|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 983.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 2 AAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 82 SDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQI 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 162 IADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 242 KSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 322 RIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 402 ATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKG-NYGYNA 480
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2516816294 481 ATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELMENK 528
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKK 528
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-526 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 908.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 2 AAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 82 SDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQI 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 162 IADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 242 KSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 322 RIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 402 ATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNYGYNAA 481
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2516816294 482 TGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELME 526
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPE 525
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-523 |
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: 899.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 4 KQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKTSD 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 84 NAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQIIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 164 DAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVAKS 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 244 SRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAKRI 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 324 EVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 404 RAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNYGYNAATG 483
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2516816294 484 EYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVE 523
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-523 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 872.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 1 MAAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 81 TSDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQ 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 161 IIADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 241 AKSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 321 KRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 401 HATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNYGYNA 480
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2516816294 481 ATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVE 523
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAE 523
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-526 |
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: 867.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 3 AKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKTS 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 83 DNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQII 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 163 ADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 243 SSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 323 IEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 403 TRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNYGYNAAT 482
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2516816294 483 GEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELME 526
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-526 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 808.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 1 MAAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 81 TSDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQ 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 161 IIADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 241 AKSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 321 KRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 401 HATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNYGYNA 480
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2516816294 481 ATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELME 526
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPK 526
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-524 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 802.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 1 MAAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 81 TSDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQ 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 161 IIADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 241 AKSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 321 KRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 401 HATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKG-NYGYN 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2516816294 480 AATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVEL 524
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAEL 525
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-523 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 763.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 2 AAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 82 SDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQI 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 162 IADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 242 KSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 322 RIEVAKENTTIIDGAGDGKSIearvkqiraqieeatsdydreklqervaklaggvaVIRVGAATEVEMKEKKARVEDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 402 ATRAAVEEGVVPGGGVALLRAKQAITGLKGDTA-DQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGK-GNYGYN 479
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2516816294 480 AATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVE 523
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-528 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 742.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 2 AAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 82 SDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQI 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 162 IADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 242 KSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEE-TGMSLEKATLQDLGQA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 321 KRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 401 HATRAAVEEGVVPGGGVALLRAKQAITGLKGD---TADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGK-GNY 476
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEEDnelTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2516816294 477 GYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELMENK 528
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEK 544
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 673.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 3 AKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASKTS 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 83 DNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQII 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 163 ADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIR-DLLPVLEQVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 242 KSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 322 RIEVAKENTTIIdGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 402 ATRAAVEEGVVPGGGVALLRAKQ-----AITGLKGdtaDQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVLNGKGNY 476
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSEnlktwAKNNLKE---DELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEI 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2516816294 477 GYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELMENK 528
Cdd:CHL00093 478 GYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-524 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 660.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 1 MAAKQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 81 TSDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQ 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 161 IIADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 241 AKSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 321 KRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 401 HATRAAVEEGVVPGGGVALLRAKQAITGLKGDTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVL-NGKGNYGYN 479
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILeKEQYSYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2516816294 480 AATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVEL 524
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAEL 525
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-526 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 542.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 2 AAKQVLFADE--ARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLVKDVAS 79
Cdd:PLN03167 55 AAKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 80 KTSDNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSkEIAQVGSISANSDASIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 160 QIIADAMDKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINSPEKQVAALDDPYVLIYDKKVSNIRDLLPVLEQ 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 240 VAKSSRPLLIIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKAMLEDIAILTGGTVISEETGMSLEKATLQDLGQ 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 320 AKRIEVAKENTTIIDGAGDGKSIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAATEVEMKEKKARVEDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 400 LHATRAAVEEGVVPGGGVALLRAKQAITGLKG--DTADQNAGIKLILRAVEEPLRTIVTNAGDEASVVVNTVL-NGKGNY 476
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLsNDNPKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2516816294 477 GYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVELME 526
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE 583
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-522 |
5.52e-152 |
|
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: 443.41 E-value: 5.52e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 4 KQVLFADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSD 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEV----EHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 84 NAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKP--VTTSKEIAQVGSISANS------D 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 156 ASIGQIIADAMDKVGKE------GVITVEDGKS---LENELdvVEGMQFDRGYLSPYFInspekqvAALDDPYVLIYDKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 227 VSNirdllpvleqvakssrplLIIAED-VEGEALATLVVNNIrgilktTAVKApgfgdRRKAMLEDIAILTGGTVISeet 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 306 gmSLEKATLQDLGQAKRIEVAK----ENTTIIDGAGdgksiearvkqiraqieeatsdydreklqervaklaGGVAVIRV 381
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 382 GAATEVEMKEKKARVEDALHATRAAVEE-GVVPGGGVALLRAKQAITGL-KGDTADQNAGIKLILRAVEEPLRTIVTNAG 459
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516816294 460 DEASVVVNTVL----NGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVV 522
Cdd:cd00309 398 LDPIEVVTKLRakhaEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-523 |
1.83e-82 |
|
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: 265.61 E-value: 1.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEI----QHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 103 GLKYVAAGFNPIDLKRGIDKAVAAAVEELK-KLSKPVT--TSKEIAQVGSISANSDAS------IGQIIADA-------- 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsIISIPVEdvDREDLLKVARTSLSSKIIsresdfLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 166 -MDKVGKEGVITVEdGKSLEnELDVVEGMQFDRGYLSPyfiNSPEKqvaaLDDPYVLIYDKKVSNIRD------------ 232
Cdd:pfam00118 157 gSFDLGNIGVVKIL-GGSLE-DSELVDGVVLDKGPLHP---DMPKR----LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 233 ------------LLPVLEQVAKSSRPLLIIAEDVEGEALATLVVNNIRGILKTtavkapgfgdrRKAMLEDIAILTGGTV 300
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 301 ISeetgmSLEKATLQDLGQAKRIEVAK---ENTTIIDGAGDGKSiearvkqiraqieeatsdydreklqervaklaggvA 377
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVEEEKigdEKYTFIEGCKSPKA-----------------------------------A 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 378 VIRVGAATEVEMKEKKARVEDALHATRAAVEE-GVVPGGGVALLRAKQAI-TGLKGDTADQNAGIKLILRAVEEPLRTIV 455
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALrEYAKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2516816294 456 TNAGDEASVVVNTVL----NGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVVE 523
Cdd:pfam00118 417 ENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKA 488
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
9.26e-42 |
|
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: 149.15 E-value: 9.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 142 KEIAQVGSISANS-----DASIGQIIADAMDKVGKE------GVITVEDGKS---LENELdvVEGMQFDRGYLSPYFIns 207
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYMP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 208 pekqvAALDDPYVLIYDKKVSNirdllpvleqvakssrplLIIAED-VEGEALATLVVNNIrgilktTAVKApgfgdRRK 286
Cdd:cd03333 78 -----KRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 287 AMLEDIAILTGGTVISeetgmSLEKATLQDLGQAKRIEV----AKENTTIIDGAGdgksiearvkqiraqieeatsdydr 362
Cdd:cd03333 124 EDLERIARATGATIVS-----SLEDLTPEDLGTAELVEEtkigEEKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2516816294 363 eklqervaklaGGVAVIRVGAATEVEMKEKKARVEDALHATRAAVEE 409
Cdd:cd03333 174 -----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
22-515 |
1.16e-25 |
|
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: 110.43 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 22 VLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQ 101
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 102 EGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTS-----KEIAQVGSISANSDAS---IGQIIADAMDKVGKEG 173
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlRKIAKTSLTGKGAEAAkdkLADLVVDAVLQVAEKR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 174 ------------VITVEDGKSLENELdvVEGMQFDRGYLSPyfiNSPEK----QVAALDDPYVLIYDKKVSNIR------ 231
Cdd:cd03343 182 dgkyvvdldnikIEKKTGGSVDDTEL--IRGIVIDKEVVHP---GMPKRvenaKIALLDAPLEVKKTEIDAKIRitspdq 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 232 ----------DLLPVLEQVAKSSRPLLIIAEDVEGEALATLVVnniRGILKTTAVKapgfgdrrKAMLEDIAILTGGTVI 301
Cdd:cd03343 257 lqafleqeeaMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAK---AGILAVRRVK--------KSDMEKLARATGAKIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 302 SeetgmSLEKATLQDLGQAKRIE---VAKENTTIIDGAGDGKSIearvkqiraqieeatsdydreklqervaklaggvaV 378
Cdd:cd03343 326 T-----NIDDLTPEDLGEAELVEerkVGDDKMVFVEGCKNPKAV-----------------------------------T 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 379 IRVGAATEVEMKEKKARVEDALHATRAAVEEG-VVPGGG-----VAL-LRAKQAITGLKGDTAdqnagIKLILRAVEEPL 451
Cdd:cd03343 366 ILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGaveieLAKrLREYARSVGGREQLA-----VEAFADALEEIP 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516816294 452 RTIVTNAGDEAsvvVNTVL-------NGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLL 515
Cdd:cd03343 441 RTLAENAGLDP---IDTLVelraaheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMIL 508
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
17-522 |
1.50e-14 |
|
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: 76.34 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 17 VRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKfeniGAQLVKDVASKTSDNAGDGTTTATVLA 96
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 97 QAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSK--------EIAQVGSIS---ANSDASIGQIIADA 165
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrelleKCAATALSSkliSHNKEFFSKMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 166 MDKVGKE-------GVITVEDGkSLENELdVVEGMQFDRGYLSPYFINSPekqvaalddpyvliydKKVSNIRDLLPVLE 238
Cdd:TIGR02345 180 VLSLDRDdldlkliGIKKVQGG-ALEDSQ-LVNGVAFKKTFSYAGFEQQP----------------KKFANPKILLLNVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 239 QVAKSSRP-LLIIAEDVEG-----EALATLVVNNIRGILKTTA----VKAPgFGDRRKAMLEDIAILTGGTVISEetgms 308
Cdd:TIGR02345 242 LELKAEKDnAEIRVEDVEDyqaivDAEWAIIFRKLEKIVESGAnvvlSKLP-IGDLATQYFADRDIFCAGRVSAE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 309 lekatlqDLGQakrieVAKENTTIIDGAGDGksIEARVKQIRAQIEEATSDYDREKLQERVAKLAGGVAVIRVGAatEVE 388
Cdd:TIGR02345 316 -------DLKR-----VIKACGGSIQSTTSD--LEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGA--EQF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 389 MKEKKARVEDALHATRAAVE-EGVVPGGGV------ALLRAKQAITGLKgdtadQNAGIKLILRAVEEPLRTIVTNAGDE 461
Cdd:TIGR02345 380 IEEAERSLHDAIMIVRRALKnKKIVAGGGAiemelsKCLRDYSKTIDGK-----QQLIINAFAKALEIIPRQLCENAGFD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2516816294 462 ASVVVNTV----LNGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLLTAEAAVV 522
Cdd:TIGR02345 455 SIEILNKLrsrhAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETIT 519
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
23-141 |
1.27e-12 |
|
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: 70.22 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLvkdvaSKTSDNA-GDGTTTATVLAQAVVQ 101
Cdd:TIGR02343 39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL-----SKSQDDEiGDGTTGVVVLAGALLE 113
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2516816294 102 EGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTS 141
Cdd:TIGR02343 114 QAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAD 153
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
11-143 |
1.39e-12 |
|
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: 70.01 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 11 EARVRIVRGVN---VLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKfeniGAQLVKDVASKTSDNAGD 87
Cdd:cd03340 13 QGKGQLISNINacqAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGD 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2516816294 88 GTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSkpVTTSKE 143
Cdd:cd03340 89 GTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA--VNIDKE 142
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-143 |
4.00e-12 |
|
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: 68.48 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQE 102
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDV----DHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2516816294 103 GLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKE 143
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD 151
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-143 |
5.08e-12 |
|
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: 68.12 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 9 ADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSF--GAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGV----DNPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2516816294 87 DGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKE 143
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-515 |
5.55e-11 |
|
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: 65.00 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKFENIGAQLvkdvaSKTSD-NAGDGTTTATVLAQAVVQ 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDiEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 102 EGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGS---------ISANSDaSIGQIIADAMDKVGKE 172
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSattslnskvVSQYSS-LLAPIAVDAVLKVIDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 173 GVITVED----------GKSLENElDVVEGM----QFDRGYLSPYFIN-----------SPEK-----QVAALDdpYVLI 222
Cdd:cd03338 174 ATATNVDlkdirivkklGGTIEDT-ELVDGLvftqKASKKAGGPTRIEkakigliqfclSPPKtdmdnNIVVND--YAQM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 223 yDKKVSNIRD-LLPVLEQVAKSSRPLLIIAEDVEGEALATLVVnNIRGILKTTAVKapgfgDRRKAMLEDIAILTGGTVI 301
Cdd:cd03338 251 -DRILREERKyILNMCKKIKKSGCNVLLIQKSILRDAVSDLAL-HFLAKLKIMVVK-----DIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 302 SeetgmSLEKATLQDLGQAKRievakenttiidgagdgksiearvkqiraqIEEATSDYDREKLQERVAKLAGGVAVIrV 381
Cdd:cd03338 324 A-----SIDHFTEDKLGSADL------------------------------VEEVSLGDGKIVKITGVKNPGKTVTIL-V 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 382 GAATEVEMKEKKARVEDALHATRAAVEE-GVVPGGG-----VALLRAKQAITgLKGDTAdqnagikLILRAVEEPLRTIV 455
Cdd:cd03338 368 RGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGapeieIALQLSEWART-LTGVEQ-------YCVRAFADALEVIP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516816294 456 T----NAGDEASVVV----NTVLNGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLL 515
Cdd:cd03338 440 YtlaeNAGLNPISIVtelrNRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-518 |
1.02e-10 |
|
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: 64.20 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIElkdkFENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQE 102
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 103 GLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKP--VTTSKEIA-QVGSISANSDASIG------QIIADAMDKVGKEG 173
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPveIDTDRELLlSVARTSLRTKLHADladqltEIVVDAVLAIYKPD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 174 ---------VITVEDGKSLENELdvVEGMQFDRGYLSPyfiNSPEKqvaaLDDPYVLI------YDKK----------VS 228
Cdd:cd03342 180 epidlhmveIMQMQHKSDSDTKL--IRGLVLDHGARHP---DMPKR----VENAYILTcnvsleYEKTevnsgffysvVI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 229 NIRDLLPV-LEQVAKSsrplliiaedvegealatlvvnnirGILKTTAVKapgfgdRRKamLEDIAILTGGTVISeetgm 307
Cdd:cd03342 251 NQKGIDPPsLDMLAKE-------------------------GILALRRAK------RRN--MERLTLACGGVAMN----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 308 SLEKATLQDLGQAKRI---EVAKENTTIIDGAGDGKS----IEARVKQIRAQIEEAtsdydreklqervaklaggvavir 380
Cdd:cd03342 293 SVDDLSPECLGYAGLVyerTLGEEKYTFIEGVKNPKSctilIKGPNDHTITQIKDA------------------------ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 381 vgaatevemkekkarVEDALHATRAAVEEG-VVPGGGVALLRAKQAITGLKGDTADQNagiKLILRAVEEPL----RTIV 455
Cdd:cd03342 349 ---------------IRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLKEFKKSVKGKA---KLGVQAFADALlvipKTLA 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516816294 456 TNAGDEASVVVNTVLN----GKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVAS-LLLTAE 518
Cdd:cd03342 411 ENSGLDVQETLVKLQDeyaeGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDE 478
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-515 |
2.04e-10 |
|
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: 63.34 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 9 ADEARVRIVRGVNVLANAVKTTLGPKGRNVVLER--SFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 87 DGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLS-----KPVTTSKEIAQVGSISANSDA----- 156
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIARTTLSSKIlsqhk 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 157 -SIGQIIADAMDKVGKEG------VITVEDGKSLENELDvvEGMQFDR--GYLSPYFINSPEKQVA--ALDDPYVLIYDK 225
Cdd:TIGR02341 168 dHFAQLAVDAVLRLKGSGnleaiqIIKKLGGSLADSYLD--EGFLLDKkiGVNQPKRIENAKILIAntGMDTDKVKIFGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 226 KVSniRDLLPVLEQVAKSSRPLL------IIAEDVEGEALATLVVNNIRGILKTTAVKAPGFGDRRKamLEDIAILTGGT 299
Cdd:TIGR02341 246 RVR--VDSTAKVAELEHAEKEKMkekvekILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 300 VISeetgmSLEKATLQDLGQAKRIEvakentTIIDGagdgksiearvkqiraqieeatsdydREKLQERVAKLAGGVAVI 379
Cdd:TIGR02341 322 IVS-----TFDHPELVKLGSCDLIE------EIMIG--------------------------EDKLLKFSGVKLGEACTI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 380 RVGAATEVEMKEKKARVEDALHATRAAVEEG-VVPGGGVALLRAKQAITGLKGDTADQNA-GIKLILRAVEEPLRTIVTN 457
Cdd:TIGR02341 365 VLRGATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEAlAVEAFARALRQLPTIIADN 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2516816294 458 AGDEASVVVNTV----LNGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLL 515
Cdd:TIGR02341 445 AGFDSAELVAQLraahYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVIL 506
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-135 |
3.10e-10 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 62.74 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 9 ADEARVRIVRGVNVLANAVKTTLGPKGRNVVLE------RSfGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVaSKTS 82
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegpRS-GNVTVTNDGATILKSVWL----DNPAAKILVDI-SKTQ 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2516816294 83 DN-AGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLS 135
Cdd:PTZ00212 94 DEeVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-515 |
2.09e-09 |
|
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: 59.80 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 8 FADEARVRIVRGVNVLA-----NAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELKDKfeniGAQLVKDVASKTS 82
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAakavaDAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 83 DNAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQII 162
Cdd:TIGR02342 77 IEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 163 ADAMDKVGKEGVITVEDGKSLEN-----------------ELDVVEGMQFDRGY----------------LSPYFINSP- 208
Cdd:TIGR02342 157 SSLLAPLAVDAVLKVIDPENAKNvdlndikvvkklggtidDTELIEGLVFTQKAsksaggptriekakigLIQFQISPPk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 209 ---EKQVAALDdpYVLIyDKKVSNIRD-LLPVLEQVAKSSRPLLIIAEDVEGEALATLVVN--NIRGILKTTAVkapgfg 282
Cdd:TIGR02342 237 tdmENQIIVND--YAQM-DRVLKEERAyILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHflAKMKIMVVKDI------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 283 DRrkamlEDIAILTGGtvISEETGMSLEKATLQDLGQAkriEVAKENTTiidgaGDGKSIeaRVKQIRAqieeatsdydr 362
Cdd:TIGR02342 308 ER-----EEIEFICKT--IGCKPIASIDHFTADKLGSA---ELVEEVDS-----DGGKII--KITGIQN----------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 363 eklqervaklAGGVAVIRVGAATEVEMKEKKARVEDALHATRAAVEE-GVVPGGGVALLRAKQAITGLkgdTADQNAGIK 441
Cdd:TIGR02342 360 ----------AGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKY---ARTMKGVES 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 442 LILRAVEEPLR----TIVTNAGDEASVVV----NTVLNGKGNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASL 513
Cdd:TIGR02342 427 YCVRAFADALEvipyTLAENAGLNPIKVVtelrNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRS 506
|
..
gi 2516816294 514 LL 515
Cdd:TIGR02342 507 IL 508
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-515 |
8.80e-09 |
|
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: 57.83 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQE 102
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 103 GLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSISANSDASIGQIIADAMDKVGKEGVITVEDGKS 182
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDEN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 183 LENELD-------------------VVEGMQFDRGYLSP---YFINSPekQVAALDDPyvLIYDKKVS--NI-------- 230
Cdd:TIGR02344 184 GRKEIDikryakvekipggdiedscVLKGVMINKDVTHPkmrRYIENP--RIVLLDCP--LEYKKGESqtNIeitkeedw 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 231 -RDLLPVLEQVAK------SSRPLLIIAED-VEGEALATLVVNNIRGILKTtavkapgfgdrRKAMLEDIAILTGGTVIS 302
Cdd:TIGR02344 260 nRILQMEEEYVQLmcediiAVKPDLVITEKgVSDLAQHYLLKANITAIRRV-----------RKTDNNRIARACGATIVN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 303 EetgmsLEKATLQDLGQ-AKRIEVAK---ENTTIIDGAGDGKSiearvkqiraqieeatsdydreklqervaklaggVAV 378
Cdd:TIGR02344 329 R-----PEELRESDVGTgCGLFEVKKigdEYFTFITECKDPKA----------------------------------CTI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 379 IRVGAATEVeMKEKKARVEDALHATRAAVEEG-VVPGGGVALLRAKQAITglkgDTADQNAGI-KLILRAVEEPL----R 452
Cdd:TIGR02344 370 LLRGASKDI-LNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALT----EKSKKLEGVeQWPYRAVADALeiipR 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 453 TIVTNAGdeASVVVN-TVLNGK------GNYGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLL 515
Cdd:TIGR02344 445 TLAQNCG--ANVIRTlTELRAKhaqennCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLL 512
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-515 |
3.34e-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: 56.28 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 23 LANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTTTATVLAQAVVQE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQI----QHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 103 GLKYVAAGFNPIDLKRGIDKAVAAAVEELK--KLSKPVTTSKEI-AQVGSISANSDASIG------QIIADAMDKVGKEG 173
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREFlLNVARTSLRTKLPADladqltEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 174 ------VITVEDGKS-LENELDVVEGMQFDRGYLSPyfiNSPEKqvaaLDDPYVLI------YDK---------KVSNIR 231
Cdd:TIGR02347 184 edidlfMVEIMEMKHkSATDTTLIRGLVLDHGARHP---DMPRR----VKNAYILTcnvsleYEKtevnsgffySSAEQR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 232 DLLPVLEQVAKSSRPLLII---AEDVEGEALATLVVNNIRGI-------LKTTAVKAPGFGDRRKamLEDIAILTGGTVI 301
Cdd:TIGR02347 257 EKLVKAERKFVDDRVKKIIelkKKVCGKSPDKGFVVINQKGIdppsldlLAKEGIMALRRAKRRN--MERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 302 SeetgmSLEKATLQDLGQAK---RIEVAKENTTIIDGAGDGKSIearvkqiraqieeatsdydreklqervaklaggvaV 378
Cdd:TIGR02347 335 N-----SVEDLTPECLGWAGlvyETTIGEEKYTFIEECKNPKSC-----------------------------------T 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 379 IRVGAATEVEMKEKKARVEDALHATRAAVEEG-VVPGGG---VALLRA-KQAITGLKGdtaDQNAGIKLILRAVEEPLRT 453
Cdd:TIGR02347 375 ILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGafeIAAYRHlKEYKKSVKG---KAKLGVEAFANALLVIPKT 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2516816294 454 IVTNAG-DEASVVVNTV--LNGKGNY-GYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLL 515
Cdd:TIGR02347 452 LAENSGfDAQDTLVKLEdeHDEGGEVvGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLL 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
11-515 |
1.06e-07 |
|
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: 54.61 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 11 EARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTT 90
Cdd:cd03337 16 KAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 91 TATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSKPVTTSKEIAQVGSIsansDASIG-QIIADAMDKV 169
Cdd:cd03337 92 SVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKII----KSCIGtKFVSRWSDLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 170 GK---EGVITVEDGKSLEN-ELD-------------------VVEGMQFDRGYLSP---YFINSPekQVAALDDP--YVL 221
Cdd:cd03337 168 CNlalDAVKTVAVEENGRKkEIDikryakvekipggeiedsrVLDGVMLNKDVTHPkmrRRIENP--RIVLLDCPleYLV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 222 IYDKKVSnirDLlpvleqvakssrplliiaedvegeALATLVVNNIRGILKTtavkapgfgdrRKAMLEDIAILTGGTVI 301
Cdd:cd03337 246 ITEKGVS---DL------------------------AQHYLVKAGITALRRV-----------RKTDNNRIARACGATIV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 302 SEEtgmslEKATLQDLGQ-AKRIEVAK---ENTTIIDGAGDGK--SIearvkqiraqieeatsdydreklqervaklagg 375
Cdd:cd03337 288 NRP-----EELTESDVGTgAGLFEVKKigdEYFTFITECKDPKacTI--------------------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 376 vaVIRvGAATEVeMKEKKARVEDALHATRAAVEEG-VVPGGG-------VALLRAKQAITGLKgdtadqnagiKLILRAV 447
Cdd:cd03337 330 --LLR-GASKDV-LNEVERNLQDAMAVARNIILNPkLVPGGGatemavsHALSEKAKSIEGVE----------QWPYKAV 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516816294 448 EEPL----RTIVTNAGdeASVV-VNTVLNGK----GN--YGYNAATGEYGDLVEQGVLDPTKVTRTALQNAASVASLLL 515
Cdd:cd03337 396 ASALevipRTLAQNCG--ANVIrTLTELRAKhaqgENstWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLL 472
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
9-197 |
2.08e-07 |
|
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: 53.57 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 9 ADEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDG 88
Cdd:TIGR02346 16 LEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEV----QHPAAKLLVMASEMQENEIGDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 89 TTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLSkpVTTSKEIAQVGSISANSDASI---------- 158
Cdd:TIGR02346 92 TNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELV--VWEVKDLRDKDELIKALKASIsskqygnedf 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2516816294 159 -GQIIADAMDKVGKEGVIT--VED-------GKSLENElDVVEGMQFDR 197
Cdd:TIGR02346 170 lAQLVAQACSTVLPKNPQNfnVDNirvckilGGSLSNS-EVLKGMVFNR 217
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
10-133 |
4.22e-07 |
|
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: 52.80 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 10 DEARVRIVRGVNVLANAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGT 89
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEV----EHPAAKILVELAQLQDREVGDGT 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2516816294 90 TTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKK 133
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE 130
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
17-169 |
7.55e-07 |
|
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: 51.90 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 17 VRGVNVLA-----NAVKTTLGPKGRNVVLERSFGAPTVTKDGVSVAKEIELkdkfENIGAQLVKDVASKTSDNAGDGTTT 91
Cdd:cd03335 9 VRTQNVTAamaiaNIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEV----EHPAAKILVELAQLQDKEVGDGTTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 92 ATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKK-LSKPVTT-SKE----IAQVgSISA---NSDASI-GQI 161
Cdd:cd03335 85 VVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNlGKEslinVAKT-SMSSkiiGADSDFfANM 163
|
....*...
gi 2516816294 162 IADAMDKV 169
Cdd:cd03335 164 VVDAILAV 171
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
9-516 |
3.26e-06 |
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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: 49.53 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 9 ADEARVRIVRGVNVLANAVKTTLGPKGRN--VV--LERSFgaptVTKDGVSVAKEIElkdkFENIGAQLVKDvASKTSD- 83
Cdd:cd03341 6 LEEAVLRNIEACKELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEe 76
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 84 NAGDGTTTATVLAQAVVQEGLKYVAAGFNPIDLKRGIDKAVAAAVEELKKLS----KPVTTSKEIAQVGSISANSDAS-- 157
Cdd:cd03341 77 EIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvykiEDLRNKEEVSKALKTAIASKQYgn 156
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 158 ---IGQIIADAMDKV--GKEGVITVE-------DGKSLENElDVVEGMQFDRGylspyfinsPEKQVAALDDPYVLIY-- 223
Cdd:cd03341 157 edfLSPLVAEACISVlpENIGNFNVDnirvvkiLGGSLEDS-KVVRGMVFKRE---------PEGSVKRVKKAKVAVFsc 226
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 224 --DKKVSNIrdllpvleqVAKSSrplliiaedVEGEALATLvvnNIRGILkttAVKAPG-FGDRRkamledIAILTGGTV 300
Cdd:cd03341 227 pfDIGVNVI---------VAGGS---------VGDLALHYC---NKYGIM---VIKINSkFELRR------LCRTVGATP 276
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 301 IseetgMSLEKATLQDLGQAKRIEVakenttiidgagdgKSIEARVKQIRAQIEEATSdydreklqervaklaggVAVIR 380
Cdd:cd03341 277 L-----PRLGAPTPEEIGYCDSVYV--------------EEIGDTKVVVFRQNKEDSK-----------------IATIV 320
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516816294 381 VGAATEVEMKEKKARVEDALHATRAAVEEG-VVPGGGVALLRAKQAIT--GLKGDTADQNAgIKLILRAVEEPLRTIVTN 457
Cdd:cd03341 321 LRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKKLKeyGEKTPGLEQYA-IKKFAEAFEVVPRTLAEN 399
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490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2516816294 458 AGDEASVVVNTVL----NGKGNYGYNAATGEYG--DLVEQGVLDPTKVTRTALQNAASVASLLLT 516
Cdd:cd03341 400 AGLDATEVLSELYaahqKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLATEAAVTVLR 464
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