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T-complex protein 1 subunit theta [Mus musculus]
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: 898.69
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 10 G F A QM LK D G AK HFSGLEEAV YR NI Q ACKEL A Q T TRT AY GPNGMNKMVIN R LEKLFVTNDAATILRELEVQHPAAK MI VMA 89
Cdd:TIGR02346 1 G I A SL LK E G YR HFSGLEEAV IK NI E ACKEL S Q I TRT SL GPNGMNKMVIN H LEKLFVTNDAATILRELEVQHPAAK LL VMA 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 90 S H MQE Q E V GDGTN F VLV F AG A LL EL AEEL L R I GL SV SE V I S GYE I A C KKA H EIL P ELV CCSA K N LRD V 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 L KKA M EIL E ELV VWEV K D LRD K DE LIKA L KA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 170 SKQYG S E T FLA K L I AQAC VSIF P - DSG NFNVDNIRVCKILG SGIYS 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 SKQYG N E D FLA Q L V AQAC STVL P k NPQ NFNVDNIRVCKILG GSLSN 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 126723461 249 MI TETKGTVLI KT AEEL M N F SKGEEN LMD A QV KAIA GT G A NVIVTGG K V A D I ALHY A NKYNIM LVRLN SK WD LRRLCKTV 328
Cdd:TIGR02346 241 AT TETKGTVLI HN AEEL L N Y SKGEEN QIE A MI KAIA DS G V NVIVTGG S V G D M ALHY L NKYNIM VLKIP SK FE LRRLCKTV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 329 GAT A LP K L TP P VQ 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 LP R L 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 126723461 409 V PG G GATEIELA KQI T S YGE TC PGL E QYAIKKFAEAFE A IPR A LAEN S G VK ANEVI S KLY SV 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 KLY AA H KK GNK SK G I DIEAE SDG 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126723461 489 VKD ML EA S I L D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAKPAGGPKPP S GK 539
Cdd:TIGR02346 481 VKD AS EA G I 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: 898.69
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 10 G F A QM LK D G AK HFSGLEEAV YR NI Q ACKEL A Q T TRT AY GPNGMNKMVIN R LEKLFVTNDAATILRELEVQHPAAK MI VMA 89
Cdd:TIGR02346 1 G I A SL LK E G YR HFSGLEEAV IK NI E ACKEL S Q I TRT SL GPNGMNKMVIN H LEKLFVTNDAATILRELEVQHPAAK LL VMA 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 90 S H MQE Q E V GDGTN F VLV F AG A LL EL AEEL L R I GL SV SE V I S GYE I A C KKA H EIL P ELV CCSA K N LRD V 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 L KKA M EIL E ELV VWEV K D LRD K DE LIKA L KA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 170 SKQYG S E T FLA K L I AQAC VSIF P - DSG NFNVDNIRVCKILG SGIYS 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 SKQYG N E D FLA Q L V AQAC STVL P k NPQ NFNVDNIRVCKILG GSLSN 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 126723461 249 MI TETKGTVLI KT AEEL M N F SKGEEN LMD A QV KAIA GT G A NVIVTGG K V A D I ALHY A NKYNIM LVRLN SK WD LRRLCKTV 328
Cdd:TIGR02346 241 AT TETKGTVLI HN AEEL L N Y SKGEEN QIE A MI KAIA DS G V NVIVTGG S V G D M ALHY L NKYNIM VLKIP SK FE LRRLCKTV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 329 GAT A LP K L TP P VQ 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 LP R L 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 126723461 409 V PG G GATEIELA KQI T S YGE TC PGL E QYAIKKFAEAFE A IPR A LAEN S G VK ANEVI S KLY SV 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 KLY AA H KK GNK SK G I DIEAE SDG 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126723461 489 VKD ML EA S I L D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAKPAGGPKPP S GK 539
Cdd:TIGR02346 481 VKD AS EA G I 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: 819.16
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 20 K H F SGLEEAV Y RNI Q ACKEL A Q T TRT A YGPNGMNKMVIN R LEKLFVT 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 YGPNGMNKMVIN H LEKLFVT S DAATILRELEVQHPAAK LL VMAS Q MQE E E I GD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 100 GTN F V L V F AG A LLE L AEELLR I GL SV SE V I S GYE I A C KKA H EIL P ELV CCSAKN LR DVD EVS SL L R T S I M SKQYG S E T FL 179
Cdd:cd03341 81 GTN L V V V L AG E LLE K AEELLR M GL HP SE I I E GYE K A L KKA L EIL E ELV VYKIED LR NKE EVS KA L K T A I A SKQYG N E D FL 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 180 AK L I A Q AC V S IF P - DS GNFNVDNIRV C KILG SGIYS 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 GNFNVDNIRV 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 126723461 259 iktaeelmnfskgeenlmdaqvkaiag T G A NVIV T GG K V A D I ALHY A NKY N IM LVRL NSK WD LRRLC K TVGAT A LP K L TP 338
Cdd:cd03341 230 --------------------------- I G V NVIV A GG S V G D L ALHY C NKY G IM VIKI NSK FE LRRLC R TVGAT P LP R L GA 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 339 P VQ 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 126723461 419 LAK QITS YGE TC PGLEQYAIKKFAEAFE AI PR A LAEN S G VK A N EV I S K LY SV HQ E GNK NV G L DIE AEVPAV KD ML EA S I L 498
Cdd:cd03341 363 LAK KLKE YGE KT PGLEQYAIKKFAEAFE VV PR T LAEN A G LD A T EV L S E LY AA HQ K GNK SA G V DIE SGDEGT KD AK EA G I F 442
490 500 510
....*....|....*....|....*....|
gi 126723461 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
0e+00
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain]
Cd Length: 489
Bit Score: 520.99
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 39 LA QTT RT AY GP N GM N KM VI N RLEKLF 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 126723461 119 L RI G LSVSEV I S GYE I A CK KA H EIL PELVCCSAKNL r D VDEVSSLL RTS IM SK QYGS E T - FLAKL IAQ A CVS I FPDS G N F 197
Cdd:pfam00118 81 L AA G VHPTTI I E GYE 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 126723461 198 NVD NI R V C KILG SGIYS 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 126723461 276 MDAQ V KA I AGT G A NV I V TGGKVA D I ALH YAN K YN IM LV R LNS K W DL R RL C K TV GA T A LPK L TPPVQEEM G HCDS V YLSEV 355
Cdd:pfam00118 240 ILEI V EK I IDS G V NV V V 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 126723461 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 126723461 436 Y AI KK FAEA F E A IP RA LAEN S G VKAN EV ISK L YSV H QE G N K NV G L D I E AE vp AVK DM L EA SIL 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 RAA H AS G E K HA G I D V E TG -- EII DM K EA GVV D PLKV K RQ A L K S AT E AA 476
490
....*....|...
gi 126723461 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
5.02e-117
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 355.73
E-value: 5.02e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 LK D G AKHF SG l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINR L EKLFV TND AA TIL R E LEVQ HPAAKMIV MASHM Q E 94
Cdd:NF041082 6 LK E G 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 126723461 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVIS GY EI A CK KA H EIL P E L vccs A KNLR -- D VDEVSSLLR T SIMS K Q 172
Cdd:NF041082 85 D EVGDGT TTAV V L AG E LL KK AEELL DQDIHPTIIAE GY RL A AE KA L EIL D E I ---- A IKVD pd D KETLKKIAA T AMTG K G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 173 YGS - ETF LA K L IAQ A CVSIFPDS G NF NVD -- NI R V C K IL G SG I YS S SVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P FD 247
Cdd:NF041082 161 AEA a KDK 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 126723461 248 GMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA IA GT GANV IVTGGKVA D I 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 IA DS GANV VFCQKGID 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 126723461 328 V GA --- T ALPK L T P pvq 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 126723461 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 Y S V 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 R S A H EK GNK TA GLD VYT 476
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 126723461 485 E vp A V K DMLE ASILDTYLG 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 IGVVEPLRV 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
3.58e-109
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 335.77
E-value: 3.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 LK D G AKHFS G l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINR L EKLFV TND A ATIL R E LE VQHPAAKM I V MASHM Q E 94
Cdd:NF041083 6 LK E G 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 126723461 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVIS GY EI A CK KA H EIL P E L vccs A K -- NLR D VDEVSSLLR TS IM SK Q 172
Cdd:NF041083 85 D EVGDGT TTAV V L AG E LL KK AEELL DQNIHPTIIAN GY RL A AE KA I EIL D E I ---- A E kv DPD D RETLKKIAE TS LT SK G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 173 YGSE - TF LA KLIAQ A CVSIFPDSG --- NFNV DNI RVC K IL G SG I YSSSVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P F 246
Cdd:NF041083 161 VEEA r DY 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 L 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 247 DGMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA I AG TGANV IVTGGKVA D I A L HY AN K YN I ML VR LNS K W D LRR L C K 326
Cdd:NF041083 241 EVKK TE IDAEIR I TDPDQ L QK F LDQ EE KMLKEM V DK I KA TGANV VFCQKGID D L A Q HY LA K AG I LA VR RVK K S D MEK L A K 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 327 TV GA --- T ALPK LTP pvq 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 GVNTFKVLT 403
Cdd:NF041083 321 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 ALSVVADAV 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 404 R 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 Y S V H QE G N K NV G LDIE 483
Cdd:NF041083 397 E 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 R S A H EK G K K WA G INVF 476
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 126723461 484 AE vp A V K DM L E ASILDTYLG K YW AIK L AT N AA VTV LR V D QI I M AK 528
Cdd:NF041083 477 TG -- E V V DM W E LGVIEPLRV 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
4.02e-64
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 217.25
E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 26 E E A VYR NI QAC K E LA QTTRTAY GP N G M N K M VINRLEKLFV TND AA TI LR E L E VQH P ---- A A KMIVMASHMQEQ E V GDGT 101
Cdd:COG0459 9 E D A RRA NI RGV K A LA DAVKVTL GP K G R N V M LVKSFGDPTI TND GV TI AK E I E LED P fenm G A QLVKEVASKTND E A GDGT 88
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 102 NFVL V F AGALL ELAEE L LRI G LSVSEVIS G YEI A CK KA H E I L PEL vccs AK NLR D VD E VSSLLRT S IMSKQ ygset FLAK 181
Cdd:COG0459 89 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 ANGDE ----- EIGE 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 182 LIA Q A CVSIFP D s G NFN V D nirvcki L G S G IYSSS - V LH GM V F K K E --------- T E GDVTSVKD A K I A vyscpfdgm I T 251
Cdd:COG0459 160 LIA E A MEKVGK D - G VIT V E ------- E G K G LETEL e V VE GM Q F D K G ylspyfvtd P E KMPAELEN A Y I L --------- L T 222
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 252 ET K gtvl I KTAEE L M nfskgeenlmd AQVKAI A GT G ANVIVTGGKVADI AL HYANKYN I ML V R ----------- LNS K WD 320
Cdd:COG0459 223 DK K ---- I SSIQD L L ----------- PLLEKV A QS G KPLLIIAEDIDGE AL ATLVVNG I RG V L rvvavkapgfg DRR K AM 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 321 L RRLCKTV G ATA -------- L PKL T P pvq EEM G HCDS V YLSE vg D TQVV V fk HEKEDGAIST I VLRGS T DNLMDDIE R A V 392
Cdd:COG0459 288 L EDIAILT G GRV isedlglk L EDV T L --- DDL 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 126723461 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 LYS 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 VRA --- 436
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126723461 473 EGN K NV G L D IEAEV pa VK DMLEA SIL 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 DMLEA GVI 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
3.32e-63
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 216.05
E-value: 3.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 13 Q M LK D GA KHFS G l E E A VYRNIQACKEL A QTTR T AY GP N GM N K MVI ----- N R LEKLF 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 ILQ pmseg P R SGNVT VTND G ATIL KSVWLDN PAAK IL V 87
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 88 MA S HM Q EQ EVGDGT NF V L V F AG A LL EL AE E LL RIGLSVSEV I S G YEI A CKK A HEI L P E LVCCSAKNLRDVD E vs S LL --- 164
Cdd:PTZ00212 88 DI S KT Q DE EVGDGT TS V V V L AG E LL RE AE K LL DQKIHPQTI I E G WRM A LDV A RKA L E E IAFDHGSDEEKFK E -- D LL nia 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 165 RT SIM SK -- QYGSET F l AKL IAQ A CVSI fpd S G NF N V D N I RVC K IL G SGIYS S SVLH G MVFK K E - TE G DVTSVKDA KI A V 241
Cdd:PTZ00212 166 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 V 241
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 242 YSC P F D GMITETK G T - V LIKTA E ELMNFSKG E ENL M DAQ V KA I AGT G A NV IVTGGKVADIALHYANKYN IM LVR l NSKW D 320
Cdd:PTZ00212 242 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 D 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 321 - LR RL CKTV GA TALPKLTP P VQEEM GHCD SVYLSEV G DTQVVV F KHEKEDG A i S TIVLRG STDNLM D DI ER AVD D GVNTF 399
Cdd:PTZ00212 321 g ME RL AAAL GA EIVSTFDT P EKVKL GHCD LIEEIMI G EDKLIR F SGCAKGE A - C TIVLRG ASTHIL D EA ER SLH D ALCVL 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 400 KVLTR 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 YSV H QE GNK NV G 479
Cdd:PTZ00212 400 SQTVK 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 RAE H YK GNK TA G 479
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126723461 480 L D I E AEVPA vk DM L E AS I LDT Y LG K YWAIKL AT N AA VTV LRVD Q II MAK P 529
Cdd:PTZ00212 480 I D M E KGTVG -- DM K E LG I 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: 898.69
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 10 G F A QM LK D G AK HFSGLEEAV YR NI Q ACKEL A Q T TRT AY GPNGMNKMVIN R LEKLFVTNDAATILRELEVQHPAAK MI VMA 89
Cdd:TIGR02346 1 G I A SL LK E G YR HFSGLEEAV IK NI E ACKEL S Q I TRT SL GPNGMNKMVIN H LEKLFVTNDAATILRELEVQHPAAK LL VMA 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 90 S H MQE Q E V GDGTN F VLV F AG A LL EL AEEL L R I GL SV SE V I S GYE I A C KKA H EIL P ELV CCSA K N LRD V 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 L KKA M EIL E ELV VWEV K D LRD K DE LIKA L KA SI S 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 170 SKQYG S E T FLA K L I AQAC VSIF P - DSG NFNVDNIRVCKILG SGIYS 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 SKQYG N E D FLA Q L V AQAC STVL P k NPQ NFNVDNIRVCKILG GSLSN 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 126723461 249 MI TETKGTVLI KT AEEL M N F SKGEEN LMD A QV KAIA GT G A NVIVTGG K V A D I ALHY A NKYNIM LVRLN SK WD LRRLCKTV 328
Cdd:TIGR02346 241 AT TETKGTVLI HN AEEL L N Y SKGEEN QIE A MI KAIA DS G V NVIVTGG S V G D M ALHY L NKYNIM VLKIP SK FE LRRLCKTV 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 329 GAT A LP K L TP P VQ 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 LP R L 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 126723461 409 V PG G GATEIELA KQI T S YGE TC PGL E QYAIKKFAEAFE A IPR A LAEN S G VK ANEVI S KLY SV 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 KLY AA H KK GNK SK G I DIEAE SDG 480
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126723461 489 VKD ML EA S I L D TYLG K Y WAIKLAT N AAVTVLRVDQIIMAKPAGGPKPP S GK 539
Cdd:TIGR02346 481 VKD AS EA G I 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: 819.16
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 20 K H F SGLEEAV Y RNI Q ACKEL A Q T TRT A YGPNGMNKMVIN R LEKLFVT 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 YGPNGMNKMVIN H LEKLFVT S DAATILRELEVQHPAAK LL VMAS Q MQE E E I GD 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 100 GTN F V L V F AG A LLE L AEELLR I GL SV SE V I S GYE I A C KKA H EIL P ELV CCSAKN LR DVD EVS SL L R T S I M SKQYG S E T FL 179
Cdd:cd03341 81 GTN L V V V L AG E LLE K AEELLR M GL HP SE I I E GYE K A L KKA L EIL E ELV VYKIED LR NKE EVS KA L K T A I A SKQYG N E D FL 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 180 AK L I A Q AC V S IF P - DS GNFNVDNIRV C KILG SGIYS 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 GNFNVDNIRV 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 126723461 259 iktaeelmnfskgeenlmdaqvkaiag T G A NVIV T GG K V A D I ALHY A NKY N IM LVRL NSK WD LRRLC K TVGAT A LP K L TP 338
Cdd:cd03341 230 --------------------------- I G V NVIV A GG S V G D L ALHY C NKY G IM VIKI NSK FE LRRLC R TVGAT P LP R L GA 282
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 339 P VQ 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 126723461 419 LAK QITS YGE TC PGLEQYAIKKFAEAFE AI PR A LAEN S G VK A N EV I S K LY SV HQ E GNK NV G L DIE AEVPAV KD ML EA S I L 498
Cdd:cd03341 363 LAK KLKE YGE KT PGLEQYAIKKFAEAFE VV PR T LAEN A G LD A T EV L S E LY AA HQ K GNK SA G V DIE SGDEGT KD AK EA G I F 442
490 500 510
....*....|....*....|....*....|
gi 126723461 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
0e+00
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain]
Cd Length: 489
Bit Score: 520.99
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 39 LA QTT RT AY GP N GM N KM VI N RLEKLF 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 126723461 119 L RI G LSVSEV I S GYE I A CK KA H EIL PELVCCSAKNL r D VDEVSSLL RTS IM SK QYGS E T - FLAKL IAQ A CVS I FPDS G N F 197
Cdd:pfam00118 81 L AA G VHPTTI I E GYE 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 126723461 198 NVD NI R V C KILG SGIYS 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 126723461 276 MDAQ V KA I AGT G A NV I V TGGKVA D I ALH YAN K YN IM LV R LNS K W DL R RL C K TV GA T A LPK L TPPVQEEM G HCDS V YLSEV 355
Cdd:pfam00118 240 ILEI V EK I IDS G V NV V V 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 126723461 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 126723461 436 Y AI KK FAEA F E A IP RA LAEN S G VKAN EV ISK L YSV H QE G N K NV G L D I E AE vp AVK DM L EA SIL 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 RAA H AS G E K HA G I D V E TG -- EII DM K EA GVV D PLKV K RQ A L K S AT E AA 476
490
....*....|...
gi 126723461 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
1.29e-170
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: 490.79
E-value: 1.29e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 20 K HFSGL EEA VYR NI Q A C K E LA QTTR T AY GP N GM N KM VINR 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 126723461 100 GT NF V L V F AG A LL EL AE E LL RI G LSVS E V I S GYE I A CK KA H EIL P E LVCC sa KNLR D VD E VSSLLR TS IM SK Q - Y G SET 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 K E IAVP -- IDVE D RE E LLKVAT TS LN SK L v S G GDD F 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 179 L AK L IAQ A CVSIFPDS G NFNVDN IRV C K IL G SGIYS 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 126723461 257 vliktaeelmnfskgeenlmdaqvkaiagtga N V IVTGGKVA D I ALHY AN K YN IM L VR LNS K W DL R R LC K TV GAT ALPK L 336
Cdd:cd00309 230 -------------------------------- Y V VIAEKGID D E ALHY LA K LG IM A VR RVR K E DL E R IA K AT GAT IVSR L 277
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 337 TPPVQ 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 126723461 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 YSV H Q EG NK N V G L D I E AE vp AVK DM L EA S 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 RAK H A EG GG N A G G D V E TG -- EIV DM K EA G 434
490 500 510
....*....|....*....|....*....|
gi 126723461 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
thermosome_alpha
NF041082 thermosome subunit alpha;
15-528
5.02e-117
thermosome subunit alpha;
Pssm-ID: 469009
Cd Length: 518
Bit Score: 355.73
E-value: 5.02e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 LK D G AKHF SG l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINR L EKLFV TND AA TIL R E LEVQ HPAAKMIV MASHM Q E 94
Cdd:NF041082 6 LK E G 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 126723461 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVIS GY EI A CK KA H EIL P E L vccs A KNLR -- D VDEVSSLLR T SIMS K Q 172
Cdd:NF041082 85 D EVGDGT TTAV V L AG E LL KK AEELL DQDIHPTIIAE GY RL A AE KA L EIL D E I ---- A IKVD pd D KETLKKIAA T AMTG K G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 173 YGS - ETF LA K L IAQ A CVSIFPDS G NF NVD -- NI R V C K IL G SG I YS S SVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P FD 247
Cdd:NF041082 161 AEA a KDK 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 126723461 248 GMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA IA GT GANV IVTGGKVA D I 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 IA DS GANV VFCQKGID 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 126723461 328 V GA --- T ALPK L T P pvq 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 126723461 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 Y S V 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 R S A H EK GNK TA GLD VYT 476
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 126723461 485 E vp A V K DMLE ASILDTYLG 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 IGVVEPLRV K TQ AIK S AT E AAV MI LR I D DV I A A A 518
cpn60
cd03343 cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
15-528
8.30e-117
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: 355.42
E-value: 8.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 LK D G AKHF SG l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINR L EKLFV TND A ATIL R E LEVQ HPAAKM I V MASHM Q E 94
Cdd:cd03343 4 LK E G 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 126723461 95 Q EVGDGT NFVL V F AG A LLE L AE E LL RIGLSVSEV I S GY EI A CK KA H E I L P E LV cc SAKNLR D V D EVSSLLR TS IMS K QYG 174
Cdd:cd03343 83 E EVGDGT TTAV V L AG E LLE K AE D LL DQNIHPTVI I E GY RL A AE KA L E L L D E IA -- IKVDPD D K D TLRKIAK TS LTG K GAE 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 175 SET - F LA K L IAQ A CVSIF --- PDSGNFNV DNI RVC K IL G SGIYSSSVLH 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 126723461 249 MI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA IA G TGANV IVTGGKVA D I 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 IA D TGANV VFCQKGID 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 126723461 329 GA --- T ALPK LTP pvq 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 126723461 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 YSV 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 RAA H EK GNKN A GLD VYTG 476
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 126723461 486 VPA vk DMLE ASILDTYLG K YW AIK L AT N AA VTV LR V D QI I M AK 528
Cdd:cd03343 477 EVV -- DMLE KGVIEPLRV K KQ AIK S AT E AA TMI LR I D DV I A AK 517
thermosome_arch
TIGR02339 thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
14-527
6.51e-111
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: 340.12
E-value: 6.51e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 14 M LK D G AKHF SG l EE A VYR NI Q A C K EL A QTTRTAY GP N GM N KM VINR L EKLFV TND A ATIL R E LEVQ HPAAKM I V MASHM Q 93
Cdd:TIGR02339 4 I LK E G 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 126723461 94 EQ EVGDGT NFVL V F AG A LLE L AE E LL RIGLSVSEV I S GY EI A CK KA H EI LP E LV cc SAKNLR D V D EVSSLLR TS IM SK QY 173
Cdd:TIGR02339 83 DE EVGDGT TTAV V L AG E LLE K AE D LL EQDIHPTVI I E GY RK A AE KA L EI ID E IA -- TKISPE D R D LLKKIAY TS LT SK AS 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 174 GSET -- F LA K L IAQ A CVSI ---- FPDSGNFNV DNI RVC K IL G SG I YSSSVLH 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 VKQV aelr GDGKYYVDL 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 126723461 246 FDGMI TE TKGTVL I KTAEELMN F SKG EE NLMDAQ V KA IA GT GANV IVTGGKVA D I 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 GANV VICQKGID 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 126723461 326 KTV GA TALPKLTPPVQEEM G HCDS V YLSE VG DTQV V VFKHE K EDG A I s TI V LRG S T DNLM D DI ER AVD D GVNTFKVLTR D 405
Cdd:TIGR02339 321 RAT GA RIVSSIDEITESDL G YAEL V EERK VG EDKM V FVEGC K NPK A V - TI L LRG G T EHVV D EL ER SIQ D ALHVVANALE D 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 406 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 YSV H QE GNKN V G LDIEAE 485
Cdd:TIGR02339 400 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 RAK H EK GNKN A G INVFTG 479
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 126723461 486 vp AVK DMLE ASILDTYLG K YW AIK L AT N AA VTV LR V D QI I M A 527
Cdd:TIGR02339 480 -- EIE DMLE LGVIEPLRV K EQ AIK S AT E AA TMI LR I D DV I A A 519
thermosome_beta
NF041083 thermosome subunit beta;
15-528
3.58e-109
thermosome subunit beta;
Pssm-ID: 469010
Cd Length: 519
Bit Score: 335.77
E-value: 3.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 LK D G AKHFS G l EE A VYR NI Q A C K EL A QTT RT AY GP N GM N KM VINR L EKLFV TND A ATIL R E LE VQHPAAKM I V MASHM Q E 94
Cdd:NF041083 6 LK E G 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 126723461 95 Q EVGDGT NFVL V F AG A LL EL AEELL RIGLSVSEVIS GY EI A CK KA H EIL P E L vccs A K -- NLR D VDEVSSLLR TS IM SK Q 172
Cdd:NF041083 85 D EVGDGT TTAV V L AG E LL KK AEELL DQNIHPTIIAN GY RL A AE KA I EIL D E I ---- A E kv DPD D RETLKKIAE TS LT SK G 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 173 YGSE - TF LA KLIAQ A CVSIFPDSG --- NFNV DNI RVC K IL G SG I YSSSVLH G M V FK KE T -- E G DVTS V KD AKIA VYSC P F 246
Cdd:NF041083 161 VEEA r DY 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 L 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 247 DGMI TE TKGTVL I KTAEE L MN F SKG EE NLMDAQ V KA I AG TGANV IVTGGKVA D I A L HY AN K YN I ML VR LNS K W D LRR L C K 326
Cdd:NF041083 241 EVKK TE IDAEIR I TDPDQ L QK F LDQ EE KMLKEM V DK I KA TGANV VFCQKGID D L A Q HY LA K AG I LA VR RVK K S D MEK L A K 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 327 TV GA --- T ALPK LTP pvq 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 GVNTFKVLT 403
Cdd:NF041083 321 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 ALSVVADAV 396
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 404 R 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 Y S V H QE G N K NV G LDIE 483
Cdd:NF041083 397 E 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 R S A H EK G K K WA G INVF 476
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 126723461 484 AE vp A V K DM L E ASILDTYLG K YW AIK L AT N AA VTV LR V D QI I M AK 528
Cdd:NF041083 477 TG -- E V V DM W E LGVIEPLRV 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
7.10e-88
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: 280.33
E-value: 7.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 32 NIQA C K EL A QTT RT AY GP N GM N KM VINRLEKLFV 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 126723461 112 L ELA E E LL RI G LSVSEVISGYE IA C KKA H EIL PEL vc CSAKN L R D VDEVSSLLR TS IM SK --- QY G S et F LA KLIAQ A CV 188
Cdd:cd03338 93 L SAC E S LL KK G IHPTVISESFQ IA A KKA V EIL DSM -- SIPVD L N D RESLIKSAT TS LN SK vvs QY S S -- L LA PIAVD A VL 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 189 SIFPDSGNF NVD -- N IR VC K I LG SG I YSSSVLH G M VF KKE --- TE G DV T SVKD AKI AVYSCPFDGMI T ETKGTVLIKTAE 263
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 GLIQFCLSPPK T DMDNNIVVNDYA 248
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 264 ELMNFSKG E ENLMDAQV K A I AGT G A NV IVTGGK ----- V A D I ALH YAN K YN IM L V RLNSKWDLRRL CKT V G ATALPKLTP 338
Cdd:cd03338 249 QMDRILRE 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 CKPVASIDH 328
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 339 PVQEEM 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 T EIE 418
Cdd:cd03338 329 FTEDKL 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 P EIE 408
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 419 L A K Q ITSYGE T CP G L EQY AIKK FA E A F E A IP RA LAEN S G VKANEVISK L YSV H QE G N KN V G LDIEAE vp A VKDM LE ASIL 498
Cdd:cd03338 409 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 ENVV 486
490 500
....*....|....*....|....*....
gi 126723461 499 DTY L GKYW AI K LAT NAAVTV L RV D Q I IM A 527
Cdd:cd03338 487 QPL 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
2.68e-84
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: 271.47
E-value: 2.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 23 SG l EEAVYR N IQ A CKEL A QTTRTAY GP N G MN KM VINRLEKLFV 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 126723461 103 F V LVF A GA LL EL A E EL LRIGLSVSEV ISGY EI ACK K A HEILP E LVCC S AK NL - RDV de VSSLLR TS IM SK QY G SET - F L A 180
Cdd:cd03335 84 S V VII A AE LL KR A N EL VKQKIHPTTI ISGY RL ACK E A VKYIK E HLSI S VD NL g KES -- LINVAK TS MS SK II G ADS d F F A 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 181 KLIAQ A -- C V SIFPDS G N -- FNVDNIRVC K IL G SGIYS S SVLH G MVFK -- KETE G DV T S VK D AKIA VYS cp F DGMI T ET K 254
Cdd:cd03335 162 NMVVD A il A V KTTNEK G K tk YPIKAVNIL K AH G KSAKE S YLVN G YALN ct RASQ G MP T R VK N AKIA CLD -- F NLQK T KM K 239
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 255 - G T - V LIKTA E E L MNFSKG E ENLMDAQV K A I AGT GANV IV T G G KVA D IA L H Y ANKYNI M L VR LNS K W DLRR LC K TV GAT A 332
Cdd:cd03335 240 l G V q V VVTDP E K L EKIRQR E SDITKERI K K I LAA GANV VL T T G GID D MC L K Y FVEAGA M A VR RVK K E DLRR IA K AT GAT L 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 333 LPK L TPPVQ EE ------ M G HCDS V YLSEV GD TQVVVF K HE K e DGAIST I V LRG ST D NLM D DI ER AVD D GVNTF K VLTRDK 406
Cdd:cd03335 320 VST 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 ALCVV K RTLESN 398
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 407 RL 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 YSV H -------- QEGN K NV 478
Cdd:cd03335 399 SV 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 RAY H aaaqvkpd KKHL K WY 478
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126723461 479 GLD IEAEV pa V K D M LEA SI L DTYLG K YWAI K L AT N AA V T V LR V D QI I MAK P 529
Cdd:cd03335 479 GLD LINGK -- V R D N LEA GV 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
5.54e-84
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: 270.82
E-value: 5.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 18 G AKHF SG l EEAVYR N IQ A CKEL A QTTR T AY GP N G MN KM VINRLEKLFV 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 126723461 98 GDGT NF V LVF A GA LL EL A E EL LRIGLSVSE VISGY EI ACK K A HEILP E LVCC S AKN L RD v DEVSSLLR TS IM SK QY G SET 177
Cdd:TIGR02340 83 GDGT TS V VII A AE LL KR A D EL VKNKIHPTS VISGY RL ACK E A VKYIK E NLSV S VDE L GR - EALINVAK TS MS SK II G LDS 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 178 - F LAKLIAQ A CVSIFPDSG N ---- FNVDN I RVC K IL G SGIYS S SVLH G MVFK -- KETEGDVTSV K D AKIA V yscp F D GMI 250
Cdd:TIGR02340 162 d F FSNIVVD A VLAVKTTNE N getk 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 126723461 251 TET K --- G T - VLIKTA E E L MNFSKG E ENLMDAQV K A I AGT GANV IV T G G KVA D IA 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 LDA GANV VL T T G GID D MC 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 126723461 327 TV GAT ALPK L TPPVQ 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 126723461 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 YSV 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 RAY H aaaqlkpe K 476
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 126723461 473 EGN K NV GLD IEAEV pa VK D ML EA SI 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 EA GV 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
3.43e-82
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: 265.49
E-value: 3.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 32 NI Q A C K EL A QTT RT AY GP N GM N KM VINRLEKLFV 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 126723461 112 L ELA E E LL RI G LSVSEVISGYEI A CKK A HE IL P E L vc CSAKN L R D VDEVSSLLR TS IM SK --- QY G S et F LA K L IAQ A CV 188
Cdd:TIGR02342 94 L GAC E R LL NK G IHPTIISESFQS A ADE A IK IL D E M -- SIPVD L S D REQLLKSAT TS LS SK vvs QY S S -- L LA P L AVD A VL 169
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 189 SIFPDSGNF NVD -- N I R V C K I LG SG I YSSSVLH 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 126723461 264 ELMNFS K G E ENLMDAQ VK A I AG TG A NV I ----- VTGGK V A D I ALH YAN K YN IM L V RLNSKWDLRRL CKT V G ATALPKLTP 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 126723461 339 PVQEEM 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 126723461 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 YSV H QE G N K NV G LDIEAEVPA vk D MLE ASI 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 126723461 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
chap_CCT_epsi
TIGR02343 T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
16-525
8.78e-76
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: 249.33
E-value: 8.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 16 K D GA K HFS GLE e A VYR NI Q A C K EL A QTT RT AY GP N GM N KM V I NRLEKLF VTND A ATIL RELE V QHPA AK MI V MA S HM Q EQ 95
Cdd:TIGR02343 17 Q D NK K RLK GLE - A 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 95
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 96 E V GDGT NF V L V F AGALLE L AEELL RI G LSVSEVIS G Y E I A CKK A H E I L P E L vcc S AKNLR D VDEVSS L LR --- TS IM SK - 171
Cdd:TIGR02343 96 E I GDGT TG V V V L AGALLE Q AEELL DK G IHPIKIAD G F E E A ARI A V E H L E E I --- S DEISA D NNNREP L IQ aak TS LG SK i 172
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 172 QYGSETFL A KLIAQ A CVSIFP - DSGNFNV D N I R V CKIL G SGIYSSSVLH G MVFK K ETEGD -- VTS V K DAKIA VYS CPF DG 248
Cdd:TIGR02343 173 VSKCHRRF A EIAVD A VLNVAD m ERRDVDF D L I K V EGKV G GSLEDTKLIK G IIID K DFSHP qm PKE V E DAKIA ILT CPF EP 252
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 249 MITE TK GTVL I KTA EE LMNFS K G E ENLMDAQVKA I AGT GAN VIVTGGKVA D I A L H YANKYNIML VR LNSKWD L RRLCKTV 328
Cdd:TIGR02343 253 PKPK TK HKLD I SSV EE YKKLQ K Y E QQKFKEMIDD I KKS GAN LVICQWGFD D E A N H LLLQNDLPA VR WVGGQE L ELIAIAT 332
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 329 G ATAL P KLTPPVQEEM 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 406
Cdd:TIGR02343 333 G GRIV P RFQELSKDKL 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 411
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 407 R L V P GGGA T EI ELAKQITSYGETC PG L EQYAI KK FA E A F E A IP R ALAENSG VKANEVI S K L Y S VH - Q E G N K N V G L D IEAE 485
Cdd:TIGR02343 412 R I V Y GGGA A EI SCSLAVSQEADKY PG V EQYAI RA FA D A L E T IP M ALAENSG LDPIGTL S T L K S LQ l K E K N P N L G V D CLGY 491
490 500 510 520
....*....|....*....|....*....|....*....|
gi 126723461 486 vp AVK DM L E ASILD T YL GK YWA I K LAT NAAVTV L RV D QI I 525
Cdd:TIGR02343 492 -- GTN DM K E QFVFE T LI GK KQQ I L LAT QLVRMI L KI D DV I 529
TCP1_epsilon
cd03339 TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
27-525
4.36e-74
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455
Cd Length: 526
Bit Score: 244.52
E-value: 4.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 27 EA VYRN I Q A C K EL A QTT RT AY GP N GM N K MVINRLEKLF 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 126723461 107 F AGALLE L AE E LL RI G LSVSEVIS GYE I ACK K A H E I L P E L vcc SA K NLRDV D EVSS L LR --- TS IM SK - QYGSETFL A KL 182
Cdd:cd03339 103 L AGALLE Q AE K LL DR G IHPIRIAD GYE Q ACK I A V E H L E E I --- 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 126723461 183 IAQ A CV S IFP - DSGNF N VDN I R V CKIL G SGIYSSSVLH 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 126723461 260 KTA E ELMNFSKG E ENLMDAQ V KAIAGT GAN VIVTGGKVA D I A L H YANKYNIML VR LNSKWDLRRLCKTV G ATAL P KLTPP 339
Cdd:cd03339 260 TSV E DYKKLQEY E QKYFREM V EQVKDA GAN LVICQWGFD D E A N H LLLQNGLPA VR WVGGVEIELIAIAT G GRIV P RFEDL 339
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 340 VQ 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 T EI 417
Cdd:cd03339 340 SP 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 A EI 418
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 418 ELAKQITSYGET C P G L EQYA IKK FA E A F E A IP R ALAENSG VKAN E VI S KLYSVH - Q E G N KNV G L D IEAE vp AVK DM L E AS 496
Cdd:cd03339 419 SCSLAVEKAADK C S G I EQYA MRA FA D A L E S IP L ALAENSG LNPI E TL S EVKARQ v K E K N PHL G I D CLGR -- GTN DM K E QK 496
490 500
....*....|....*....|....*....
gi 126723461 497 ILD T YLG K YWA I K LAT NAAVTV L RV D QI I 525
Cdd:cd03339 497 VFE T LIS K KQQ I L LAT QVVKMI L KI D DV I 525
TCP1_eta
cd03340 TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
14-530
7.80e-70
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: 233.33
E-value: 7.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 14 M LK D G AKHFS G LEEAV y R NI Q AC KEL A QTT RT AY GP N GM N K MVINRLE K LFVT ND A ATIL RE L EVQ HPAAK MI V MASHM Q 93
Cdd:cd03340 4 L LK E G 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 126723461 94 EQ EVGDGT NF V L V F AG AL L EL A EELLRI G LSVSEV I S GY EI A CKK A H E ILP E L vccs A K N L -- R D VD E VSS LL ---- R T S 167
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 KIK E I ---- A V N I dk E D KE E QRE LL ekca A T A 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 168 IM SK QYG SE - T F L AK LIAQ A CV S IFP D sgn FNV D N I RVC K IL G SGIYS S SVLH G MV FKK E ----- T E GDVTSV K DA KI AV 241
Cdd:cd03340 159 LN SK LIA SE 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 LL 235
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 242 YSCPFDGMITETKGT V LIKTA EE LMNFSKG E ENLMDAQVKA I AGT GANV IVTGGKVA D I A LH Y ANKYN I MLVRLNSKW DL 321
Cdd:cd03340 236 LNVELELKAEKDNAE V RVEDP EE YQAIVDA E WKIIYDKLEK I VKS GANV VLSKLPIG D L A TQ Y FADRD I FCAGRVPEE DL 315
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 322 R R LCKTV G ATALPKLTPPVQEEM G H C DSVYLSE VG DTQVVV F K h EKEDGAIS TI V LRG STDNLMDDI ER AVD D GVNTFKV 401
Cdd:cd03340 316 K R VAQAT G GSIQTTVSNITDDVL G T C GLFEERQ VG GERYNI F T - GCPKAKTC TI I LRG GAEQFIEEA ER SLH D AIMIVRR 394
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 402 LTRDKRL 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 YSV H QE G N - K NV G L 480
Cdd:cd03340 395 AIKNDSV 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 V 474
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126723461 481 DI EA E vp AVK D ML EA SILDTY L G K YW A IKL AT N AA VTV L R VD QI I MAKPA 530
Cdd:cd03340 475 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
2.30e-68
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: 229.26
E-value: 2.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 14 M LK D G AKHFS G LEEAV y R NI Q AC KEL A QTTR T AY GP N GM N K MVINRLE K LFVT ND A ATIL RE L EVQ HPAAK MI V MASHM Q 93
Cdd:TIGR02345 6 L LK E G 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 126723461 94 EQ EVGDGT NF V LVF AG A LL EL A EELLRI G LSVSEV I SG Y EI A CKK A H E ILP E LVCCSAKNLRDVD 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 KIK E IAVTIDEEKGEQR E L l EKCAA T ALS SK L 164
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 173 YGSET - F LA K L I AQ A CV S I fp D SGNFNVDN I RVC K IL G SGIYS 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 126723461 247 DGMITETKGTVLIKTA E ELMNFSKG E ENLMDAQVKA I AGT GANV IVTGGKVA D I A LH Y ANKYN I MLVRLN S KW DL R R LC K 326
Cdd:TIGR02345 243 ELKAEKDNAEIRVEDV E DYQAIVDA E WAIIFRKLEK I VES GANV VLSKLPIG 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 126723461 327 TV G ATALPKLTPPVQEEM G H C DSVYLSEV G DTQVVV F K h EKEDGAIS TI V LRG STDNLMDDI ER AVD D GVNTFKVLTRD K 406
Cdd:TIGR02345 323 AC G GSIQSTTSDLEADVL G T C ALFEERQI G SERYNY F T - GCPHAKTC TI I LRG GAEQFIEEA ER SLH D AIMIVRRALKN K 401
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 407 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 Y S V H QE G N K NV G L DI EA E v 486
Cdd:TIGR02345 402 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 R S R H AK G G K WY G V DI NT E - 480
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 126723461 487 p AVK D ML EA SILDTY L G K YW A I K L A TN AA V T V L R VD QI I MAK 528
Cdd:TIGR02345 481 - 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
TCP1_gamma
cd03337 TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
14-525
3.08e-67
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: 225.25
E-value: 3.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 14 M L KDGA K HF SG l EE A VYR NIQA C K EL A QTT RT AY GP NG M N KM VINRLEKLFV 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 126723461 94 EQ EVGDGT NF V LVF AG AL L EL AE EL L RI G LSVSEV I SG Y EI A CKK A HE IL P E lvc C S AK - NLR D VDEVSSLLRTS I MS K - 171
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 E E --- I S IP v DVN D RAQMLKIIKSC I GT K f 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 172 -- QYGS et FLAK L IAQ A -- C V SIFPDSGNFNV D --- NIR V C KI L G SG I YS S S VL H G MVFK K eteg DVT S ------ VKDAK 238
Cdd:cd03337 160 vs RWSD -- LMCN 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 233
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 239 I AVYS CP FDGM - ITE tkgtvliktaeelmnfs KG eenlmdaqvkaiagtganvivtggk V A D I A L HY AN K YN I MLV R LNS 317
Cdd:cd03337 234 I VLLD CP LEYL v ITE ----------------- KG ------------------------- V S D L A Q HY LV K AG I TAL R RVR 271
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 318 K W D LR R LCKTV GAT ALPKLTPPVQEEM G HCDSVYLSEVGDTQVVV F KH E KE D GAIS TI V LRG STDNLMDDI ER AVD D GVN 397
Cdd:cd03337 272 K T D NN R IARAC GAT IVNRPEELTESDV G TGAGLFEVKKIGDEYFT F IT E CK D PKAC TI L LRG ASKDVLNEV ER NLQ D AMA 351
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 398 TFKVLTRDKR LVPGGGATE IELAKQITSYGETCP G L EQ YAI K KF A E A F E A IPR A LA E N S G VKANEVISK L YSV H - Q EG N K 476
Cdd:cd03337 352 VARNIILNPK LVPGGGATE MAVSHALSEKAKSIE G V EQ WPY K AV A S A L E V IPR T LA Q N C G ANVIRTLTE L RAK H a Q GE N S 431
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 126723461 477 NV G L D ie A E VPAVK DM L E AS I L D TYLG K YWAI K L A TN AA VTV LR V D Q I I 525
Cdd:cd03337 432 TW G I D -- G E TGDIV DM K E LG I 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 ...
15-525
5.17e-65
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: 220.38
E-value: 5.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 L KDGA K HF SG l EE A VYR NIQA C K EL A QTT RT AY GP NG M N KM VINRLEKLFV TND AAT ILRE LE V Q HPAAK MIVMA S HM Q E 94
Cdd:TIGR02344 5 L NQNT K RE SG - RK A QLS 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 D 83
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 95 Q EVGDGT NF V LVF AG AL L EL AE EL L RIGLSVSEV I SG Y EI A CKK A HEI L P E LVC cs AKNLR D VDEVSS L LRTS I MS K --- 171
Cdd:TIGR02344 84 E EVGDGT TS V IIL AG EM L SV AE PF L EQNIHPTVI I RA Y RK A LDD A LSV L E E ISI -- PVDVN D DAAMLK L IQSC I GT K fvs 161
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 172 QYGSETFLAK L I A QAC V S i FPDS G NFNV D --- NIR V C KI L G SG I YS S S VL H G MVFK K eteg DVT S ------ VKDAK I AVY 242
Cdd:TIGR02344 162 RWSDLMCDLA L D A VRT V 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 VLL 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 243 S CP FDGMIT E TKGTVL I KTA E ELMNFSKG EE NLMDAQVKA I AGTGANVIV T GGK V A D I A L HY AN K Y NI MLV R LNS K W D LR 322
Cdd:TIGR02344 237 D CP LEYKKG E SQTNIE I TKE E DWNRILQM EE EYVQLMCED I IAVKPDLVI T EKG V S D L A Q HY LL K A NI TAI R RVR K T D NN 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 323 R LCKTV GAT ALPKLTPPVQEEM G - H C DSVYLSEV GD t QVVV F KH E KE D GAIS TI V LRG STDNLMDDI ER AVD D GVNTFKV 401
Cdd:TIGR02344 317 R IARAC GAT IVNRPEELRESDV G t G C GLFEVKKI GD - EYFT F IT E CK D PKAC TI L LRG ASKDILNEV ER NLQ D AMAVARN 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 402 LTR D KR LVPGGGATE IELAKQI T SYGETCP G L EQ YAIKKF A E A F E A IPR A LA E N S G VKANEVISK L YSV H - QE G N KNV G l 480
Cdd:TIGR02344 396 VLL D PK LVPGGGATE MAVSVAL T EKSKKLE G V EQ WPYRAV A D A L E I IPR T LA Q N C G ANVIRTLTE L RAK H a QE N N CTW G - 474
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 126723461 481 d I EA E VPAVK DM L E AS I LDTYLG K YWAI K L A TNA A VTV LR V D Q I I 525
Cdd:TIGR02344 475 - I DG E TGKIV DM K E KG I WEPLAV K LQTY K T A IES A CLL LR I D D I V 518
GroEL
COG0459 Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
26-535
4.02e-64
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227
Cd Length: 497
Bit Score: 217.25
E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 26 E E A VYR NI QAC K E LA QTTRTAY GP N G M N K M VINRLEKLFV TND AA TI LR E L E VQH P ---- A A KMIVMASHMQEQ E V GDGT 101
Cdd:COG0459 9 E D A RRA NI RGV K A LA DAVKVTL GP K G R N V M LVKSFGDPTI TND GV TI AK E I E LED P fenm G A QLVKEVASKTND E A GDGT 88
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 102 NFVL V F AGALL ELAEE L LRI G LSVSEVIS G YEI A CK KA H E I L PEL vccs AK NLR D VD E VSSLLRT S IMSKQ ygset FLAK 181
Cdd:COG0459 89 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 ANGDE ----- EIGE 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 182 LIA Q A CVSIFP D s G NFN V D nirvcki L G S G IYSSS - V LH GM V F K K E --------- T E GDVTSVKD A K I A vyscpfdgm I T 251
Cdd:COG0459 160 LIA E A MEKVGK D - G VIT V E ------- E G K G LETEL e V VE GM Q F D K G ylspyfvtd P E KMPAELEN A Y I L --------- L T 222
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 252 ET K gtvl I KTAEE L M nfskgeenlmd AQVKAI A GT G ANVIVTGGKVADI AL HYANKYN I ML V R ----------- LNS K WD 320
Cdd:COG0459 223 DK K ---- I SSIQD L L ----------- PLLEKV A QS G KPLLIIAEDIDGE AL ATLVVNG I RG V L rvvavkapgfg DRR K AM 287
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 321 L RRLCKTV G ATA -------- L PKL T P pvq EEM G HCDS V YLSE vg D TQVV V fk HEKEDGAIST I VLRGS T DNLMDDIE R A V 392
Cdd:COG0459 288 L EDIAILT G GRV isedlglk L EDV T L --- DDL 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 126723461 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 LYS 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 VRA --- 436
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126723461 473 EGN K NV G L D IEAEV pa VK DMLEA SIL 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 DMLEA GVI 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
3.32e-63
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514
Cd Length: 533
Bit Score: 216.05
E-value: 3.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 13 Q M LK D GA KHFS G l E E A VYRNIQACKEL A QTTR T AY GP N GM N K MVI ----- N R LEKLF 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 ILQ pmseg P R SGNVT VTND G ATIL KSVWLDN PAAK IL V 87
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 88 MA S HM Q EQ EVGDGT NF V L V F AG A LL EL AE E LL RIGLSVSEV I S G YEI A CKK A HEI L P E LVCCSAKNLRDVD E vs S LL --- 164
Cdd:PTZ00212 88 DI S KT Q DE EVGDGT TS V V V L AG E LL RE AE K LL DQKIHPQTI I E G WRM A LDV A RKA L E E IAFDHGSDEEKFK E -- D LL nia 165
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 165 RT SIM SK -- QYGSET F l AKL IAQ A CVSI fpd S G NF N V D N I RVC K IL G SGIYS S SVLH G MVFK K E - TE G DVTSVKDA KI A V 241
Cdd:PTZ00212 166 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 V 241
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 242 YSC P F D GMITETK G T - V LIKTA E ELMNFSKG E ENL M DAQ V KA I AGT G A NV IVTGGKVADIALHYANKYN IM LVR l NSKW D 320
Cdd:PTZ00212 242 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 D 320
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 321 - LR RL CKTV GA TALPKLTP P VQEEM GHCD SVYLSEV G DTQVVV F KHEKEDG A i S TIVLRG STDNLM D DI ER AVD D GVNTF 399
Cdd:PTZ00212 321 g ME RL AAAL GA EIVSTFDT P EKVKL GHCD LIEEIMI G EDKLIR F SGCAKGE A - C TIVLRG ASTHIL D EA ER SLH D ALCVL 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 400 KVLTR 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 YSV H QE GNK NV G 479
Cdd:PTZ00212 400 SQTVK 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 RAE H YK GNK TA G 479
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126723461 480 L D I E AEVPA vk DM L E AS I LDT Y LG K YWAIKL AT N AA VTV LRVD Q II MAK P 529
Cdd:PTZ00212 480 I D M E KGTVG -- DM K E LG I 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
3.32e-59
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain]
Cd Length: 517
Bit Score: 204.87
E-value: 3.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 15 LKDGA KHFS G l E E A VYRNIQACKELAQTTR T AY GP N GM N K MVI -- N R LEKLF VTND A ATIL RELE V QH PAAK MI V MA S HM 92
Cdd:cd03336 2 LKDGA QEEK G - E T A RLSSFVGAIAIGDLVK T TL GP K GM D K ILQ sv G R SGGVT VTND G ATIL KSIG V DN PAAK VL V DI S KV 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 93 Q EQ EVGDGT NF V L V F A GA LL EL AE E L LRIGLSVSEV I S GY EI A CKK A H E I L PELVCC --- SAKNL R D vd EVSSLL RT SIM 169
Cdd:cd03336 81 Q DD EVGDGT TS V T V L A AE LL RE AE K L VAQKIHPQTI I E GY 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 126723461 170 SK -- QYGS E T F l A K L IAQ A CVSI fpd S G NF N V D N I RVC K I LG SGIYS 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 126723461 247 D GMITETK G T - V LIKTAEELMNFSKG E ENL M DAQ V KA I AGT G A N VIVTGGKVADIALHYANKYN 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 126723461 326 KTV G ATALPKLTP P VQEEM 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 ELVKL 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 126723461 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 YSV 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 RAA H YN GN TTA GLD M -- R 471
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 126723461 486 VPA V K DM L E AS I LDTYLG K YWAIKL A TN AA VTV LRVD Q II MAK P 529
Cdd:cd03336 472 KGT V G DM K E LG I 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
4.12e-56
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: 187.29
E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 158 DEVSSLLR TS IM SK QYGSET FL A KL IAQ A CVSIF PD SGNFNVDN I R V C KI L G SGIYS 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 126723461 236 D AKI AVYS CP FD gmitetkgtvliktaeelmnfskgeenlmdaqvkaiagtga N V IVTGGKVA D I ALHY AN K YN IM L VR L 315
Cdd:cd03333 82 N AKI LLLD CP LE ----------------------------------------- Y V VIAEKGID D L ALHY LA K AG IM A VR R 120
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 316 NS K W DL R R LCKTV GAT ALPK L TPPVQ 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 126723461 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 ...
13-529
1.66e-52
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: 186.99
E-value: 1.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 13 Q ML KDGA KHFSG l E E A VYRNIQACKELAQTTRTAY GP N GM N K MVI -- NRLEKLF VTND A ATIL RELE V QH PAAK MI V MA S 90
Cdd:TIGR02341 1 Q IF KDGA DEERA - E N A RLSSFVGAIAIGDLVKSTL GP K GM D K ILQ ss SSDASIM VTND G ATIL KSIG V DN PAAK VL V DM S 79
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 91 HM Q EQ EVGDGT NF V L V F A GA LL EL AE E L LRIGLSVSEV I S GY EI A C K K A HEI L PELVCCSAKNLRDV - DEVSSLL RT SIM 169
Cdd:TIGR02341 80 KV Q DD EVGDGT TS V T V L A AE LL RE AE K L INQKIHPQTI I A GY RE A T K A A RDA L LKSAVDNGSDEVKF r QDLMNIA RT TLS 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 170 SK QYGS - ETFL A K L IAQ A CVSI fpd S G NF N VDN I RVC K I LG SGIYS S SVLH G MVF - KK ETEGDVTSVKD AKI AVYSCPF D 247
Cdd:TIGR02341 160 SK ILSQ h KDHF A Q L AVD A VLRL --- K G SG N LEA I QII K K LG GSLAD S YLDE G FLL d KK IGVNQPKRIEN AKI LIANTGM D 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 248 GMITETK G T - V LIKTAEELMNFSKG E ENL M DAQ V KA I AGT G A N VIVTGGKVADIALHYANKYNI M LVRLNSKWDLR RL CK 326
Cdd:TIGR02341 237 TDKVKIF G S r V RVDSTAKVAELEHA E KEK M KEK V EK I LKH G I N CFINRQLIYNYPEQLFADAGV M AIEHADFEGVE RL AL 316
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 327 TV G ATALPKLTP P VQEEM G H CD SVYLSEV G DTQVVV F KHE K E d G AIS TIVLRG S T DNLM D DI ER AVD D GVNTFKVLTRDK 406
Cdd:TIGR02341 317 VT G GEIVSTFDH P ELVKL G S CD LIEEIMI G EDKLLK F SGV K L - G EAC TIVLRG A T QQIL D EA ER SLH D ALCVLSQTVKES 395
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 407 R L V P GGG AT E IELA K QI T SYGETC PG L E QY A IKK FA E A FEAI P RAL A E N S G VKAN E VISK L YSV H QE GN KNV GLD IEAE v 486
Cdd:TIGR02341 396 R T V L GGG CS E MLMS K AV T QEAQRT PG K E AL A VEA FA R A LRQL P TII A D N A G FDSA E LVAQ L RAA H YN GN TTM GLD MNEG - 474
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 126723461 487 p AVK DM LEAS I LDT Y LG K YWAIKL A TN AA VTV LRVD Q II M A K P 529
Cdd:TIGR02341 475 - TIA DM RQLG I TES Y KV K RAVVSS A AE AA EVI 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
3.64e-44
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: 164.14
E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 28 A VYR NI Q A CKE L AQTTR T AY GP N G MN KM VINRLEKLFV 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 126723461 108 A G A LL EL AE ELLRI G LSVSEVIS G Y EIA C K K A HEI L PELVCCSAKNL r D VDEVSSLL RTS IMS K QYGSET - F L AKLIAQ A 186
Cdd:TIGR02347 97 I G E LL KQ AE RYILE G VHPRIITE G F EIA R K E 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 126723461 187 CVS I FP D SGNFNVDNIRVCKILGSGIYSSSVLH 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 126723461 265 LMNFS K G E ENLM D AQ VK A I A --------- GTGANVI V TGG K VA D - IA L HYAN K YN IM LV R LNSKWDLR RL CKTV G AT AL P 334
Cdd:TIGR02347 256 REKLV K A E RKFV D DR VK K I I elkkkvcgk SPDKGFV V 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 126723461 335 KLTPPVQ 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 G GA 414
Cdd:TIGR02347 336 SVEDLTP 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 A GA 414
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 415 T EI ELAKQITS Y GETCP G LEQYAIKK FA E A FEA IP RA LAENSG VK A NEVIS KL YSV H Q EG NKN VG L D IEAEV P AVKD ml E 494
Cdd:TIGR02347 415 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 -- I 492
490 500 510
....*....|....*....|....*....|...
gi 126723461 495 AS I L D T Y LG K YWA I KL AT NA A VTV L R VD QIIM A 527
Cdd:TIGR02347 493 KG I 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
6.89e-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: 159.73
E-value: 6.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 27 E A VYR NI Q A C K E L AQTTR T AY GP N G MN KM VINRLEKLFV 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 126723461 107 FA G A LL EL AE ELLRI G LSVSEVIS G Y E I A CK KA HEI L PELVC c SAKNLR D VDEVS S LL RTS IMS K QYGS - ETF L AKLIAQ 185
Cdd:cd03342 92 LI G E LL KQ AE RYIQE G VHPRIITE G F E L A KN KA LKF L ESFKV - PVEIDT D RELLL S VA RTS LRT K LHAD l ADQ L TEIVVD 170
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 186 A CVS I FPDSGNFNVDNIRV ckilgsgiysssvlhg 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 126723461 262 AEELMNFS K G E E N lmdaqvkai A G TGAN V IVTGGKVADIA L HYAN K YN I MLV R LNSKWDLR RL CKTV G AT A LPKLTPPVQ 341
Cdd:cd03342 229 CNVSLEYE K T E V N --------- S G FFYS V VINQKGIDPPS L DMLA K EG I LAL R RAKRRNME RL TLAC G GV A MNSVDDLSP 299
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 342 E EM 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 IE L AK 421
Cdd:cd03342 300 E CL 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 VA L YA 378
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 422 QITSYGETCP G LEQYAIKK FA E A FEA IP RA LAENSG VKAN E VIS KL YSVHQ EG NKNV G L D IEAEV P AVK dm LEAS I L D T Y 501
Cdd:cd03342 379 HLKEFKKSVK G KAKLGVQA FA D A LLV IP KT LAENSG LDVQ E TLV KL QDEYA EG GQVG G V D LDTGE P MDP -- ESEG I W D N Y 456
490 500
....*....|....*....|....*.
gi 126723461 502 LG K YWAIKL AT NA A VTV L R VD Q II M A 527
Cdd:cd03342 457 SV K RQILHS AT VI A SQL L L VD E II R A 482
Fab1_TCP
cd03334 TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
163-393
1.18e-10
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: 62.24
E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 163 L LRTS I MSKQYGSET f L AK L IAQ A CVSIF PD SGNFNVDN IR ---- VC KI L G SGIYS S S V LH G M VF K K E -- TEGDVTSV K D 236
Cdd:cd03334 8 L KDEG I SNDESWLDI - L LP L VWK A ASNVK PD VRAGDDMD IR qyvk IK KI P G GSPSD S E V VD G V VF T K N va HKRMPSKI K N 86
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 237 AK I AVYSC P FDGMIT E T K GTV L ikta EELM nfs KG E ENLMDAQ V KA I AGTGAN VI VTGGK V AD IA LHYANKYN I M LV r LN 316
Cdd:cd03334 87 PR I LLLQG P LEYQRV E N K LLS L ---- DPVI --- LQ E KEYLKNL V SR I VALRPD VI LVEKS V SR IA QDLLLEAG I T LV - LN 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 317 S K WD - L R R LCKTV GA TALPK ---- LT P P V qee M G H C D S V ---- Y LS E V G DTQVVV F -- KHE KE D G A is TI V LRG STDNLM 385
Cdd:cd03334 159 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 GCP KE L G C -- TI L LRG GDLEEL 233
....*...
gi 126723461 386 DDIE R A V D 393
Cdd:cd03334 234 KKVK R V V E 241
GroEL
cd03344 GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
391-499
4.35e-05
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: 46.30
E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 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 sv 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 126723461 471 hq E GNKNV G L D ie A EVPAVK DM L EA S I L D 499
Cdd:cd03344 468 -- E SPDGF G Y D -- A ATGEYV DM I EA G I I D 492
groEL
CHL00093 chaperonin GroEL
367-529
6.07e-04
chaperonin GroEL
Pssm-ID: 177025
Cd Length: 529
Bit Score: 42.40
E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 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 126723461 446 E A IPRAL AEN S G VKANEV I S K L ysvh QE GNKNV G LD ie A EVPAVKD M L EA S I 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 EA G I I D PAKVTRS A LQN A ASI A SMI L TTEC II 522
....
gi 126723461 526 MA K P 529
Cdd:CHL00093 523 VD K K 526
groEL
PRK00013 chaperonin GroEL; Reviewed
409-499
3.09e-03
chaperonin GroEL; Reviewed
Pssm-ID: 234573
Cd Length: 542
Bit Score: 40.11
E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723461 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 lys 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 126723461 489 VK DM L EA S I L D 499
Cdd:PRK00013 485 YV DM I EA G I 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
