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Conserved domains on  [gi|1274081555|gb|ATQ62685|]
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GroEL protein, partial [Streptococcus respiraculi]

Protein Classification

TCP-1/cpn60 chaperonin family protein( domain architecture ID 16)

TCP-1/cpn60 chaperonin family protein similar to mycobacterial 60 kDa chaperonin (GroEL) that together with its co-chaperonin GroES, plays an essential role in assisting protein folding

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
chaperonin_like super family cl02777
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 1-254 1.05e-168

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.


The actual alignment was detected with superfamily member PRK00013:

Pssm-ID: 351886  Cd Length: 542  Bit Score: 476.54  E-value: 1.05e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK00013  193 QFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK00013  273 VAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQI 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK00013  353 EETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLN 432

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK00013  433 GDEATGINIVLRALE 447
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-254 1.05e-168

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 476.54  E-value: 1.05e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK00013  193 QFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK00013  273 VAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQI 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK00013  353 EETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLN 432

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK00013  433 GDEATGINIVLRALE 447
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-254 2.19e-147

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: 421.87  E-value: 2.19e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:cd03344   191 QFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKV 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:cd03344   271 CAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQI 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAK- 239
Cdd:cd03344   351 EETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLKALn 430

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:cd03344   431 GDEKLGIEIVRRALE 445
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-254 1.25e-143

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: 412.46  E-value: 1.25e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:TIGR02348 192 QFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNV 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:TIGR02348 272 CAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQI 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAKG 240
Cdd:TIGR02348 352 EETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDG 431

                         250
                  ....*....|....*
gi 1274081555 241 -DEATGRNIVLRALE 254
Cdd:TIGR02348 432 eDEAIGIDIVKRALE 446
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-254 2.75e-112

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 331.66  E-value: 2.75e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:COG0459   193 QFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIahrigvikaqi 160
Cdd:COG0459   273 VAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI----------- 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 etttsefdreklqerlaklsggvaVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAK- 239
Cdd:COG0459   342 ------------------------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAKl 397

                         250
                  ....*....|....*.
gi 1274081555 240 -GDEATGRNIVLRALE 254
Cdd:COG0459   398 eGDEQLGIEIVARALE 413
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-254 4.34e-24

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: 100.35  E-value: 4.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSqymvtdnEKMVAELDNPYILITDKKISNIQE------------------------ILPLLESILQSSRPLLI 56
Cdd:pfam00118 184 VLDKGPLH-------PDMPKRLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVV 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  57 IADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIAILTGGTVITDdlgleLKDATIEALGQASKVSVDK-- 134
Cdd:pfam00118 257 CQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAVSS-----LDDLTPDDLGTAGKVEEEKig 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 135 -DTTVIVEGTgdvaaiahrigvikaqietttsefdreklqerlakLSGGVAVIKVGAATETELKEMKLRIEDALNATRAA 213
Cdd:pfam00118 321 dEKYTFIEGC-----------------------------------KSPKAATILLRGATDHVLDEIERSIHDALCVVKNA 365

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1274081555 214 VEE-GIVAGGGTAFVNVIDAVASIEAK--GDEATGRNIVLRALE 254
Cdd:pfam00118 366 IEDpRVVPGGGAVEMELARALREYAKSvsGKEQLAIEAFAEALE 409
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-254 1.05e-168

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 476.54  E-value: 1.05e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK00013  193 QFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK00013  273 VAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQI 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK00013  353 EETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLN 432

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK00013  433 GDEATGINIVLRALE 447
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-254 2.19e-147

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: 421.87  E-value: 2.19e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:cd03344   191 QFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKV 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:cd03344   271 CAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQI 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAK- 239
Cdd:cd03344   351 EETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLKALn 430

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:cd03344   431 GDEKLGIEIVRRALE 445
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-254 1.25e-143

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: 412.46  E-value: 1.25e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:TIGR02348 192 QFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNV 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:TIGR02348 272 CAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQI 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAKG 240
Cdd:TIGR02348 352 EETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDG 431

                         250
                  ....*....|....*
gi 1274081555 241 -DEATGRNIVLRALE 254
Cdd:TIGR02348 432 eDEAIGIDIVKRALE 446
groEL PRK12849
chaperonin GroEL; Reviewed
 1-254 2.13e-143

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 412.28  E-value: 2.13e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK12849  193 QFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK12849  273 AAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIRRQI 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK12849  353 EETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEGIVPGGGVALLRAAKALDELAgLN 432

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK12849  433 GDQAAGVEIVRRALE 447
groEL PRK12850
chaperonin GroEL; Reviewed
 1-254 6.48e-133

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 386.00  E-value: 6.48e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK12850  194 QFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKS 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK12850  274 VAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRVLITKENTTIIDGAGDKKNIEARVKQIRAQI 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK12850  354 EETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRARSALRGLKgAN 433

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK12850  434 ADETAGIDIVRRALE 448
groEL PRK12851
chaperonin GroEL; Reviewed
 1-254 1.63e-123

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 361.75  E-value: 1.63e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK12851  194 QFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKV 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK12851  274 AAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQI 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK12851  354 EETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRAVKALDKLEtAN 433

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK12851  434 GDQRTGVEIVRRALE 448
groEL PRK12852
chaperonin GroEL; Reviewed
 1-254 8.37e-119

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 349.91  E-value: 8.37e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK12852  194 KFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKV 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK12852  274 AAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIKAQI 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-AK 239
Cdd:PRK12852  354 EETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEGIVPGGGVALLRAKKAVGRINnDN 433

                         250
                  ....*....|....*
gi 1274081555 240 GDEATGRNIVLRALE 254
Cdd:PRK12852  434 ADVQAGINIVLKALE 448
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-254 1.35e-113

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 336.88  E-value: 1.35e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PTZ00114  205 SFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKV 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDD-LGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQ 159
Cdd:PTZ00114  285 CAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQ 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 160 IETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIE-- 237
Cdd:PTZ00114  365 IERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEEGIVPGGGVALLRASKLLDKLEed 444

                         250
                  ....*....|....*....
gi 1274081555 238 --AKGDEATGRNIVLRALE 254
Cdd:PTZ00114  445 neLTPDQRTGVKIVRNALR 463
groEL CHL00093
chaperonin GroEL
 1-253 1.61e-113

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 335.92  E-value: 1.61e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNI-QEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFN 79
Cdd:CHL00093  193 RFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVTKTKRPLLIIAEDVEKEALATLVLNKLRGIVN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  80 VVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVeGTGDVAAIAHRIGVIKAQ 159
Cdd:CHL00093  273 VVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTTII-ADGNEEQVKARCEQLRKQ 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 160 IETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAV---ASI 236
Cdd:CHL00093  352 IEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIVPGGGATLVHLSENLktwAKN 431

                         250
                  ....*....|....*..
gi 1274081555 237 EAKGDEATGRNIVLRAL 253
Cdd:CHL00093  432 NLKEDELIGALIVARAI 448
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-254 2.75e-112

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 331.66  E-value: 2.75e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:COG0459   193 QFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIahrigvikaqi 160
Cdd:COG0459   273 VAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI----------- 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 etttsefdreklqerlaklsggvaVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAK- 239
Cdd:COG0459   342 ------------------------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAKl 397

                         250
                  ....*....|....*.
gi 1274081555 240 -GDEATGRNIVLRALE 254
Cdd:COG0459   398 eGDEQLGIEIVARALE 413
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-253 8.95e-97

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 293.48  E-value: 8.95e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PRK14104  194 QFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKV 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PRK14104  274 AAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENTTIVNGAGKKADIEARVAQIKAQI 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNVIDAVASIEAKG 240
Cdd:PRK14104  354 EETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGIVPGGGVALLRASEQLKGIKTKN 433

                         250
                  ....*....|....
gi 1274081555 241 -DEATGRNIVLRAL 253
Cdd:PRK14104  434 dDQKTGVEIVRKAL 447
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-253 9.05e-87

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 269.10  E-value: 9.05e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTDNEKMVAELDNPYILITDKKISNIQEILPLLESILQSSRPLLIIADDVDGEALPTLVLNKIRGTFNV 80
Cdd:PLN03167  248 QFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKI 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  81 VAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDATIEALGQASKVSVDKDTTVIVEGTGDVAAIAHRIGVIKAQI 160
Cdd:PLN03167  328 AALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLI 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 161 ETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEEGIVAGGGTAFVNV---IDAVASIE 237
Cdd:PLN03167  408 EAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLaskVDAIKDTL 487

                         250
                  ....*....|....*.
gi 1274081555 238 AKGDEATGRNIVLRAL 253
Cdd:PLN03167  488 ENDEQKVGADIVKRAL 503
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-254 6.71e-43

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: 151.43  E-value: 6.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTdnekmvaELDNPYILITDKKISNiqeilpllesilqssrplLIIADD-VDGEALPTLVLNKIrgtfn 79
Cdd:cd00309   202 VFDKGYLSPYMPK-------RLENAKILLLDCKLEY------------------VVIAEKgIDDEALHYLAKLGI----- 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  80 vVAVKApgfgdRRKAMLEDIAILTGGTVITddlglELKDATIEALGQASKVSVDK----DTTVIVEGTGdvaaiahrigv 155
Cdd:cd00309   252 -MAVRR-----VRKEDLERIAKATGATIVS-----RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG----------- 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 156 ikaqietttsefdreklqerlaklsGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEE-GIVAGGGTAFVNVIDAVA 234
Cdd:cd00309   310 -------------------------GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALE 364

                         250       260
                  ....*....|....*....|..
gi 1274081555 235 SIEAK--GDEATGRNIVLRALE 254
Cdd:cd00309   365 ELAKTlpGKEQLGIEAFADALE 386
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 1-216 2.74e-30

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: 112.17  E-value: 2.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSQYMVTdnekmvaELDNPYILITDKKISNiqeilpllesilqssrplLIIADD-VDGEALPTLVLNKIrgtfn 79
Cdd:cd03333    66 VFDKGYASPYMPK-------RLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI----- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  80 vVAVKApgfgdRRKAMLEDIAILTGGTVITddlglELKDATIEALGQASKVSVDK---DTTVIVEGTGDvaaiahrigvi 156
Cdd:cd03333   116 -MAVRR-----VKKEDLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKigeEKLTFIEGCKG----------- 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 157 kaqietttsefdreklqerlaklsGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEE 216
Cdd:cd03333   174 ------------------------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-254 4.34e-24

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: 100.35  E-value: 4.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555   1 QFDRGYLSqymvtdnEKMVAELDNPYILITDKKISNIQE------------------------ILPLLESILQSSRPLLI 56
Cdd:pfam00118 184 VLDKGPLH-------PDMPKRLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVV 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555  57 IADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIAILTGGTVITDdlgleLKDATIEALGQASKVSVDK-- 134
Cdd:pfam00118 257 CQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAVSS-----LDDLTPDDLGTAGKVEEEKig 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274081555 135 -DTTVIVEGTgdvaaiahrigvikaqietttsefdreklqerlakLSGGVAVIKVGAATETELKEMKLRIEDALNATRAA 213
Cdd:pfam00118 321 dEKYTFIEGC-----------------------------------KSPKAATILLRGATDHVLDEIERSIHDALCVVKNA 365

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1274081555 214 VEE-GIVAGGGTAFVNVIDAVASIEAK--GDEATGRNIVLRALE 254
Cdd:pfam00118 366 IEDpRVVPGGGAVEMELARALREYAKSvsGKEQLAIEAFAEALE 409
 
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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