|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-535 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 1002.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 2 AAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 82 NDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEK 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 162 IAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAVV 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 242 QSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 322 RVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 402 ATRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTSFGFNA 481
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1859807952 482 STDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKSPAMPA 535
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPM 534
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-533 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 950.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 2 AAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 82 NDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEK 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 162 IAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAVV 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 242 QSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 322 RVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 402 ATRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDtSFGFNA 481
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELED-GFGFNA 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1859807952 482 STDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKSPAM 533
Cdd:PRK12849 480 ATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPG 531
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-524 |
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: 919.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 4 KEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKTND 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 84 IAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEKIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 164 EAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAVVQS 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 244 GRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTAKRV 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 324 TIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 404 RAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTsFGFNAST 483
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDG-FGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1859807952 484 DTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAE 524
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-535 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 914.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 1 MAAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 81 TNDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGE 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 161 KIAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 241 VQSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 321 KRVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 401 HATRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDtSFGFN 480
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPG-NFGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1859807952 481 ASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKSPAMPA 535
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAG 534
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-535 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 881.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 1 MAAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 81 TNDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGE 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 161 KIAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 241 VQSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 321 KRVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 401 HATRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTSFGFN 480
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1859807952 481 ASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELP-EDKSPAMPA 535
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPkKDAAPAMPA 536
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-527 |
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: 878.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 3 AKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKTN 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 83 DIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEKI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 163 AEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAVVQ 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 243 SGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 323 VTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 403 TRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDtSFGFNAS 482
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKG-NFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1859807952 483 TDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPE 527
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-535 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 832.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 1 MAAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 81 TNDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGE 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 161 KIAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 241 VQSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 321 KRVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 401 HATRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQnDTSFGFN 480
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK-PGGYGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1859807952 481 ASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKSPAMPA 535
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAP 534
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-532 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 793.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 2 AAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 82 NDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEK 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 162 IAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAVV 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 242 QSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 322 RVTIDKDNTTIVDGAGDADAIkgrteairaqienttsdydreklqerlaklaggvaVIKVGGATEVEVKERKDRVDDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 402 ATRAAVEEGIVPGGGTALLYATKALDGL-KGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTSFGFN 480
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1859807952 481 ASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKSPA 532
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-531 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 789.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 2 AAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 82 NDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEK 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 162 IAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAVV 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 242 QSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISED-LGIKLETVTVGMLGTA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 321 KRVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 401 HATRAAVEEGIVPGGGTALLYATKALDGLKGVND---DQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTSF 477
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1859807952 478 GFNASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKSP 531
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-535 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 759.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 1 MAAKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 81 TNDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGE 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 161 KIAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEAV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 241 VQSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 321 KRVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 401 HATRAAVEEGIVPGGGTALLYATKALDGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTSFGFN 480
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSYGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1859807952 481 ASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDKS--PAMPA 535
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGagPAMPP 537
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-529 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 668.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 3 AKEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVASKTN 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 83 DIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEKI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 163 AEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNL-QAMLPILEAVV 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 242 QSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGTAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 322 RVTIDKDNTTIVdGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 402 ATRAAVEEGIVPGGGTALLYATKALDGLKGVN--DDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKlLDQNDTSFGF 479
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEK-VQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1859807952 480 NASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPEDK 529
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| 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: 556.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 2 AAKEVKFSRD--ARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMGAQMVREVAS 79
Cdd:PLN03167 55 AAKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 80 KTNDIAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSnEVAQVGIISANGDREVG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 160 EKIAEAMEKVGKEGVITVEEAKGLEFELDVVEGMQFDRGYLSPYFITNPEKMTVELNDPYILIHEKKLSNLQAMLPILEA 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 240 VVQSGRPLLIIAEDIEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTAGELISEDLGIKLETVTVGMLGT 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 320 AKRVTIDKDNTTIVDGAGDADAIKGRTEAIRAQIENTTSDYDREKLQERLAKLAGGVAVIKVGGATEVEVKERKDRVDDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 400 LHATRAAVEEGIVPGGGTALLYATKALDGLKGV--NDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQNDTSF 477
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTleNDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1859807952 478 GFNASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVAELPE 527
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE 583
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-523 |
1.65e-151 |
|
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: 442.25 E-value: 1.65e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 4 KEVKFSRDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTND 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEV----EHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 84 IAGDGTTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKP--VSGSNEVAQVGIISAN------GD 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 156 REVGEKIAEAMEKVGKE------GVITVEEAKG---LEFELdvVEGMQFDRGYLSPYfitnpekMTVELNDPYILIHEKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 227 LSNlqamlpileavvqsgrplLIIAED-IEGEALATLVVnklrggLKVAAVKApgfgdRRKAMLEDIAILTAGELISEdl 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 306 gikLETVTVGMLGTAKRVTIDK----DNTTIVDGAGdadaikgrteairaqienttsdydreklqerlaklaGGVAVIKV 381
Cdd:cd00309 277 ---LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 382 GGATEVEVKERKDRVDDALHATRAAVEE-GIVPGGGTALLYATKALDGL-KGVNDDQTRGIDIVRKSLTALVRQIAQNAG 459
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859807952 460 HDGAVVSGKLL---DQNDTSFGFNASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATVA 523
Cdd:cd00309 398 LDPIEVVTKLRakhAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-522 |
1.19e-83 |
|
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: 268.69 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEI----QHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVEDIKA-RSKPVSGSN--EVAQVGIISANGD------REVGEKIAEAMEKVGKE- 172
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEDVDreDLLKVARTSLSSKiisresDFLAKLVVDAVLAIPKNd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 173 --------GVITVEEakGLEFELDVVEGMQFDRGYLSPyfitnpeKMTVELNDPYILIHEKKLSN--------------- 229
Cdd:pfam00118 157 gsfdlgniGVVKILG--GSLEDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYektetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 230 ---------LQAMLPILEAVVQSGRPLLIIAEDIEGEALATLVVNKLRGGLKVaavkapgfgdrRKAMLEDIAILTAGEL 300
Cdd:pfam00118 228 qlerflkaeEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 301 ISedlgiKLETVTVGMLGTAKRV---TIDKDNTTIVDGAGDadaikgrteairaqienttsdydreklqerlaklaGGVA 377
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 378 VIKVGGATEVEVKERKDRVDDALHATRAAVEE-GIVPGGGTALLYATKAL-DGLKGVNDDQTRGIDIVRKSLTALVRQIA 455
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALrEYAKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 456 QNAGHDGAVVSGKLLD---QNDTSFGFNASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATV 522
Cdd:pfam00118 417 ENAGLDPIEVLAELRAahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
4.56e-39 |
|
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: 141.83 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 142 NEVAQVGIISAN-----GDREVGEKIAEAMEKVGKE------GVITVEEAKG---LEFELdvVEGMQFDRGYLSPYfitn 207
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 208 pekMTVELNDPYILIHEKKLSNlqamlpileavvqsgrplLIIAED-IEGEALATLVVnklrggLKVAAVKApgfgdRRK 286
Cdd:cd03333 76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 287 AMLEDIAILTAGELISEdlgikLETVTVGMLGTAKRVTIDKD----NTTIVDGAGdadaikgrteairaqienttsdydr 362
Cdd:cd03333 124 EDLERIARATGATIVSS-----LEDLTPEDLGTAELVEETKIgeekLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1859807952 363 eklqerlaklaGGVAVIKVGGATEVEVKERKDRVDDALHATRAAVEE 409
Cdd:cd03333 174 -----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
10-512 |
3.88e-19 |
|
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: 90.40 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 10 RDARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGT 89
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 90 TTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGI----ISANGDREVGEKIAE- 164
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIaktsLTGKGAEAAKDKLADl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 165 --------AMEKVGKEGV----ITVEEAKGLEFE-LDVVEGMQFDRGYLSP----------------------------Y 203
Cdd:cd03343 170 vvdavlqvAEKRDGKYVVdldnIKIEKKTGGSVDdTELIRGIVIDKEVVHPgmpkrvenakialldaplevkkteidakI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 204 FITNPEKMTVELndpyilihEKKLSNLQAMlpiLEAVVQSGRPLLIIAEDIEGEALATLVVnklRGGLKVAAVKapgfgd 283
Cdd:cd03343 250 RITSPDQLQAFL--------EQEEAMLKEM---VDKIADTGANVVFCQKGIDDLAQHYLAK---AGILAVRRVK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 284 rrKAMLEDIAILTAGELISedlgiKLETVTVGMLGTAKRVTIDK---DNTTIVDGAGDADAIkgrteairaqienttsdy 360
Cdd:cd03343 310 --KSDMEKLARATGAKIVT-----NIDDLTPEDLGEAELVEERKvgdDKMVFVEGCKNPKAV------------------ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 361 dreklqerlaklaggvaVIKVGGATEVEVKERKDRVDDALHATRAAVEEG-IVPGGGTALLYATKAL-DGLKGVNDDQTR 438
Cdd:cd03343 365 -----------------TILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLrEYARSVGGREQL 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859807952 439 GIDIVRKSLTALVRQIAQNAGHDGAVVSGKLL---DQNDTSFGFNASTDTYENLVAAGVIDPTKVVRTALQNAASVA 512
Cdd:cd03343 428 AVEAFADALEEIPRTLAENAGLDPIDTLVELRaahEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAA 504
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
6.09e-15 |
|
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: 77.49 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKdkfeNMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVEDIKarskpvsgsnEVAqVGIISANGD-REVGEK----------IAEAMEKVGK 171
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIK----------EIA-VTIDEEKGEqRELLEKcaatalssklISHNKEFFSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 172 EGVITVEEAKGLEFELDV----------------VEGMQFDRGYLSPYFITNPEKmtveLNDPYILIHEKKLSnLQAMLP 235
Cdd:TIGR02345 175 MIVDAVLSLDRDDLDLKLigikkvqggaledsqlVNGVAFKKTFSYAGFEQQPKK----FANPKILLLNVELE-LKAEKD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 236 ILEAVVQSgrplliiAEDIEG--EALATLVVNKLR----GGLKVAAVKAPgFGDRRKAMLEDIAILTAGELISEDLgikl 309
Cdd:TIGR02345 250 NAEIRVED-------VEDYQAivDAEWAIIFRKLEkiveSGANVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDL---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 310 etvtvgmlgtaKRVTidkdnttivdgAGDADAIKGRTEAIRAQIENTTSDYDREKL-QERLAKLAGG-----VAVIKVGG 383
Cdd:TIGR02345 318 -----------KRVI-----------KACGGSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGCphaktCTIILRGG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 384 ATEVeVKERKDRVDDALHATRAAVE-EGIVPGGGTALLYATKAL-DGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHD 461
Cdd:TIGR02345 376 AEQF-IEEAERSLHDAIMIVRRALKnKKIVAGGGAIEMELSKCLrDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1859807952 462 GAVVSGKLL---DQNDTSFGFNASTDTYENLVAAGVIDPTKVVRTALQNAASVAGLLITTEATV 522
Cdd:TIGR02345 455 SIEILNKLRsrhAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
22-522 |
3.41e-12 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 68.85 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 22 ILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfenmgaqmVREVASKTNDIA-------GDGTTTATV 94
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI-----------VHPAAKTLVDIAksqdaevGDGTTSVVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 95 LAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQvgiisangdREVGEKIAE--------AM 166
Cdd:cd03340 96 LAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQ---------RELLEKCAAtalnskliAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 167 EK--VGKegvITVEEAKGLEFELD------------------VVEGMQFDR-----GY-LSPYFITNP------------ 208
Cdd:cd03340 167 EKefFAK---MVVDAVLSLDDDLDldmigikkvpggsledsqLVNGVAFKKtfsyaGFeQQPKKFKNPkilllnvelelk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 209 -EKMTVE--LNDP----------YILIHEKklsnlqamlpiLEAVVQSGrplliiaediegealATLVVNKLRGGlkvaA 275
Cdd:cd03340 244 aEKDNAEvrVEDPeeyqaivdaeWKIIYDK-----------LEKIVKSG---------------ANVVLSKLPIG----D 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 276 VKAPGFGDRRkamlediaILTAGELISEDLgikletvtvgmlgtaKRVtidkdnttivdgagdadaikgrTEAIRAQIEN 355
Cdd:cd03340 294 LATQYFADRD--------IFCAGRVPEEDL---------------KRV----------------------AQATGGSIQT 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 356 TTSDYDREKL------------QERLAKLAGG-----VAVIKVGGATEVeVKERKDRVDDALHATRAAVEEG-IVPGGGT 417
Cdd:cd03340 329 TVSNITDDVLgtcglfeerqvgGERYNIFTGCpkaktCTIILRGGAEQF-IEEAERSLHDAIMIVRRAIKNDsVVAGGGA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 418 ALLYATKAL-DGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKL----LDQNDTSFGFNASTDTYENLVAA 492
Cdd:cd03340 408 IEMELSKYLrDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLrqkhAQGGGKWYGVDINNEGIADNFEA 487
|
570 580 590
....*....|....*....|....*....|
gi 1859807952 493 GVIDPTKVVRTALQNAASVAGLLITTEATV 522
Cdd:cd03340 488 FVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-143 |
7.34e-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: 67.70 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKdkfeNMGAQMVREVaSKTNDI-AGDGTTTATVLAQAIVR 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVL----HPAAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1859807952 102 EGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNE 143
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDR 136
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-512 |
1.23e-11 |
|
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: 66.90 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGR-NVVIDKSfGAPRITKDGVSVAKEIElkdkFENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVR 101
Cdd:cd03342 24 LQDVLKTNLGPKGTlKMLVSGA-GDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 102 EGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKA--RSKPVSGSNEVAqVGIISANGDREVGEKIAEAMEKVGKEGVITVEE 179
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLESfkVPVEIDTDRELL-LSVARTSLRTKLHADLADQLTEIVVDAVLAIYK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 180 AkGLEFELDVVEGMQFD----------RGYLSPYFITNPEkMTVELNDPYILI------HEKKLSNLQAMLPILeaVVQS 243
Cdd:cd03342 178 P-DEPIDLHMVEIMQMQhksdsdtkliRGLVLDHGARHPD-MPKRVENAYILTcnvsleYEKTEVNSGFFYSVV--INQK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 244 GrplliiaedIEGEALATLVVNKLrgglkVAAVKApgfgdRRKAMlEDIAILTAGELIS--EDLgikletvTVGMLGTAK 321
Cdd:cd03342 254 G---------IDPPSLDMLAKEGI-----LALRRA-----KRRNM-ERLTLACGGVAMNsvDDL-------SPECLGYAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 322 RV---TIDKDNTTIVDGAGDADA----IKGRTEAIRAQIenttsdydreklqerlaklaggvavikvggatevevkerKD 394
Cdd:cd03342 307 LVyerTLGEEKYTFIEGVKNPKSctilIKGPNDHTITQI---------------------------------------KD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 395 RVDDALHATRAAVEEG-IVPGGGTALLYATKAL-DGLKGVNDDQTRGIDIVRKSLTALVRQIAQNAGHDGAVVSGKLLDQ 472
Cdd:cd03342 348 AIRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLkEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDE 427
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1859807952 473 NDTS---FGFNASTDTYENLVAAGVIDPTKVVRTALQNAASVA 512
Cdd:cd03342 428 YAEGgqvGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIA 470
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
11-143 |
6.91e-11 |
|
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: 64.66 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 11 DARERIMKGVDILADAVKVTLGPKGRNVVI--DKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDG 88
Cdd:cd03336 13 TARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGV----DNPAAKVLVDISKVQDDEVGDG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1859807952 89 TTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNE 143
Cdd:cd03336 89 TTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-142 |
1.22e-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: 60.57 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKdkfeNMGAQMVREVaSKTNDI-AGDGTTTATVLAQAIVR 101
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQDIeAGDGTTSVVILAGALLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1859807952 102 EGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSN 142
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD 136
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
23-125 |
5.79e-09 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 58.50 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPR-----ITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTTTATVLAQ 97
Cdd:PTZ00212 34 VADLVKTTLGPKGMDKILQPMSEGPRsgnvtVTNDGATILKSVWL----DNPAAKILVDISKTQDEEVGDGTTSVVVLAG 109
|
90 100
....*....|....*....|....*...
gi 1859807952 98 AIVREGMKSVAAGMNPMDLKRGIDIAVT 125
Cdd:PTZ00212 110 ELLREAEKLLDQKIHPQTIIEGWRMALD 137
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-129 |
6.80e-09 |
|
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: 58.21 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQI----QHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100
....*....|....*....|....*..
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVE 129
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQ 130
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
23-192 |
1.14e-08 |
|
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: 57.50 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELKDKFENMgaqMVREVASKTNDIaGDGTTTATVLAQAIVRE 102
Cdd:TIGR02343 39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKL---MVELSKSQDDEI-GDGTTGVVVLAGALLEQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANgdREVGEKIA----EAMEKVGKEGVITVE 178
Cdd:TIGR02343 115 AEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAK--TSLGSKIVskchRRFAEIAVDAVLNVA 192
|
170
....*....|....*.
gi 1859807952 179 --EAKGLEFELDVVEG 192
Cdd:TIGR02343 193 dmERRDVDFDLIKVEG 208
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
11-144 |
1.38e-07 |
|
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: 54.10 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 11 DARERIMKGVDILADAVKVTLGPKGRNVVI--DKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDG 88
Cdd:TIGR02341 14 NARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVGDG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1859807952 89 TTTATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAvTKVVEDIKARSKPVSGSNEV 144
Cdd:TIGR02341 90 TTSVTVLAAELLREAEKLINQKIHPQTIIAGYREA-TKAARDALLKSAVDNGSDEV 144
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
11-134 |
1.96e-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: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 11 DARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTT 90
Cdd:TIGR02340 12 DVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEV----EHPAAKILVELAQLQDREVGDGTT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1859807952 91 TATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIKAR 134
Cdd:TIGR02340 88 SVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEN 131
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-192 |
1.38e-05 |
|
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: 47.68 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDV----DHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANgdREVGEKIA----EAMEKVGKEGVITVE 178
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTAM--TSLGSKIVsrchRQFAEIAVDAVLSVA 188
|
170
....*....|....*.
gi 1859807952 179 --EAKGLEFELDVVEG 192
Cdd:cd03339 189 dlERKDVNFELIKVEG 204
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-189 |
3.64e-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: 46.27 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANGDREVGEKIAEAMEKVGKEGVITVEEAKG 182
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDEN 183
|
....*..
gi 1859807952 183 LEFELDV 189
Cdd:TIGR02344 184 GRKEIDI 190
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-230 |
3.06e-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: 43.44 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 103 GMKSVAAGMNPMDLKRGIDIAVTKVVEDIKARSKPVSGSNEVAQVGIISANgdreVGEKI----AEAMEKVGKEGVITVE 178
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSC----IGTKFvsrwSDLMCNLALDAVKTVA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859807952 179 -EAKGLEFELD-------------------VVEGMQFDRGYLSP---YFITNPEKMTVELNDPYILIHEKKLSNL 230
Cdd:cd03337 180 vEENGRKKEIDikryakvekipggeiedsrVLDGVMLNKDVTHPkmrRRIENPRIVLLDCPLEYLVITEKGVSDL 254
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
11-132 |
4.14e-04 |
|
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: 43.04 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859807952 11 DARERIMKGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELkdkfENMGAQMVREVASKTNDIAGDGTT 90
Cdd:cd03335 8 DVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEV----EHPAAKILVELAQLQDKEVGDGTT 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1859807952 91 TATVLAQAIVREGMKSVAAGMNPMDLKRGIDIAVTKVVEDIK 132
Cdd:cd03335 84 SVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIK 125
|
|
| |
