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Conserved domains on  [gi|488432175|ref|WP_002501560|]
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chaperonin GroEL [Staphylococcus epidermidis]

Protein Classification

chaperonin GroEL( domain architecture ID 10791561)

chaperonin GroEL, together with its co-chaperonin GroES, acts as an essential chaperone that assists in protein folding in the cell

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
1-527 0e+00

chaperonin GroEL; Reviewed


:

Pssm-ID: 234573  Cd Length: 542  Bit Score: 959.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK00013   1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK00013  81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 488432175 478 ATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPENN 527
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
1-527 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 959.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK00013   1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK00013  81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 488432175 478 ATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPENN 527
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
3-519 0e+00

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: 860.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   3 KDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:cd03344    1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  83 IAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:cd03344   81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 162 EAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQS 241
Cdd:cd03344  161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 242 SRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANKV 321
Cdd:cd03344  241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 322 EVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNST 401
Cdd:cd03344  321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 402 RAAVEEGIVAGGGTALVNIYQKVSEIKAE-GDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAATN 480
Cdd:cd03344  401 RAAVEEGIVPGGGVALLRASPALDKLKALnGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 488432175 481 EWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 519
Cdd:cd03344  481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVV 519
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
2-523 0e+00

chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274089  Cd Length: 524  Bit Score: 830.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:TIGR02348   1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:TIGR02348  81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  321 VEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNS 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  401 TRAAVEEGIVAGGGTALVNIYQKVSEIKAEG-DVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 488432175  480 NEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
1-525 0e+00

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 754.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:COG0459    1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:COG0459   81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:COG0459  161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:COG0459  241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIdarvgqikaqieetdsefdkeklqerlaklaggvaVIKVGAASETELKERKLRIEDALN 399
Cdd:COG0459  321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFN 476
Cdd:COG0459  366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 488432175 477 AATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:COG0459  446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
22-521 1.65e-88

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: 281.01  E-value: 1.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  102 GLKNVTSGANPVGLRQGIDKAVQVAIEAL---HEISQKVENKNEIAQVGAISAA-------DEEIGRYISEA-------- 163
Cdd:pfam00118  77 AEKLLAAGVHPTTIIEGYEKALEKALEILdsiISIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVDAvlaipknd 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  164 -MDKVGNDGVITIEESNGFNTELevVEGMQFDRGYQSPymvtdsdKMIAELERPYILVTDKKITSFQD------------ 230
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  231 ------------ILPLLEQVVQSSRPILIVADEVEGDALTNIVLNRMRGTFTAvavkapgfgdrRKAMLEDLAILTGAQV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  299 ITDdlgleLKDASLDMLGTANKVEVTK---DHTTVVDGNGDennidarvgqikaqieetdsefdkeklqerlaklaGGVA 375
Cdd:pfam00118 297 VSS-----LDDLTPDDLGTAGKVEEEKigdEKYTFIEGCKS-----------------------------------PKAA 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  376 VIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKA--EGDVETGVNIVLQALQAPVRQIA 452
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKsvSGKEQLAIEAFAEALEVIPKTLA 416
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432175  453 ENAGLEGSIIVERLKHA----EAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASI 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
1-527 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 959.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK00013   1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK00013  81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 488432175 478 ATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPENN 527
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
3-519 0e+00

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: 860.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   3 KDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:cd03344    1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  83 IAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:cd03344   81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 162 EAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQS 241
Cdd:cd03344  161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 242 SRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANKV 321
Cdd:cd03344  241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 322 EVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNST 401
Cdd:cd03344  321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 402 RAAVEEGIVAGGGTALVNIYQKVSEIKAE-GDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAATN 480
Cdd:cd03344  401 RAAVEEGIVPGGGVALLRASPALDKLKALnGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 488432175 481 EWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 519
Cdd:cd03344  481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVV 519
groEL PRK12849
chaperonin GroEL; Reviewed
1-526 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 859.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12849   1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12849  81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPEN 526
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
2-523 0e+00

chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274089  Cd Length: 524  Bit Score: 830.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:TIGR02348   1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:TIGR02348  81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  321 VEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNS 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  401 TRAAVEEGIVAGGGTALVNIYQKVSEIKAEG-DVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 488432175  480 NEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
groEL PRK12850
chaperonin GroEL; Reviewed
1-523 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 794.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12850   2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12850  82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPK 526
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
1-525 0e+00

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 754.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:COG0459    1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:COG0459   81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:COG0459  161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:COG0459  241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIdarvgqikaqieetdsefdkeklqerlaklaggvaVIKVGAASETELKERKLRIEDALN 399
Cdd:COG0459  321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFN 476
Cdd:COG0459  366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 488432175 477 AATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:COG0459  446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
groEL PRK12851
chaperonin GroEL; Reviewed
1-525 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 742.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12851   2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12851  82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKE 528
groEL PRK12852
chaperonin GroEL; Reviewed
1-525 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 700.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12852   2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12852  82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 488432175 478 ATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKD 529
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
2-526 0e+00

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 698.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:PTZ00114  14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:PTZ00114  94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDD-LGLELKDASLDMLGTAN 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK----AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSFG 493
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488432175 475 FNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPEN 526
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
groEL CHL00093
chaperonin GroEL
1-523 0e+00

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 685.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:CHL00093   1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:CHL00093  81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSF-QDILPLLEQV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 239 VQSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 319 NKVEVTKDHTTVVdGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 399 NSTRAAVEEGIVAGGGTALVNIYQKV---SEIKAEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 488432175 476 NAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
PRK14104 PRK14104
chaperonin GroEL; Provisional
2-523 0e+00

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 605.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:PRK14104   3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:PRK14104  83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 321 VEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNS 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 401 TRAAVEEGIVAGGGTALVNIYQKVSEIKAEG-DVETGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNdDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
2-525 0e+00

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 541.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   2 AKDLKFSED--ARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANK 79
Cdd:PLN03167  56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  80 TNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENkNEIAQVGAISAADE-EIGR 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNyEVGN 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 159 YISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 239 VQSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 319 NKVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 399 NSTRAAVEEGIVAGGGTALVNIYQKVSEIKA--EGDVE-TGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488432175 475 FNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
3-519 5.71e-148

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: 433.01  E-value: 5.71e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   3 KDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEdpyeNMGAKLVQEVANKTNE 82
Cdd:cd00309    1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  83 IAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQK--VENKNEIAQVGAISAA-------D 153
Cdd:cd00309   77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsggD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 154 EEIGRYISEAMDKVG------NDGVITIEESNGFN-TELEVVEGMQFDRGYQSPYmvtdsdkMIAELERPYILVTDKKit 226
Cdd:cd00309  157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCK-- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 227 sfqdilplLEQVVqssrpilIVADEVEGDALTNIVLNRMrgtftaVAVKApgfgdRRKAMLEDLAILTGAQVITddlglE 306
Cdd:cd00309  228 --------LEYVV-------IAEKGIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS-----R 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 307 LKDASLDMLGTANKVEVTK----DHTTVVDGNGdennidarvgqikaqieetdsefdkeklqerlaklaGGVAVIKVGAA 382
Cdd:cd00309  277 LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRGA 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 383 SETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKA--EGDVETGVNIVLQALQAPVRQIAENAGLEG 459
Cdd:cd00309  321 TEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtlPGKEQLGIEAFADALEVIPRTLAENAGLDP 400
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432175 460 SIIVERL--KHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 519
Cdd:cd00309  401 IEVVTKLraKHAEGGgnAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
22-521 1.65e-88

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: 281.01  E-value: 1.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  102 GLKNVTSGANPVGLRQGIDKAVQVAIEAL---HEISQKVENKNEIAQVGAISAA-------DEEIGRYISEA-------- 163
Cdd:pfam00118  77 AEKLLAAGVHPTTIIEGYEKALEKALEILdsiISIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVDAvlaipknd 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  164 -MDKVGNDGVITIEESNGFNTELevVEGMQFDRGYQSPymvtdsdKMIAELERPYILVTDKKITSFQD------------ 230
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  231 ------------ILPLLEQVVQSSRPILIVADEVEGDALTNIVLNRMRGTFTAvavkapgfgdrRKAMLEDLAILTGAQV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  299 ITDdlgleLKDASLDMLGTANKVEVTK---DHTTVVDGNGDennidarvgqikaqieetdsefdkeklqerlaklaGGVA 375
Cdd:pfam00118 297 VSS-----LDDLTPDDLGTAGKVEEEKigdEKYTFIEGCKS-----------------------------------PKAA 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  376 VIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKA--EGDVETGVNIVLQALQAPVRQIA 452
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKsvSGKEQLAIEAFAEALEVIPKTLA 416
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432175  453 ENAGLEGSIIVERLKHA----EAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASI 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
140-407 4.99e-37

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: 136.06  E-value: 4.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 140 KNEIAQVGAISAA------DEEIGRYISEAMDKVG------NDGVITIEESNGFN-TELEVVEGMQFDRGYQSPYMvtds 206
Cdd:cd03333    1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYM---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 207 dkmIAELERPYILVTDKKitsfqdilplLEQVVqssrpilIVADEVEGDALTNIVLNRMrgtftaVAVKApgfgdRRKAM 286
Cdd:cd03333   77 ---PKRLENAKILLLDCP----------LEYVV-------IAEKGIDDLALHYLAKAGI------MAVRR-----VKKED 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 287 LEDLAILTGAQVITddlglELKDASLDMLGTANKVEVTKDhttvvdgngdennidarvgqikaqIEETDSEFDKEKlqer 366
Cdd:cd03333  126 LERIARATGATIVS-----SLEDLTPEDLGTAELVEETKI------------------------GEEKLTFIEGCK---- 172
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488432175 367 laklAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEE 407
Cdd:cd03333  173 ----GGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
9-520 5.96e-32

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: 128.92  E-value: 5.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   9 EDARQAMLRGVDKLANAVKVTIGPKGrnvvLDKDYTTPL----ITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIA 84
Cdd:cd03343   14 RDAQRMNIAAAKAVAEAVRTTLGPKG----MDKMLVDSLgdvtITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  85 GDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNE-----IAQVGAISAADEEIGRY 159
Cdd:cd03343   86 GDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAKDK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISE-AMDKV-----GNDGVITIEESN--------GFNTELEVVEGMQFDRGYQSPYM---VTDSDKMIA----ELERPYI 218
Cdd:cd03343  166 LADlVVDAVlqvaeKRDGKYVVDLDNikiekktgGSVDDTELIRGIVIDKEVVHPGMpkrVENAKIALLdaplEVKKTEI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 219 lVTDKKITSFQDILPLLEqvvQSSRPILIVADEVEgDALTNIVL-----NRMRGTFTAvavKAPGFGDRR--KAMLEDLA 291
Cdd:cd03343  246 -DAKIRITSPDQLQAFLE---QEEAMLKEMVDKIA-DTGANVVFcqkgiDDLAQHYLA---KAGILAVRRvkKSDMEKLA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 292 ILTGAQVITDdlgleLKDASLDMLGTANKVEVTKDhttvvdgnGDENnidarvgqiKAQIEEtdsefdkeklqerlAKLA 371
Cdd:cd03343  318 RATGAKIVTN-----IDDLTPEDLGEAELVEERKV--------GDDK---------MVFVEG--------------CKNP 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 372 GGVAVIKVGaASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPV 448
Cdd:cd03343  362 KAVTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYarSVGGREQLAVEAFADALEEIP 440
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488432175 449 RQIAENAGLEG-SIIVE-RLKHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVAS 520
Cdd:cd03343  441 RTLAENAGLDPiDTLVElRAAHEKGNknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
22-512 4.64e-19

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: 90.04  E-value: 4.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  22 LANAVKVTIGPKGrnvvLDKDYTTP----LITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQS 97
Cdd:cd03338   20 VADAIRTSLGPRG----MDKMIQTGkgevIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  98 MIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQV-GAISAADEEIGRYISEAMDKVGNDGVITIE 176
Cdd:cd03338   92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIkSATTSLNSKVVSQYSSLLAPIAVDAVLKVI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 177 ESNGFNT-----------------ELEVVEGMQFDRGYQS------------------------PYM-----VTDSDKM- 209
Cdd:cd03338  172 DPATATNvdlkdirivkklggtieDTELVDGLVFTQKASKkaggptriekakigliqfclsppkTDMdnnivVNDYAQMd 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 210 -IAELERPYILVTDKKITSfqdilplleqvvqSSRPILIVADEVEGDALTNI---VLNRMRgtftAVAVKapgfgDRRKA 285
Cdd:cd03338  252 rILREERKYILNMCKKIKK-------------SGCNVLLIQKSILRDAVSDLalhFLAKLK----IMVVK-----DIERE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 286 MLEDLAILTGAQVITDdlgleLKDASLDMLGTANKVevtkdhttvvdgngdennidarvgqikaqiEETDSEFDKEKLQE 365
Cdd:cd03338  310 EIEFICKTIGCKPVAS-----IDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKIT 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 366 RLAKLAGGVAVIkVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEikaEGDVETGVNIVL--- 441
Cdd:cd03338  355 GVKNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSE---WARTLTGVEQYCvra 430
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488432175 442 --QALQAPVRQIAENAGLEG-SIIVE-RLKHAEAGV--GFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFL 512
Cdd:cd03338  431 faDALEVIPYTLAENAGLNPiSIVTElRNRHAQGEKnaGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
9-520 1.86e-16

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: 82.14  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:TIGR02342   8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   89 TTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKN-EIAQVGAISAADEEIGRYISEAMDKV 167
Cdd:TIGR02342  84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDrEQLLKSATTSLSSKVVSQYSSLLAPL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  168 GNDGVITIEES-NGFNTEL----------------EVVEGMQFDRGYQS------------------------PYM---- 202
Cdd:TIGR02342 164 AVDAVLKVIDPeNAKNVDLndikvvkklggtiddtELIEGLVFTQKASKsaggptriekakigliqfqisppkTDMenqi 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  203 -VTDSDKM--IAELERPYILVTDKKItsfqdilplleqvVQSSRPILIVADEVEGDALTNI---VLNRMRgtftAVAVKa 276
Cdd:TIGR02342 244 iVNDYAQMdrVLKEERAYILNIVKKI-------------KKTGCNVLLIQKSILRDAVNDLalhFLAKMK----IMVVK- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  277 pgfgDRRKAMLEDLAILTGAQVITDDLGLelkdaSLDMLGTANKVE-VTKDHTTVVDGNGDENnidarvgqikaqieetd 355
Cdd:TIGR02342 306 ----DIEREEIEFICKTIGCKPIASIDHF-----TADKLGSAELVEeVDSDGGKIIKITGIQN----------------- 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  356 sefdkeklqerlaklAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKAEGDVE 434
Cdd:TIGR02342 360 ---------------AGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYARTMKGV 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  435 TG--VNIVLQALQAPVRQIAENAGLEGSIIVERL--KHA--EAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVA 508
Cdd:TIGR02342 425 ESycVRAFADALEVIPYTLAENAGLNPIKVVTELrnRHAngEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETV 504
                         570
                  ....*....|..
gi 488432175  509 AMFLTTEAVVAS 520
Cdd:TIGR02342 505 RSILKIDDIVFT 516
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
10-520 1.58e-15

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: 79.46  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   10 DARQAMLRGVDKLANAVKVTIGPKGRNVVL---DKDYTtplITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAGD 86
Cdd:TIGR02343  27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLispDGDIT---VTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   87 GTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVgAISAADEEIGRYI----SE 162
Cdd:TIGR02343 100 GTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREP-LIQAAKTSLGSKIvskcHR 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  163 AMDKVGNDGVITIE--ESNGFNTEL--------------EVVEGMQFDRGYQSPYMVTD-SDKMIAELERPY---ILVTD 222
Cdd:TIGR02343 179 RFAEIAVDAVLNVAdmERRDVDFDLikvegkvggsledtKLIKGIIIDKDFSHPQMPKEvEDAKIAILTCPFeppKPKTK 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  223 KK--ITSFQDILPLLEQVVQSSRPILivaDEVEgDALTNIVL---------NRMRGTFTAVAVKAPGFGDrrkamLEDLA 291
Cdd:TIGR02343 259 HKldISSVEEYKKLQKYEQQKFKEMI---DDIK-KSGANLVIcqwgfddeaNHLLLQNDLPAVRWVGGQE-----LELIA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  292 ILTGAQVITddlglELKDASLDMLGTANKVE-----VTKDHTTVVDgngdennidaRVGQIKAqieetdsefdkeklqer 366
Cdd:TIGR02343 330 IATGGRIVP-----RFQELSKDKLGKAGLVReisfgTTKDRMLVIE----------QCKNSKA----------------- 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  367 laklaggvAVIKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQA 443
Cdd:TIGR02343 378 --------VTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEadKYPGVEQYAIRAFADA 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  444 LQAPVRQIAENAGLE-----GSIIVERLKHAEAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVV 518
Cdd:TIGR02343 450 LETIPMALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529

                  ..
gi 488432175  519 AS 520
Cdd:TIGR02343 530 SP 531
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
9-190 2.46e-14

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: 75.41  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   9 EDARQAMLRGVD----------KLANAVKVTIGPKGrnvvLDKDYTTP----LITNDGVTIAKEIELEDPYenmgAKLVQ 74
Cdd:cd03339   12 EQEKKKRLKGLEahkshilaakSVANILRTSLGPRG----MDKILVSPdgevTVTNDGATILEKMDVDHQI----AKLLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  75 EVANKTNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVE----NKNEIAQVGAIS 150
Cdd:cd03339   84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspdNKEPLIQTAMTS 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488432175 151 AADEEIGRYiSEAMDKVGNDGVITIE--ESNGFNTELEVVEG 190
Cdd:cd03339  164 LGSKIVSRC-HRQFAEIAVDAVLSVAdlERKDVNFELIKVEG 204
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
9-135 1.25e-13

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 73.14  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVL-----DKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEI 83
Cdd:PTZ00212  21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILqpmseGPRSGNVTVTNDGATILKSVWLDNP----AAKILVDISKTQDEE 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488432175  84 AGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQ 135
Cdd:PTZ00212  97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAF 148
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
9-135 1.97e-13

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: 72.75  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVL--DKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGD 86
Cdd:cd03336   12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKVQDDEVGD 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488432175  87 GTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQ 135
Cdd:cd03336   88 GTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAV 136
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
5-518 3.33e-13

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: 72.10  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    5 LKFSEDARQAML------RGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVAN 78
Cdd:TIGR02345   7 LKEGTDTSQGKGqlisniNACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   79 KTNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKN----EIAQVGAISAADE 154
Cdd:TIGR02345  83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrELLEKCAATALSS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  155 EIGRYISEAMDKVGNDGVITIEESN-------------GFNTELEVVEGMQFDR-----GY-QSPYMVtdSDKMI----- 210
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSLDRDDldlkligikkvqgGALEDSQLVNGVAFKKtfsyaGFeQQPKKF--ANPKIlllnv 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  211 -----AELERPYILVTDKKitSFQD--------ILPLLEQVVQSSrpilivadevegdalTNIVLNRMrgtftavavkap 277
Cdd:TIGR02345 241 elelkAEKDNAEIRVEDVE--DYQAivdaewaiIFRKLEKIVESG---------------ANVVLSKL------------ 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  278 GFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAnkvevtkdhttvvdgngdeNNIDARVGQIKAQIEETDSE 357
Cdd:TIGR02345 292 PIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTT-------------------SDLEADVLGTCALFEERQIG 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  358 FDKEKLQERLAKLAGGVAVIKVGAASETELKERKLriEDALNSTRAAVE-EGIVAGGGTALVNIYQKVSEI--KAEGDVE 434
Cdd:TIGR02345 353 SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSL--HDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYskTIDGKQQ 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  435 TGVNIVLQALQAPVRQIAENAGLEGSIIVE--RLKHAEAGV--GFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAM 510
Cdd:TIGR02345 431 LIINAFAKALEIIPRQLCENAGFDSIEILNklRSRHAKGGKwyGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACT 510

                  ....*...
gi 488432175  511 FLTTEAVV 518
Cdd:TIGR02345 511 ILSVDETI 518
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
21-142 1.32e-11

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: 66.93  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  21 KLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQSMIQ 100
Cdd:cd03340   27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488432175 101 EGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNE 142
Cdd:cd03340  103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDK 144
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
9-139 2.01e-10

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: 63.20  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:TIGR02340  11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488432175   89 TTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHE-ISQKVEN 139
Cdd:TIGR02340  87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDE 138
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
9-521 8.66e-10

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: 61.29  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    9 EDARQAMLRGVDK---LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAG 85
Cdd:TIGR02344  12 ESGRKAQLSNIQAakaVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   86 DGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA--ADEEIGRYiSEA 163
Cdd:TIGR02344  88 DGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSciGTKFVSRW-SDL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  164 MDKVGNDGVITIEESNGFNTELE-------------------VVEGMQFDRGYQSPymvtdsdKMIAELERPYILVTD-- 222
Cdd:TIGR02344 167 MCDLALDAVRTVQRDENGRKEIDikryakvekipggdiedscVLKGVMINKDVTHP-------KMRRYIENPRIVLLDcp 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  223 --------------KKITSFQDILPLLEQVVQ-------SSRPILIVADEVEGDALTNIVLnrmRGTFTAvavkapgFGD 281
Cdd:TIGR02344 240 leykkgesqtnieiTKEEDWNRILQMEEEYVQlmcediiAVKPDLVITEKGVSDLAQHYLL---KANITA-------IRR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  282 RRKAMLEDLAILTGAQVItddlglelkdasldmlgtaNKVEVTKdhttvvdgngdENNIDARVG--QIKAQIEETDSEFD 359
Cdd:TIGR02344 310 VRKTDNNRIARACGATIV-------------------NRPEELR-----------ESDVGTGCGlfEVKKIGDEYFTFIT 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  360 KEKLQERLAKLAGGvavikvgaASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETG 436
Cdd:TIGR02344 360 ECKDPKACTILLRG--------ASKDILNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKskKLEGVEQWP 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  437 VNIVLQALQAPVRQIAENAGLE--GSIIVERLKHAEAG---VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMF 511
Cdd:TIGR02344 432 YRAVADALEIIPRTLAQNCGANviRTLTELRAKHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLL 511
                         570
                  ....*....|
gi 488432175  512 LTTEAVVASI 521
Cdd:TIGR02344 512 LRIDDIVSGV 521
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
9-139 1.11e-09

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: 60.76  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:cd03335    7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488432175  89 TTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHE-ISQKVEN 139
Cdd:cd03335   83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDN 134
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
8-130 1.46e-09

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: 60.26  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175    8 SEDARQAMLRGVDKLANAVKVTIGPKGRNVVL--DKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAG 85
Cdd:TIGR02341  12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVDNP----AAKVLVDMSKVQDDEVG 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 488432175   86 DGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEAL 130
Cdd:TIGR02341  88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDAL 132
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
22-187 4.76e-09

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: 58.85  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  22 LANAVKVTIGPKGR-NVVLDKDYTTpLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQSMIQ 100
Cdd:cd03337   28 VADVIRTCLGPRAMlKMLLDPMGGI-VLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 101 EGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAAdeeIG-RYISEAMDKVGN---DGVITIE 176
Cdd:cd03337  103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSC---IGtKFVSRWSDLMCNlalDAVKTVA 179
                        170
                 ....*....|..
gi 488432175 177 -ESNGFNTELEV 187
Cdd:cd03337  180 vEENGRKKEIDI 191
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
6-518 1.26e-08

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: 57.23  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   6 KFSEDARQAMLRGVD---KLANAVKVTIGPKGRN--VV--LDKDYttplITNDGVTIAKEIELEDPyenmGAKLVQEVAN 78
Cdd:cd03341    1 RHYSGLEEAVLRNIEackELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQHP----AAKLLVMASQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  79 KTNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEIS-QKVENKNEIAQV-GAISAAdeeI 156
Cdd:cd03341   73 MQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIEDLRNKEEVsKALKTA---I 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 157 GRYISEAMD---KVGNDGVITI--EESNGFN--------------TELEVVEGMQFDRgyqspymvtdsdkmiaELERPY 217
Cdd:cd03341  150 ASKQYGNEDflsPLVAEACISVlpENIGNFNvdnirvvkilggslEDSKVVRGMVFKR----------------EPEGSV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 218 ILVTDKKITSFQDILPLLEQVVqssrpilIVADEVEGDALTniVLNRmrgtFTAVAVKAPG-FGDRRkamledLAILTGA 296
Cdd:cd03341  214 KRVKKAKVAVFSCPFDIGVNVI-------VAGGSVGDLALH--YCNK----YGIMVIKINSkFELRR------LCRTVGA 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 297 QVITddlglELKDASLDMLGTANKVEVTKDHTTVVdgngdennidarvgqIKAQIEETDSEfdkeklqerlaklaggVAV 376
Cdd:cd03341  275 TPLP-----RLGAPTPEEIGYCDSVYVEEIGDTKV---------------VVFRQNKEDSK----------------IAT 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 377 IKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKvseIKAEGDVETG-----VNIVLQALQAPVRQ 450
Cdd:cd03341  319 IVLRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKK---LKEYGEKTPGleqyaIKKFAEAFEVVPRT 395
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432175 451 IAENAGLEGSIIVERL--KHAE----AGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVV 518
Cdd:cd03341  396 LAENAGLDATEVLSELyaAHQKgnksAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
22-522 5.11e-08

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: 55.49  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:TIGR02346  30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  102 GLKNVTSGANPVGLRQGIDKAVQVAIEALHEIS----QKVENKNEIAQVGAISAADEEIGRYisEAMDKVGNDGVITI-- 175
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDELIKALKASISSKQYGNE--DFLAQLVAQACSTVlp 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  176 EESNGFNTEL--------------EVVEGMQFDRgyqspymvtDSDKMIAELERPYILV---------TDKK----ITSF 228
Cdd:TIGR02346 184 KNPQNFNVDNirvckilggslsnsEVLKGMVFNR---------EAEGSVKSVKNAKVAVfscpldtatTETKgtvlIHNA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  229 QDILPLL---EQVVQSSrpILIVADE-----VEGDALTNIVLNRMRgTFTAVAVKAPGfgdrrKAMLEDLAILTGAQVIt 300
Cdd:TIGR02346 255 EELLNYSkgeENQIEAM--IKAIADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----KFELRRLCKTVGATPL- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  301 ddlgLELKDASLDMLGTANKVEVTKdhttvvdgngdennidarVGQIKAQIeetdseFDKEKLQERlaklaggVAVIKVG 380
Cdd:TIGR02346 326 ----PRLGAPTPEEIGYVDSVYVSE------------------IGGDKVTV------FKQENGDSK-------ISTIILR 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  381 AASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPVRQIAENAGL 457
Cdd:TIGR02346 371 GSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYgeKLPGLDQYAIKKFAEAFEIIPRTLAENAGL 450
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488432175  458 EGSIIVERL------KHAEAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIP 522
Cdd:TIGR02346 451 NANEVIPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
22-518 5.13e-08

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: 55.51  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175   22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKlvqeVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:TIGR02347  28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIAR----AATAQDDITGDGTTSTVLLIGELLKQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  102 GLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNE----------------------------IAQVGAISAAD 153
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDrefllnvartslrtklpadladqlteivVDAVLAIKKDG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  154 EEIGRYISEAMDKVGNdgvitieesngFNTELEVVEGMQFDRGYQSPYM------------------------------- 202
Cdd:TIGR02347 184 EDIDLFMVEIMEMKHK-----------SATDTTLIRGLVLDHGARHPDMprrvknayiltcnvsleyektevnsgffyss 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  203 VTDSDKMiAELERPYILVTDKKITSFQDILplleqvvqssrpilivadeVEGDALTNIVLNRMRGT--FTAVAVKAPGFG 280
Cdd:TIGR02347 253 AEQREKL-VKAERKFVDDRVKKIIELKKKV-------------------CGKSPDKGFVVINQKGIdpPSLDLLAKEGIM 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  281 DRRKAM---LEDLAILTGAQVITDdlgleLKDASLDMLGTANKV---EVTKDHTTVVDGNGDENNIdarvgqikaqieet 354
Cdd:TIGR02347 313 ALRRAKrrnMERLTLACGGEALNS-----VEDLTPECLGWAGLVyetTIGEEKYTFIEECKNPKSC-------------- 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  355 dsefdkeklqerlaklaggvaVIKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEIK--AEG 431
Cdd:TIGR02347 374 ---------------------TILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKksVKG 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  432 DVETGVNIVLQALQAPVRQIAENAGLEgsiIVERL-----KHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHA 504
Cdd:TIGR02347 433 KAKLGVEAFANALLVIPKTLAENSGFD---AQDTLvkledEHDEGGevVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSA 509
                         570
                  ....*....|....
gi 488432175  505 ASVAAMFLTTEAVV 518
Cdd:TIGR02347 510 TVIASQLLLVDEVM 523
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
22-512 7.59e-06

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: 48.41  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175  22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKlvqeVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:cd03342   24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIAR----AATAQDDITGDGTTSNVLLIGELLKQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 102 GLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKN--EIAQVGAISAADEEIGRYISEAMDKVGNDGVITIEESN 179
Cdd:cd03342  100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTdrELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 180 ---------------GFNTELEVVEGMQFDRGYQSPYMVTDsdkmiaeLERPYILVTDKKI--------TSFqdilplLE 236
Cdd:cd03342  180 epidlhmveimqmqhKSDSDTKLIRGLVLDHGARHPDMPKR-------VENAYILTCNVSLeyektevnSGF------FY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 237 QVVQSSRPIlivaDEVEGDALT--NIV-LNRMRgtftavavkapgfgdRRKamLEDLAILTGAQVIT--DDLglelkdaS 311
Cdd:cd03342  247 SVVINQKGI----DPPSLDMLAkeGILaLRRAK---------------RRN--MERLTLACGGVAMNsvDDL-------S 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 312 LDMLGTANKVEVTK---DHTTVVdgngdENNIDARVGQIkaqieetdsefdkeklqerlaklaggvaVIKvgAASETELK 388
Cdd:cd03342  299 PECLGYAGLVYERTlgeEKYTFI-----EGVKNPKSCTI----------------------------LIK--GPNDHTIT 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 389 ERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEIK--AEGDVETGVNIVLQALQAPVRQIAENAGLEgsiIVER 465
Cdd:cd03342  344 QIKDAIRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLKEFKksVKGKAKLGVQAFADALLVIPKTLAENSGLD---VQET 420
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488432175 466 L-----KHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFL 512
Cdd:cd03342  421 LvklqdEYAEGGqvGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLL 474
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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