|
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: 960.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 2 AAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 82 SDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGER 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 162 IAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 242 KAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 322 RIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 402 ATRAAVEEGIVPGGGVALLRARANI-TVKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSG-NYGYNA 479
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALeALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 736784039 480 ANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEIADDKA 528
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKA 529
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-522 |
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: 877.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 4 KEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRTSD 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 84 NAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGERIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 164 EAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQVAKA 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 244 GRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQAKRI 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 324 EVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 404 RAAVEEGIVPGGGVALLRARANI-TVKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSGNYGYNAANG 482
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALdKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 736784039 483 TYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCE 522
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 874.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 2 AAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 82 SDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGER 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 162 IAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 242 KAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 322 RIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 402 ATRAAVEEGIVPGGGVALLRARANIT-VKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSGNYGYNAA 480
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDeLAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 736784039 481 NGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEIADDKA 528
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 850.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 1 MAAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASR 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 81 TSDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGE 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 161 RIAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 241 AKAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 321 KRIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 401 HATRAAVEEGIVPGGGVALLRARANIT-VKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSGNYGYNA 479
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRgLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 736784039 480 ANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEIADDKA 528
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-523 |
0e+00 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 840.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 3 AKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRTS 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 83 DNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGERI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 163 AEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 243 AGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 323 IEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 403 TRAAVEEGIVPGGGVALLRARANI-TVKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSGNYGYNAAN 481
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALeGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 736784039 482 GTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEI 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADK 522
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-523 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 777.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 1 MAAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASR 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 81 TSDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGE 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 161 RIAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 241 AKAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 321 KRIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 401 HATRAAVEEGIVPGGGVALLRARANI-TVKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSGNYGYNA 479
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALdKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 736784039 480 ANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEI 523
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEK 524
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-523 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 773.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 1 MAAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASR 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 81 TSDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGE 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 161 RIAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 241 AKAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 321 KRIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 401 HATRAAVEEGIVPGGGVALLRARANIT-VKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSG-NYGYN 478
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGrINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 736784039 479 AANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEI 523
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAEL 525
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 746.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 2 AAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 82 SDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGER 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 162 IAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 242 KAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 322 RIEVGKENTIVIDGAGEAASIearvkqvrvqieeatsdydreklqervaklaggvaVIKVGAATEVEMKEKKARVEDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 402 ATRAAVEEGIVPGGGVALLRARA---NITVKGDNpDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAA-VLAGSGNYGY 477
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARalrELAAKLEG-DEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKvRAAKDKGFGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 736784039 478 NAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEIADDKA 528
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-528 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 729.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 2 AAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 82 SDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGER 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 162 IAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 242 KAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEE-VGLTLEKVTLAELGQA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 321 KRIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 401 HATRAAVEEGIVPGGGVALLRARANI-TVKGDN---PDQDAGIKIVLRAMEEPLRMIVQNAGEE-ASVVVAAVLAGSGNY 475
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLdKLEEDNeltPDQRTGVKIVRNALRLPTKQIAENAGVEgAVVVEKILEKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 736784039 476 GYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEIADDKA 528
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-520 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 671.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 3 AKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASRTS 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 83 DNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGERI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 163 AEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIR-DLLPVLEQVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 242 KAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 322 RIEVGKENTIVIdGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 402 ATRAAVEEGIVPGGGVALLRARANITVKGDN---PDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSGNYGYN 478
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNnlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYN 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 736784039 479 AANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMV 520
Cdd:CHL00093 481 AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECII 522
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-523 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 638.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 1 MAAKEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVASR 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 81 TSDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGE 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 161 RIAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 241 AKAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 321 KRIEVGKENTIVIDGAGEAASIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 401 HATRAAVEEGIVPGGGVALLRARANIT-VKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSG-NYGYN 478
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKgIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 736784039 479 AANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEI 523
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAEL 525
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-525 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 524.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 2 AAKEVVFGDAARA--KMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLMNMGAQMVKEVAS 79
Cdd:PLN03167 55 AAKELHFNKDGSAikKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 80 RTSDNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTkEIAQVGAISANSDYSIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 160 ERIAEAMEKVGKEGVITVEDGKSLNDELDIVEGMQFDRGYLSPYFINNPEKQVAVLDSPFVLLCDKKISNIRDLLPVLEQ 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 240 VAKAGRPLLIIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELGQ 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 320 AKRIEVGKE-NTIVIDGAGEAAsIEARVKQVRVQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVED 398
Cdd:PLN03167 374 AAKVVLTKDtTTIVGDGSTQEA-VNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVED 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 399 ALHATRAAVEEGIVPGGGVALLRARAN---ITVKGDNPDQDAGIKIVLRAMEEPLRMIVQNAGEEASVVVAAVLAGSG-N 474
Cdd:PLN03167 453 ALNATKAAVEEGIVVGGGCTLLRLASKvdaIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpK 532
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 736784039 475 YGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMVCEIAD 525
Cdd:PLN03167 533 FGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE 583
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-520 |
1.87e-146 |
|
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: 429.16 E-value: 1.87e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 4 KEVVFGDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTSD 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 84 NAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARP--CTTTKEIAQVGAISANS------D 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 156 YSIGERIAEAMEKVGKE------GVITVEDGKS---LNDELdiVEGMQFDRGYLSPYFInnpekqvAVLDSPFVLLCDKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 227 ISNirdllpvleqvakagrplLIIAED-IEGEALATLVVNNIrgilktCAVKApgfgdRRKAMLEDIAVLTGGQVIAeev 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 306 glTLEKVTLAELGQAKRIEVGK----ENTIVIDGAGeaasiearvkqvrvqieeatsdydreklqervaklaGGVAVIKV 381
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 382 GAATEVEMKEKKARVEDALHATRAAVEE-GIVPGGGVALLRARANIT--VKGDNPDQDAGIKIVLRAMEEPLRMIVQNAG 458
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736784039 459 EEASVV----VAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMV 520
Cdd:cd00309 398 LDPIEVvtklRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-520 |
5.76e-81 |
|
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: 261.75 E-value: 5.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLmnmgAQMVKEVASRTSDNAGDGTTTATVLAQAIVRE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 103 GMKFVAAGMNPMDLKRGIDKAVAATVEEL-AKIARPCT--TTKEIAQVGAISANSDYS------IGERIAEAMEKVGKE- 172
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILdSIISIPVEdvDREDLLKVARTSLSSKIIsresdfLAKLVVDAVLAIPKNd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 173 --------GVITVEdGKSLNDeLDIVEGMQFDRGYLSPyfinnpeKQVAVLDSPFVLLCDKKISNIRD------------ 232
Cdd:pfam00118 157 gsfdlgniGVVKIL-GGSLED-SELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 233 ------------LLPVLEQVAKAGRPLLIIAEDIEGEALATLVVNNIRGILKTcavkapgfgdrRKAMLEDIAVLTGGQV 300
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 301 IAEEVGLTLEkvtlaELGQAKRIE---VGKENTIVIDGAGEaasiearvkqvrvqieeatsdydreklqervaklaGGVA 377
Cdd:pfam00118 297 VSSLDDLTPD-----DLGTAGKVEeekIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 378 VIKVGAATEVEMKEKKARVEDALHATRAAVEE-GIVPGGGVAL------LRARANiTVKGDnpDQDAgIKIVLRAMEEPL 450
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEmelaraLREYAK-SVSGK--EQLA-IEAFAEALEVIP 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736784039 451 RMIVQNAG----EEASVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMV 520
Cdd:pfam00118 413 KTLAENAGldpiEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
8.66e-40 |
|
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: 143.76 E-value: 8.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 142 KEIAQVGAISANS-----DYSIGERIAEAMEKVGKE------GVITVEDGKS---LNDELdiVEGMQFDRGYLSPYFInn 207
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYMP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 208 pekqvAVLDSPFVLLCDKKISNirdllpvleqvakagrplLIIAED-IEGEALATLVVNNIrgilktCAVKApgfgdRRK 286
Cdd:cd03333 78 -----KRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 287 AMLEDIAVLTGGQVIAeevglTLEKVTLAELGQAKRIEV----GKENTIVIDGAGeaasiearvkqvrvqieeatsdydr 362
Cdd:cd03333 124 EDLERIARATGATIVS-----SLEDLTPEDLGTAELVEEtkigEEKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 736784039 363 eklqervaklaGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 409
Cdd:cd03333 174 -----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
22-520 |
3.58e-23 |
|
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: 103.11 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 22 ILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTSDNAGDGTTTATVLAQAIVR 101
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 102 EGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCT-----TTKEIAQV---GAISANSDYSIGERIAEAMEKVGKEG 173
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDpddkdTLRKIAKTsltGKGAEAAKDKLADLVVDAVLQVAEKR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 174 -----------VITVEDGKSLNDElDIVEGMQFDRGYLSPyfiNNPEK----QVAVLDSPFVLlcdKK--------ISNI 230
Cdd:cd03343 182 dgkyvvdldniKIEKKTGGSVDDT-ELIRGIVIDKEVVHP---GMPKRvenaKIALLDAPLEV---KKteidakirITSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 231 RDLLPVLEQ-----------VAKAGRPLLIIAEDIEGEALATLVVnniRGILKTCAVKapgfgdrrKAMLEDIAVLTGGQ 299
Cdd:cd03343 255 DQLQAFLEQeeamlkemvdkIADTGANVVFCQKGIDDLAQHYLAK---AGILAVRRVK--------KSDMEKLARATGAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 300 VIAeevglTLEKVTLAELGQAKRIE---VGKENTIVIDGAGEAASIearvkqvrvqieeatsdydreklqervaklaggv 376
Cdd:cd03343 324 IVT-----NIDDLTPEDLGEAELVEerkVGDDKMVFVEGCKNPKAV---------------------------------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 377 aVIKVGAATEVEMKEKKARVEDALHATRAAVEEG-IVPGGG-----VAL-LRARANiTVKGDnpDQDAgIKIVLRAMEEP 449
Cdd:cd03343 365 -TILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGaveieLAKrLREYAR-SVGGR--EQLA-VEAFADALEEI 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736784039 450 LRMIVQNAG----EEASVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMV 520
Cdd:cd03343 440 PRTLAENAGldpiDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVI 514
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
23-356 |
3.77e-13 |
|
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: 71.76 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLmnmgAQMVKEVASRTSDNAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02343 39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 103 GMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSdySIGERIA----EAMEKVGKEGVITVE 178
Cdd:TIGR02343 115 AEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAKT--SLGSKIVskchRRFAEIAVDAVLNVA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 179 D-----------------GKSLNDElDIVEGMQFDRGYLSPYFINNPEK-QVAVLDSPFVLLCDKK-----ISNIRD--- 232
Cdd:TIGR02343 193 DmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDaKIAILTCPFEPPKPKTkhkldISSVEEykk 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 233 --------LLPVLEQVAKAGRPLLIIAEDIEGEALATLVVNNIRgilktcAVKAPGFGDrrkamLEDIAVLTGGQVIAEE 304
Cdd:TIGR02343 272 lqkyeqqkFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLP------AVRWVGGQE-----LELIAIATGGRIVPRF 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 736784039 305 VGLTLEKvtLAELGQAKRIEVG--KENTIVIDGAGEAASIEARVKQV-RVQIEEA 356
Cdd:TIGR02343 341 QELSKDK--LGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGnKMIIEEA 393
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-517 |
1.09e-12 |
|
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: 70.39 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVelkdKLMNMGAQMVKEVaSRTSD-NAGDGTTTATVLAQAIVR 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQM----SVLHPAAKMLVEL-SKAQDiEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 102 EGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGA---------ISANSDySIGERIAEAMEKVGKE 172
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSattslnskvVSQYSS-LLAPIAVDAVLKVIDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 173 GVITVED----------GKSLNDElDIVEGM----QFDRGYLSPYFINNP----------------EKQVAVLDSPfvlL 222
Cdd:cd03338 174 ATATNVDlkdirivkklGGTIEDT-ELVDGLvftqKASKKAGGPTRIEKAkigliqfclsppktdmDNNIVVNDYA---Q 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 223 CDKKISNIRD-LLPVLEQVAKAGRPLLIIAEDIEGEALATLVVnNIRGILKTCAVKapgfgDRRKAMLEDIAVLTGGQVI 301
Cdd:cd03338 250 MDRILREERKyILNMCKKIKKSGCNVLLIQKSILRDAVSDLAL-HFLAKLKIMVVK-----DIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 302 AEEVGLTLEKVTLAELgqakrievgkentividgageaasiearvkqvrvqIEEATSDYDREKLQERVAKLAGGVAVIkV 381
Cdd:cd03338 324 ASIDHFTEDKLGSADL-----------------------------------VEEVSLGDGKIVKITGVKNPGKTVTIL-V 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 382 GAATEVEMKEKKARVEDALHATRAAVEE-GIVPGGG-----VALLRARANITVKGdnpdqdaGIKIVLRAMEEPLRMI-- 453
Cdd:cd03338 368 RGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGapeieIALQLSEWARTLTG-------VEQYCVRAFADALEVIpy 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 454 --VQNAG----EEASVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTD 517
Cdd:cd03338 441 tlAENAGlnpiSIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKID 510
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-135 |
5.26e-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: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 9 GDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSF--GAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTSDNAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 736784039 87 DGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIA 135
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSA 135
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
13-135 |
3.02e-11 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 65.77 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 13 RAKMVEGVN---ILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELkdklMNMGAQMVKEVASRTSDNAGDGT 89
Cdd:cd03340 15 KGQLISNINacqAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGT 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 736784039 90 TTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIA 135
Cdd:cd03340 91 TSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA 136
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-135 |
3.19e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 65.82 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 9 GDAARAKMVEGVNILANAVKVTLGPKGRNVVLE------RSfGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTS 82
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegpRS-GNVTVTNDGATILKSVWLD----NPAAKILVDISKTQD 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 736784039 83 DNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIA 135
Cdd:PTZ00212 95 EEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-135 |
3.41e-11 |
|
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: 65.55 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVElkdkLMNMGAQMVKEVASRTSDNAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLD----IVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110
....*....|....*....|....*....|...
gi 736784039 103 GMKFVAAGMNPMDLKRGIDKAVAATVEELAKIA 135
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIA 138
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-520 |
4.75e-11 |
|
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: 65.19 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 8 FGDAARAKMVEGVNILA-----NAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELkdklMNMGAQMVKEVASRTS 82
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAakavaDAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVELSKAQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 83 DNAGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGERI 162
Cdd:TIGR02342 77 IEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 163 AEAMEKVGKEGVITVEDGKS-----LND------------ELDIVEGMQFDRGYL----SPYFINNP------------- 208
Cdd:TIGR02342 157 SSLLAPLAVDAVLKVIDPENaknvdLNDikvvkklggtidDTELIEGLVFTQKASksagGPTRIEKAkigliqfqisppk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 209 ---EKQVAVLDSPFVllcDKKISNIRD-LLPVLEQVAKAGRPLLIIAEDIEGEALATLVVN--NIRGILktcAVKapgfg 282
Cdd:TIGR02342 237 tdmENQIIVNDYAQM---DRVLKEERAyILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHflAKMKIM---VVK----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 283 DRRKAMLEDIAVLTGGQVIAEEVGLTLEKVTLAELgqakrievgkentividgageaasiearvkqvrvqIEEATSDYDR 362
Cdd:TIGR02342 306 DIEREEIEFICKTIGCKPIASIDHFTADKLGSAEL-----------------------------------VEEVDSDGGK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 363 EKLQERVAKLAGGVAVIKVGaATEVEMKEKKARVEDALHATRAAVEE-GIVPGGGVALLRARANITVKGDnpDQDAGIKI 441
Cdd:TIGR02342 351 IIKITGIQNAGKTVTVVVRG-SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYAR--TMKGVESY 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 442 VLRAMEEPLRMI----VQNAG----EEASVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLM 513
Cdd:TIGR02342 428 CVRAFADALEVIpytlAENAGlnpiKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSI 507
|
....*..
gi 736784039 514 LTTDCMV 520
Cdd:TIGR02342 508 LKIDDIV 514
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-517 |
4.13e-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: 62.18 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 9 GDAARAKMVEGVNILANAVKVTLGPKGRNVVLER--SFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTSDNAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 87 DGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIA-----RPCTTTKEIAQVGAISANSdySIGER 161
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIARTTLSS--KILSQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 162 IAEAMEKVGKEGVITVEDGKSLnDELDIVE--GMQFDRGYLSPYFI-------NNPEK--QVAVLDSPFVLLCDK-KISN 229
Cdd:TIGR02341 166 HKDHFAQLAVDAVLRLKGSGNL-EAIQIIKklGGSLADSYLDEGFLldkkigvNQPKRieNAKILIANTGMDTDKvKIFG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 230 IR---DLLPVLEQVAKAGRPLL------IIAEDIEGEALATLVVNNIRGILKTCAVKAPGFGDRRKamLEDIAVLTGGQV 300
Cdd:TIGR02341 245 SRvrvDSTAKVAELEHAEKEKMkekvekILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGEI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 301 IAeevglTLEKVTLAELGQAKRIE---VGKENTIVIDG--AGEAASIEARvkqvrvqieeatsdydreklqervaklagg 375
Cdd:TIGR02341 323 VS-----TFDHPELVKLGSCDLIEeimIGEDKLLKFSGvkLGEACTIVLR------------------------------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 376 vavikvgAATEVEMKEKKARVEDALHATRAAVEEG-IVPGGGVA-LLRARANITVKGDNPDQDA-GIKIVLRAMEEPLRM 452
Cdd:TIGR02341 368 -------GATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSeMLMSKAVTQEAQRTPGKEAlAVEAFARALRQLPTI 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736784039 453 IVQNAG----EEASVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTD 517
Cdd:TIGR02341 441 IADNAGfdsaELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVD 509
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-520 |
4.06e-09 |
|
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: 58.96 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 9 GDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKlmnmGAQMVKEVASRTSDNAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 89 TTTATVLAQAIVREGMKFVAAGMNPMDLKRG-----------IDKAVAATVEELAKIA-RPCTTTKEIAQVgaISANSDY 156
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGyrlackeavkyIKENLSVSVDELGREAlINVAKTSMSSKI--IGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 157 --SIGERIAEAMEKVGKEGVIT--VED-------GKSLNDELdIVEGMQFDRGYLS---PYFINNPekQVAVLDspFVLL 222
Cdd:TIGR02340 164 fsNIVVDAVLAVKTTNENGETKypIKAinilkahGKSARESM-LVKGYALNCTVASqqmPKRIKNA--KIACLD--FNLQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 223 CDK---KISNIRDLLPVLEQVAKagRPLLIIAEDIEG--EALATlVVNNIRGILKTCA---VKAPGFGDRR--KAMLEDI 292
Cdd:TIGR02340 239 KAKmalGVQIVVDDPEKLEQIRQ--READITKERIKKilDAGAN-VVLTTGGIDDMCLkyfVEAGAMGVRRckKEDLKRI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 293 AVLTGGQVIaeevgltlekVTLAELGQAKRIEVGKentividgAGEAASIEarvkQVRVQieeatsdyDREKLQERVAKL 372
Cdd:TIGR02340 316 AKATGATLV----------STLADLEGEETFEASY--------LGFADEVV----QERIA--------DDECILIKGTKK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 373 AGGVAVIKVGaATEVEMKEKKARVEDALHATRAAVEEG-IVPGGG---VALLRARANITVKGDNPDQDAgIKIVLRAMEE 448
Cdd:TIGR02340 366 RKSASIILRG-ANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveAALSIYLENFATTLGSREQLA-IAEFARALLI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 449 PLRMIVQNAGEEA------------SVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTT 516
Cdd:TIGR02340 444 IPKTLAVNAAKDStelvaklrayhaAAQLKPEKKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRI 523
|
....
gi 736784039 517 DCMV 520
Cdd:TIGR02340 524 DDLI 527
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
13-192 |
6.93e-09 |
|
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: 58.46 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 13 RAKMVEGV--NILA-----NAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKLmnmgAQMVKEVASRTSDNA 85
Cdd:cd03339 18 RLKGLEAHksHILAaksvaNILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 86 GDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKE----IAQVGAISANSdySIGER 161
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDnkepLIQTAMTSLGS--KIVSR 171
|
170 180 190
....*....|....*....|....*....|...
gi 736784039 162 IAEAMEKVGKEGVITVED--GKSLNDELDIVEG 192
Cdd:cd03339 172 CHRQFAEIAVDAVLSVADleRKDVNFELIKVEG 204
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-169 |
3.86e-08 |
|
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: 55.75 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 9 GDAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKDKlmnmGAQMVKEVASRTSDNAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 89 TTTATVLAQAIVREGMKFVAAGMNP--------MDLK---RGIDKAVAATVEELAK-----IARPCTTTKeiaqvgAISA 152
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPttiisgyrLACKeavKYIKEHLSISVDNLGKeslinVAKTSMSSK------IIGA 155
|
170
....*....|....*..
gi 736784039 153 NSDYsIGERIAEAMEKV 169
Cdd:cd03335 156 DSDF-FANMVVDAILAV 171
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
10-134 |
4.80e-08 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 55.51 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 10 DAARAKMVEGVNI-----LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTSDN 84
Cdd:TIGR02347 10 ESLRRDAALMMNInaargLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDI 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 736784039 85 AGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKI 134
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKF 135
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-520 |
6.01e-07 |
|
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: 52.05 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVaSRTSDN-AGDGTTTATVLAQAIVR 101
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIEL-SRTQDEeVGDGTTSVIILAGEMLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 102 EGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGERIAEAMEKVGKEGVITVEDGK 181
Cdd:TIGR02344 103 VAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 182 SLNDELDI-----VE--------------GMQFDRGYLSP---YFINNPekQVAVLDSPFVLLCDKKISNI--------- 230
Cdd:TIGR02344 183 NGRKEIDIkryakVEkipggdiedscvlkGVMINKDVTHPkmrRYIENP--RIVLLDCPLEYKKGESQTNIeitkeedwn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 231 RDLLPVLEQVAK------AGRPLLIIAED-IEGEALATLVVNNIRGILKTcavkapgfgdrRKAMLEDIAVLTGGQVIAE 303
Cdd:TIGR02344 261 RILQMEEEYVQLmcediiAVKPDLVITEKgVSDLAQHYLLKANITAIRRV-----------RKTDNNRIARACGATIVNR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 304 EVGLTLEKV-TLAELGQAKRIevGKENTIVIDGAGE--AASIEARvkqvrvqieeatsdydreklqervaklaggvavik 380
Cdd:TIGR02344 330 PEELRESDVgTGCGLFEVKKI--GDEYFTFITECKDpkACTILLR----------------------------------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 381 vGAATEVeMKEKKARVEDALHATRAAVEEG-IVPGGGVALLRARANITVKGD--NPDQDAGIKIVLRAMEEPLRMIVQNA 457
Cdd:TIGR02344 373 -GASKDI-LNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKSKklEGVEQWPYRAVADALEIIPRTLAQNC 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736784039 458 GEEASVVVAA-----VLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTDCMV 520
Cdd:TIGR02344 451 GANVIRTLTElrakhAQENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
10-151 |
3.74e-05 |
|
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: 46.25 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 10 DAARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKD---KLMNMGAQMVKEvasrtsdNAG 86
Cdd:TIGR02346 17 EEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHpaaKLLVMASEMQEN-------EIG 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736784039 87 DGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIArpCTTTKEIAQVGAIS 151
Cdd:TIGR02346 90 DGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELV--VWEVKDLRDKDELI 152
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
10-137 |
4.71e-05 |
|
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: 46.10 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 10 DAARAKMVEGVNI-----LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVASRTSDN 84
Cdd:cd03342 6 EVLRRGQALAVNIsaakgLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQ----HPTASMIARAATAQDDI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 736784039 85 AGDGTTTATVLAQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARP 137
Cdd:cd03342 82 TGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVP 134
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-189 |
4.51e-04 |
|
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: 43.05 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRNVVLERSFGAPTVTKDGVSVAKEVELKdklmNMGAQMVKEVaSRTSD-NAGDGTTTATVLAQAIVR 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIEL-SRTQDeEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 102 EGMKFVAAGMNPMDLKRGIDKAVAATVEELAKIARPCTTTKEIAQVGAISANSDYSIGERIAEAMEKVGKEGVITVEDGK 181
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAVEE 182
|
....*....
gi 736784039 182 S-LNDELDI 189
Cdd:cd03337 183 NgRKKEIDI 191
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
388-517 |
5.24e-04 |
|
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: 42.63 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 388 EMKEKKARVEDALHATRAAVEEG-IVPGGG---VAL---LRARANiTVKGDNpdqdagiKIVLRAMEEPLRMI----VQN 456
Cdd:cd03342 341 TITQIKDAIRDGLRAVKNAIEDKcVVPGAGafeVALyahLKEFKK-SVKGKA-------KLGVQAFADALLVIpktlAEN 412
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736784039 457 AG----EEASVVVAAVLAGSGNYGYNAANGTYGDMVEMGVLDPAKVTRSALQNAASIASLMLTTD 517
Cdd:cd03342 413 SGldvqETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVD 477
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-131 |
8.72e-04 |
|
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: 41.82 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736784039 23 LANAVKVTLGPKGRN--VV--LERSFgaptVTKDGVSVAKEVELKD---KLMNMGAQMVKEvasrtsdNAGDGTTTATVL 95
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQHpaaKLLVMASQMQEE-------EIGDGTNLVVVL 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 736784039 96 AQAIVREGMKFVAAGMNPMDLKRGIDKAVAATVEEL 131
Cdd:cd03341 89 AGELLEKAEELLRMGLHPSEIIEGYEKALKKALEIL 124
|
|
| |
