|
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: 976.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 2 AAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 82 SNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNI 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 162 IADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 242 KSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 322 RITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 402 ATRAAVEEGIVAGGGVALLRCVKVIDALQ-LEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKG-NYGYNV 479
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 501343239 480 ATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKEK 528
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKA 529
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 898.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 2 AAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 82 SNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNI 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 162 IADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 242 KSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 322 RITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 402 ATRAAVEEGIVAGGGVALLRCVKVIDAL-QLEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKGNYGYNVA 480
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELaGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501343239 481 TDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKEK 528
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| 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: 896.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 4 KQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKTSN 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 84 AAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNIIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 164 DAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTVAKS 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 244 GKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRAKRI 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 324 TVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 404 RAAVEEGIVAGGGVALLRCVKVIDALQ-LEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKGNYGYNVATD 482
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKaLNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 501343239 483 KYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITE 522
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-525 |
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: 872.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 3 AKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKTS 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 83 NAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNII 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 163 ADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 243 SGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 323 ITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 403 TRAAVEEGIVAGGGVALLRCVKVIDALQLEG-DEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKGNYGYNVAT 481
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 501343239 482 DKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPE 525
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-527 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 840.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 1 MAAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 81 TSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGN 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 161 IIADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 241 AKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 321 KRITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 401 HATRAAVEEGIVAGGGVALLRCVKVIDALQ-LEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKGNYGYNV 479
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501343239 480 ATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKE 527
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 797.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 1 MAAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 81 TSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGN 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 161 IIADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 241 AKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 321 KRITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 401 HATRAAVEEGIVAGGGVALLRCVKVIDALQ-LEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKGNYGYNV 479
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 501343239 480 ATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKEK 528
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEP 529
|
|
| 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: 791.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 2 AAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 82 SNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNI 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 162 IADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 242 KSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 322 RITVDKENTTIVEGAGKSSDIqgrvkqirrqidettsdydreklqerlaklaggvaVINVGAATETEMKEKKARVEDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 402 ATRAAVEEGIVAGGGVALLRCVKVIDAL--QLEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNK-GNYGYN 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501343239 479 VATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKEK 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 767.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 1 MAAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 81 TSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGN 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 161 IIADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 241 AKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 321 KRITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 401 HATRAAVEEGIVAGGGVALLRCVKVIDALQLEG-DEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKG-NYGYN 478
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNaDVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501343239 479 VATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKEK 528
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDA 530
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-528 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 732.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 2 AAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 82 SNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNI 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 162 IADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 242 KSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITED-LGIKLENVQVSDLGRA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 321 KRITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 401 HATRAAVEEGIVAGGGVALLRCVKVIDAL----QLEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNK-GNY 475
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLeednELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 501343239 476 GYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKEK 528
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-527 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 679.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 3 AKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASKTS 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 83 NAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGNII 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 163 ADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSL-QDLLPLLQTVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 242 KSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 322 RITVDKENTTIVeGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 402 ATRAAVEEGIVAGGGVALlrcVKVIDALQ------LEGDEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKGNY 475
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATL---VHLSENLKtwaknnLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEI 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 501343239 476 GYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKE 527
Cdd:CHL00093 478 GYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-526 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 670.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 1 MAAKQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 81 TSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDREEIRQVATVSANWDETIGN 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 161 IIADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQTV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 241 AKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGRA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 321 KRITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 401 HATRAAVEEGIVAGGGVALLRCVKVIDALQLEG-DEKIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKG-NYGYN 478
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNdDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501343239 479 VATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEK 526
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-527 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 550.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 2 AAKQLLF--DESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYENMGAQMVKEVAS 79
Cdd:PLN03167 55 AAKELHFnkDGSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 80 KTSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVNDrEEIRQVATVSANWDETIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 160 NIIADAMDKVGKDGTITVEEAKSIETTLDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISSLQDLLPLLQT 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 240 VAKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVCAVKAPGFGDRRKAMLEDIAVLTGGRCITEDLGIKLENVQVSDLGR 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 320 AKRITVDKENTTIVEGAGKSSDIQGRVKQIRRQIDETTSDYDREKLQERLAKLAGGVAVINVGAATETEMKEKKARVEDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 400 LHATRAAVEEGIVAGGGVALLRCVKVIDALQ--LEGDE-KIGSQIVRRAVEHPIRMLCQNAGVEGAVVVGEILSNKG-NY 475
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKdtLENDEqKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 501343239 476 GYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMITEIPEKE 527
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-521 |
1.11e-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: 444.95 E-value: 1.11e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 4 KQLLFDESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELpdpyENMGAQMVKEVASKTSN 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEV----EHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 84 AAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKK--VNDREEIRQVATVSAN------WD 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 156 ETIGNIIADAMDKVGK------DGTITVEEAKS---IETTLdvVEGMQFDKGYLSPYFatnaeaqEAILEDAYVLIHEKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYM-------PKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 227 ISSlqdllpllqtvaksgkplLVIAEE-VEGEALAALVVNKIrgtlnvCAVKApgfgdRRKAMLEDIAVLTGGRCITEdl 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 306 gikLENVQVSDLGRAKRITVDK----ENTTIVEGAGkssdiqgrvkqirrqidettsdydreklqerlaklaGGVAVINV 381
Cdd:cd00309 277 ---LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 382 GAATETEMKEKKARVEDALHATRAAVEE-GIVAGGGVALLRCVKVID--ALQLEGDEKIGSQIVRRAVEHPIRMLCQNAG 458
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501343239 459 VEGAVVVGEILS----NKGNYGYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMIT 521
Cdd:cd00309 398 LDPIEVVTKLRAkhaeGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-520 |
4.43e-85 |
|
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: 272.15 E-value: 4.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYenmgAQMVKEVASKTSNAAGDGTTTATVLAEAIYKE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 103 GLKNVTAGSNPVYLKRGIDKAVEAAVTELARV---SKKVNDREEIRQVATVSAN------WDETIGNIIADA-------- 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIisiPVEDVDREDLLKVARTSLSskiisrESDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 166 -MDKVGKDGTITVEEAKSIETTLdvVEGMQFDKGYLSPyfatnaeAQEAILEDAYVLI-------------HEKKISS-- 229
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLlncsleyektetkATVVLSDae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 230 ---------LQDLLPLLQTVAKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVcavkapgfgdrRKAMLEDIAVLTGGRC 300
Cdd:pfam00118 228 qlerflkaeEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 301 ITedlgiKLENVQVSDLGRAKRITVDK---ENTTIVEGagkssdiqgrvkqirrqidettsdydreklqerlaKLAGGVA 377
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVEEEKigdEKYTFIEG-----------------------------------CKSPKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 378 VINVGAATETEMKEKKARVEDALHATRAAVEE-GIVAGGGVALLRCVKVIDAL--QLEGDEKIGSQIVRRAVEHPIRMLC 454
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYakSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 455 QNAGVEGAVVVGEIL----SNKGNYGYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMI 520
Cdd:pfam00118 417 ENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
141-409 |
8.18e-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: 8.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 141 REEIRQVATVSAN-----WDETIGNIIADAMDKVGKD------GTITVEEAKS---IETTLdvVEGMQFDKGYLSPYFat 206
Cdd:cd03333 1 RELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 207 naeaqEAILEDAYVLIHEKKISSlqdllpllqtvaksgkplLVIAEE-VEGEALAALVVNKIrgtlnvCAVKApgfgdRR 285
Cdd:cd03333 77 -----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 286 KAMLEDIAVLTGGRCITEdlgikLENVQVSDLGRAKRITV----DKENTTIVEGAGkssdiqgrvkqirrqidettsdyd 361
Cdd:cd03333 123 KEDLERIARATGATIVSS-----LEDLTPEDLGTAELVEEtkigEEKLTFIEGCKG------------------------ 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501343239 362 reklqerlaklaGGVAVINVGAATETEMKEKKARVEDALHATRAAVEE 409
Cdd:cd03333 174 ------------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
23-520 |
7.64e-26 |
|
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: 111.20 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKE 102
Cdd:cd03343 27 VAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 103 GLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVN--DREEIRQVATVS------ANWDETIGNIIADAMDKV--GKD 172
Cdd:cd03343 103 AEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDpdDKDTLRKIAKTSltgkgaEAAKDKLADLVVDAVLQVaeKRD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 173 GTITVE---------EAKSIETTlDVVEGMQFDKGYLSPYFATNAEAQEAILEDAYVLIHEKKISS---------LQDLL 234
Cdd:cd03343 183 GKYVVDldnikiekkTGGSVDDT-ELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAkiritspdqLQAFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 235 --------PLLQTVAKSGKPLLVIAEEVEGEALAALVVNKIRGTLNVcavkapgfgdrRKAMLEDIAVLTGGRCITedlg 306
Cdd:cd03343 262 eqeeamlkEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRV-----------KKSDMEKLARATGAKIVT---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 307 iKLENVQVSDLGRAKRITVDK---ENTTIVEGagkssdiqgrvkqirrqidettsdydreklqerlAKLAGGVAVINVGa 383
Cdd:cd03343 327 -NIDDLTPEDLGEAELVEERKvgdDKMVFVEG----------------------------------CKNPKAVTILLRG- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 384 ATETEMKEKKARVEDALHATRAAVEEG-IVAGGGVALLRCVKVID--ALQLEGDEKIGSQIVRRAVEHPIRMLCQNAGVE 460
Cdd:cd03343 371 GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLReyARSVGGREQLAVEAFADALEEIPRTLAENAGLD 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501343239 461 GAVVVGEILS----NKGNYGYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMI 520
Cdd:cd03343 451 PIDTLVELRAahekGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVI 514
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
6-514 |
2.76e-14 |
|
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: 75.22 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 6 LLFDESAR----------QKILRGVELL----------SRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDP 65
Cdd:TIGR02343 2 LAFDEYGRpfiiikdqdnKKRLKGLEAKksniaaaksvASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 66 YenmgAQMVKEVASKTSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKV----NDR 141
Cdd:TIGR02343 82 I----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsadnNNR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 142 EEIRQVATVS------ANWDETIGNIIADA----MDKVGKD---GTITVEE--AKSIETTlDVVEGMQFDKGYLSPYFAT 206
Cdd:TIGR02343 158 EPLIQAAKTSlgskivSKCHRRFAEIAVDAvlnvADMERRDvdfDLIKVEGkvGGSLEDT-KLIKGIIIDKDFSHPQMPK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 207 NAE-AQEAILEDAY-----VLIHEKKISSLQDLLPL-----------LQTVAKSGKPLLVIAEEVEGEALAALVVNkirg 269
Cdd:TIGR02343 237 EVEdAKIAILTCPFeppkpKTKHKLDISSVEEYKKLqkyeqqkfkemIDDIKKSGANLVICQWGFDDEANHLLLQN---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 270 tlNVCAVKAPGFGDrrkamLEDIAVLTGGRCITedlgiKLENVQVSDLGRAKRIT-----VDKENTTIVEGAGKSSDIqg 344
Cdd:TIGR02343 313 --DLPAVRWVGGQE-----LELIAIATGGRIVP-----RFQELSKDKLGKAGLVReisfgTTKDRMLVIEQCKNSKAV-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 345 rvkqirrqidettsdydreklqerlaklaggvaVINVGAATETEMKEKKARVEDALHATRAAVEEG-IVAGGGVALLRCV 423
Cdd:TIGR02343 379 ---------------------------------TIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCS 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 424 KVID--ALQLEGDEKIGSQIVRRAVEHPIRMLCQNAGVE-----GAVVVGEILSNKGNYGYNVATDKYEDLVKAGVVDPT 496
Cdd:TIGR02343 426 LAVSqeADKYPGVEQYAIRAFADALETIPMALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETL 505
|
570
....*....|....*...
gi 501343239 497 KVTRTALQNAASVAGLLL 514
Cdd:TIGR02343 506 IGKKQQILLATQLVRMIL 523
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
5-521 |
2.79e-12 |
|
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: 69.02 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 5 QLLFDESARQKIlrgvellSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNA 84
Cdd:TIGR02345 19 QLISNINACVAI-------AEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 85 AGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVS-----KKVNDREEIRQVATVS------AN 153
Cdd:TIGR02345 88 VGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAvtideEKGEQRELLEKCAATAlsskliSH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 154 WDETIGNIIADAMDKVGKD----GTITVEEAK--SIETTLdVVEGMQFDKGYLSPYFatnaEAQEAiledayvLIHEKKI 227
Cdd:TIGR02345 168 NKEFFSKMIVDAVLSLDRDdldlKLIGIKKVQggALEDSQ-LVNGVAFKKTFSYAGF----EQQPK-------KFANPKI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 228 SSLQDLLPLlqTVAKSGKPLLViaEEVEG-----EALAALVVNKIRGTL----NVCAVKAPgFGDRRKAMLEDIAVLTGG 298
Cdd:TIGR02345 236 LLLNVELEL--KAEKDNAEIRV--EDVEDyqaivDAEWAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADRDIFCAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 299 RCITEDLGiklenvqvsdlgrakritvdkentTIVEGAGKSsdIQGRVKQIRRQIDETTSDYDREKL-QERLAKLAGGVa 377
Cdd:TIGR02345 311 RVSAEDLK------------------------RVIKACGGS--IQSTTSDLEADVLGTCALFEERQIgSERYNYFTGCP- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 378 viNVGAAT-------ETEMKEKKARVEDALHATRAAVE-EGIVAGGG---VALLRCVKVIdALQLEGDEKIGSQIVRRAV 446
Cdd:TIGR02345 364 --HAKTCTiilrggaEQFIEEAERSLHDAIMIVRRALKnKKIVAGGGaieMELSKCLRDY-SKTIDGKQQLIINAFAKAL 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501343239 447 EHPIRMLCQNAGVEGAVVVGEILSNKGN----YGYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAGLLLTTECMIT 521
Cdd:TIGR02345 441 EIIPRQLCENAGFDSIEILNKLRSRHAKggkwYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETIT 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-523 |
6.32e-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: 68.08 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKE 102
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 103 GLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKV--NDREEIRQVATVSAN------WDETIGNIIADAMDKVGKDGT 174
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNskvvsqYSSLLAPIAVDAVLKVIDPAT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 175 ITVEEAKSIE-------TTLD--VVEGMQFD-KGYLSPYFATNAE-AQEAILE----------DAYVLIH---------- 223
Cdd:cd03338 176 ATNVDLKDIRivkklggTIEDteLVDGLVFTqKASKKAGGPTRIEkAKIGLIQfclsppktdmDNNIVVNdyaqmdrilr 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 224 -EKKIsslqdLLPLLQTVAKSGKPLLVIAEEVEGEALAALVVNkIRGTLNVCAVKAPgfgDRrkamlEDIAVltggrcIT 302
Cdd:cd03338 256 eERKY-----ILNMCKKIKKSGCNVLLIQKSILRDAVSDLALH-FLAKLKIMVVKDI---ER-----EEIEF------IC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 303 EDLGIK----LENVQVSDLGRAKRI-TVDKENTTIVegagKSSDIQGRVKqirrqidettsdydreklqerlaklagGVA 377
Cdd:cd03338 316 KTIGCKpvasIDHFTEDKLGSADLVeEVSLGDGKIV----KITGVKNPGK---------------------------TVT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 378 VInVGAATETEMKEKKARVEDALHATRAAVEE-GIVAGGG---VALLRCVKVIdALQLEGDEKIGSQIVRRAVEHPIRML 453
Cdd:cd03338 365 IL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGapeIEIALQLSEW-ARTLTGVEQYCVRAFADALEVIPYTL 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501343239 454 CQNAGVEGAVVVGEILSN----KGNYGYNVATDKYEDLVKAGVVDPTKVTRTALQnaasvagllLTTEC--MITEI 523
Cdd:cd03338 443 AENAGLNPISIVTELRNRhaqgEKNAGINVRKGAITNILEENVVQPLLVSTSAIT---------LATETvrMILKI 509
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
6-151 |
7.17e-11 |
|
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: 64.63 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 6 LLFDESARQKILRGVE------LLSRAV----KVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELpdpyENMGAQMVK 75
Cdd:cd03339 8 IIVREQEKKKRLKGLEahkshiLAAKSVanilRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDV----DHQIAKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 76 EVASKTSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKV----NDREEIRQVATVS 151
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIefspDNKEPLIQTAMTS 163
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
26-147 |
5.17e-10 |
|
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: 61.92 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 26 AVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKEGLK 105
Cdd:cd03340 31 AVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKP 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 501343239 106 NVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVN--DREEIRQV 147
Cdd:cd03340 107 FIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDkeDKEEQREL 150
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-519 |
9.17e-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: 61.12 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPYenmgAQMVKEVASKTSNAAGDGTTTATVLAEAIYKE 102
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPT----ASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 103 GLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKV---NDREEIRQVAT------VSANWDETIGNIIADAMDKVGKDG 173
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVeidTDRELLLSVARtslrtkLHADLADQLTEIVVDAVLAIYKPD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 174 T---------ITVEEAKSIETTLdvVEGMQFDKGYLSPyfatnaeAQEAILEDAYVLI------HEKKisslqdllpllq 238
Cdd:cd03342 180 EpidlhmveiMQMQHKSDSDTKL--IRGLVLDHGARHP-------DMPKRVENAYILTcnvsleYEKT------------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 239 tvaksgkpllviaeEVEGEALAALVVNKiRG----TLNVCAvKAPGFGDRR--KAMLEDIAVLTGGRCITEdlgikLENV 312
Cdd:cd03342 239 --------------EVNSGFFYSVVINQ-KGidppSLDMLA-KEGILALRRakRRNMERLTLACGGVAMNS-----VDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 313 QVSDLGRAKRI---TVDKENTTIVEG--AGKSSD--IQGRVKQIRRQIdettsdydreklqerlaklaggvavinvgaat 385
Cdd:cd03342 298 SPECLGYAGLVyerTLGEEKYTFIEGvkNPKSCTilIKGPNDHTITQI-------------------------------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 386 etemkekKARVEDALHATRAAVEEG-IVAGGGVALLRCVKVI--DALQLEGDEKIGSQIVRRAVEHPIRMLCQNAGVEG- 461
Cdd:cd03342 346 -------KDAIRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLkeFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVq 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501343239 462 ---AVVVGEILSNKGNYGYNVATDKYEDLVKAGVVDPTKVTRTALQNAASVAG-LLLTTECM 519
Cdd:cd03342 419 etlVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEII 480
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
26-169 |
1.06e-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: 60.95 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 26 AVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKEGLK 105
Cdd:TIGR02342 24 AIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGTTSVVILAGALLGACER 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501343239 106 NVTAGSNPVYLKRGIDKAVEAAVTELARVSKKVN--DREEIRQVATVSAN------WDETIGNIIADAMDKV 169
Cdd:TIGR02342 100 LLNKGIHPTIISESFQSAADEAIKILDEMSIPVDlsDREQLLKSATTSLSskvvsqYSSLLAPLAVDAVLKV 171
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
10-127 |
2.85e-08 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 56.19 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 10 ESARQKILRGVELLSRAVKVTLGPKGrnvvIDK---------KFGSPTVTKDGVTVAKEVELpdpyENMGAQMVKEVASK 80
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKG----MDKilqpmsegpRSGNVTVTNDGATILKSVWL----DNPAAKILVDISKT 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 501343239 81 TSNAAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAA 127
Cdd:PTZ00212 93 QDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVA 139
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-127 |
6.57e-08 |
|
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: 55.03 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 10 ESARQKILRGVELLSRAVKVTLGPKGrnvvIDK------KFGSPTVTKDGVTVAKEVELpdpyENMGAQMVKEVASKTSN 83
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKG----MDKilqsvgRSGGVTVTNDGATILKSIGV----DNPAAKVLVDISKVQDD 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 501343239 84 AAGDGTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAA 127
Cdd:cd03336 84 EVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAA 127
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-222 |
2.13e-07 |
|
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: 53.58 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHP----TASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 103 GLKNVTAGSNPVYLKRGIDKAVEAAVTELARVSKKV---NDREEIRQVATVS------ANWDETIGNIIADAMDKVGKDG 173
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKedeVDREFLLNVARTSlrtklpADLADQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501343239 174 T---------ITVEEAKSIETTLdvVEGMQFDKGYLSPYFATNaeaqeaiLEDAYVLI 222
Cdd:TIGR02347 184 EdidlfmveiMEMKHKSATDTTL--IRGLVLDHGARHPDMPRR-------VKNAYILT 232
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
10-151 |
1.72e-06 |
|
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: 50.49 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 10 ESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGT 89
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501343239 90 TTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELA-RVSKKVND--REEIRQVATVS 151
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKeNLSVSVDElgREALINVAKTS 151
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
27-230 |
2.19e-06 |
|
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: 50.37 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 27 VKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKEGLKN 106
Cdd:cd03337 32 IRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILAVAEPF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 107 VTAGSNPVYLKRGIDKAVEAAVTELARVSKKV--NDREEIRQV------ATVSANWDETIGNIIADAMDKVGKDGTITVE 178
Cdd:cd03337 108 LERGIHPTVIIKAYRKALEDALKILEEISIPVdvNDRAQMLKIikscigTKFVSRWSDLMCNLALDAVKTVAVEENGRKK 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501343239 179 E------AK-------SIETTLdVVEGMQFDKGYLSPYFATNAEAQEAILEDA---YVLIHEKKISSL 230
Cdd:cd03337 188 EidikryAKvekipggEIEDSR-VLDGVMLNKDVTHPKMRRRIENPRIVLLDCpleYLVITEKGVSDL 254
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-135 |
2.84e-06 |
|
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: 49.86 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 10 ESARQKILRGVELLSRAVKVTLGPKGRNVVI--DKKFGSPTVTKDGVTVAKEVelpdPYENMGAQMVKEVASKTSNAAGD 87
Cdd:TIGR02341 13 ENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSI----GVDNPAAKVLVDMSKVQDDEVGD 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 501343239 88 GTTTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVS 135
Cdd:TIGR02341 89 GTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA 136
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-144 |
2.44e-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: 47.02 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVI----DKKFgsptVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEA 98
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVinhlEKLF----VTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501343239 99 IYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELARVS----KKVNDREEI 144
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDEL 151
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
10-169 |
4.18e-05 |
|
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: 46.12 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 10 ESARQKILRGVELLSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGT 89
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 90 TTATVLAEAIYKEGLKNVTAGSNPVYLKRGIDKAVEAAVTELA-RVSKKVND--REEIRQVATVS-----ANWD-ETIGN 160
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKeHLSISVDNlgKESLINVAKTSmsskiIGADsDFFAN 162
|
....*....
gi 501343239 161 IIADAMDKV 169
Cdd:cd03335 163 MVVDAILAV 171
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
27-174 |
5.11e-05 |
|
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: 45.88 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 27 VKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKEGLKN 106
Cdd:TIGR02344 32 IRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAEPF 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501343239 107 VTAGSNPVYLKRGIDKAVEAAVTELARVSK--KVNDREEIRQV------ATVSANWDETIGNIIADAMDKVGKDGT 174
Cdd:TIGR02344 108 LEQNIHPTVIIRAYRKALDDALSVLEEISIpvDVNDDAAMLKLiqscigTKFVSRWSDLMCDLALDAVRTVQRDEN 183
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-150 |
1.24e-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: 44.52 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343239 23 LSRAVKVTLGPKGRNVVIDKKFGSPTVTKDGVTVAKEVELPDPyenmGAQMVKEVASKTSNAAGDGTTTATVLAEAIYKE 102
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHP----AAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 501343239 103 GLKNVTAGSNPVYLKRGIDKAVEAAVTELAR-VSKKVNDREEIRQVATV 150
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEElVVYKIEDLRNKEEVSKA 144
|
|
| |
