 L YA EANP G LD Q Y AV RKY A SSF E VVA RTLAE AS G FNGT D MVTQ L E A D H NA G K K YQ G ANLND G TTL D AV E A G IV EP HMT K FW 499
Cdd:cd03343 416 E YA RSVG G RE Q L AV EAF A DAL E EIP RTLAE NA G LDPI D TLVE L R A A H EK G N K NA G LDVYT G EVV D ML E K G VI EP LRV K KQ 495
490 500
....*....|....*....|..
gi 2752564595 500 AI RL AT DTVLTV L SVNQI I V AK 521
Cdd:cd03343 496 AI KS AT EAATMI L RIDDV I A AK 517
thermosome_beta
NF041083 thermosome subunit beta;
26-521
2.59e-117
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 356.18
E-value: 2.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRELSKIT R SSM GP N G LC KM VINH L NKLFV T H D A ATIL R E LE V E HPAAK L LV QA A NAMQE EVGDGT NFV V T L C GEL 105
Cdd:NF041083 22 NI M A AKAVAEAV R TTL GP K G MD KM LVDS L GDIVI T N D G ATIL K E MD V Q HPAAK M LV EV A KTQDD EVGDGT TTA V V L A GEL 101
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L SQ AE S L VRMGL HP SE I IE GY KK A GS K SL E L LD TMVC K - SV DD clr K E QVMDAIR TS IA SK QYGYE - D F LA GVVAD A CIN 183
Cdd:NF041083 102 L KK AE E L LDQNI HP TI I AN GY RL A AE K AI E I LD EIAE K v DP DD --- R E TLKKIAE TS LT SK GVEEA r D Y LA EIAVK A VKQ 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 184 V CPSNVRSFN VD -- N VRVV K LD G E SI LS T K L VR G F VI GRN - TESNL - K HLKS AK V A VYSCAVD V PSL E TKGTAL I ENAED 259
Cdd:NF041083 179 V AEKRDGKYY VD ld N IQIE K KH G G SI ED T Q L IY G I VI DKE v VHPGM p K RVEN AK I A LLDAPLE V KKT E IDAEIR I TDPDQ 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 260 L IQYSRK EE EIMQ E IISN I HKS GAN LIVSNSTFG DLA L H FINRL G MM AVR IPS K FELRR L CA A V GAR VM T RL D APSM ED M 339
Cdd:NF041083 259 L QKFLDQ EE KMLK E MVDK I KAT GAN VVFCQKGID DLA Q H YLAKA G IL AVR RVK K SDMEK L AK A T GAR IV T NI D DLTP ED L 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 340 G ACDS V DVLDI G GKNVT a FV QDRDDS K LS TI VV RG A T QN V L D DV ERA ID D GVN V FKALTK D KRV VAG A GA V E M EL Q K E L T 419
Cdd:NF041083 339 G YAEL V EERKV G DDKMV - FV EGCKNP K AV TI LI RG G T EH V V D EA ERA LE D ALS V VADAVE D GKI VAG G GA P E V EL A K R L R 417
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 420 L YA EANP G LD Q Y AV RKY A SSF E VVA RTLAE AS G FNGT D MVTQ L EAD H NA GKK YQ G A N LND G TTL D AV E A G IV EP HMT K FW 499
Cdd:NF041083 418 E YA ATVG G RE Q L AV EAF A EAL E IIP RTLAE NA G LDPI D ILVK L RSA H EK GKK WA G I N VFT G EVV D MW E L G VI EP LRV K TQ 497
490 500
....*....|....*....|..
gi 2752564595 500 AI RL AT DTVLTV L SVNQI I V AK 521
Cdd:NF041083 498 AI KS AT EAATMI L RIDDV I A AK 519
thermosome_arch
TIGR02339 thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
8-520
3.99e-113
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: 345.52
E-value: 3.99e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 8 P QSM LK D G SAFV -- D D PVLK NI E A CRELSKITR S SM GP N G LC KM VINH L NKLFV T H D A ATIL R E LEV EHPAAK L LV QA A N 85
Cdd:TIGR02339 1 P VFI LK E G TQRT sg R D AQRN NI A A AKAVAEAVK S TL GP R G MD KM LVDS L GDVTI T N D G ATIL K E MDI EHPAAK M LV EV A K 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 86 AMQ EEVGDGT NFV V T L C GELL SQ AE S L VRMGL HP SE IIEGY K KA GS K S LE LL D TMVC K - S VD D clr KEQVMDAIR TS IA S 164
Cdd:TIGR02339 81 TQD EEVGDGT TTA V V L A GELL EK AE D L LEQDI HP TV IIEGY R KA AE K A LE II D EIAT K i S PE D --- RDLLKKIAY TS LT S 157
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 165 K QYG -- YE D F LA GV V AD A CIN V C --- PSNVRSFNV DN VRV VK LD G E SI LS T K LV R G F V IGRNT -- ESNL K HLKS AK V A VY 237
Cdd:TIGR02339 158 K ASA ev AK D K LA DL V VE A VKQ V A elr GDGKYYVDL DN IKI VK KK G G SI ED T E LV E G I V VDKEV vh PGMP K RVEN AK I A LL 237
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 238 SCAVD V PSL E TKGTAL I ENAEDLIQYSRK EE EIMQ E IISN I HKS GAN LIVSNSTFG D L A L H FINRL G MM AVR IPS K FELR 317
Cdd:TIGR02339 238 DAPLE V EKT E IDAKIR I TDPDQIKKFLDQ EE AMLK E MVDK I ASA GAN VVICQKGID D V A Q H YLAKA G IL AVR RVK K SDIE 317
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 318 R L CA A V GAR VMTRL D APSME D M G ACDS V DVLDI G GKNVT a FV QDRDDS K LS TI VV RG A T QN V L D DV ER A I D D GVN V FKAL 397
Cdd:TIGR02339 318 K L AR A T GAR IVSSI D EITES D L G YAEL V EERKV G EDKMV - FV EGCKNP K AV TI LL RG G T EH V V D EL ER S I Q D ALH V VANA 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 398 TK D KRV VAG A GAVE M EL QKE L TL YA EANP G LD Q Y A VRKY A SSF E VVA R T LAE AS G FNGT D MVTQ L E A D H NA G K K YQ G A N L 477
Cdd:TIGR02339 397 LE D GKI VAG G GAVE I EL ALR L RS YA RSVG G RE Q L A IEAF A DAL E EIP R I LAE NA G LDPI D ALVD L R A K H EK G N K NA G I N V 476
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2752564595 478 ND G TTL D AV E A G IV EP HMT K FW AI RL AT DTVLTV L SVNQI I V A 520
Cdd:TIGR02339 477 FT G EIE D ML E L G VI EP LRV K EQ AI KS AT EAATMI L RIDDV I A A 519
TCP1_delta
cd03338 TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
24-520
8.44e-92
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: 290.34
E-value: 8.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 24 L K NI E A CRELSKIT R S S M GP N G LC KM VINHLNKLFV T H D A ATIL RELE V E HPAAK L LV QAAN A MQE E V GDGT NF VV T L C G 103
Cdd:cd03338 11 L S NI Q A AKAVADAI R T S L GP R G MD KM IQTGKGEVII T N D G ATIL KQMS V L HPAAK M LV ELSK A QDI E A GDGT TS VV V L A G 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 104 E LLS QA ESL VRM G L HP SE I I E GYKK A GS K SL E L LD T M VCK - SVD D clr K E QVMDAIR TS IA SK --- QY G ye DF LA GVVA D 179
Cdd:cd03338 91 A LLS AC ESL LKK G I HP TV I S E SFQI A AK K AV E I LD S M SIP v DLN D --- R E SLIKSAT TS LN SK vvs QY S -- SL LA PIAV D 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 180 A CIN V CPSNVRS f NVD -- NV R V VK LD G ES I LS T K LV R G F V IGR --- NTESNLKHLKS AK VAVYSCAVDV P SLETKGTALI 254
Cdd:cd03338 166 A VLK V IDPATAT - NVD lk DI R I VK KL G GT I ED T E LV D G L V FTQ kas KKAGGPTRIEK AK IGLIQFCLSP P KTDMDNNIVV 244
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 255 E -- NAE D L I Q ys R K E EEIMQEIISN I H KSG A N - L IVSN S ---- TFG DLALHF INR L GM M A V RIPSKF E LRRL C AAV G ARV 327
Cdd:cd03338 245 N dy AQM D R I L -- R E E RKYILNMCKK I K KSG C N v L LIQK S ilrd AVS DLALHF LAK L KI M V V KDIERE E IEFI C KTI G CKP 322
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 328 MTRL D APSMEDM G AC D S V DVLDI G GKNVTAFVQDRDDS K LS TI V VRG ATQN VLD DV ER AID D GVN V FKA L T K DKRVVA G A 407
Cdd:cd03338 323 VASI D HFTEDKL G SA D L V EEVSL G DGKIVKITGVKNPG K TV TI L VRG SNKL VLD EA ER SLH D ALC V IRC L V K KRALIP G G 402
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 408 GA V E M E LQKE L TLY A EANP G LD QY A VR KY A SSF EV VAR TLAE AS G F N GTDM VT Q L EAD H NA G K K YQ G A N LND G TTLDAV E 487
Cdd:cd03338 403 GA P E I E IALQ L SEW A RTLT G VE QY C VR AF A DAL EV IPY TLAE NA G L N PISI VT E L RNR H AQ G E K NA G I N VRK G AITNIL E 482
490 500 510
....*....|....*....|....*....|...
gi 2752564595 488 AGI V E P HMTKFW AI R LAT D TV LTV L SVNQ I IV A 520
Cdd:cd03338 483 ENV V Q P LLVSTS AI T LAT E TV RMI L KIDD I VL A 515
chap_CCT_alpha
TIGR02340 T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
20-518
1.53e-89
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: 285.08
E-value: 1.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 20 D D PVLK N IE A CRELSK I TRS S M GP N GL C KM VINHLNKLFV T H D A ATIL RE LEVEHPAAK L LV QA A NAMQE EVGDGT NF VV 99
Cdd:TIGR02340 11 Q D VRTQ N VT A AMAIAN I VKT S L GP V GL D KM LVDDIGDVTI T N D G ATIL KL LEVEHPAAK I LV EL A QLQDR EVGDGT TS VV 90
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 100 TLCG ELL SQ A ES LV RMGL HP SEI I E GY KK A GSKSLELLDTMVCK SVD D c L RK E QVMDAIR TS IA SK QY G YE - DF LAGV V A 178
Cdd:TIGR02340 91 IIAA ELL KR A DE LV KNKI HP TSV I S GY RL A CKEAVKYIKENLSV SVD E - L GR E ALINVAK TS MS SK II G LD s DF FSNI V V 169
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 179 DA CIN V CPS N VR --- SFNVDNVRVV K LD G E S ILSTK LV R G FVIGRNTE S NL -- K HL K S AK V A VYSCAVDVPSLETKGTAL 253
Cdd:TIGR02340 170 DA VLA V KTT N EN get KYPIKAINIL K AH G K S ARESM LV K G YALNCTVA S QQ mp K RI K N AK I A CLDFNLQKAKMALGVQIV 249
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 254 IENA E D L I Q YSRK E EE I MQ E I I SN I HKS GAN LIVSNSTFG D LA L HFINRL G M M A VR IPS K FE L R R LCA A V GA RVMTR L DA 333
Cdd:TIGR02340 250 VDDP E K L E Q IRQR E AD I TK E R I KK I LDA GAN VVLTTGGID D MC L KYFVEA G A M G VR RCK K ED L K R IAK A T GA TLVST L AD 329
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 334 PSM E D ------ M G AC D S V DVLD I GGKNVT a FVQDRDDS K LST I VV RGA TQNV LD DV ER AID D GVN V F K ALTKDKR VV A G A 407
Cdd:TIGR02340 330 LEG E E tfeasy L G FA D E V VQER I ADDECI - LIKGTKKR K SAS I IL RGA NDFM LD EM ER SLH D ALC V V K RTLESNS VV P G G 408
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 408 GAVE ME L QKE L TLY A EANPGLD Q Y A VRKY A SSFEVVAR TLA EASGFNG T DM V TQ L E A D H N A -------- GK K YQ G AN L ND 479
Cdd:TIGR02340 409 GAVE AA L SIY L ENF A TTLGSRE Q L A IAEF A RALLIIPK TLA VNAAKDS T EL V AK L R A Y H A A aqlkpekk HL K WY G LD L VN 488
490 500 510
....*....|....*....|....*....|....*....
gi 2752564595 480 G TTL D AV EAG IV EP HMT K FWAIRL AT DTVL T V L SVNQI I 518
Cdd:TIGR02340 489 G KIR D NK EAG VL EP TVS K VKSLKF AT EAAI T I L RIDDL I 527
TCP1_alpha
cd03335 TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
25-518
7.16e-89
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: 283.02
E-value: 7.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 25 K N IE A CRELSK I TR SS M GP N GL C KM VINHLNKLFV T H D A ATIL RE LEVEHPAAK L LV QA A NAMQE EVGDGT NF VV TLCG E 104
Cdd:cd03335 12 Q N VT A AMAIAN I VK SS L GP V GL D KM LVDDIGDVTI T N D G ATIL KL LEVEHPAAK I LV EL A QLQDK EVGDGT TS VV IIAA E 91
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 105 LL SQ A ES LV RMGL HP SE II E GY KK A GSKSLELLDTMVCK SVD D c L R KE QVMDAIR TS IA SK QY G YE - DF L A GV V A DA CIN 183
Cdd:cd03335 92 LL KR A NE LV KQKI HP TT II S GY RL A CKEAVKYIKEHLSI SVD N - L G KE SLINVAK TS MS SK II G AD s DF F A NM V V DA ILA 170
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 184 V CPS N VRS --- FNVDN V RVV K LD G E S ILSTK LV R G FVI -- G R NTESNLKHL K S AK V A V ysca V D VPSLE TK --- G TA - LI 254
Cdd:cd03335 171 V KTT N EKG ktk YPIKA V NIL K AH G K S AKESY LV N G YAL nc T R ASQGMPTRV K N AK I A C ---- L D FNLQK TK mkl G VQ v VV 246
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 255 ENA E D L IQYSRK E EE I MQ E I I SN I HKS GAN LIVSNSTFG D LA L HFINRL G M MAVR IPS K FE LRR LCA A V GA RVMTR L --- 331
Cdd:cd03335 247 TDP E K L EKIRQR E SD I TK E R I KK I LAA GAN VVLTTGGID D MC L KYFVEA G A MAVR RVK K ED LRR IAK A T GA TLVST L anl 326
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 332 ----- DA PS M ed M G ACDS V DVLD IG GKNVT a FVQDRDDSKLST I VV RGA TQNV LD DV ER AID D GVN V F K ALTKDKR VV A G 406
Cdd:cd03335 327 egeet FD PS Y -- L G EAEE V VQER IG DDELI - LIKGTKKRSSAS I IL RGA NDFM LD EM ER SLH D ALC V V K RTLESNS VV P G 403
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 407 A GAVE ME L QKE L TLY A EANPGLD Q Y A VRKY A SSFE V VAR TLA EASGFNG T DM V TQ L E A D H N A GK -------- K YQ G AN L N 478
Cdd:cd03335 404 G GAVE TA L SIY L ENF A TTLGSRE Q L A IAEF A EALL V IPK TLA VNAAKDA T EL V AK L R A Y H A A AQ vkpdkkhl K WY G LD L I 483
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2752564595 479 D G TTL D AV EAG IV EP HMT K FWAIRL AT DTVL T V L SVNQI I 518
Cdd:cd03335 484 N G KVR D NL EAG VL EP TVS K IKSLKF AT EAAI T I L RIDDL I 523
chap_CCT_delta
TIGR02342 T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
26-521
1.21e-88
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: 282.06
E-value: 1.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRELSKIT R S S M GP N G LC KM VINHLNKLFV T H D A ATIL RELE V E HPAAK L LV QAAN A MQE E V GDGT NF VV T L C G E L 105
Cdd:TIGR02342 14 NI V A AKAVADAI R T S L GP K G MD KM IQDGKGEVII T N D G ATIL KQMA V L HPAAK M LV ELSK A QDI E A GDGT TS VV I L A G A L 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L SQA E S L VRM G L HP SE I I E GYKK A GSKSLEL LD T M v CKS VD DCL R k EQ VMDAIR TS IA SK QYG - Y EDF LA GVVA DA CIN V 184
Cdd:TIGR02342 94 L GAC E R L LNK G I HP TI I S E SFQS A ADEAIKI LD E M - SIP VD LSD R - EQ LLKSAT TS LS SK VVS q Y SSL LA PLAV DA VLK V 171
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 185 C - P S N VRSFNVDNVR VVK LD G ES I LS T K L VR G F V IGRNTE --- SNLKHLKS AK VAVYSCAVDV P SLETKGTALIENAEDL 260
Cdd:TIGR02342 172 I d P E N AKNVDLNDIK VVK KL G GT I DD T E L IE G L V FTQKAS ksa GGPTRIEK AK IGLIQFQISP P KTDMENQIIVNDYAQM 251
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 261 IQYSRK E EEIMQE I ISN I H K S G A N LI ----- VSNSTFG DLALHF INRLGM M A V RIPSKF E LRRL C AAV G ARVMTRL D APS 335
Cdd:TIGR02342 252 DRVLKE E RAYILN I VKK I K K T G C N VL liqks ILRDAVN DLALHF LAKMKI M V V KDIERE E IEFI C KTI G CKPIASI D HFT 331
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 336 MEDM G ACDS V DVL D IG G KNVTAFVQDRDDS K LS T I VVRG ATQN V L D DV ER AID D GVN V FKA L T K DKRVV AG A GA V E M E LQ 415
Cdd:TIGR02342 332 ADKL G SAEL V EEV D SD G GKIIKITGIQNAG K TV T V VVRG SNKL V I D EA ER SLH D ALC V IRC L V K KRGLI AG G GA P E I E IA 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 416 KE L TL YA EANP G LDQ Y A VR KY A SSF EV VAR TLAE AS G F N GTDM VT Q L EAD H NA G K K YQ G ANLND G TTLDAV E AGIVE P HM 495
Cdd:TIGR02342 412 RR L SK YA RTMK G VES Y C VR AF A DAL EV IPY TLAE NA G L N PIKV VT E L RNR H AN G E K TA G ISVRK G GITNML E EHVLQ P LL 491
490 500
....*....|....*....|....*.
gi 2752564595 496 TKFW AI R LA TD TV LTV L SVNQ I IVAK 521
Cdd:TIGR02342 492 VTTS AI T LA SE TV RSI L KIDD I VFTR 517
chap_CCT_epsi
TIGR02343 T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
21-518
1.37e-86
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: 277.07
E-value: 1.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 21 DPVLK NI E A CRELSK I T R S S M GP N G LC KM V I NHLNKLF VT H D A ATIL RELE V EHPA AKL L V QAANAMQE E V GDGT NF VV T 100
Cdd:TIGR02343 27 EAKKS NI A A AKSVAS I L R T S L GP K G MD KM L I SPDGDIT VT N D G ATIL SQMD V DNQI AKL M V ELSKSQDD E I GDGT TG VV V 106
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 101 L C G E LL S QAE S L VRM G L HP SE I IE G YKK A GSKSL E L L DTMVCKSVD D CLRK E QVMD A IR TS IA SK - QYGYEDFL A GVVA D 179
Cdd:TIGR02343 107 L A G A LL E QAE E L LDK G I HP IK I AD G FEE A ARIAV E H L EEISDEISA D NNNR E PLIQ A AK TS LG SK i VSKCHRRF A EIAV D 186
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 180 A CI NV CPSNV R SFNV D NVR V VKLD G E S ILS TKL VR G FV I GRNTE -- SNL K HLKS AK V A VYS C AVDV P SLE TK GTAL I ENA 257
Cdd:TIGR02343 187 A VL NV ADMER R DVDF D LIK V EGKV G G S LED TKL IK G II I DKDFS hp QMP K EVED AK I A ILT C PFEP P KPK TK HKLD I SSV 266
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 258 E DLIQYSRK E EEIMQ E I I SN I H KSGANL IVSNST F G D L A L H FINRLGMM AVR IPSKF EL RRLCA A V G A R VMT R LDAP S ME 337
Cdd:TIGR02343 267 E EYKKLQKY E QQKFK E M I DD I K KSGANL VICQWG F D D E A N H LLLQNDLP AVR WVGGQ EL ELIAI A T G G R IVP R FQEL S KD 346
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 338 DM G ACDS V DVLDI G - G K NVTAFVQDRDD SK LS TI VV RG ATQNVLDDVE R A I D D GVN V FKA L T KD K R V V A G A GA V E MELQK 416
Cdd:TIGR02343 347 KL G KAGL V REISF G t T K DRMLVIEQCKN SK AV TI FI RG GNKMIIEEAK R S I H D ALC V VRN L I KD S R I V Y G G GA A E ISCSL 426
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 417 ELTLY A EAN PG LD QYA V R KY A SSF E VVART LAE A SG FNGTDMVTQ L EADHNAG K KYQ - G ANLNDGT T L D AV E AGIV E PHM 495
Cdd:TIGR02343 427 AVSQE A DKY PG VE QYA I R AF A DAL E TIPMA LAE N SG LDPIGTLST L KSLQLKE K NPN l G VDCLGYG T N D MK E QFVF E TLI 506
490 500
....*....|....*....|...
gi 2752564595 496 T K FWA I R LAT DT V LTV L SVNQI I 518
Cdd:TIGR02343 507 G K KQQ I L LAT QL V RMI L KIDDV I 529
TCP1_epsilon
cd03339 TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
21-519
6.80e-86
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: 275.33
E-value: 6.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 21 DPVLKN I E A CRELSK I T R S S M GP N G LC K MVINHLNKLF VT H D A ATIL RELE V E H PA AKLLV QAANAMQE E V GDGT NF VV T 100
Cdd:cd03339 23 EAHKSH I L A AKSVAN I L R T S L GP R G MD K ILVSPDGEVT VT N D G ATIL EKMD V D H QI AKLLV ELSKSQDD E I GDGT TG VV V 102
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 101 L C G E LL S QAE S L VRM G L HP SE I IE GY KK A GSKSL E L L DTMVC K SVDDCLR KE QVMDAIR TS IA SK - QYGYEDFL A GVVA D 179
Cdd:cd03339 103 L A G A LL E QAE K L LDR G I HP IR I AD GY EQ A CKIAV E H L EEIAD K IEFSPDN KE PLIQTAM TS LG SK i VSRCHRQF A EIAV D 182
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 180 A CIN V CPSNVRSF N VDNVR V VKLD G ESILS TKLV R G F VI grnt ESNLK H ------ L K S AK V A VYS C AVDV P SLE TK GTAL 253
Cdd:cd03339 183 A VLS V ADLERKDV N FELIK V EGKV G GRLED TKLV K G I VI ---- DKDFS H pqmpke V K D AK I A ILT C PFEP P KPK TK HKLD 258
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 254 I ENA ED LIQYSRK E EEIMQ E IISNIHKS GANL IVSNST F G D L A L H FINRL G MM AVR IPSKF E LRRLCA A V G A R VMT R LDA 333
Cdd:cd03339 259 I TSV ED YKKLQEY E QKYFR E MVEQVKDA GANL VICQWG F D D E A N H LLLQN G LP AVR WVGGV E IELIAI A T G G R IVP R FED 338
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 334 P S M E DM G ACDS V DVLDI G G - K NVTAFVQDRDD SK LS TI VV RG ATQNVLDDVE R AID D GVN V FKA L TK D K R V V A G A GA V E M 412
Cdd:cd03339 339 L S P E KL G KAGL V REISF G T t K DKMLVIEGCPN SK AV TI FI RG GNKMIIEEAK R SLH D ALC V VRN L IR D N R I V Y G G GA A E I 418
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 413 ELQKELTLY A EANP G LD QYA V R KY A SSF E VVART LAE A SG F N GTDMVTQLE A DHNAG K K - YQ G ANLNDGT T L D AV E AGIV 491
Cdd:cd03339 419 SCSLAVEKA A DKCS G IE QYA M R AF A DAL E SIPLA LAE N SG L N PIETLSEVK A RQVKE K N p HL G IDCLGRG T N D MK E QKVF 498
490 500
....*....|....*....|....*...
gi 2752564595 492 E PHMT K FWA I R LAT DT V LTV L SVNQI IV 519
Cdd:cd03339 499 E TLIS K KQQ I L LAT QV V KMI L KIDDV IV 526
TCP1_eta
cd03340 TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
23-523
2.30e-81
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: 263.38
E-value: 2.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 23 VLK NI E AC RELSKIT R SSM GP N G LC K MVINHLN K LFVTH D A ATIL RE L EVE HPAAK L LV QA A NAMQE EVGDGT NF VV T L C 102
Cdd:cd03340 18 LIS NI N AC QAIADAV R TTL GP R G MD K LIVDGRG K VTISN D G ATIL KL L DIV HPAAK T LV DI A KSQDA EVGDGT TS VV V L A 97
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 103 GE L L SQ A ESLVRM G L HP SE II E GY K KA GSKSL E LLDTM --- VC K SVDDCL R k E QVMDAIR T SIA SK QY - GYED F L A GV V A 178
Cdd:cd03340 98 GE F L KE A KPFIED G V HP QI II R GY R KA LQLAI E KIKEI avn ID K EDKEEQ R - E LLEKCAA T ALN SK LI a SEKE F F A KM V V 176
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 179 DA cinvcpsn V R S F ---- NV D NVRVV K LD G E S ILSTK LV R G f V IGRN T ------ E SNL K HL K SA K V avys CAVD V p S LE T 248
Cdd:cd03340 177 DA -------- V L S L dddl DL D MIGIK K VP G G S LEDSQ LV N G - V AFKK T fsyagf E QQP K KF K NP K I ---- LLLN V - E LE L 242
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 249 K gt A LIE NAE ---- D LIQ Y SR --- K E EE I MQEIISN I H KSGAN LIV S NSTF GDLA LHFINRLGMM - A V R I P SK f E L R R LC 320
Cdd:cd03340 243 K -- A EKD NAE vrve D PEE Y QA ivd A E WK I IYDKLEK I V KSGAN VVL S KLPI GDLA TQYFADRDIF c A G R V P EE - D L K R VA 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 321 A A V G ARVM T RLDAPSMEDM G A C DSVDVLDI GG KNVTA F v QDRDDS K LS TI VV RG ATQNVLDDV ER AID D GVNVFKALT K D 400
Cdd:cd03340 320 Q A T G GSIQ T TVSNITDDVL G T C GLFEERQV GG ERYNI F - TGCPKA K TC TI IL RG GAEQFIEEA ER SLH D AIMIVRRAI K N 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 401 KR VVAG A GA V EMEL Q K E L TL Y AEANP G LD Q YAVRKY A SSF E VVA R T L AEAS GF NG TD MVTQ L EAD H - NA G K K YQ G ANL N D 479
Cdd:cd03340 399 DS VVAG G GA I EMEL S K Y L RD Y SRTIA G KQ Q LVINAF A KAL E IIP R Q L CDNA GF DA TD ILNK L RQK H a QG G G K WY G VDI N N 478
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2752564595 480 GTTL D AV EA GIV EP HMT K FW A IRL AT DTVLTV LSV NQI I VAKQA 523
Cdd:cd03340 479 EGIA D NF EA FVW EP SLV K IN A LTA AT EAACLI LSV DET I KNPKS 522
chap_CCT_eta
TIGR02345 T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
23-523
5.47e-81
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: 262.39
E-value: 5.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 23 VLK NI E AC RELSKITRSSM GP N G LC K MVINHLN K LFVTH D A ATIL RE L EVE HPAAK L LV QA A NAMQE EVGDGT NF V VT L C 102
Cdd:TIGR02345 20 LIS NI N AC VAIAEALKTTL GP R G MD K LIVGSNG K ATISN D G ATIL KL L DIV HPAAK T LV DI A KSQDA EVGDGT TS V TI L A 99
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 103 GELL SQ A ESLVRM G L HP SE II EG Y KK A G S KSL E LLDTMVCKSVDDCLRKEQVMDAI - R T SIA SK QYG - YED F LAGVVA DA 180
Cdd:TIGR02345 100 GELL KE A KPFIEE G V HP QL II RC Y RE A L S LAV E KIKEIAVTIDEEKGEQRELLEKC a A T ALS SK LIS h NKE F FSKMIV DA 179
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 181 CINVCPSNVRS fnv DNVRVV K LD G ESILSTK LV R G FVIGRN ----- T E SNL K HLKSA K VAVYSCAVDVPSLETKGTALI E 255
Cdd:TIGR02345 180 VLSLDRDDLDL --- KLIGIK K VQ G GALEDSQ LV N G VAFKKT fsyag F E QQP K KFANP K ILLLNVELELKAEKDNAEIRV E 256
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 256 NA ED LIQYSRK E EE I MQEIISN I HK SGAN LIV S NSTF GDLA LHFINRLGMM - A V R IPSK f E L R R LCA A V G ARVMTRLDAP 334
Cdd:TIGR02345 257 DV ED YQAIVDA E WA I IFRKLEK I VE SGAN VVL S KLPI GDLA TQYFADRDIF c A G R VSAE - D L K R VIK A C G GSIQSTTSDL 335
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 335 SMEDM G A C DSVDVLD IG GKNVTA F v QDRDDS K LS TI VV RG ATQNVLDDV ER AID D GVNVFKALT K D K RV VAG A GA V EMEL 414
Cdd:TIGR02345 336 EADVL G T C ALFEERQ IG SERYNY F - TGCPHA K TC TI IL RG GAEQFIEEA ER SLH D AIMIVRRAL K N K KI VAG G GA I EMEL 414
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 415 Q K E L TL Y AEANP G LD Q YAVRKY A SSF E VVA R T L A E AS GF NGTDMVTQ L EAD H NA G K K YQ G ANL N DGTTL D AV EA GIV EP H 494
Cdd:TIGR02345 415 S K C L RD Y SKTID G KQ Q LIINAF A KAL E IIP R Q L C E NA GF DSIEILNK L RSR H AK G G K WY G VDI N TEDIG D NF EA FVW EP A 494
490 500
....*....|....*....|....*....
gi 2752564595 495 MT K FW A IRL A TDTVL T V LSV NQI I VAKQA 523
Cdd:TIGR02345 495 LV K IN A LKA A FEAAC T I LSV DET I TNPKS 523
TCP1_gamma
cd03337 TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
24-518
6.75e-76
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: 247.59
E-value: 6.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 24 L K NI E A CRELSKIT R SSM GP NGLC KM VINHLNKLFV T H D AAT ILRE LE V E HPAAK LLVQAANAMQ EEVGDGT NF V VT L C G 103
Cdd:cd03337 19 L G NI Q A AKTVADVI R TCL GP RAML KM LLDPMGGIVL T N D GNA ILRE ID V A HPAAK SMIELSRTQD EEVGDGT TS V II L A G 98
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 104 E L L SQ AE SLVRM G L HP SE II EG Y K KA GSKS L EL L DTM vck S VD - D CLRKE Q VMDA I RTS I AS K QYG - YE D FLAGVVA DA C 181
Cdd:cd03337 99 E I L AV AE PFLER G I HP TV II KA Y R KA LEDA L KI L EEI --- S IP v D VNDRA Q MLKI I KSC I GT K FVS r WS D LMCNLAL DA V 175
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 182 IN V - CPS N V R SFNV D --- NVR V V K LD G ES I LSTKLVR G FVIGRN - T ESNLK - HLKSAKVAVYS C avdvp S LE tkgtalie 255
Cdd:cd03337 176 KT V a VEE N G R KKEI D ikr YAK V E K IP G GE I EDSRVLD G VMLNKD v T HPKMR r RIENPRIVLLD C ----- P LE -------- 242
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 256 naedliq Y srkeeeimqeiisnihksgan L IVSNSTFG DLA L H FINRL G MM A V R IPS K FELR R LCA A V GA RVMT R LDAPS 335
Cdd:cd03337 243 ------- Y --------------------- L VITEKGVS DLA Q H YLVKA G IT A L R RVR K TDNN R IAR A C GA TIVN R PEELT 294
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 336 ME D M G ACDSVDVLDIG G KNVTA F VQDRD D S K LS TI VV RGA TQN VL DD VER AID D GVN V FKALTKDKRV V A G A GA V EM ELQ 415
Cdd:cd03337 295 ES D V G TGAGLFEVKKI G DEYFT F ITECK D P K AC TI LL RGA SKD VL NE VER NLQ D AMA V ARNIILNPKL V P G G GA T EM AVS 374
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 416 KE L TLY A EANP G LD Q YAVRKY AS SF EV VA RTLA EAS G F N GTDMV T Q L E A D H - NAGKKYQ G ANLND G TTL D AV E A GI VE P H 494
Cdd:cd03337 375 HA L SEK A KSIE G VE Q WPYKAV AS AL EV IP RTLA QNC G A N VIRTL T E L R A K H a QGENSTW G IDGET G DIV D MK E L GI WD P L 454
490 500
....*....|....*....|....
gi 2752564595 495 MT K FWAIRL A TDTVLTV L SVNQ I I 518
Cdd:cd03337 455 AV K AQTYKT A IEAACML L RIDD I V 478
chap_CCT_gamma
TIGR02344 T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
24-518
7.79e-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: 248.88
E-value: 7.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 24 L K NI E A CRELSK I T R SSM GP NGLC KM VINHLNKLFV T H D AAT ILRE LE V E HPAAK LLVQAANAMQ EEVGDGT NF V VT L C G 103
Cdd:TIGR02344 19 L S NI Q A AKAVAD I I R TCL GP RSML KM LLDPMGGIVM T N D GNA ILRE ID V A HPAAK SMIELSRTQD EEVGDGT TS V II L A G 98
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 104 E L LS Q AE SLVRMGL HP SE II EG Y K KA GSKS L EL L DTM - VCKS V D D clr KEQVMDA I RTS I AS K QYG - YE D FLAGVVA DA C 181
Cdd:TIGR02344 99 E M LS V AE PFLEQNI HP TV II RA Y R KA LDDA L SV L EEI s IPVD V N D --- DAAMLKL I QSC I GT K FVS r WS D LMCDLAL DA V 175
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 182 IN V CPSNVRSFNV D --- NVR V V K LD G ES I LSTKLVR G FV I GRN - T ESNL - KHLKSAKVAVYS C AVDVPSL E TKGTAL I EN 256
Cdd:TIGR02344 176 RT V QRDENGRKEI D ikr YAK V E K IP G GD I EDSCVLK G VM I NKD v T HPKM r RYIENPRIVLLD C PLEYKKG E SQTNIE I TK 255
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 257 A ED LIQYSRK EEE IM Q EIISN I HKSGAN L IVSNSTFG DLA L H FINRLGMM A V R IPS K FELR R LCA A V GA RVMT R LDAPSM 336
Cdd:TIGR02344 256 E ED WNRILQM EEE YV Q LMCED I IAVKPD L VITEKGVS DLA Q H YLLKANIT A I R RVR K TDNN R IAR A C GA TIVN R PEELRE 335
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 337 E D M G A - C DSVD V LD IG GKNV T a F VQDRD D S K LS TI VV RGA TQNV L DD VER AID D GVN V FKALTK D KRV V A G A GA V EM ELQ 415
Cdd:TIGR02344 336 S D V G T g C GLFE V KK IG DEYF T - F ITECK D P K AC TI LL RGA SKDI L NE VER NLQ D AMA V ARNVLL D PKL V P G G GA T EM AVS 414
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 416 KE LT LYAEANP G LD Q YAV R KY A SSF E VVA RTLA EAS G F N GTDMV T Q L E A D H NAG - KKYQ G ANLND G TTL D AV E A GI V EP H 494
Cdd:TIGR02344 415 VA LT EKSKKLE G VE Q WPY R AV A DAL E IIP RTLA QNC G A N VIRTL T E L R A K H AQE n NCTW G IDGET G KIV D MK E K GI W EP L 494
490 500
....*....|....*....|....
gi 2752564595 495 MT K FWAIRL A TDTVLTV L SVNQ I I 518
Cdd:TIGR02344 495 AV K LQTYKT A IESACLL L RIDD I V 518
TCP1_beta
cd03336 TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
36-521
5.78e-73
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: 241.08
E-value: 5.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 36 ITRSSM GP N G LC K MVI -- NHLNKLF VT H D A ATIL RELE V EH PAAK L LV QAANAMQE EVGDGT NF V VT L CG ELL SQ AE S LV 113
Cdd:cd03336 28 LVKTTL GP K G MD K ILQ sv GRSGGVT VT N D G ATIL KSIG V DN PAAK V LV DISKVQDD EVGDGT TS V TV L AA ELL RE AE K LV 107
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 114 RMGL HP SE IIEGY KK A GSKSL E - LL DTM V CK S V D DCLRK E QVMDAI RT SIA SK QYGYE - DFL A GVVA DA CINVCP S N vrs 191
Cdd:cd03336 108 AQKI HP QT IIEGY RM A TAAAR E a LL SSA V DH S S D EEAFR E DLLNIA RT TLS SK ILTQD k EHF A ELAV DA VLRLKG S G --- 184
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 192 f N V D NVRVV K LD G E S ILSTK L VR GF V ---- IG R N TE snl K HLKS AK VAVYSCAV D VPSLETK G TAL - IENAEDLIQYSRK 266
Cdd:cd03336 185 - N L D AIQII K KL G G S LKDSY L DE GF L ldkk IG V N QP --- K RIEN AK ILIANTPM D TDKIKIF G AKV r VDSTAKVAEIEEA 260
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 267 E E E I M QEIISN I H K S G A N LIVSNSTFGDLALHFINRL G M MA VRIPS k F E - LR RL CAAV G ARVMTRL D A P SMEDM G A C DSV 345
Cdd:cd03336 261 E K E K M KNKVEK I L K H G I N CFINRQLIYNYPEQLFADA G I MA IEHAD - F D g VE RL ALVT G GEIASTF D H P ELVKL G T C KLI 339
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 346 DVLD IG GKNVTA F VQDRD d SKLS TIV V RGA T Q NV LD DV ER AID D GVN V FKALT KD K RVV A G A G AV EM ELQ K ELTLY A EAN 425
Cdd:cd03336 340 EEIM IG EDKLIR F SGVAA - GEAC TIV L RGA S Q QI LD EA ER SLH D ALC V LAQTV KD T RVV L G G G CS EM LMA K AVEEL A KKT 418
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 426 PG LDQY A VRKY A SSFEVVARTL A EAS G FNGTDM V T QL E A D H NA G KKYQ G ANLND GT TL D AV E A GI V E PHMT K FWAIRL A T 505
Cdd:cd03336 419 PG KKSL A IEAF A KALRQLPTII A DNA G YDSAEL V A QL R A A H YN G NTTA G LDMRK GT VG D MK E L GI T E SFKV K RQVLLS A S 498
490
....*....|....*.
gi 2752564595 506 DTVLTV L S V NQ II VAK 521
Cdd:cd03336 499 EAAEMI L R V DD II KCA 514
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
3-518
6.46e-71
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 236.08
E-value: 6.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 3 F M QTG P QSM LK D G SAFV -- DDPV L KNIEACRELSKITRSSM GP N G LC K MVI ----- NHLNKLF VT H D A ATIL RELEVEH P 75
Cdd:PTZ00212 2 I M ANV P PQV LK Q G AQEE kg ETAR L QSFVGAIAVADLVKTTL GP K G MD K ILQ pmseg PRSGNVT VT N D G ATIL KSVWLDN P 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 76 AAK L LV QAANAMQ EEVGDGT NF VV T L C GELL SQ AE S L VRMGL HP SE IIEG YKK A GSKSLEL L DTM - VCKSV D DCLR KE QV 154
Cdd:PTZ00212 82 AAK I LV DISKTQD EEVGDGT TS VV V L A GELL RE AE K L LDQKI HP QT IIEG WRM A LDVARKA L EEI a FDHGS D EEKF KE DL 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 155 MDAI RT SIA SK QYGY E - D FL A GVVA DA CINV cpsn VR S F N V D NVRVV K LD G ESILSTK L VR GF V ---- IG RNTESN L KHL 229
Cdd:PTZ00212 162 LNIA RT TLS SK LLTV E k D HF A KLAV DA VLRL ---- KG S G N L D YIQII K KP G GTLRDSY L ED GF I lekk IG VGQPKR L ENC 237
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 230 K --------- SA K VAV Y SCA V D V P S L E T kg T A L IE N AE dliqysrke E E I M QEIISN I HKS G A N LIVSNSTFGDLALHFI 300
Cdd:PTZ00212 238 K ilvantpmd TD K IKI Y GAK V K V D S M E K -- V A E IE A AE --------- K E K M KNKVDK I LAH G C N VFINRQLIYNYPEQLF 306
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 301 NRL G M MA VR i PSK F E - LR RL C AA V GA RVMTRL D A P SMEDM G A CD SVDVLD IG GKNVTA F vqdrdd S KLS ----- TIV V RG 374
Cdd:PTZ00212 307 AEA G I MA IE - HAD F D g ME RL A AA L GA EIVSTF D T P EKVKL G H CD LIEEIM IG EDKLIR F ------ S GCA kgeac TIV L RG 379
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 375 A TQNV LD DV ER AID D GVN V FKALT KD K RVV A G A G AV EM ELQKELTLY A EANP G LDQY A VRKY A SSFEVVARTL A EAS G FN 454
Cdd:PTZ00212 380 A STHI LD EA ER SLH D ALC V LSQTV KD T RVV L G G G CS EM LMANAVEEL A KKVE G KKSL A IEAF A KALRQIPTII A DNG G YD 459
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2752564595 455 GTDM V TQ L E A D H NA G K K YQ G ANLND GT TL D AV E A GI V E PHMT K FWAIRL AT DTVLTV L S V NQ II 518
Cdd:PTZ00212 460 SAEL V SK L R A E H YK G N K TA G IDMEK GT VG D MK E L GI T E SYKV K LSQLCS AT EAAEMI L R V DD II 523
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
25-528
6.65e-67
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 224.57
E-value: 6.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 25 K NI EACRE L SKITRSSM GP N G LCK M VINHLNKLFV T H D AA TI LR E L E V E H P ---- A A K L LVQA A NAMQE E V GDGT NFVVT 100
Cdd:COG0459 14 A NI RGVKA L ADAVKVTL GP K G RNV M LVKSFGDPTI T N D GV TI AK E I E L E D P fenm G A Q L VKEV A SKTND E A GDGT TTATV 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 101 L C G E LL SQAES LV RM G LH P SE I IE G YK KA GS K SL E L L DTMV c K S VDD clr KE QVMDAIRT S IASK qygye DFLAGVV A D A 180
Cdd:COG0459 94 L A G A LL KEGLK LV AA G AN P TD I KR G ID KA VE K AV E E L KKIA - K P VDD --- KE ELAQVATI S ANGD ----- EEIGELI A E A 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 181 cinvcpsnvrsfn VDN V --- R V VKLD -- GESILSTKL V R G FVIGR --------- NT E SNLKH L KS A KVAVYSCA vdvpsl 246
Cdd:COG0459 165 ------------- MEK V gkd G V ITVE eg KGLETELEV V E G MQFDK gylspyfvt DP E KMPAE L EN A YILLTDKK ------ 225
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 247 etkgtal I ENAE DL I qysrkeeeimq EIISNIHK SG AN L IVSNSTFGDL AL HFINRL G MM ------ AV RI P S ----- K FE 315
Cdd:COG0459 226 ------- I SSIQ DL L ----------- PLLEKVAQ SG KP L LIIAEDIDGE AL ATLVVN G IR gvlrvv AV KA P G fgdrr K AM 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 316 L RRLCAAV G A RV MTR ----- L DAPSME D M G ACDS V D V ldig G K NV T AF V QDRDDS K LST I V V RG AT QNVLDDVE R AID D G 390
Cdd:COG0459 288 L EDIAILT G G RV ISE dlglk L EDVTLD D L G RAKR V E V ---- D K DN T TI V EGAGNP K AIV I L V GA AT EVEVKERK R RVE D A 363
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 391 VNVFK A LTKDK r V V A G A GA VEMELQKE L TLY A EANP G LD Q YAVRKY A SSF E VVA R TL AE AS G FN G TDM V TQLE A dhn A GK 470
Cdd:COG0459 364 LHATR A AVEEG - I V P G G GA ALLRAARA L REL A AKLE G DE Q LGIEIV A RAL E APL R QI AE NA G LD G SVV V EKVR A --- A KD 439
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2752564595 471 K YQ G ANLND G TTL D AV EAG IVE P HMT K FW A IRL A TDTVLTV L SVNQI I VA K QAGGPKN 528
Cdd:COG0459 440 K GF G FDAAT G EYV D ML EAG VID P AKV K RS A LQN A ASVAGLI L TTEAV I AD K PEKEEAA 497
chap_CCT_beta
TIGR02341 T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
36-520
6.96e-64
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: 217.03
E-value: 6.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 36 ITR S SM GP N G LC K MVI -- NHLNKLF VT H D A ATIL RELE V EH PAAK L LV QAANAMQE EVGDGT NF V VT L CG ELL SQ AE S L V 113
Cdd:TIGR02341 29 LVK S TL GP K G MD K ILQ ss SSDASIM VT N D G ATIL KSIG V DN PAAK V LV DMSKVQDD EVGDGT TS V TV L AA ELL RE AE K L I 108
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 114 RMGL HP SE II E GY KK A GSKSLE - LL DTM V CKSV D DCLRKEQV M DAI RT SIA SK QYG - YE D FL A GVVA DA CINVCP S N vrs 191
Cdd:TIGR02341 109 NQKI HP QT II A GY RE A TKAARD a LL KSA V DNGS D EVKFRQDL M NIA RT TLS SK ILS q HK D HF A QLAV DA VLRLKG S G --- 185
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 192 f N VDNVRVV K LD G E S ILSTK L VR GF VIGRNTES N L - K HLKS AK VAVYSCAV D VPSLETK G TAL - IENAEDLIQYSRK E E E 269
Cdd:TIGR02341 186 - N LEAIQII K KL G G S LADSY L DE GF LLDKKIGV N Q p K RIEN AK ILIANTGM D TDKVKIF G SRV r VDSTAKVAELEHA E K E 264
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 270 I M Q E IISN I H K S G A N LIVSNSTFGDLALHFINRL G M MA VRIPSKFELR RL CAAV G ARVMTRL D A P SMEDM G A CD SVDVLD 349
Cdd:TIGR02341 265 K M K E KVEK I L K H G I N CFINRQLIYNYPEQLFADA G V MA IEHADFEGVE RL ALVT G GEIVSTF D H P ELVKL G S CD LIEEIM 344
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 350 IG GKNVTA F v QDRDDSKLS TIV V RGATQ NV LD DV ER AID D GVN V FKALT K DK R V V A G A G AV EM ELQ K EL T LY A EAN PG LD 429
Cdd:TIGR02341 345 IG EDKLLK F - SGVKLGEAC TIV L RGATQ QI LD EA ER SLH D ALC V LSQTV K ES R T V L G G G CS EM LMS K AV T QE A QRT PG KE 423
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 430 QY AV RKY A SSFEVVARTL A EAS GF NGTDM V T QL E A D H NA G KKYQ G ANL N D GT TL D AVEA GI V E PHMT K FWAIRL A TDTVL 509
Cdd:TIGR02341 424 AL AV EAF A RALRQLPTII A DNA GF DSAEL V A QL R A A H YN G NTTM G LDM N E GT IA D MRQL GI T E SYKV K RAVVSS A AEAAE 503
490
....*....|.
gi 2752564595 510 TV L S V NQ II V A 520
Cdd:TIGR02341 504 VI L R V DN II K A 514
TCP1_zeta
cd03342 TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
26-520
5.80e-61
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: 208.27
E-value: 5.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A CRE L SKITRSSM GP N G LC KM VINHLNKLFV T H D AATI L R E LEVE HP A A KLLVQ AA N A MQEEV GDGT NFV V T L C GEL 105
Cdd:cd03342 17 NI S A AKG L QDVLKTNL GP K G TL KM LVSGAGDIKL T K D GNVL L S E MQIQ HP T A SMIAR AA T A QDDIT GDGT TSN V L L I GEL 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L S QAE SLVRM G L HP SE I I EG YKK A GS K S L EL L DTMV c KS V DDCLRK E QVMDAI RTS IAS K - QYGYE D F L AGV V A DA CINV 184
Cdd:cd03342 97 L K QAE RYIQE G V HP RI I T EG FEL A KN K A L KF L ESFK - VP V EIDTDR E LLLSVA RTS LRT K l HADLA D Q L TEI V V DA VLAI 175
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 185 CPSN v RSFNVDN V RVVKLDGE S ILS TKL V RG F V I --- G R N te SNLKH l KSAKVAVYS C A V dvp SLE tkgtal I E NA E dli 261
Cdd:cd03342 176 YKPD - EPIDLHM V EIMQMQHK S DSD TKL I RG L V L dhg A R H -- PDMPK - RVENAYILT C N V --- SLE ------ Y E KT E --- 239
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 262 qysrkeeeimqeiisn IHKSGANLI V S N STFG D - LA L HFINRL G MM A V R IPSKFELR RL CA A V G ARV M TRL D AP S M E DM G 340
Cdd:cd03342 240 ---------------- VNSGFFYSV V I N QKGI D p PS L DMLAKE G IL A L R RAKRRNME RL TL A C G GVA M NSV D DL S P E CL G 303
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 341 ACDS V DVLDI G GKNV T a F VQDRDDS K LS TI VVR G ATQNVLDDVER AI D DG VNVF K ALTK DK R VV A GAGA V E ME L QKE L TL 420
Cdd:cd03342 304 YAGL V YERTL G EEKY T - F IEGVKNP K SC TI LIK G PNDHTITQIKD AI R DG LRAV K NAIE DK C VV P GAGA F E VA L YAH L KE 382
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 421 YAEANP G LDQYA V RKY A SSFE V VAR TLAE A SG FNGTDMVTQ L EADHNA G KKYQ G AN L ND G TTL D AVEA GI VEPHMT K FWA 500
Cdd:cd03342 383 FKKSVK G KAKLG V QAF A DALL V IPK TLAE N SG LDVQETLVK L QDEYAE G GQVG G VD L DT G EPM D PESE GI WDNYSV K RQI 462
490 500
....*....|....*....|
gi 2752564595 501 IRL AT DTVLTV L S V NQ II V A 520
Cdd:cd03342 463 LHS AT VIASQL L L V DE II R A 482
chap_CCT_zeta
TIGR02347 T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
26-520
5.09e-59
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: 204.58
E-value: 5.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 26 NI E A C R E L SKITRSSM GP N G LC KM VINHLNKLFV T H D AATI L R E LEVE HP A A KLLVQ AA N A MQEEV GDGT NFV V T L C GEL 105
Cdd:TIGR02347 21 NI N A A R G L QDVLKTNL GP K G TL KM LVSGAGDIKL T K D GNVL L N E MQIQ HP T A SMIAR AA T A QDDIT GDGT TST V L L I GEL 100
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 106 L S QAE SLVRM G L HP SE I I EG YKK A GSKS L EL LD TMVC K s VD D CLRK E QVMDAI RTS IAS K QY - GYE D F L AGV V A DA CINV 184
Cdd:TIGR02347 101 L K QAE RYILE G V HP RI I T EG FEI A RKEA L QF LD KFKV K - KE D EVDR E FLLNVA RTS LRT K LP a DLA D Q L TEI V V DA VLAI 179
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 185 CPSN v RSFNVDN V RVVKLDGE S ILS T K L V RG F V IGRNT - ESNLKH l KSAKVAVYS C A V dvp SLE TKG T AL -------- I E 255
Cdd:TIGR02347 180 KKDG - EDIDLFM V EIMEMKHK S ATD T T L I RG L V LDHGA r HPDMPR - RVKNAYILT C N V --- SLE YEK T EV nsgffyss A E 254
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 256 NA E D L IQYS RK - EEEIMQE II S ---- NIH KS G - ANLI V S N STFG D L - A L HFINRL G M MA V R IPSKFELR RL CA A V G ARVM 328
Cdd:TIGR02347 255 QR E K L VKAE RK f VDDRVKK II E lkkk VCG KS P d KGFV V I N QKGI D P p S L DLLAKE G I MA L R RAKRRNME RL TL A C G GEAL 334
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 329 TRLDAPSM E DM G ACDS V DVLD IG GKNV T a F VQDRDDS K LS TI VVR G ATQNVLDDVER A ID DG VNVF K ALTK DK R VV A GAG 408
Cdd:TIGR02347 335 NSVEDLTP E CL G WAGL V YETT IG EEKY T - F IEECKNP K SC TI LIK G PNDHTIAQIKD A VR DG LRAV K NAIE DK C VV P GAG 413
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 409 A V E MELQKE L TL Y AEANP G LDQYA V RKY A SSFE V VAR TLAE A SGF NGT D MVTQ LE AD H NA G KKYQ G AN LN D G TTL D AVEA 488
Cdd:TIGR02347 414 A F E IAAYRH L KE Y KKSVK G KAKLG V EAF A NALL V IPK TLAE N SGF DAQ D TLVK LE DE H DE G GEVV G VD LN T G EPI D PEIK 493
490 500 510
....*....|....*....|....*....|..
gi 2752564595 489 GI VEPHMT K FWA I RL AT DTVLTV L S V NQIIV A 520
Cdd:TIGR02347 494 GI WDNYRV K KQL I QS AT VIASQL L L V DEVMR A 525
chaperonin_like
cd03333 chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
151-400
1.13e-52
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: 178.04
E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 151 K E QVMDAIR TS IA SK QYGYE DFL AGV V A DA CIN V C P S N v R SFNVDNVR V V K LD G E S ILSTK LV R G F V IGRNTE S N -- L K H 228
Cdd:cd03333 1 R E LLLQVAT TS LN SK LSSWD DFL GKL V V DA VLK V G P D N - R MDDLGVIK V E K IP G G S LEDSE LV V G V V FDKGYA S P ym P K R 79
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 229 L KS AK VAVYS C AVD vpsletkgtalienaedliqysrkeeeimqeiisnihksga NLIVSNSTFG DLALH FINRL G M MAV 308
Cdd:cd03333 80 L EN AK ILLLD C PLE ----------------------------------------- YVVIAEKGID DLALH YLAKA G I MAV 118
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 309 R IPS K FE L R R LCA A V GA RVMTR L DAPSM ED M G ACDS V DVLD IG GKNV T AFVQDR d DS K LS TI VV RGAT QNV LD D V E R AID 388
Cdd:cd03333 119 R RVK K ED L E R IAR A T GA TIVSS L EDLTP ED L G TAEL V EETK IG EEKL T FIEGCK - GG K AA TI LL RGAT EVE LD E V K R SLH 197
250
....*....|..
gi 2752564595 389 D GVNVFK A LTKD 400
Cdd:cd03333 198 D ALCAVR A AVEE 209
PLN03167
PLN03167 Chaperonin-60 beta subunit; Provisional
13-147
1.78e-05
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain]
Cd Length: 600
Bit Score: 47.61
E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 13 KDGSA fvddpv L K NIE A - CRE L SKITRSSM GP N G LCKMVINHLNKLFVTH D AA T ILR E L E V E H P ---- A AKL LV QAA NAM 87
Cdd:PLN03167 63 KDGSA ------ I K KLQ A g VNK L ADLVGVTL GP K G RNVVLESKYGSPKIVN D GV T VAK E V E L E D P veni G AKL VR QAA AKT 136
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 88 QEEV GDGT NFV V T L CGE L LSQAESL V RM G LH P SE I IE G YK K AGSKSLEL L DT M v C K S V D D 147
Cdd:PLN03167 137 NDLA GDGT TTS V V L AQG L IAEGVKV V AA G AN P VQ I TR G IE K TAKALVKE L KK M - S K E V E D 195
Fab1_TCP
cd03334 TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
171-385
1.89e-05
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: 46.45
E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 171 D F L AGV V AD A CI NV C P s N VR SFNVDNV R ---- VV K LD G E S ILSTKL V R G F V IGR N TES nl K H ---- L K SAKVAVYSCAVD 242
Cdd:cd03334 21 D I L LPL V WK A AS NV K P - D VR AGDDMDI R qyvk IK K IP G G S PSDSEV V D G V V FTK N VAH -- K R mpsk I K NPRILLLQGPLE 97
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 243 VPSL E T K GTA L iena EDL I QY srk E E E IMQEII S N I HKSGANL I VSNSTFGDL A LHFINRL G MMA V RIPSKFE L R R LCAA 322
Cdd:cd03334 98 YQRV E N K LLS L ---- DPV I LQ --- E K E YLKNLV S R I VALRPDV I LVEKSVSRI A QDLLLEA G ITL V LNVKPSV L E R ISRC 170
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2752564595 323 V GA RV mtrld AP SM E D ------ M G A C D S VD V LDI ----- GG K NVTA F vqdrdd SKLS ----- TI VV RG ATQNV L DD V E R 385
Cdd:cd03334 171 T GA DI ----- IS SM D D lltspk L G T C E S FR V RTY veehg RS K TLMF F ------ EGCP kelgc TI LL RG GDLEE L KK V K R 238
groEL
CHL00093 chaperonin GroEL
360-522
1.03e-03
chaperonin GroEL
Pssm-ID: 177025
Cd Length: 529
Bit Score: 41.63
E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 360 Q D R D d S KLS ---- T I V V RG AT QNVLD D VERAID D GV N VF KA LTKDK r V V A G A GA VEME L QKE L TLY A EA N PGL D Q ---- Y 431
Cdd:CHL00093 365 Q E R L - A KLS ggva V I K V GA AT ETEMK D KKLRLE D AI N AT KA AVEEG - I V P G G GA TLVH L SEN L KTW A KN N LKE D E liga L 442
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2752564595 432 A V RK yas SFEVVARTL AE AS G F NG TDMVTQL - E A D HNA G kk Y QG AN lnd GTTLDAV EAGI VE P HMTKFW A IRL A TDTVLT 510
Cdd:CHL00093 443 I V AR --- AILAPLKRI AE NA G K NG SVIIEKV q E Q D FEI G -- Y NA AN --- NKFVNMY EAGI ID P AKVTRS A LQN A ASIASM 514
170
....*....|..
gi 2752564595 511 V L SVNQ IIV A K Q 522
Cdd:CHL00093 515 I L TTEC IIV D K K 526
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
