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T-complex protein 1 subunit theta isoform 1 [Homo sapiens]
Protein Classification
T-complex protein 1 subunit theta ( domain architecture ID 10798023 )
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
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
10-539
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: 885.21
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 10 G F A QM LKEG AK HFSGLEEAV YR NI Q ACKEL A Q T TRT AY GPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAK MI VMA 89
Cdd:TIGR02346 1 G I A SL LKEG YR HFSGLEEAV IK NI E ACKEL S Q I TRT SL GPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAK LL VMA 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 90 S H MQE Q E V GDGTN F VLV F AG A LL EL AEEL L R I GL SV SE V I E GYE I A CR KA H EIL PN LV CCSA K N LRD I DE VSSL L RT SI M 169
Cdd:TIGR02346 81 S E MQE N E I GDGTN L VLV L AG E LL NK AEEL I R M GL HP SE I I K GYE M A LK KA M EIL EE LV VWEV K D LRD K DE LIKA L KA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 170 SKQYGNE V FLA K L I AQAC VSIF P - DSGH FNVDNIRVCKILG SGI S S S S VL H GMVF KK E T EG D V T SVK D AK I AV Y SCP F D G 248
Cdd:TIGR02346 161 SKQYGNE D FLA Q L V AQAC STVL P k NPQN FNVDNIRVCKILG GSL S N S E VL K GMVF NR E A EG S V K SVK N AK V AV F SCP L D T 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 249 MI TETKGTVLI KT AEEL M N F SKGEEN LMD A QV KAIAD T G A NV V VTGG K V A DMALHY A NKYNIM LVRLN SK WD LRRLCKTV 328
Cdd:TIGR02346 241 AT TETKGTVLI HN AEEL L N Y SKGEEN QIE A MI KAIAD S G V NV I VTGG S V G DMALHY L NKYNIM VLKIP SK FE LRRLCKTV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 329 GAT A LPRL TP P VL EE M G HC DSVY L SE V G DTQ V V VFK H E KE D GA ISTI V LRGSTDNL M DDIERA V DDGVNT F K V L TR D K RL 408
Cdd:TIGR02346 321 GAT P LPRL GA P TP EE I G YV DSVY V SE I G GDK V T VFK Q E NG D SK ISTI I LRGSTDNL L DDIERA I DDGVNT V K A L VK D G RL 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 409 V PG G GATEIELA KQI T S YGE TC PGL E QYAIKKFAEAFE A IPR A LAEN S G VK ANEVI S KLYA V H QE GNK NV G L DIEAE VPA 488
Cdd:TIGR02346 401 L PG A GATEIELA SRL T K YGE KL PGL D QYAIKKFAEAFE I IPR T LAEN A G LN ANEVI P KLYA A H KK GNK SK G I DIEAE SDG 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 48762932 489 VKD ML EAGI L D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAKPAGGPKPP S GK 539
Cdd:TIGR02346 481 VKD AS EAGI Y D MLAT K K WAIKLAT E AAVTVLRVDQIIMAKPAGGPKPP Q GK 531
Name
Accession
Description
Interval
E-value
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
10-539
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: 885.21
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 10 G F A QM LKEG AK HFSGLEEAV YR NI Q ACKEL A Q T TRT AY GPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAK MI VMA 89
Cdd:TIGR02346 1 G I A SL LKEG YR HFSGLEEAV IK NI E ACKEL S Q I TRT SL GPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAK LL VMA 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 90 S H MQE Q E V GDGTN F VLV F AG A LL EL AEEL L R I GL SV SE V I E GYE I A CR KA H EIL PN LV CCSA K N LRD I DE VSSL L RT SI M 169
Cdd:TIGR02346 81 S E MQE N E I GDGTN L VLV L AG E LL NK AEEL I R M GL HP SE I I K GYE M A LK KA M EIL EE LV VWEV K D LRD K DE LIKA L KA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 170 SKQYGNE V FLA K L I AQAC VSIF P - DSGH FNVDNIRVCKILG SGI S S S S VL H GMVF KK E T EG D V T SVK D AK I AV Y SCP F D G 248
Cdd:TIGR02346 161 SKQYGNE D FLA Q L V AQAC STVL P k NPQN FNVDNIRVCKILG GSL S N S E VL K GMVF NR E A EG S V K SVK N AK V AV F SCP L D T 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 249 MI TETKGTVLI KT AEEL M N F SKGEEN LMD A QV KAIAD T G A NV V VTGG K V A DMALHY A NKYNIM LVRLN SK WD LRRLCKTV 328
Cdd:TIGR02346 241 AT TETKGTVLI HN AEEL L N Y SKGEEN QIE A MI KAIAD S G V NV I VTGG S V G DMALHY L NKYNIM VLKIP SK FE LRRLCKTV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 329 GAT A LPRL TP P VL EE M G HC DSVY L SE V G DTQ V V VFK H E KE D GA ISTI V LRGSTDNL M DDIERA V DDGVNT F K V L TR D K RL 408
Cdd:TIGR02346 321 GAT P LPRL GA P TP EE I G YV DSVY V SE I G GDK V T VFK Q E NG D SK ISTI I LRGSTDNL L DDIERA I DDGVNT V K A L VK D G RL 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 409 V PG G GATEIELA KQI T S YGE TC PGL E QYAIKKFAEAFE A IPR A LAEN S G VK ANEVI S KLYA V H QE GNK NV G L DIEAE VPA 488
Cdd:TIGR02346 401 L PG A GATEIELA SRL T K YGE KL PGL D QYAIKKFAEAFE I IPR T LAEN A G LN ANEVI P KLYA A H KK GNK SK G I DIEAE SDG 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 48762932 489 VKD ML EAGI L D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAKPAGGPKPP S GK 539
Cdd:TIGR02346 481 VKD AS EAGI Y D MLAT K K WAIKLAT E AAVTVLRVDQIIMAKPAGGPKPP Q GK 531
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
20-528
0e+00
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain]
Cd Length: 472
Bit Score: 801.82
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 20 K H F SGLEEAV Y RNI Q ACKEL A Q T TRT A YGPNGMNKMVINHLEKLFVT N DAATILRELEVQHPAAK MI VMAS H MQE Q E V GD 99
Cdd:cd03341 1 R H Y SGLEEAV L RNI E ACKEL S Q I TRT S YGPNGMNKMVINHLEKLFVT S DAATILRELEVQHPAAK LL VMAS Q MQE E E I GD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 100 GTN F V L V F AG A LLE L AEELLR I GL SV SE V IEGYE I A CR KA H EIL PN LV CCSAKN LR DID EVS SL L R T S I M SKQYGNE V FL 179
Cdd:cd03341 81 GTN L V V V L AG E LLE K AEELLR M GL HP SE I IEGYE K A LK KA L EIL EE LV VYKIED LR NKE EVS KA L K T A I A SKQYGNE D FL 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 180 AK L I A Q AC V S IF P - DS G H FNVDNIRV C KILG SGISS S S V LH GMVFK K E T EG D V TS VK D AK I AV Y SCPFD gmitetkgtvl 258
Cdd:cd03341 161 SP L V A E AC I S VL P e NI G N FNVDNIRV V KILG GSLED S K V VR GMVFK R E P EG S V KR VK K AK V AV F SCPFD ----------- 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 259 iktaeelmnfskgeenlmdaqvkaiad T G A NV V V T GG K V A D M ALHY A NKY N IM LVRL NSK WD LRRLC K TVGAT A LPRL TP 338
Cdd:cd03341 230 --------------------------- I G V NV I V A GG S V G D L ALHY C NKY G IM VIKI NSK FE LRRLC R TVGAT P LPRL GA 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 339 P VL EE M G H CDSVY LS E V GDT Q VVVF KHE KED GA I S TIVLRG S T D N LM DD I ERA V DDGVN T FK V LT R D K R L VPG G GATEIE 418
Cdd:cd03341 283 P TP EE I G Y CDSVY VE E I GDT K VVVF RQN KED SK I A TIVLRG A T Q N IL DD V ERA I DDGVN V FK S LT K D G R F VPG A GATEIE 362
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 419 LAK QITS YGE TC PGLEQYAIKKFAEAFE AI PR A LAEN S G VK A N EV I S K LYA V HQ E GNK NV G L DIE AEVPAV KD ML EAGI L 498
Cdd:cd03341 363 LAK KLKE YGE KT PGLEQYAIKKFAEAFE VV PR T LAEN A G LD A T EV L S E LYA A HQ K GNK SA G V DIE SGDEGT KD AK EAGI F 442
490 500 510
....*....|....*....|....*....|
gi 48762932 499 D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAK 528
Cdd:cd03341 443 D HLAT K K WAIKLAT E AAVTVLRVDQIIMAK 472
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
39-528
2.73e-179
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: 514.06
E-value: 2.73e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 39 LA QTT RT AY GP N GM N KM VI N HLEKLF VTND A ATIL R ELE V QHPAAK MI V M A SHM Q EQ EVGDGT NF V L V F AG A LLE L AE E L 118
Cdd:pfam00118 1 LA DIV RT SL GP K GM D KM LV N SGGDVT VTND G ATIL K ELE I QHPAAK LL V E A AKA Q DE EVGDGT TT V V V L AG E LLE E AE K L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 119 L RI G LSVSEV IEGYE I A CR KA H EIL PNLVCCSAKNL r D IDEVSSLL RTS IM SK QYGN E V - FLAKL IAQ A CVS I FPDS G H F 197
Cdd:pfam00118 81 L AA G VHPTTI IEGYE K A LE KA L EIL DSIISIPVEDV - D REDLLKVA RTS LS SK IISR E S d FLAKL VVD A VLA I PKND G S F 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 198 NVD NI R V C KILG SGISS S SVLH G M V FK K ETEGD -- VTSVKD AK IAVYS C PFDGMI TETK G TV LIKT AE E L MN F S K G EE NL 275
Cdd:pfam00118 160 DLG NI G V V KILG GSLED S ELVD G V V LD K GPLHP dm PKRLEN AK VLLLN C SLEYEK TETK A TV VLSD AE Q L ER F L K A EE EQ 239
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 276 MDAQ V KA I A D T G A NVVV TGGKVA D M ALH YAN K YN IM LV R LNS K W DL R RL C K TV GA T A LPR L TPPVLEEM G HCDS V YLSEV 355
Cdd:pfam00118 240 ILEI V EK I I D S G V NVVV CQKGID D L ALH FLA K NG IM AL R RVK K R DL E RL A K AT GA R A VSS L DDLTPDDL G TAGK V EEEKI 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 356 GD TQVVVFKHE K e DGAIS TI V LRG S TD NLM D D IER AVD D GVNTF K VLTR D K R L VPGGGA T E I ELA KQITS Y GETCP G L EQ 435
Cdd:pfam00118 320 GD EKYTFIEGC K - SPKAA TI L LRG A TD HVL D E IER SIH D ALCVV K NAIE D P R V VPGGGA V E M ELA RALRE Y AKSVS G K EQ 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 436 Y AI KK FAEA F E A IP RA LAEN S G VKAN EV ISK L Y A V H QE G N K NV G L D I E AE vp AVK DM L EAG IL D TYLG K YW A I K L AT N AA 515
Cdd:pfam00118 399 L AI EA FAEA L E V IP KT LAEN A G LDPI EV LAE L R A A H AS G E K HA G I D V E TG -- EII DM K EAG VV D PLKV K RQ A L K S AT E AA 476
490
....*....|...
gi 48762932 516 V T V LR V D Q II M AK 528
Cdd:pfam00118 477 S T I LR I D D II K AK 489
thermosome_alpha
NF041082 thermosome subunit alpha;
15-528
6.67e-115
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 350.34
E-value: 6.67e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 15 LKEG AKHF SG l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINH L EKLFV TND AA TIL R E LEVQ HPAAKMIV MASHM Q E 94
Cdd:NF041082 6 LKEG TQRT SG - RD A QRN NI M A A K AV A EAV RT TL GP K GM D KM LVDS L GDVVI TND GV TIL K E MDIE HPAAKMIV EVAKT Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVI EGY EI A CR KA H EIL PNL vccs A KNLR -- D IDEVSSLLR T SIMS K Q 172
Cdd:NF041082 85 D EVGDGT TTAV V L AG E LL KK AEELL DQDIHPTIIA EGY RL A AE KA L EIL DEI ---- A IKVD pd D KETLKKIAA T AMTG K G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 173 YGNEV - F LA K L IAQ A CVSIFPDS G HF NVD -- NI R V C K IL G SG I SS S SVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P FD 247
Cdd:NF041082 161 AEAAK d K LA D L VVD A VKAVAEKD G GY NVD ld NI K V E K KV G GS I ED S ELVE G V V ID KE R vh P G MPKR V EN AKIA LLDA P LE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 248 GMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA IAD T GANVV VTGGKVA D M A L HY AN K YN I ML VR LNS K W D LRR L C K T 327
Cdd:NF041082 241 VKK TE IDAKIS I TDPDQ L QA F LDQ EE KMLKEM V DK IAD S GANVV FCQKGID D L A Q HY LA K EG I LA VR RVK K S D MEK L A K A 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 328 V GA --- T ALPR L T P pvl E EM G HCDS V YLSE VG DTQVVVFKHE K EDG A I s TI V LRG S T DNLM D DI ERA VD D GVNTFK V LTR 404
Cdd:NF041082 321 T GA riv T SIDD L S P --- E DL G YAGL V EERK VG GDKMIFVEGC K NPK A V - TI L LRG G T EHVV D EV ERA LE D ALRVVR V VLE 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 405 D KRL V P GGGA T E I ELA KQITS Y GETCP G L EQ Y AI KK FAEA F E A IPR A LAEN S G VKANEVISK L YAV H QE GNK NV GLD IEA 484
Cdd:NF041082 397 D GKV V A GGGA P E V ELA LRLRE Y AASVG G R EQ L AI EA FAEA L E I IPR T LAEN A G LDPIDALVE L RSA H EK GNK TA GLD VYT 476
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 48762932 485 E vp A V K DMLE A G ILDTYLG K YW AIK L AT N AAV TV LR V D QI I M A K 528
Cdd:NF041082 477 G -- K V V DMLE I G VVEPLRV K TQ AIK S AT E AAV MI LR I D DV I A A A 518
thermosome_beta
NF041083 thermosome subunit beta;
15-528
1.45e-108
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 334.23
E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 15 LKEG AKHFS G l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINH L EKLFV TND A ATIL R E LE VQHPAAKM I V MASHM Q E 94
Cdd:NF041083 6 LKEG TQRTK G - RD A QRN NI M A A K AV A EAV RT TL GP K GM D KM LVDS L GDIVI TND G ATIL K E MD VQHPAAKM L V EVAKT Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVIE GY EI A CR KA H EIL PNL vccs A KNL r D I D EVSS L LR --- TS IM SK 171
Cdd:NF041083 85 D EVGDGT TTAV V L AG E LL KK AEELL DQNIHPTIIAN GY RL A AE KA I EIL DEI ---- A EKV - D P D DRET L KK iae TS LT SK 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 172 QYG - NEVF LA KLIAQ A CVSIFPDSG --- HFNV DNI RVC K IL G SG I SSSSVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P 245
Cdd:NF041083 160 GVE e ARDY LA EIAVK A VKQVAEKRD gky YVDL DNI QIE K KH G GS I EDTQLIY G I V ID KE V vh P G MPKR V EN AKIA LLDA P 239
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 246 FDGMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA I AD TGANVV VTGGKVA D M A L HY AN K YN I ML VR LNS K W D LRR L C 325
Cdd:NF041083 240 LEVKK TE IDAEIR I TDPDQ L QK F LDQ EE KMLKEM V DK I KA TGANVV FCQKGID D L A Q HY LA K AG I LA VR RVK K S D MEK L A 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 326 K TV GA --- T ALPR LTP pvl E EM G HCDS V YLSE VGD TQV V VFKHE K EDG A I s TI VL RG S T DNLM D DI ERA VD D GVNTFKVL 402
Cdd:NF041083 320 K AT GA riv T NIDD LTP --- E DL G YAEL V EERK VGD DKM V FVEGC K NPK A V - TI LI RG G T EHVV D EA ERA LE D ALSVVADA 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 403 TR D KRL V P GGGA T E I ELAK QITS Y GE T CP G L EQ Y A IKK FAEA F E A IPR A LAEN S G VKANEVIS KL YAV H QE G N K NV G LDI 482
Cdd:NF041083 396 VE D GKI V A GGGA P E V ELAK RLRE Y AA T VG G R EQ L A VEA FAEA L E I IPR T LAEN A G LDPIDILV KL RSA H EK G K K WA G INV 475
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 48762932 483 EAE vp A V K DM L E A G ILDTYLG K YW AIK L AT N AA VTV LR V D QI I M AK 528
Cdd:NF041083 476 FTG -- E V V DM W E L G VIEPLRV K TQ AIK S AT E AA TMI LR I D DV I A AK 519
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
26-535
4.70e-64
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 217.25
E-value: 4.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 26 E E A VYR NI QAC K E LA QTTRTAY GP N G M N K M vinh L E K L F ---- V TND AA TI LR E L E VQH P ---- A A KMIVMASHMQEQ E V 97
Cdd:COG0459 9 E D A RRA NI RGV K A LA DAVKVTL GP K G R N V M ---- L V K S F gdpt I TND GV TI AK E I E LED P fenm G A QLVKEVASKTND E A 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 98 GDGT NFVL V F AGALL ELAEE L LRI G LSVSEVIE G YEI A CR KA H E I L PNL vccs AK NLR D ID E VSSLLRT S I mskqy GNEV 177
Cdd:COG0459 85 GDGT TTAT V L AGALL KEGLK L VAA G ANPTDIKR G IDK A VE KA V E E L KKI ---- AK PVD D KE E LAQVATI S A ----- NGDE 155
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 178 FLAK LIA Q A CVSIFP D s G HFN V D nirvck ILGSGISSSS V LH GM V F K K E --------- T E GDVTSVKD A K I A vyscpfdg 248
Cdd:COG0459 156 EIGE LIA E A MEKVGK D - G VIT V E ------ EGKGLETELE V VE GM Q F D K G ylspyfvtd P E KMPAELEN A Y I L -------- 220
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 249 m I T ET K gtvl I KTAEE L M nfskgeenlmd AQVKAI A DT G ANVVVTGGKVADM AL HYANKYN I ML V R ----------- LNS 317
Cdd:COG0459 221 - L T DK K ---- I SSIQD L L ----------- PLLEKV A QS G KPLLIIAEDIDGE AL ATLVVNG I RG V L rvvavkapgfg DRR 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 318 K WD L RRLCKTV G ATALPRLTPPV LE EM ----- G HCDS V YLSE vg D TQVV V fk HEKEDGAIST I VLRGS T DNLMDDIE R A V 392
Cdd:COG0459 285 K AM L EDIAILT G GRVISEDLGLK LE DV tlddl G RAKR V EVDK -- D NTTI V -- EGAGNPKAIV I LVGAA T EVEVKERK R R V 360
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 393 D D GVNTFKVLTRDK r L VPGGGA TEIEL A KQITSYGETCP G L EQ YA I KKF A E A F EA IP R AL AEN S G VKANE V IS K LY A vhq 472
Cdd:COG0459 361 E D ALHATRAAVEEG - I VPGGGA ALLRA A RALRELAAKLE G D EQ LG I EIV A R A L EA PL R QI AEN A G LDGSV V VE K VR A --- 436
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48762932 473 EGN K NV G L D IEAEV pa VK DMLEAG IL D TYLG K YW A IKL A TNA A VTV L RVDQI I MA KP AGGPKP 535
Cdd:COG0459 437 AKD K GF G F D AATGE -- YV DMLEAG VI D PAKV K RS A LQN A ASV A GLI L TTEAV I AD KP EKEEAA 497
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
13-529
1.22e-59
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 206.42
E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 13 Q M LK E GA KHFS G l E E A VYRNIQACKEL A QTTR T AY GP N GM N K MVINHL E ----- KLF VTND A ATIL RELEVQH PAAK MI V 87
Cdd:PTZ00212 9 Q V LK Q GA QEEK G - E T A RLQSFVGAIAV A DLVK T TL GP K GM D K ILQPMS E gprsg NVT VTND G ATIL KSVWLDN PAAK IL V 87
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 88 MA S HM Q EQ EVGDGT NF V L V F AG A LL EL AE E LL RIGLSVSEV IEG YEI A CRK A HE ilp N L VCCSAKNLR D IDEVSSL L --- 164
Cdd:PTZ00212 88 DI S KT Q DE EVGDGT TS V V V L AG E LL RE AE K LL DQKIHPQTI IEG WRM A LDV A RK --- A L EEIAFDHGS D EEKFKED L lni 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 165 - RT SIM SK -- QYGNEV F l AKL IAQ A CVSI fpd S G HF N V D N I RVC K IL G SGISS S SVLH G MVFK K E - TE G DVTSVKDA KI A 240
Cdd:PTZ00212 165 a RT TLS SK ll TVEKDH F - AKL AVD A VLRL --- K G SG N L D Y I QII K KP G GTLRD S YLED G FILE K K i GV G QPKRLENC KI L 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 241 V YSC P F D GMITETK G T - V LIKTA E ELMNFSKG E ENL M DAQ V KA I ADT G A NV VVTGGKVADMALHYANKYN IM LVR l NSKW 319
Cdd:PTZ00212 241 V ANT P M D TDKIKIY G A k V KVDSM E KVAEIEAA E KEK M KNK V DK I LAH G C NV FINRQLIYNYPEQLFAEAG IM AIE - HADF 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 320 D - LR RL CKTV GA TALPRLTP P VLEEM GHCD SVYLSEV G DTQVVV F KHEKEDG A i S TIVLRG STDNLM D DI ER AVD D GVNT 398
Cdd:PTZ00212 320 D g ME RL AAAL GA EIVSTFDT P EKVKL GHCD LIEEIMI G EDKLIR F SGCAKGE A - C TIVLRG ASTHIL D EA ER SLH D ALCV 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 399 FKVLTR D K R L V P GGG AT E IEL A KQITSYGETCP G LEQY AI KK FA E A FEA IP RAL A E N S G VKAN E VI SKL Y A V H QE GNK NV 478
Cdd:PTZ00212 399 LSQTVK D T R V V L GGG CS E MLM A NAVEELAKKVE G KKSL AI EA FA K A LRQ IP TII A D N G G YDSA E LV SKL R A E H YK GNK TA 478
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 48762932 479 G L D I E AEVPA vk DM L E A GI LDT Y LG K YWAIKL AT N AA VTV LRVD Q II MAK P 529
Cdd:PTZ00212 479 G I D M E KGTVG -- DM K E L GI TES Y KV K LSQLCS AT E AA EMI LRVD D II RCA P 527
Name
Accession
Description
Interval
E-value
chap_CCT_theta
TIGR02346 T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
10-539
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: 885.21
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 10 G F A QM LKEG AK HFSGLEEAV YR NI Q ACKEL A Q T TRT AY GPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAK MI VMA 89
Cdd:TIGR02346 1 G I A SL LKEG YR HFSGLEEAV IK NI E ACKEL S Q I TRT SL GPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAK LL VMA 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 90 S H MQE Q E V GDGTN F VLV F AG A LL EL AEEL L R I GL SV SE V I E GYE I A CR KA H EIL PN LV CCSA K N LRD I DE VSSL L RT SI M 169
Cdd:TIGR02346 81 S E MQE N E I GDGTN L VLV L AG E LL NK AEEL I R M GL HP SE I I K GYE M A LK KA M EIL EE LV VWEV K D LRD K DE LIKA L KA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 170 SKQYGNE V FLA K L I AQAC VSIF P - DSGH FNVDNIRVCKILG SGI S S S S VL H GMVF KK E T EG D V T SVK D AK I AV Y SCP F D G 248
Cdd:TIGR02346 161 SKQYGNE D FLA Q L V AQAC STVL P k NPQN FNVDNIRVCKILG GSL S N S E VL K GMVF NR E A EG S V K SVK N AK V AV F SCP L D T 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 249 MI TETKGTVLI KT AEEL M N F SKGEEN LMD A QV KAIAD T G A NV V VTGG K V A DMALHY A NKYNIM LVRLN SK WD LRRLCKTV 328
Cdd:TIGR02346 241 AT TETKGTVLI HN AEEL L N Y SKGEEN QIE A MI KAIAD S G V NV I VTGG S V G DMALHY L NKYNIM VLKIP SK FE LRRLCKTV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 329 GAT A LPRL TP P VL EE M G HC DSVY L SE V G DTQ V V VFK H E KE D GA ISTI V LRGSTDNL M DDIERA V DDGVNT F K V L TR D K RL 408
Cdd:TIGR02346 321 GAT P LPRL GA P TP EE I G YV DSVY V SE I G GDK V T VFK Q E NG D SK ISTI I LRGSTDNL L DDIERA I DDGVNT V K A L VK D G RL 400
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 409 V PG G GATEIELA KQI T S YGE TC PGL E QYAIKKFAEAFE A IPR A LAEN S G VK ANEVI S KLYA V H QE GNK NV G L DIEAE VPA 488
Cdd:TIGR02346 401 L PG A GATEIELA SRL T K YGE KL PGL D QYAIKKFAEAFE I IPR T LAEN A G LN ANEVI P KLYA A H KK GNK SK G I DIEAE SDG 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 48762932 489 VKD ML EAGI L D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAKPAGGPKPP S GK 539
Cdd:TIGR02346 481 VKD AS EAGI Y D MLAT K K WAIKLAT E AAVTVLRVDQIIMAKPAGGPKPP Q GK 531
TCP1_theta
cd03341 TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
20-528
0e+00
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain]
Cd Length: 472
Bit Score: 801.82
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 20 K H F SGLEEAV Y RNI Q ACKEL A Q T TRT A YGPNGMNKMVINHLEKLFVT N DAATILRELEVQHPAAK MI VMAS H MQE Q E V GD 99
Cdd:cd03341 1 R H Y SGLEEAV L RNI E ACKEL S Q I TRT S YGPNGMNKMVINHLEKLFVT S DAATILRELEVQHPAAK LL VMAS Q MQE E E I GD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 100 GTN F V L V F AG A LLE L AEELLR I GL SV SE V IEGYE I A CR KA H EIL PN LV CCSAKN LR DID EVS SL L R T S I M SKQYGNE V FL 179
Cdd:cd03341 81 GTN L V V V L AG E LLE K AEELLR M GL HP SE I IEGYE K A LK KA L EIL EE LV VYKIED LR NKE EVS KA L K T A I A SKQYGNE D FL 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 180 AK L I A Q AC V S IF P - DS G H FNVDNIRV C KILG SGISS S S V LH GMVFK K E T EG D V TS VK D AK I AV Y SCPFD gmitetkgtvl 258
Cdd:cd03341 161 SP L V A E AC I S VL P e NI G N FNVDNIRV V KILG GSLED S K V VR GMVFK R E P EG S V KR VK K AK V AV F SCPFD ----------- 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 259 iktaeelmnfskgeenlmdaqvkaiad T G A NV V V T GG K V A D M ALHY A NKY N IM LVRL NSK WD LRRLC K TVGAT A LPRL TP 338
Cdd:cd03341 230 --------------------------- I G V NV I V A GG S V G D L ALHY C NKY G IM VIKI NSK FE LRRLC R TVGAT P LPRL GA 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 339 P VL EE M G H CDSVY LS E V GDT Q VVVF KHE KED GA I S TIVLRG S T D N LM DD I ERA V DDGVN T FK V LT R D K R L VPG G GATEIE 418
Cdd:cd03341 283 P TP EE I G Y CDSVY VE E I GDT K VVVF RQN KED SK I A TIVLRG A T Q N IL DD V ERA I DDGVN V FK S LT K D G R F VPG A GATEIE 362
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 419 LAK QITS YGE TC PGLEQYAIKKFAEAFE AI PR A LAEN S G VK A N EV I S K LYA V HQ E GNK NV G L DIE AEVPAV KD ML EAGI L 498
Cdd:cd03341 363 LAK KLKE YGE KT PGLEQYAIKKFAEAFE VV PR T LAEN A G LD A T EV L S E LYA A HQ K GNK SA G V DIE SGDEGT KD AK EAGI F 442
490 500 510
....*....|....*....|....*....|
gi 48762932 499 D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAK 528
Cdd:cd03341 443 D HLAT K K WAIKLAT E AAVTVLRVDQIIMAK 472
Cpn60_TCP1
pfam00118 TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
39-528
2.73e-179
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: 514.06
E-value: 2.73e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 39 LA QTT RT AY GP N GM N KM VI N HLEKLF VTND A ATIL R ELE V QHPAAK MI V M A SHM Q EQ EVGDGT NF V L V F AG A LLE L AE E L 118
Cdd:pfam00118 1 LA DIV RT SL GP K GM D KM LV N SGGDVT VTND G ATIL K ELE I QHPAAK LL V E A AKA Q DE EVGDGT TT V V V L AG E LLE E AE K L 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 119 L RI G LSVSEV IEGYE I A CR KA H EIL PNLVCCSAKNL r D IDEVSSLL RTS IM SK QYGN E V - FLAKL IAQ A CVS I FPDS G H F 197
Cdd:pfam00118 81 L AA G VHPTTI IEGYE K A LE KA L EIL DSIISIPVEDV - D REDLLKVA RTS LS SK IISR E S d FLAKL VVD A VLA I PKND G S F 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 198 NVD NI R V C KILG SGISS S SVLH G M V FK K ETEGD -- VTSVKD AK IAVYS C PFDGMI TETK G TV LIKT AE E L MN F S K G EE NL 275
Cdd:pfam00118 160 DLG NI G V V KILG GSLED S ELVD G V V LD K GPLHP dm PKRLEN AK VLLLN C SLEYEK TETK A TV VLSD AE Q L ER F L K A EE EQ 239
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 276 MDAQ V KA I A D T G A NVVV TGGKVA D M ALH YAN K YN IM LV R LNS K W DL R RL C K TV GA T A LPR L TPPVLEEM G HCDS V YLSEV 355
Cdd:pfam00118 240 ILEI V EK I I D S G V NVVV CQKGID D L ALH FLA K NG IM AL R RVK K R DL E RL A K AT GA R A VSS L DDLTPDDL G TAGK V EEEKI 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 356 GD TQVVVFKHE K e DGAIS TI V LRG S TD NLM D D IER AVD D GVNTF K VLTR D K R L VPGGGA T E I ELA KQITS Y GETCP G L EQ 435
Cdd:pfam00118 320 GD EKYTFIEGC K - SPKAA TI L LRG A TD HVL D E IER SIH D ALCVV K NAIE D P R V VPGGGA V E M ELA RALRE Y AKSVS G K EQ 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 436 Y AI KK FAEA F E A IP RA LAEN S G VKAN EV ISK L Y A V H QE G N K NV G L D I E AE vp AVK DM L EAG IL D TYLG K YW A I K L AT N AA 515
Cdd:pfam00118 399 L AI EA FAEA L E V IP KT LAEN A G LDPI EV LAE L R A A H AS G E K HA G I D V E TG -- EII DM K EAG VV D PLKV K RQ A L K S AT E AA 476
490
....*....|...
gi 48762932 516 V T V LR V D Q II M AK 528
Cdd:pfam00118 477 S T I LR I D D II K AK 489
chaperonin_type_I_II
cd00309 chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
20-526
4.85e-169
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: 486.94
E-value: 4.85e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 20 K HFSGL EEA VYR NI Q A C K E LA QTTR T AY GP N GM N KM VINH L EKLFV TND A ATIL R E L EV Q HPAAK MI V MASHM Q EQ EVGD 99
Cdd:cd00309 1 K EREFG EEA RLS NI N A A K A LA DAVK T TL GP K GM D KM LVDS L GDPTI TND G ATIL K E I EV E HPAAK LL V EVAKS Q DD EVGD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 100 GT NF V L V F AG A LL EL AE E LL RI G LSVS E V I E GYE I A CR KA H EIL PNLVCC sa KNLR D ID E VSSLLR TS IM SK Q - Y G NEV F 178
Cdd:cd00309 81 GT TT V V V L AG E LL KE AE K LL AA G IHPT E I I R GYE K A VE KA L EIL KEIAVP -- IDVE D RE E LLKVAT TS LN SK L v S G GDD F 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 179 L AK L IAQ A CVSIFPDS G HFNVDN IRV C K IL G SGISS S SVLH GMVF K K ETEGDV -- TSVKD AKI AVYS C PFD gmitetkgt 256
Cdd:cd00309 159 L GE L VVD A VLKVGKEN G DVDLGV IRV E K KK G GSLED S ELVV GMVF D K GYLSPY mp KRLEN AKI LLLD C KLE --------- 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 257 vliktaeelmnfskgeenlmdaqvkaiadtga N VV VTGGKVA D M ALHY AN K YN IM L VR LNS K W DL R R LC K TV GAT ALP RL 336
Cdd:cd00309 230 -------------------------------- Y VV IAEKGID D E ALHY LA K LG IM A VR RVR K E DL E R IA K AT GAT IVS RL 277
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 337 TPPVL E EM G HCDS V YLSEV GD TQVVVFKHE K e D G AIS TI V LRG S T DNLM D DI ER AVD D GVNTFKVLTR D KRL VPGGGA T E 416
Cdd:cd00309 278 EDLTP E DL G TAGL V EETKI GD EKYTFIEGC K - G G KVA TI L LRG A T EVEL D EA ER SLH D ALCAVRAAVE D GGI VPGGGA A E 356
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 417 IEL A K QITSYGE T C PG L EQ YA I KK FA E A F E A IPR A LAEN S G VKAN EV IS KL Y A V H Q EG NK N V G L D I E AE vp AVK DM L EAG 496
Cdd:cd00309 357 IEL S K ALEELAK T L PG K EQ LG I EA FA D A L E V IPR T LAEN A G LDPI EV VT KL R A K H A EG GG N A G G D V E TG -- EIV DM K EAG 434
490 500 510
....*....|....*....|....*....|
gi 48762932 497 I L D TYLG K YW A I K L AT N AA VTV L RV D Q II M 526
Cdd:cd00309 435 I I D PLKV K RQ A L K S AT E AA SLI L TI D D II V 464
cpn60
cd03343 cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
15-528
1.35e-115
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239459 [Multi-domain]
Cd Length: 517
Bit Score: 352.34
E-value: 1.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 15 LKEG AKHF SG l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINH L EKLFV TND A ATIL R E LEVQ HPAAKM I V MASHM Q E 94
Cdd:cd03343 4 LKEG TQRT SG - RD A QRM NI A A A K AV A EAV RT TL GP K GM D KM LVDS L GDVTI TND G ATIL K E MDIE HPAAKM L V EVAKT Q D 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 95 Q EVGDGT NFVL V F AG A LLE L AE E LL RIGLSVSEV IEGY EI A CR KA H E I L PNLV cc SAKNLR D I D EVSSLLR TS IMS K QYG 174
Cdd:cd03343 83 E EVGDGT TTAV V L AG E LLE K AE D LL DQNIHPTVI IEGY RL A AE KA L E L L DEIA -- IKVDPD D K D TLRKIAK TS LTG K GAE 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 175 NEV - F LA K L IAQ A CVSIF --- PDSGHFNV DNI RVC K IL G SGISSSSVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P FDG 248
Cdd:cd03343 161 AAK d K LA D L VVD A VLQVA ekr DGKYVVDL DNI KIE K KT G GSVDDTELIR G I V ID KE V vh P G MPKR V EN AKIA LLDA P LEV 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 249 MI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA IADTGANVV VTGGKVA D M A L HY AN K YN I ML VR LNS K W D LRR L CKTV 328
Cdd:cd03343 241 KK TE IDAKIR I TSPDQ L QA F LEQ EE AMLKEM V DK IADTGANVV FCQKGID D L A Q HY LA K AG I LA VR RVK K S D MEK L ARAT 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 329 GA --- T ALPR LTP pvl E EM G HCDS V YLSE VGD TQV V VFKHE K EDG A I s TI V LRG S T DNLM D DI ERA VD D GVNTFKVLTR D 405
Cdd:cd03343 321 GA kiv T NIDD LTP --- E DL G EAEL V EERK VGD DKM V FVEGC K NPK A V - TI L LRG G T EHVV D EL ERA LE D ALRVVADALE D 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 406 KRL V P GGGA T EIELAK QITS Y GETCP G L EQ Y A IKK FA E A F E A IPR A LAEN S G VKANEVISK L Y A V H QE GNKN V GLD IEAE 485
Cdd:cd03343 397 GKV V A GGGA V EIELAK RLRE Y ARSVG G R EQ L A VEA FA D A L E E IPR T LAEN A G LDPIDTLVE L R A A H EK GNKN A GLD VYTG 476
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 48762932 486 VPA vk DMLE A G ILDTYLG K YW AIK L AT N AA VTV LR V D QI I M AK 528
Cdd:cd03343 477 EVV -- DMLE K G VIEPLRV K KQ AIK S AT E AA TMI LR I D DV I A AK 517
thermosome_alpha
NF041082 thermosome subunit alpha;
15-528
6.67e-115
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 350.34
E-value: 6.67e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 15 LKEG AKHF SG l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINH L EKLFV TND AA TIL R E LEVQ HPAAKMIV MASHM Q E 94
Cdd:NF041082 6 LKEG TQRT SG - RD A QRN NI M A A K AV A EAV RT TL GP K GM D KM LVDS L GDVVI TND GV TIL K E MDIE HPAAKMIV EVAKT Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVI EGY EI A CR KA H EIL PNL vccs A KNLR -- D IDEVSSLLR T SIMS K Q 172
Cdd:NF041082 85 D EVGDGT TTAV V L AG E LL KK AEELL DQDIHPTIIA EGY RL A AE KA L EIL DEI ---- A IKVD pd D KETLKKIAA T AMTG K G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 173 YGNEV - F LA K L IAQ A CVSIFPDS G HF NVD -- NI R V C K IL G SG I SS S SVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P FD 247
Cdd:NF041082 161 AEAAK d K LA D L VVD A VKAVAEKD G GY NVD ld NI K V E K KV G GS I ED S ELVE G V V ID KE R vh P G MPKR V EN AKIA LLDA P LE 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 248 GMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA IAD T GANVV VTGGKVA D M A L HY AN K YN I ML VR LNS K W D LRR L C K T 327
Cdd:NF041082 241 VKK TE IDAKIS I TDPDQ L QA F LDQ EE KMLKEM V DK IAD S GANVV FCQKGID D L A Q HY LA K EG I LA VR RVK K S D MEK L A K A 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 328 V GA --- T ALPR L T P pvl E EM G HCDS V YLSE VG DTQVVVFKHE K EDG A I s TI V LRG S T DNLM D DI ERA VD D GVNTFK V LTR 404
Cdd:NF041082 321 T GA riv T SIDD L S P --- E DL G YAGL V EERK VG GDKMIFVEGC K NPK A V - TI L LRG G T EHVV D EV ERA LE D ALRVVR V VLE 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 405 D KRL V P GGGA T E I ELA KQITS Y GETCP G L EQ Y AI KK FAEA F E A IPR A LAEN S G VKANEVISK L YAV H QE GNK NV GLD IEA 484
Cdd:NF041082 397 D GKV V A GGGA P E V ELA LRLRE Y AASVG G R EQ L AI EA FAEA L E I IPR T LAEN A G LDPIDALVE L RSA H EK GNK TA GLD VYT 476
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 48762932 485 E vp A V K DMLE A G ILDTYLG K YW AIK L AT N AAV TV LR V D QI I M A K 528
Cdd:NF041082 477 G -- K V V DMLE I G VVEPLRV K TQ AIK S AT E AAV MI LR I D DV I A A A 518
thermosome_arch
TIGR02339 thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
14-527
7.16e-110
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: 337.43
E-value: 7.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 14 M LKEG AKHF SG l EE A VYR NI Q A C K EL A QTTRTAY GP N GM N KM VINH L EKLFV TND A ATIL R E LEVQ HPAAKM I V MASHM Q 93
Cdd:TIGR02339 4 I LKEG TQRT SG - RD A QRN NI A A A K AV A EAVKSTL GP R GM D KM LVDS L GDVTI TND G ATIL K E MDIE HPAAKM L V EVAKT Q 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 94 EQ EVGDGT NFVL V F AG A LLE L AE E LL RIGLSVSEV IEGY EI A CR KA H EI LPNLV cc SAKNLR D I D EVSSLLR TS IM SK QY 173
Cdd:TIGR02339 83 DE EVGDGT TTAV V L AG E LLE K AE D LL EQDIHPTVI IEGY RK A AE KA L EI IDEIA -- TKISPE D R D LLKKIAY TS LT SK AS 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 174 GNEV -- F LA K L IAQ A CVSIF --- P D SGH - FNV DNI RVC K IL G SG I SSSSVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P 245
Cdd:TIGR02339 161 AEVA kd K LA D L VVE A VKQVA elr G D GKY y VDL DNI KIV K KK G GS I EDTELVE G I V VD KE V vh P G MPKR V EN AKIA LLDA P 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 246 FDGMI TE TKGTVL I KTAEELMN F SKG EE NLMDAQ V KA IA DT GANVV VTGGKVA D M A L HY AN K YN I ML VR LNS K W D LRR L C 325
Cdd:TIGR02339 241 LEVEK TE IDAKIR I TDPDQIKK F LDQ EE AMLKEM V DK IA SA GANVV ICQKGID D V A Q HY LA K AG I LA VR RVK K S D IEK L A 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 326 KTV GA --- TALPRL T P pvl EEM G HCDS V YLSE VG DTQV V VFKHE K EDG A I s TI V LRG S T DNLM D DI ER AVD D GVNTFKVL 402
Cdd:TIGR02339 321 RAT GA riv SSIDEI T E --- SDL G YAEL V EERK VG EDKM V FVEGC K NPK A V - TI L LRG G T EHVV D EL ER SIQ D ALHVVANA 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 403 TR D KRL V P GGGA T EIELA KQIT SY GETCP G L EQ Y AI KK FA E A F E A IPR A LAEN S G VKANEVISK L Y A V H QE GNKN V G LDI 482
Cdd:TIGR02339 397 LE D GKI V A GGGA V EIELA LRLR SY ARSVG G R EQ L AI EA FA D A L E E IPR I LAEN A G LDPIDALVD L R A K H EK GNKN A G INV 476
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 48762932 483 EAE vp AVK DMLE A G ILDTYLG K YW AIK L AT N AA VTV LR V D QI I M A 527
Cdd:TIGR02339 477 FTG -- EIE DMLE L G VIEPLRV K EQ AIK S AT E AA TMI LR I D DV I A A 519
thermosome_beta
NF041083 thermosome subunit beta;
15-528
1.45e-108
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 334.23
E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 15 LKEG AKHFS G l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINH L EKLFV TND A ATIL R E LE VQHPAAKM I V MASHM Q E 94
Cdd:NF041083 6 LKEG TQRTK G - RD A QRN NI M A A K AV A EAV RT TL GP K GM D KM LVDS L GDIVI TND G ATIL K E MD VQHPAAKM L V EVAKT Q D 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVIE GY EI A CR KA H EIL PNL vccs A KNL r D I D EVSS L LR --- TS IM SK 171
Cdd:NF041083 85 D EVGDGT TTAV V L AG E LL KK AEELL DQNIHPTIIAN GY RL A AE KA I EIL DEI ---- A EKV - D P D DRET L KK iae TS LT SK 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 172 QYG - NEVF LA KLIAQ A CVSIFPDSG --- HFNV DNI RVC K IL G SG I SSSSVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P 245
Cdd:NF041083 160 GVE e ARDY LA EIAVK A VKQVAEKRD gky YVDL DNI QIE K KH G GS I EDTQLIY G I V ID KE V vh P G MPKR V EN AKIA LLDA P 239
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 246 FDGMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA I AD TGANVV VTGGKVA D M A L HY AN K YN I ML VR LNS K W D LRR L C 325
Cdd:NF041083 240 LEVKK TE IDAEIR I TDPDQ L QK F LDQ EE KMLKEM V DK I KA TGANVV FCQKGID D L A Q HY LA K AG I LA VR RVK K S D MEK L A 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 326 K TV GA --- T ALPR LTP pvl E EM G HCDS V YLSE VGD TQV V VFKHE K EDG A I s TI VL RG S T DNLM D DI ERA VD D GVNTFKVL 402
Cdd:NF041083 320 K AT GA riv T NIDD LTP --- E DL G YAEL V EERK VGD DKM V FVEGC K NPK A V - TI LI RG G T EHVV D EA ERA LE D ALSVVADA 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 403 TR D KRL V P GGGA T E I ELAK QITS Y GE T CP G L EQ Y A IKK FAEA F E A IPR A LAEN S G VKANEVIS KL YAV H QE G N K NV G LDI 482
Cdd:NF041083 396 VE D GKI V A GGGA P E V ELAK RLRE Y AA T VG G R EQ L A VEA FAEA L E I IPR T LAEN A G LDPIDILV KL RSA H EK G K K WA G INV 475
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 48762932 483 EAE vp A V K DM L E A G ILDTYLG K YW AIK L AT N AA VTV LR V D QI I M AK 528
Cdd:NF041083 476 FTG -- E V V DM W E L G VIEPLRV K TQ AIK S AT E AA TMI LR I D DV I A AK 519
TCP1_delta
cd03338 TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
32-527
4.37e-83
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: 268.00
E-value: 4.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 32 NIQA C K EL A QTT RT AY GP N GM N KM VINHLEKLFV TND A ATIL RELE V Q HPAAKM I V MA S HM Q EQ E V GDGT NF V L V F AGAL 111
Cdd:cd03338 13 NIQA A K AV A DAI RT SL GP R GM D KM IQTGKGEVII TND G ATIL KQMS V L HPAAKM L V EL S KA Q DI E A GDGT TS V V V L AGAL 92
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 112 L ELA E E LL RI G LSVSEVI E GYE IA CR KA H EIL PNL vc CSAKN L R D IDEVSSLLR TS IM SK --- QY GN ev F LA KLIAQ A CV 188
Cdd:cd03338 93 L SAC E S LL KK G IHPTVIS E SFQ IA AK KA V EIL DSM -- SIPVD L N D RESLIKSAT TS LN SK vvs QY SS -- L LA PIAVD A VL 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 189 SIFPDSGHF NVD -- N IR VC K I LG SG I SSSSVLH G M VF KKE --- TE G DV T SVKD AKI AV ---- Y S C P fdgm I T ETKGTVLI 259
Cdd:cd03338 169 KVIDPATAT NVD lk D IR IV K K LG GT I EDTELVD G L VF TQK ask KA G GP T RIEK AKI GL iqfc L S P P ---- K T DMDNNIVV 244
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 260 KTAEELMNFSKG E ENLMDAQV K A I ADT G A NV VVTGGK ----- V A D M ALH YAN K YN IM L V RLNSKWDLRRL CKT V G ATALP 334
Cdd:cd03338 245 NDYAQMDRILRE E RKYILNMC K K I KKS G C NV LLIQKS ilrda V S D L ALH FLA K LK IM V V KDIEREEIEFI CKT I G CKPVA 324
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 335 RLTPPVLEEM G HC D S V YLSEV GD TQV V VFKHE K ED G AIS TI VL RGS TDNLM D DI ER AVD D GVNTFKV L TRDKR L V PGGGA 414
Cdd:cd03338 325 SIDHFTEDKL G SA D L V EEVSL GD GKI V KITGV K NP G KTV TI LV RGS NKLVL D EA ER SLH D ALCVIRC L VKKRA L I PGGGA 404
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 415 T EIE L A K Q ITSYGE T CP G L EQY AIKK FA E A F E A IP RA LAEN S G VKANEVISK L YAV H QE G N KN V G LDIEAE vp A VKDM LE 494
Cdd:cd03338 405 P EIE I A L Q LSEWAR T LT G V EQY CVRA FA D A L E V IP YT LAEN A G LNPISIVTE L RNR H AQ G E KN A G INVRKG -- A ITNI LE 482
490 500 510
....*....|....*....|....*....|...
gi 48762932 495 AGILDTY L GKYW AI K LAT NAAVTV L RV D Q I IM A 527
Cdd:cd03338 483 ENVVQPL L VSTS AI T LAT ETVRMI L KI D D I VL A 515
TCP1_alpha
cd03335 TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
23-529
4.44e-83
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451
Cd Length: 527
Bit Score: 268.38
E-value: 4.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 23 SG l EEAVYR N IQ A CKEL A QTTRTAY GP N G MN KM VINHLEKLFV TND A ATIL RE LEV Q HPAAK MI V MASHM Q EQ EVGDGT N 102
Cdd:cd03335 5 SG - QDVRTQ N VT A AMAI A NIVKSSL GP V G LD KM LVDDIGDVTI TND G ATIL KL LEV E HPAAK IL V ELAQL Q DK EVGDGT T 83
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 103 F V LVF A GA LL EL A E EL LRIGLSVSEV I E GY EI AC RK A HEILPNLVCC S AK NL r DIDEVSSLLR TS IM SK QY G NEV - F L A K 181
Cdd:cd03335 84 S V VII A AE LL KR A N EL VKQKIHPTTI I S GY RL AC KE A VKYIKEHLSI S VD NL - GKESLINVAK TS MS SK II G ADS d F F A N 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 182 LIAQ A -- C V SIFPDS G H -- FNVDNIRVC K ilgsgissssv L HG MVF K KE ------------- TE G DV T S VK D AKIA VYS c 244
Cdd:cd03335 163 MVVD A il A V KTTNEK G K tk YPIKAVNIL K ----------- A HG KSA K ES ylvngyalnctra SQ G MP T R VK N AKIA CLD - 230
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 245 p F DGMI T ET K - G T - V LIKTA E E L MNFSKG E ENLMDAQV K A I ADT GANVV V T G G KVA DM A L H Y ANKYNI M L VR LNS K W DLR 322
Cdd:cd03335 231 - F NLQK T KM K l G V q V VVTDP E K L EKIRQR E SDITKERI K K I LAA GANVV L T T G GID DM C L K Y FVEAGA M A VR RVK K E DLR 309
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 323 R LC K TV GAT ALPR L TPPVL EE ------ M G HCDS V YLSEV GD TQVVVF K HE K e DGAIST I V LRG ST D NLM D DI ER AVD D GV 396
Cdd:cd03335 310 R IA K AT GAT LVST L ANLEG EE tfdpsy L G EAEE V VQERI GD DELILI K GT K - KRSSAS I I LRG AN D FML D EM ER SLH D AL 388
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 397 NTF K VLTRDKRL VPGGGA T E IE L AKQITSYGE T CPGL EQ Y AI KK FAEA FEA IP RA LA E N SGVK A N E VIS KL Y A V H ----- 471
Cdd:cd03335 389 CVV K RTLESNSV VPGGGA V E TA L SIYLENFAT T LGSR EQ L AI AE FAEA LLV IP KT LA V N AAKD A T E LVA KL R A Y H aaaqv 468
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48762932 472 --- QEGN K NV GLD IEAEV pa V K D M LEAG I L DTYLG K YWAI K L AT N AA V T V LR V D QI I MAK P 529
Cdd:cd03335 469 kpd KKHL K WY GLD LINGK -- V R D N LEAG V L EPTVS K IKSL K F AT E AA I T I LR I D DL I KLN P 527
chap_CCT_alpha
TIGR02340 T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
18-529
2.35e-82
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: 266.59
E-value: 2.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 18 G AKHF SG l EEAVYR N IQ A CKEL A QTTR T AY GP N G MN KM VINHLEKLFV TND A ATIL RE LEV Q HPAAK MI V MASHM Q EQ EV 97
Cdd:TIGR02340 4 G GERT SG - QDVRTQ N VT A AMAI A NIVK T SL GP V G LD KM LVDDIGDVTI TND G ATIL KL LEV E HPAAK IL V ELAQL Q DR EV 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 98 GDGT NF V LVF A GA LL EL A E EL LRIGLSVSE VI E GY EI AC RK A HEILPNLVCC S AKN L RD i DEVSSLLR TS IM SK QY G NEV 177
Cdd:TIGR02340 83 GDGT TS V VII A AE LL KR A D EL VKNKIHPTS VI S GY RL AC KE A VKYIKENLSV S VDE L GR - EALINVAK TS MS SK II G LDS 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 178 - F LAKLIAQ A -- C V SIFPDS G H -- FNVDN I RVC K IL G SGISS S SVLH G MVFK -- KETEGDVTSV K D AKIA V yscp F D GMI 250
Cdd:TIGR02340 162 d F FSNIVVD A vl A V KTTNEN G E tk YPIKA I NIL K AH G KSARE S MLVK G YALN ct VASQQMPKRI K N AKIA C ---- L D FNL 237
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 251 TET K --- G T - VLIKTA E E L MNFSKG E ENLMDAQV K A I A D T GANVV V T G G KVA DM A L H Y ANKYNI M L VR LNS K W DL R R LC K 326
Cdd:TIGR02340 238 QKA K mal G V q IVVDDP E K L EQIRQR E ADITKERI K K I L D A GANVV L T T G GID DM C L K Y FVEAGA M G VR RCK K E DL K R IA K 317
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 327 TV GAT ALPR L TPPVL EE ------ M G HC D S V YLSEVG D TQVVVF K HE K EDGAI S t I V LRG ST D NLM D DI ER AVD D GVNTF K 400
Cdd:TIGR02340 318 AT GAT LVST L ADLEG EE tfeasy L G FA D E V VQERIA D DECILI K GT K KRKSA S - I I LRG AN D FML D EM ER SLH D ALCVV K 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 401 VLTRDKRL VPGGGA T E IE L AKQITSYGE T CPGL EQ Y AI KK FA E A FEA IP RA LA E N SGVKAN E VIS KL Y A V H -------- Q 472
Cdd:TIGR02340 397 RTLESNSV VPGGGA V E AA L SIYLENFAT T LGSR EQ L AI AE FA R A LLI IP KT LA V N AAKDST E LVA KL R A Y H aaaqlkpe K 476
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 48762932 473 EGN K NV GLD IEAEV pa VK D ML EAG I L DTYLG K YWAI K L AT N AA V T V LR V D QI I MAK P 529
Cdd:TIGR02340 477 KHL K WY GLD LVNGK -- IR D NK EAG V L EPTVS K VKSL K F AT E AA I T I LR I D DL I KLN P 531
chap_CCT_delta
TIGR02342 T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
32-528
2.52e-77
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: 252.78
E-value: 2.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 32 NI Q A C K EL A QTT RT AY GP N GM N KM VINHLEKLFV TND A ATIL RELE V Q HPAAKM I V MA S HM Q EQ E V GDGT NF V LVF AGAL 111
Cdd:TIGR02342 14 NI V A A K AV A DAI RT SL GP K GM D KM IQDGKGEVII TND G ATIL KQMA V L HPAAKM L V EL S KA Q DI E A GDGT TS V VIL AGAL 93
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 112 L ELA E E LL RI G LSVSEVI E GYEI A CRK A HE IL PNL vc CSAKN L R D IDEVSSLLR TS IM SK --- QY GN ev F LA K L IAQ A CV 188
Cdd:TIGR02342 94 L GAC E R LL NK G IHPTIIS E SFQS A ADE A IK IL DEM -- SIPVD L S D REQLLKSAT TS LS SK vvs QY SS -- L LA P L AVD A VL 169
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 189 SIFPDSGHF NVD -- N I R V C K I LG SG I SSSSVLH G M VF KKETE --- G DV T SVKD AKI AVYSCPFDGMI T ETKGTVLIKTAE 263
Cdd:TIGR02342 170 KVIDPENAK NVD ln D I K V V K K LG GT I DDTELIE G L VF TQKAS ksa G GP T RIEK AKI GLIQFQISPPK T DMENQIIVNDYA 249
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 264 ELMNFS K G E ENLMDAQ VK A I AD TG A NV V ----- VTGGK V A D M ALH YAN K YN IM L V RLNSKWDLRRL CKT V G ATALPRLTP 338
Cdd:TIGR02342 250 QMDRVL K E E RAYILNI VK K I KK TG C NV L liqks ILRDA V N D L ALH FLA K MK IM V V KDIEREEIEFI CKT I G CKPIASIDH 329
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 339 PVLEEM G HCDS V YLSEVGDTQVVVFKHEKED G AIS T I V L RGS TDNLM D DI ER AVD D GVNTFKV L TRDKR L VP GGGA T EIE 418
Cdd:TIGR02342 330 FTADKL G SAEL V EEVDSDGGKIIKITGIQNA G KTV T V V V RGS NKLVI D EA ER SLH D ALCVIRC L VKKRG L IA GGGA P EIE 409
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 419 L A KQITS Y GE T CP G L E Q Y AIKK FA E A F E A IP RA LAEN S G VKANE V ISK L YAV H QE G N K NV G LDIEAEVPA vk D MLE AGI L 498
Cdd:TIGR02342 410 I A RRLSK Y AR T MK G V E S Y CVRA FA D A L E V IP YT LAEN A G LNPIK V VTE L RNR H AN G E K TA G ISVRKGGIT -- N MLE EHV L 487
490 500 510
....*....|....*....|....*....|
gi 48762932 499 DTY L GKYW AI K LA TNAAVTV L RV D Q I IMAK 528
Cdd:TIGR02342 488 QPL L VTTS AI T LA SETVRSI L KI D D I VFTR 517
TCP1_epsilon
cd03339 TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
27-525
1.36e-73
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: 243.36
E-value: 1.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 27 EA VYRN I Q A C K EL A QTT RT AY GP N GM N K MVINHLEKLF VTND A ATIL RELE V Q H PA AK MI V MA S HM Q EQ E V GDGT NF V L V 106
Cdd:cd03339 23 EA HKSH I L A A K SV A NIL RT SL GP R GM D K ILVSPDGEVT VTND G ATIL EKMD V D H QI AK LL V EL S KS Q DD E I GDGT TG V V V 102
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 107 F AGALLE L AE E LL RI G LSVSEVIE GYE I AC RK A H E I L PNL vcc SA K NLRDI D EVSS L LR --- TS IM SK - QYGNEVFL A KL 182
Cdd:cd03339 103 L AGALLE Q AE K LL DR G IHPIRIAD GYE Q AC KI A V E H L EEI --- AD K IEFSP D NKEP L IQ tam TS LG SK i VSRCHRQF A EI 179
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 183 IAQ A CV S IFP - DSGHF N VDN I R V CKIL G SGISSSSVLH G M V FK K ETE -- GDVTS VKDAKIA VYS CPF DGMITE TK GTVL I 259
Cdd:cd03339 180 AVD A VL S VAD l ERKDV N FEL I K V EGKV G GRLEDTKLVK G I V ID K DFS hp QMPKE VKDAKIA ILT CPF EPPKPK TK HKLD I 259
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 260 KTA E ELMNFSKG E ENLMDAQ V KAIA D T GAN V V VTGGKVA D M A L H YANKYNIML VR LNSKWDLRRLCKTV G ATAL PR --- L 336
Cdd:cd03339 260 TSV E DYKKLQEY E QKYFREM V EQVK D A GAN L V ICQWGFD D E A N H LLLQNGLPA VR WVGGVEIELIAIAT G GRIV PR fed L 339
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 337 T P pvl E EM G HCDS V YLSEV G D T Q -- VV V FKHEKEDG A I s TI VL RG STDNLMDDIE R AVD D GVNTFKV L T RD K R L V P GGGA 414
Cdd:cd03339 340 S P --- E KL G KAGL V REISF G T T K dk ML V IEGCPNSK A V - TI FI RG GNKMIIEEAK R SLH D ALCVVRN L I RD N R I V Y GGGA 415
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 415 T EI ELAKQITSYGET C P G L EQYA IKK FA E A F E A IP R ALAENSG VKAN E VI S KLY A VH - Q E G N KNV G L D IEAE vp AVK DM L 493
Cdd:cd03339 416 A EI SCSLAVEKAADK C S G I EQYA MRA FA D A L E S IP L ALAENSG LNPI E TL S EVK A RQ v K E K N PHL G I D CLGR -- GTN DM K 493
490 500 510
....*....|....*....|....*....|..
gi 48762932 494 E AGILD T YLG K YWA I K LAT NAAVTV L RV D QI I 525
Cdd:cd03339 494 E QKVFE T LIS K KQQ I L LAT QVVKMI L KI D DV I 525
chap_CCT_epsi
TIGR02343 T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
27-525
1.92e-73
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: 243.17
E-value: 1.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 27 EA VYR NI Q A C K EL A QTT RT AY GP N GM N KM V I NHLEKLF VTND A ATIL RELE V QHPA AK MI V MA S HM Q EQ E V GDGT NF V L V 106
Cdd:TIGR02343 27 EA KKS NI A A A K SV A SIL RT SL GP K GM D KM L I SPDGDIT VTND G ATIL SQMD V DNQI AK LM V EL S KS Q DD E I GDGT TG V V V 106
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 107 F AGALLE L AEELL RI G LSVSEVIE G Y E I A C R K A H E I L PNL vcc S AKNLR D IDEVSS L LR --- TS IM SK - QYGNEVFL A KL 182
Cdd:TIGR02343 107 L AGALLE Q AEELL DK G IHPIKIAD G F E E A A R I A V E H L EEI --- S DEISA D NNNREP L IQ aak TS LG SK i VSKCHRRF A EI 183
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 183 IAQ A CVSIFP - DSGHFNV D N I R V CKIL G SGISSSSVLH G MVFK K ETEGD -- VTS V K DAKIA VYS CPF DGMITE TK GTVL I 259
Cdd:TIGR02343 184 AVD A VLNVAD m ERRDVDF D L I K V EGKV G GSLEDTKLIK G IIID K DFSHP qm PKE V E DAKIA ILT CPF EPPKPK TK HKLD I 263
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 260 KTA EE LMNFS K G E ENLMDAQVKA I ADT GAN V V VTGGKVA D M A L H YANKYNIML VR LNSKWD L RRLCKTV G ATAL PR LTPP 339
Cdd:TIGR02343 264 SSV EE YKKLQ K Y E QQKFKEMIDD I KKS GAN L V ICQWGFD D E A N H LLLQNDLPA VR WVGGQE L ELIAIAT G GRIV PR FQEL 343
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 340 VLEEM G HCDS V YLSEV G D T -- QVV V FKHE K EDG A I s TI VL RG STDNLMDDIE R AVD D GVNTFKV L TR D K R L V P GGGA T EI 417
Cdd:TIGR02343 344 SKDKL G KAGL V REISF G T T kd RML V IEQC K NSK A V - TI FI RG GNKMIIEEAK R SIH D ALCVVRN L IK D S R I V Y GGGA A EI 422
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 418 ELAKQITSYGETC PG L EQYAI KK FA E A F E A IP R ALAENSG VKANEVI S K L YAVH - Q E G N K N V G L D IEAE vp AVK DM L E AG 496
Cdd:TIGR02343 423 SCSLAVSQEADKY PG V EQYAI RA FA D A L E T IP M ALAENSG LDPIGTL S T L KSLQ l K E K N P N L G V D CLGY -- GTN DM K E QF 500
490 500
....*....|....*....|....*....
gi 48762932 497 ILD T YL GK YWA I K LAT NAAVTV L RV D QI I 525
Cdd:TIGR02343 501 VFE T LI GK KQQ I L LAT QLVRMI L KI D DV I 529
TCP1_eta
cd03340 TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
14-530
3.08e-66
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: 223.70
E-value: 3.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 14 M LKEG AKHFS G LEEAV y R NI Q AC KEL A QTT RT AY GP N GM N K MVINHLE K LFVT ND A ATIL RE L EVQ HPAAK MI V MASHM Q 93
Cdd:cd03340 4 L LKEG TDTSQ G KGQLI - S NI N AC QAI A DAV RT TL GP R GM D K LIVDGRG K VTIS ND G ATIL KL L DIV HPAAK TL V DIAKS Q 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 94 EQ EVGDGT NF V L V F AG AL L EL A EELLRI G LSVSEV I E GY EI A CRK A H E IL p NLVCCSAKN l R D ID E VSS LL ---- R T SIM 169
Cdd:cd03340 83 DA EVGDGT TS V V V L AG EF L KE A KPFIED G VHPQII I R GY RK A LQL A I E KI - KEIAVNIDK - E D KE E QRE LL ekca A T ALN 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 170 SK QYGN E - V F L AK LIAQ A CV S IFP D sgh FNV D N I RVC K IL G SGISS S SVLH G MV FKK E ----- T E GDVTSV K DA KI AVYS 243
Cdd:cd03340 161 SK LIAS E k E F F AK MVVD A VL S LDD D --- LDL D M I GIK K VP G GSLED S QLVN G VA FKK T fsyag F E QQPKKF K NP KI LLLN 237
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 244 CPFDGMITETKGT V LIKTA EE LMNFSKG E ENLMDAQVKA I ADT GANVV VTGGKVA D M A LH Y ANKYN I MLVRLNSKW DL R R 323
Cdd:cd03340 238 VELELKAEKDNAE V RVEDP EE YQAIVDA E WKIIYDKLEK I VKS GANVV LSKLPIG D L A TQ Y FADRD I FCAGRVPEE DL K R 317
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 324 LCKTV G A --- T ALPRL T PP VL eem G H C DSVYLSE VG DTQVVV F K h EKEDGAIS TI V LRG STDNLMDDI ER AVD D GVNTFK 400
Cdd:cd03340 318 VAQAT G G siq T TVSNI T DD VL --- G T C GLFEERQ VG GERYNI F T - GCPKAKTC TI I LRG GAEQFIEEA ER SLH D AIMIVR 393
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 401 VLTRDKRL V P GGGA T E I EL A K QITS Y GE T CP G LE Q YA I KK FA E A F E A IPR A L AE N S G VK A NEVIS KL YAV H QE G N - K NV G 479
Cdd:cd03340 394 RAIKNDSV V A GGGA I E M EL S K YLRD Y SR T IA G KQ Q LV I NA FA K A L E I IPR Q L CD N A G FD A TDILN KL RQK H AQ G G g K WY G 473
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 48762932 480 L DI EA E vp AVK D ML EA GILDTY L G K YW A IKL AT N AA VTV L R VD QI I MAKPA 530
Cdd:cd03340 474 V DI NN E -- GIA D NF EA FVWEPS L V K IN A LTA AT E AA CLI L S VD ET I KNPKS 522
chap_CCT_eta
TIGR02345 T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
14-528
2.96e-64
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: 218.47
E-value: 2.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 14 M LKEG AKHFS G LEEAV y R NI Q AC KEL A QTTR T AY GP N GM N K MVINHLE K LFVT ND A ATIL RE L EVQ HPAAK MI V MASHM Q 93
Cdd:TIGR02345 6 L LKEG TDTSQ G KGQLI - S NI N AC VAI A EALK T TL GP R GM D K LIVGSNG K ATIS ND G ATIL KL L DIV HPAAK TL V DIAKS Q 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 94 EQ EVGDGT NF V LVF AG A LL EL A EELLRI G LSVSEV I EG Y EI A CRK A H E ILPNLVCCSAKNLRDID E V - SSLLR T SIM SK Q 172
Cdd:TIGR02345 85 DA EVGDGT TS V TIL AG E LL KE A KPFIEE G VHPQLI I RC Y RE A LSL A V E KIKEIAVTIDEEKGEQR E L l EKCAA T ALS SK L 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 173 YGNEV - F LA K L I AQ A CV S I fp D SGHFNVDN I RVC K IL G SGISS S SVLH G MV FKK E ----- T E GDVTSVKDA KI AVYSCPF 246
Cdd:TIGR02345 165 ISHNK e F FS K M I VD A VL S L -- D RDDLDLKL I GIK K VQ G GALED S QLVN G VA FKK T fsyag F E QQPKKFANP KI LLLNVEL 242
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 247 DGMITETKGTVLIKTA E ELMNFSKG E ENLMDAQVKA I ADT GANVV VTGGKVA D M A LH Y ANKYN I MLVRLN S KW DL R R LC K 326
Cdd:TIGR02345 243 ELKAEKDNAEIRVEDV E DYQAIVDA E WAIIFRKLEK I VES GANVV LSKLPIG D L A TQ Y FADRD I FCAGRV S AE DL K R VI K 322
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 327 TV G A --- TALPR L TPP VL eem G H C DSVYLSEV G DTQVVV F K h EKEDGAIS TI V LRG STDNLMDDI ER AVD D GVNTFKVLT 403
Cdd:TIGR02345 323 AC G G siq STTSD L EAD VL --- G T C ALFEERQI G SERYNY F T - GCPHAKTC TI I LRG GAEQFIEEA ER SLH D AIMIVRRAL 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 404 RD K RL V P GGGA T E I EL A K QITS Y GE T CP G LE Q YA I KK FA E A F E A IPR A L A EN S G VKAN E VIS KL YAV H QE G N K NV G L DI E 483
Cdd:TIGR02345 399 KN K KI V A GGGA I E M EL S K CLRD Y SK T ID G KQ Q LI I NA FA K A L E I IPR Q L C EN A G FDSI E ILN KL RSR H AK G G K WY G V DI N 478
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 48762932 484 A E vp AVK D ML EA GILDTY L G K YW A I K L A TN AA V T V L R VD QI I MAK 528
Cdd:TIGR02345 479 T E -- DIG D NF EA FVWEPA L V K IN A L K A A FE AA C T I L S VD ET I TNP 521
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
26-535
4.70e-64
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 217.25
E-value: 4.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 26 E E A VYR NI QAC K E LA QTTRTAY GP N G M N K M vinh L E K L F ---- V TND AA TI LR E L E VQH P ---- A A KMIVMASHMQEQ E V 97
Cdd:COG0459 9 E D A RRA NI RGV K A LA DAVKVTL GP K G R N V M ---- L V K S F gdpt I TND GV TI AK E I E LED P fenm G A QLVKEVASKTND E A 84
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 98 GDGT NFVL V F AGALL ELAEE L LRI G LSVSEVIE G YEI A CR KA H E I L PNL vccs AK NLR D ID E VSSLLRT S I mskqy GNEV 177
Cdd:COG0459 85 GDGT TTAT V L AGALL KEGLK L VAA G ANPTDIKR G IDK A VE KA V E E L KKI ---- AK PVD D KE E LAQVATI S A ----- NGDE 155
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 178 FLAK LIA Q A CVSIFP D s G HFN V D nirvck ILGSGISSSS V LH GM V F K K E --------- T E GDVTSVKD A K I A vyscpfdg 248
Cdd:COG0459 156 EIGE LIA E A MEKVGK D - G VIT V E ------ EGKGLETELE V VE GM Q F D K G ylspyfvtd P E KMPAELEN A Y I L -------- 220
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 249 m I T ET K gtvl I KTAEE L M nfskgeenlmd AQVKAI A DT G ANVVVTGGKVADM AL HYANKYN I ML V R ----------- LNS 317
Cdd:COG0459 221 - L T DK K ---- I SSIQD L L ----------- PLLEKV A QS G KPLLIIAEDIDGE AL ATLVVNG I RG V L rvvavkapgfg DRR 284
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 318 K WD L RRLCKTV G ATALPRLTPPV LE EM ----- G HCDS V YLSE vg D TQVV V fk HEKEDGAIST I VLRGS T DNLMDDIE R A V 392
Cdd:COG0459 285 K AM L EDIAILT G GRVISEDLGLK LE DV tlddl G RAKR V EVDK -- D NTTI V -- EGAGNPKAIV I LVGAA T EVEVKERK R R V 360
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 393 D D GVNTFKVLTRDK r L VPGGGA TEIEL A KQITSYGETCP G L EQ YA I KKF A E A F EA IP R AL AEN S G VKANE V IS K LY A vhq 472
Cdd:COG0459 361 E D ALHATRAAVEEG - I VPGGGA ALLRA A RALRELAAKLE G D EQ LG I EIV A R A L EA PL R QI AEN A G LDGSV V VE K VR A --- 436
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48762932 473 EGN K NV G L D IEAEV pa VK DMLEAG IL D TYLG K YW A IKL A TNA A VTV L RVDQI I MA KP AGGPKP 535
Cdd:COG0459 437 AKD K GF G F D AATGE -- YV DMLEAG VI D PAKV K RS A LQN A ASV A GLI L TTEAV I AD KP EKEEAA 497
TCP1_gamma
cd03337 TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
14-525
3.68e-61
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: 209.07
E-value: 3.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 14 M L KEGA K HF SG l EE A VYR NIQA C K EL A QTT RT AY GP NG M N KM VINHLEKLFV TND AAT ILRE LE V Q HPAAK MIVMA S HM Q 93
Cdd:cd03337 4 V L NQNT K RE SG - RK A QLG NIQA A K TV A DVI RT CL GP RA M L KM LLDPMGGIVL TND GNA ILRE ID V A HPAAK SMIEL S RT Q 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 94 EQ EVGDGT NF V LVF AG AL L EL AE EL L RI G LSVSEV I EG Y EI A CRK A HE IL PN lvc C S AK - NLR D IDEVSSLLRTS I MS K Q 172
Cdd:cd03337 83 DE EVGDGT TS V IIL AG EI L AV AE PF L ER G IHPTVI I KA Y RK A LED A LK IL EE --- I S IP v DVN D RAQMLKIIKSC I GT K F 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 173 YGNE - VFLAK L IAQ A -- C V SIFPDSGHFNV D --- NIR V C KI L G SG I SS S S VL H G MVFK K eteg DVT S ------ VKDAK I A 240
Cdd:cd03337 160 VSRW s DLMCN L ALD A vk T V AVEENGRKKEI D ikr YAK V E KI P G GE I ED S R VL D G VMLN K ---- DVT H pkmrrr IENPR I V 235
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 241 VYS CP FD gmitetkgtvliktaeelmnfskgeenlmdaqvkaiadtga NV V V T GGK V A D M A L HY AN K YN I MLV R LNS K W D 320
Cdd:cd03337 236 LLD CP LE ----------------------------------------- YL V I T EKG V S D L A Q HY LV K AG I TAL R RVR K T D 274
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 321 LR R LCKTV GAT ALP R lt P PV L E E -- M G HCDSVYLSEVGDTQVVV F KH E KE D GAIS TI V LRG STDNLMDDI ER AVD D GVNT 398
Cdd:cd03337 275 NN R IARAC GAT IVN R -- P EE L T E sd V G TGAGLFEVKKIGDEYFT F IT E CK D PKAC TI L LRG ASKDVLNEV ER NLQ D AMAV 352
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 399 FKVLTRDKR LVPGGGATE IELAKQITSYGETCP G L EQ YAI K KF A E A F E A IPR A LA E N S G VKANEVISK L Y A V H - Q EG N KN 477
Cdd:cd03337 353 ARNIILNPK LVPGGGATE MAVSHALSEKAKSIE G V EQ WPY K AV A S A L E V IPR T LA Q N C G ANVIRTLTE L R A K H a Q GE N ST 432
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 48762932 478 V G L D ie A E VPAVK DM L E A GI L D TYLG K YWAI K L A TN AA VTV LR V D Q I I 525
Cdd:cd03337 433 W G I D -- G E TGDIV DM K E L GI W D PLAV K AQTY K T A IE AA CML LR I D D I V 478
chap_CCT_gamma
TIGR02344 T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
32-525
1.50e-60
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: 208.44
E-value: 1.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 32 NIQA C K EL A QTT RT AY GP NG M N KM VINHLEKLFV TND AAT ILRE LE V Q HPAAK MIVMA S HM Q EQ EVGDGT NF V LVF AG AL 111
Cdd:TIGR02344 21 NIQA A K AV A DII RT CL GP RS M L KM LLDPMGGIVM TND GNA ILRE ID V A HPAAK SMIEL S RT Q DE EVGDGT TS V IIL AG EM 100
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 112 L EL AE EL L RIGLSVSEV I EG Y EI A CRK A HEI L PNLVC cs AKNLR D IDEVSS L LRTS I MS K --- QYGNEVFLAK L I A QAC V 188
Cdd:TIGR02344 101 L SV AE PF L EQNIHPTVI I RA Y RK A LDD A LSV L EEISI -- PVDVN D DAAMLK L IQSC I GT K fvs RWSDLMCDLA L D A VRT V 178
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 189 S i FPDS G HFNV D --- NIR V C KI L G SG I SS S S VL H G MVFK K eteg DVT S ------ VKDAK I AVYS CP FDGMIT E TKGTVL I 259
Cdd:TIGR02344 179 Q - RDEN G RKEI D ikr YAK V E KI P G GD I ED S C VL K G VMIN K ---- DVT H pkmrry IENPR I VLLD CP LEYKKG E SQTNIE I 253
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 260 KTA E ELMNFSKG EE NLMDAQVKA I ADTGANV V V T GGK V A D M A L HY AN K Y NI MLV R LNS K W D LR R LCKTV GAT ALP R LTPP 339
Cdd:TIGR02344 254 TKE E DWNRILQM EE EYVQLMCED I IAVKPDL V I T EKG V S D L A Q HY LL K A NI TAI R RVR K T D NN R IARAC GAT IVN R PEEL 333
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 340 VLEEM G - H C DSVYLSEV GD t QVVV F KH E KE D GAIS TI V LRG STDNLMDDI ER AVD D GVNTFKVLTR D KR LVPGGGATE IE 418
Cdd:TIGR02344 334 RESDV G t G C GLFEVKKI GD - EYFT F IT E CK D PKAC TI L LRG ASKDILNEV ER NLQ D AMAVARNVLL D PK LVPGGGATE MA 412
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 419 LAKQI T SYGETCP G L EQ YAIKKF A E A F E A IPR A LA E N S G VKANEVISK L Y A V H - QE G N KNV G ld I EA E VPAVK DM L E A GI 497
Cdd:TIGR02344 413 VSVAL T EKSKKLE G V EQ WPYRAV A D A L E I IPR T LA Q N C G ANVIRTLTE L R A K H a QE N N CTW G -- I DG E TGKIV DM K E K GI 490
490 500
....*....|....*....|....*...
gi 48762932 498 LDTYLG K YWAI K L A TNA A VTV LR V D Q I I 525
Cdd:TIGR02344 491 WEPLAV K LQTY K T A IES A CLL LR I D D I V 518
PTZ00212
PTZ00212 T-complex protein 1 subunit beta; Provisional
13-529
1.22e-59
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 206.42
E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 13 Q M LK E GA KHFS G l E E A VYRNIQACKEL A QTTR T AY GP N GM N K MVINHL E ----- KLF VTND A ATIL RELEVQH PAAK MI V 87
Cdd:PTZ00212 9 Q V LK Q GA QEEK G - E T A RLQSFVGAIAV A DLVK T TL GP K GM D K ILQPMS E gprsg NVT VTND G ATIL KSVWLDN PAAK IL V 87
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 88 MA S HM Q EQ EVGDGT NF V L V F AG A LL EL AE E LL RIGLSVSEV IEG YEI A CRK A HE ilp N L VCCSAKNLR D IDEVSSL L --- 164
Cdd:PTZ00212 88 DI S KT Q DE EVGDGT TS V V V L AG E LL RE AE K LL DQKIHPQTI IEG WRM A LDV A RK --- A L EEIAFDHGS D EEKFKED L lni 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 165 - RT SIM SK -- QYGNEV F l AKL IAQ A CVSI fpd S G HF N V D N I RVC K IL G SGISS S SVLH G MVFK K E - TE G DVTSVKDA KI A 240
Cdd:PTZ00212 165 a RT TLS SK ll TVEKDH F - AKL AVD A VLRL --- K G SG N L D Y I QII K KP G GTLRD S YLED G FILE K K i GV G QPKRLENC KI L 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 241 V YSC P F D GMITETK G T - V LIKTA E ELMNFSKG E ENL M DAQ V KA I ADT G A NV VVTGGKVADMALHYANKYN IM LVR l NSKW 319
Cdd:PTZ00212 241 V ANT P M D TDKIKIY G A k V KVDSM E KVAEIEAA E KEK M KNK V DK I LAH G C NV FINRQLIYNYPEQLFAEAG IM AIE - HADF 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 320 D - LR RL CKTV GA TALPRLTP P VLEEM GHCD SVYLSEV G DTQVVV F KHEKEDG A i S TIVLRG STDNLM D DI ER AVD D GVNT 398
Cdd:PTZ00212 320 D g ME RL AAAL GA EIVSTFDT P EKVKL GHCD LIEEIMI G EDKLIR F SGCAKGE A - C TIVLRG ASTHIL D EA ER SLH D ALCV 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 399 FKVLTR D K R L V P GGG AT E IEL A KQITSYGETCP G LEQY AI KK FA E A FEA IP RAL A E N S G VKAN E VI SKL Y A V H QE GNK NV 478
Cdd:PTZ00212 399 LSQTVK D T R V V L GGG CS E MLM A NAVEELAKKVE G KKSL AI EA FA K A LRQ IP TII A D N G G YDSA E LV SKL R A E H YK GNK TA 478
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 48762932 479 G L D I E AEVPA vk DM L E A GI LDT Y LG K YWAIKL AT N AA VTV LRVD Q II MAK P 529
Cdd:PTZ00212 479 G I D M E KGTVG -- DM K E L GI TES Y KV K LSQLCS AT E AA EMI LRVD D II RCA P 527
TCP1_beta
cd03336 TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
15-529
4.36e-55
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: 193.70
E-value: 4.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 15 LK E GA KHFS G l E E A VYRNIQACKELAQTTR T AY GP N GM N K MVI -- NHLEKLF VTND A ATIL RELE V QH PAAK MI V MA S HM 92
Cdd:cd03336 2 LK D GA QEEK G - E T A RLSSFVGAIAIGDLVK T TL GP K GM D K ILQ sv GRSGGVT VTND G ATIL KSIG V DN PAAK VL V DI S KV 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 93 Q EQ EVGDGT NF V L V F A GA LL EL AE E L LRIGLSVSEV IEGY EI A CRK A H E I L PNLVCC --- SAKNL R D id EVSSLL RT SIM 169
Cdd:cd03336 81 Q DD EVGDGT TS V T V L A AE LL RE AE K L VAQKIHPQTI IEGY RM A TAA A R E A L LSSAVD hss DEEAF R E -- DLLNIA RT TLS 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 170 SK -- QYGN E V F l A K L IAQ A CVSI fpd S G HF N V D N I RVC K I LG SGISS S SVLH G MVFK K ETE - GDVTSVKD AKI AVYSC P F 246
Cdd:cd03336 159 SK il TQDK E H F - A E L AVD A VLRL --- K G SG N L D A I QII K K LG GSLKD S YLDE G FLLD K KIG v NQPKRIEN AKI LIANT P M 234
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 247 D GMITETK G T - V LIKTAEELMNFSKG E ENL M DAQ V KA I ADT G A N VVVTGGKVADMALHYANKYN IM LVRLNSKWDLR RL C 325
Cdd:cd03336 235 D TDKIKIF G A k V RVDSTAKVAEIEEA E KEK M KNK V EK I LKH G I N CFINRQLIYNYPEQLFADAG IM AIEHADFDGVE RL A 314
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 326 KTV G ATALPRLTP P V L EEM G H C DSVYLSEV G DTQVVV F KHEKEDG A i S TIVLRG STDNLM D DI ER AVD D GVNTFKVLTR D 405
Cdd:cd03336 315 LVT G GEIASTFDH P E L VKL G T C KLIEEIMI G EDKLIR F SGVAAGE A - C TIVLRG ASQQIL D EA ER SLH D ALCVLAQTVK D 393
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 406 K R L V P GGG AT E IEL AK QITSYGETC PG LEQY AI KK FA E A FEAI P RAL A E N S G VKAN E VISK L Y A V H QE GN KNV GLD I ea E 485
Cdd:cd03336 394 T R V V L GGG CS E MLM AK AVEELAKKT PG KKSL AI EA FA K A LRQL P TII A D N A G YDSA E LVAQ L R A A H YN GN TTA GLD M -- R 471
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 48762932 486 VPA V K DM L E A GI LDTYLG K YWAIKL A TN AA VTV LRVD Q II MAK P 529
Cdd:cd03336 472 KGT V G DM K E L GI TESFKV K RQVLLS A SE AA EMI LRVD D II KCA P 515
chaperonin_like
cd03333 chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
158-405
6.05e-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: 176.12
E-value: 6.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 158 DEVSSLLR TS IM SK QYGNEV FL A KL IAQ A CVSIF PD SGHFNVDN I R V C KI L G SGISS S SVLH G M VF K K ETEGDV -- TSVK 235
Cdd:cd03333 2 ELLLQVAT TS LN SK LSSWDD FL G KL VVD A VLKVG PD NRMDDLGV I K V E KI P G GSLED S ELVV G V VF D K GYASPY mp KRLE 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 236 D AKI AVYS CP FD gmitetkgtvliktaeelmnfskgeenlmdaqvkaiadtga N VV VTGGKVA D M ALHY AN K YN IM L VR L 315
Cdd:cd03333 82 N AKI LLLD CP LE ----------------------------------------- Y VV IAEKGID D L ALHY LA K AG IM A VR R 120
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 316 NS K W DL R R LCKTV GAT ALPR L TPPVL E EM G HCDS V YLSEV G DTQVVVFKHE K e D G AIS TI V LRG S T DNLM D DIE R AVD D G 395
Cdd:cd03333 121 VK K E DL E R IARAT GAT IVSS L EDLTP E DL G TAEL V EETKI G EEKLTFIEGC K - G G KAA TI L LRG A T EVEL D EVK R SLH D A 199
250
....*....|
gi 48762932 396 VNTFKVLTRD 405
Cdd:cd03333 200 LCAVRAAVEE 209
chap_CCT_beta
TIGR02341 T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
44-529
1.39e-50
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: 181.60
E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 44 RTAY GP N GM N K MVI -- NHLEKLF VTND A ATIL RELE V QH PAAK MI V MA S HM Q EQ EVGDGT NF V L V F A GA LL EL AE E L LRI 121
Cdd:TIGR02341 31 KSTL GP K GM D K ILQ ss SSDASIM VTND G ATIL KSIG V DN PAAK VL V DM S KV Q DD EVGDGT TS V T V L A AE LL RE AE K L INQ 110
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 122 GLSVSEV I E GY EI A CRK A HEI L PNLVCCSAKNLRDI - DEVSSLL RT SIM SK QYG - NEVFL A K L IAQ A CVSI fpd S G HF N V 199
Cdd:TIGR02341 111 KIHPQTI I A GY RE A TKA A RDA L LKSAVDNGSDEVKF r QDLMNIA RT TLS SK ILS q HKDHF A Q L AVD A VLRL --- K G SG N L 187
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 200 DN I RVC K I LG SGISS S SVLH G MVF - KK ETEGDVTSVKD AKI AVYSCPF D GMITETK G T - V LIKTAEELMNFSKG E ENL M D 277
Cdd:TIGR02341 188 EA I QII K K LG GSLAD S YLDE G FLL d KK IGVNQPKRIEN AKI LIANTGM D TDKVKIF G S r V RVDSTAKVAELEHA E KEK M K 267
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 278 AQ V KA I ADT G A N VVVTGGKVADMALHYANKYNI M LVRLNSKWDLR RL CKTV G ATALPRLTP P V L EEM G H CD SVYLSEV G D 357
Cdd:TIGR02341 268 EK V EK I LKH G I N CFINRQLIYNYPEQLFADAGV M AIEHADFEGVE RL ALVT G GEIVSTFDH P E L VKL G S CD LIEEIMI G E 347
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 358 TQVVV F KHE K E d G AIS TIVLRG S T DNLM D DI ER AVD D GVNTFKVLTRDK R L V P GGG AT E IELA K QI T SYGETC PG L E QY A 437
Cdd:TIGR02341 348 DKLLK F SGV K L - G EAC TIVLRG A T QQIL D EA ER SLH D ALCVLSQTVKES R T V L GGG CS E MLMS K AV T QEAQRT PG K E AL A 426
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 438 IKK FA E A FEAI P RAL A E N S G VKAN E VISK L Y A V H QE GN KNV GLD IEA ev PAVK DM LEA GI LDT Y LG K YWAIKL A TN AA VT 517
Cdd:TIGR02341 427 VEA FA R A LRQL P TII A D N A G FDSA E LVAQ L R A A H YN GN TTM GLD MNE -- GTIA DM RQL GI TES Y KV K RAVVSS A AE AA EV 504
490
....*....|..
gi 48762932 518 V LRVD Q II M A K P 529
Cdd:TIGR02341 505 I LRVD N II K A A P 516
chap_CCT_zeta
TIGR02347 T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
28-527
4.62e-46
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: 169.53
E-value: 4.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 28 A VYR NI Q A CKE L AQTTR T AY GP N G MN KM VINHLEKLFV T N D AATI L R E LEV QHP A A K MI VM A SHM Q EQEV GDGT NFVLVF 107
Cdd:TIGR02347 17 A LMM NI N A ARG L QDVLK T NL GP K G TL KM LVSGAGDIKL T K D GNVL L N E MQI QHP T A S MI AR A ATA Q DDIT GDGT TSTVLL 96
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 108 A G A LL EL AE ELLRI G LSVSEVI EG Y EIA CRK A HEI L PNLVCCSAKNL r D IDEVSSLL RTS IMS K QYGNEV - F L AKLIAQ A 186
Cdd:TIGR02347 97 I G E LL KQ AE RYILE G VHPRIIT EG F EIA RKE A LQF L DKFKVKKEDEV - D REFLLNVA RTS LRT K LPADLA d Q L TEIVVD A 175
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 187 CVS I FP D SGHFNVDNIRVCKILGSGISSSSVLH G M V FKKETE -- GDVTS VK D A K I AVYSCPFDGMI TE TKGTVLIKT AE E 264
Cdd:TIGR02347 176 VLA I KK D GEDIDLFMVEIMEMKHKSATDTTLIR G L V LDHGAR hp DMPRR VK N A Y I LTCNVSLEYEK TE VNSGFFYSS AE Q 255
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 265 LMNFS K G E ENLM D AQ VK A I AD --------- TGANV VV TGG K VA D - MA L HYAN K YN IM LV R LNSKWDLR RL CKTV G AT AL - 333
Cdd:TIGR02347 256 REKLV K A E RKFV D DR VK K I IE lkkkvcgks PDKGF VV INQ K GI D p PS L DLLA K EG IM AL R RAKRRNME RL TLAC G GE AL n 335
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 334 -- PR LTP pvl E EM G HCDS VY LSEV G DTQVV v F KH E KEDGAIS TI VLR G ST D NLMDD I ER AV D DG VNTF K VLTR DK RL VPG 411
Cdd:TIGR02347 336 sv ED LTP --- E CL G WAGL VY ETTI G EEKYT - F IE E CKNPKSC TI LIK G PN D HTIAQ I KD AV R DG LRAV K NAIE DK CV VPG 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 412 G GA T EI ELAKQITS Y GETCP G LEQYAIKK FA E A FEA IP RA LAENSG VK A NEVIS KL YAV H Q EG NKN VG L D IEAEV P AVKD 491
Cdd:TIGR02347 412 A GA F EI AAYRHLKE Y KKSVK G KAKLGVEA FA N A LLV IP KT LAENSG FD A QDTLV KL EDE H D EG GEV VG V D LNTGE P IDPE 491
490 500 510
....*....|....*....|....*....|....*.
gi 48762932 492 ml EA GI L D T Y LG K YWA I KL AT NA A VTV L R VD QIIM A 527
Cdd:TIGR02347 492 -- IK GI W D N Y RV K KQL I QS AT VI A SQL L L VD EVMR A 525
TCP1_zeta
cd03342 TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
27-527
9.30e-43
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: 159.35
E-value: 9.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 27 E A VYR NI Q A C K E L AQTTR T AY GP N G MN KM VINHLEKLFV T N D AATI L R E LEV QHP A A K MI VM A SHM Q EQEV GDGT NFVLV 106
Cdd:cd03342 12 Q A LAV NI S A A K G L QDVLK T NL GP K G TL KM LVSGAGDIKL T K D GNVL L S E MQI QHP T A S MI AR A ATA Q DDIT GDGT TSNVL 91
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 107 FA G A LL EL AE ELLRI G LSVSEVI EG Y E I A CR KA HEI L PNLVC c SAKNLR D IDEVS S LL RTS IMS K QYGNEV - F L AKLIAQ 185
Cdd:cd03342 92 LI G E LL KQ AE RYIQE G VHPRIIT EG F E L A KN KA LKF L ESFKV - PVEIDT D RELLL S VA RTS LRT K LHADLA d Q L TEIVVD 170
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 186 A CVS I FPDSGHFNVDNIRV ckilgsgissssvlhg M VFKKETEG D VTSVK ---- D akiav YSCPFDG M ITETK g TVL I K T 261
Cdd:cd03342 171 A VLA I YKPDEPIDLHMVEI ---------------- M QMQHKSDS D TKLIR glvl D ----- HGARHPD M PKRVE - NAY I L T 228
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 262 AEELMNFS K G E E N lmdaqvkaiad T G -- AN VV VTGGKVADMA L HYAN K YN I MLV R LNSKWDLR RL CKTV G AT A LPR --- L 336
Cdd:cd03342 229 CNVSLEYE K T E V N ----------- S G ff YS VV INQKGIDPPS L DMLA K EG I LAL R RAKRRNME RL TLAC G GV A MNS vdd L 297
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 337 T P PV L eem G HCDS VY LSEV G DTQVV v F KHEKEDGAIS TI VLR G ST D NLMDD I ER A VD DG VNTF K VLTR DK RL VPG G GA T E 416
Cdd:cd03342 298 S P EC L --- G YAGL VY ERTL G EEKYT - F IEGVKNPKSC TI LIK G PN D HTITQ I KD A IR DG LRAV K NAIE DK CV VPG A GA F E 373
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 417 IE L AKQITSYGETCP G LEQYAIKK FA E A FEA IP RA LAENSG VKAN E VIS KL YAVHQ EG NKNV G L D IEAEV P AVK dm LEA G 496
Cdd:cd03342 374 VA L YAHLKEFKKSVK G KAKLGVQA FA D A LLV IP KT LAENSG LDVQ E TLV KL QDEYA EG GQVG G V D LDTGE P MDP -- ESE G 451
490 500 510
....*....|....*....|....*....|.
gi 48762932 497 I L D T Y LG K YWAIKL AT NA A VTV L R VD Q II M A 527
Cdd:cd03342 452 I W D N Y SV K RQILHS AT VI A SQL L L VD E II R A 482
GroEL
cd03344 GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
391-499
2.22e-06
GroEL_like type I chaperonin. 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. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460
Cd Length: 520
Bit Score: 50.15
E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 391 AV DD G V ntfkvltrdkrl VPGGG ATEIELAKQITSYGETC p G L E QYA I KKFAE A F EA IP R AL AEN S GV KANE V IS K LY av 470
Cdd:cd03344 403 AV EE G I ------------ VPGGG VALLRASPALDKLKALN - G D E KLG I EIVRR A L EA PL R QI AEN A GV DGSV V VE K VL -- 467
90 100
....*....|....*....|....*....
gi 48762932 471 hq E GNKNV G L D ie A EVPAVK DM L EAGI L D 499
Cdd:cd03344 468 -- E SPDGF G Y D -- A ATGEYV DM I EAGI I D 492
Fab1_TCP
cd03334 TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
219-393
2.71e-06
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: 49.14
E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 219 H G M VF K K E -- TEGDVTSV K DAK I AVYSC P FDGMIT E T K GTV L ikta EELM nfs KG E ENLMDAQ V KA I ADTGAN V VVTGGK 296
Cdd:cd03334 67 D G V VF T K N va HKRMPSKI K NPR I LLLQG P LEYQRV E N K LLS L ---- DPVI --- LQ E KEYLKNL V SR I VALRPD V ILVEKS 139
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 297 V ADM A LHYANKYN I M LV r LN S K WD - L R R LCKTV GA TALPR ---- LT P P V L eem G H C D S V ---- Y LS E V G DTQVVV F -- KH 365
Cdd:cd03334 140 V SRI A QDLLLEAG I T LV - LN V K PS v L E R ISRCT GA DIISS mddl LT S P K L --- G T C E S F rvrt Y VE E H G RSKTLM F fe GC 215
170 180
....*....|....*....|....*...
gi 48762932 366 E KE D G A is TI V LRG STDNLMDDIE R A V D 393
Cdd:cd03334 216 P KE L G C -- TI L LRG GDLEELKKVK R V V E 241
groEL
CHL00093 chaperonin GroEL
367-529
5.83e-05
chaperonin GroEL
Pssm-ID: 177025
Cd Length: 529
Bit Score: 45.87
E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 367 K ED G AIST I VLRGS T DNL M D D IERAVD D GV N TF K VLT r DKRL VPGGGAT EIE L AKQITSYGET - CPGL E QYAIKKF A E A F 445
Cdd:CHL00093 370 K LS G GVAV I KVGAA T ETE M K D KKLRLE D AI N AT K AAV - EEGI VPGGGAT LVH L SENLKTWAKN n LKED E LIGALIV A R A I 448
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 446 E A IPRAL AEN S G VKANEV I S K L yavh QE GNKNV G LD ie A EVPAVKD M L EAGI L D TYLGKYW A IKL A TNA A VTV L RVDQ II 525
Cdd:CHL00093 449 L A PLKRI AEN A G KNGSVI I E K V ---- QE QDFEI G YN -- A ANNKFVN M Y EAGI I D PAKVTRS A LQN A ASI A SMI L TTEC II 522
....
gi 48762932 526 MA K P 529
Cdd:CHL00093 523 VD K K 526
groEL
PRK00013 chaperonin GroEL; Reviewed
409-499
2.09e-04
chaperonin GroEL; Reviewed
Pssm-ID: 234573
Cd Length: 542
Bit Score: 43.96
E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48762932 409 VPGGG ATEIEL A KQITSYGET c P G L E QYA I KKFAE A F EA IP R AL AEN S G VKANE V IS K lya V HQEGN K NV G LD ie A EVPA 488
Cdd:PRK00013 411 VPGGG VALLRA A PALEALKGL - N G D E ATG I NIVLR A L EA PL R QI AEN A G LEGSV V VE K --- V KNGKG K GY G YN -- A ATGE 484
90
....*....|.
gi 48762932 489 VK DM L EAGI L D 499
Cdd:PRK00013 485 YV DM I EAGI I D 495
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
