|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-540 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 983.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSDK-VGHL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEeIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQIL 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 240 QQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNAS 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVNVISKVSAVE-AEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVE-LGTGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950320998 478 ATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKpEPAAPAAPAMDPSMMGGM 540
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADK-PEKKAAAPPMGGGGMGGM 542
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-520 |
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: 879.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 3 KELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 83 IAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSDK-VGHLIA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEeIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 162 DAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQILQQ 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 242 SRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNASKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 322 VVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALNAT 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 402 RAAVEEGMVSGGGTALVNVISKVSAVEAE-GDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELGTGFNAATG 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALnGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1950320998 481 EWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVAD 520
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-540 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 869.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSDK-VGHL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEeIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQIL 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 240 QQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNAS 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVNVISKVSAVE-AEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELGTGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950320998 479 TGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPAAPAAPAMDPSMMGGM 540
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGGMGGMGGMGHM 542
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-521 |
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: 855.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 2 AKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSD-KVGHLI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDeEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 161 ADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQILQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 241 QSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNASK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 321 VVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALNA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 401 TRAAVEEGMVSGGGTALVNVISKVSAVEAEG-DVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELGTGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1950320998 480 GEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADK 522
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-521 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 809.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSDK-VGHL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDEsIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQIL 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 240 QQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNAS 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVNVISKVSAVE-AEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELGTGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1950320998 479 TGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEA 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-521 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 775.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSD-KVGHL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDeEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQIL 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 240 QQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNAS 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIearvqliknqiaettsdfdreklqerlaklaggvaVVKVGAATETELKELKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVNVISKVS--AVEAEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELGT-GFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRelAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGfGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1950320998 477 AATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADK 490
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-521 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 741.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSD-KVGHL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDaEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQIL 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 240 QQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNAS 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVNVISKVSAVE-AEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELGTGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1950320998 479 TGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEK 524
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-521 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 708.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSDK-VGHL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEeVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNI-QDILPLLEQI 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 239 LQQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 319 SKVVVDKDNTTIVeGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 399 NATRAAVEEGMVSGGGTALVNVI------SKVSAVEAEgdvATGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNVELG 472
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSenlktwAKNNLKEDE---LIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFE 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1950320998 473 TGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:CHL00093 477 IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDK 525
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-521 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 705.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 1 MAKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSD-KVGHL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDaAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 160 IADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQIL 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 240 QQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNAS 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVNVISKVSAVE-AEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDK-LKNVELGTGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1950320998 478 ATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAEL 525
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-521 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 700.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 2 AKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSDKV-GHLI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEiGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 161 ADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQILQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 241 QSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDD-LGLELKDVTIENLGNAS 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 320 KVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 400 ATRAAVEEGMVSGGGTALVnVISKV-----SAVEAEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDK-LKNVELGT 473
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALL-RASKLldkleEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSF 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1950320998 474 GFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDL 540
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-540 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 614.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 2 AKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSGSD-KVGHLI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDaEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 161 ADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQILQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 241 QSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNASK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 321 VVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDALNA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 401 TRAAVEEGMVSGGGTALVNVISKVSAVEAEG-DVATGIKIVVRALEEPIRQIAENAGYEGSVIVDK-LKNVELGTGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNdDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950320998 479 TGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPAAPAAPAMDPSMMGGM 540
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMGGM 544
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-520 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 548.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 2 AKELKFAEDARA--AMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASK 79
Cdd:PLN03167 56 AKELHFNKDGSAikKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 80 TNDIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEaIAQVAAVSSGS-DKVGH 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNnYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 159 LIADAMEKVGNDGVITIEESKGIETELDVVEGMQFDRGYLSQYMVTDNDKMEAVLENPYILITDKKISNIQDILPLLEQI 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 239 LQQSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 319 SKVVVDKDNTTIVEGSGEKEAIEARVQLIKNQIAETTSDFDREKLQERLAKLAGGVAVVKVGAATETELKELKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 399 NATRAAVEEGMVSGGGTALVNVISKVSAVEAEGD---VATGIKIVVRALEEPIRQIAENAGYEGSVIVDK-LKNVELGTG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLEndeQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1950320998 475 FNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVAD 520
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVE 580
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
1.65e-155 |
|
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: 452.27 E-value: 1.65e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 3 KELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 83 IAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVD--SKEAIAQVAAVSSGS------- 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDveDREELLKVATTSLNSklvsggd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 154 DKVGHLIADAMEKVG------NDGVITIEESKG---IETELdvVEGMQFDRGYLSQYmvtdndkMEAVLENPYILITDKK 224
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 225 ISNiqdilplleqilqqsrplLIIADD-VDGEALPTLVLNKIrgtfnvVAVKApgfgdRRKAMLEDIAILTGGTVITddl 303
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 304 glELKDVTIENLGNASKVVVDK----DNTTIVEGSGekeaiearvqliknqiaettsdfdreklqerlaklaGGVAVVKV 379
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 380 GAATETELKELKLRIEDALNATRAAVEE-GMVSGGGTALVNVISKVS--AVEAEGDVATGIKIVVRALEEPIRQIAENAG 456
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950320998 457 YEGSVIVDKLKNVELGTGFNAA----TGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:cd00309 398 LDPIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-521 |
4.04e-93 |
|
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: 292.95 E-value: 4.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQ----HPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTV---VDSKEAIAQVAAVSSGS-------DKVGHLIADAME------ 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIISIpveDVDREDLLKVARTSLSSkiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 166 ---KVGNDGVITIEESKGIETELdvVEGMQFDRGYLSQYMVTDndkmeavLENPYILITDKKISNIQD------------ 230
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 231 ------------ILPLLEQILQQSRPLLIIADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIAILTGGTV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 299 ITDdlgleLKDVTIENLGNASKVVVDK---DNTTIVEGSGEkeaiearvqliknqiaettsdfdreklqerlaklaGGVA 375
Cdd:pfam00118 297 VSS-----LDDLTPDDLGTAGKVEEEKigdEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 376 VVKVGAATETELKELKLRIEDALNATRAAVEE-GMVSGGG---TALVNVISKvSAVEAEGDVATGIKIVVRALEEPIRQI 451
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGaveMELARALRE-YAKSVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950320998 452 AENAGYEGSVIVDKLKNV----ELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:pfam00118 416 AENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
2.92e-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: 150.31 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 140 KEAIAQVAAVSSGS------DKVGHLIADAMEKVG------NDGVITIEESKG---IETELdvVEGMQFDRGYLSQYMvt 204
Cdd:cd03333 1 RELLLQVATTSLNSklsswdDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 205 dndkmEAVLENPYILITDKKISNiqdilplleqilqqsrplLIIADD-VDGEALPTLVLNKIrgtfnvVAVKApgfgdRR 283
Cdd:cd03333 77 -----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 284 KAMLEDIAILTGGTVITddlglELKDVTIENLGNASKVVVDKD----NTTIVEGSGekeaiearvqliknqiaettsdfd 359
Cdd:cd03333 123 KEDLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKIgeekLTFIEGCKG------------------------ 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1950320998 360 reklqerlaklaGGVAVVKVGAATETELKELKLRIEDALNATRAAVEE 407
Cdd:cd03333 174 ------------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-519 |
1.20e-33 |
|
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: 133.93 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 9 EDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGT 88
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 89 TTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKE-----AIAQVAAVSSGSDKVGHLIADa 163
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDkdtlrKIAKTSLTGKGAEAAKDKLAD- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 164 mekVGNDGVITIEESKGIETELDV-------VEGMQFDRGYLSQYMVTD----NDKMEAVLENPYILITDKKIS------ 226
Cdd:cd03343 169 ---LVVDAVLQVAEKRDGKYVVDLdnikiekKTGGSVDDTELIRGIVIDkevvHPGMPKRVENAKIALLDAPLEvkktei 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 227 ----NIQDILPLLEQILQQSRPLLIIADdvdgealptlvlnKIRGT-FNVVAV-------------KAPGFGDRR--KAM 286
Cdd:cd03343 246 dakiRITSPDQLQAFLEQEEAMLKEMVD-------------KIADTgANVVFCqkgiddlaqhylaKAGILAVRRvkKSD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 287 LEDIAILTGGTVITDdlgleLKDVTIENLGNASKVVVDK---DNTTIVEGsgekeaiearvqliknqiaettsdfdrekl 363
Cdd:cd03343 313 MEKLARATGAKIVTN-----IDDLTPEDLGEAELVEERKvgdDKMVFVEG------------------------------ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 364 qerlAKLAGGVAVVKVGaATETELKELKLRIEDALNATRAAVEEGM-VSGGGTALVNVISKVS--AVEAEGDVATGIKIV 440
Cdd:cd03343 358 ----CKNPKAVTILLRG-GTEHVVDELERALEDALRVVADALEDGKvVAGGGAVEIELAKRLReyARSVGGREQLAVEAF 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 441 VRALEEPIRQIAENAGYEG-SVIVD---KLKNVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEA 516
Cdd:cd03343 433 ADALEEIPRTLAENAGLDPiDTLVElraAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDD 512
|
...
gi 1950320998 517 VVA 519
Cdd:cd03343 513 VIA 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-521 |
1.58e-32 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 130.84 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTVV--DSKEAIAQVA-------AVSSGSDKVGHLIADAMEKVG---N 169
Cdd:NF041083 105 AEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVdpDDRETLKKIAetsltskGVEEARDYLAEIAVKAVKQVAekrD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 170 DGV------ITIEESKG---IETELdvVEGMQFDRGYLSQYM--VTDNDKMeAVLENPY----------ILITDKkiSNI 228
Cdd:NF041083 185 GKYyvdldnIQIEKKHGgsiEDTQL--IYGIVIDKEVVHPGMpkRVENAKI-ALLDAPLevkkteidaeIRITDP--DQL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 229 QDILPLLEQILQQsrplliiaddvdgealptlVLNKIRGT-FNVVAV-------------KAPGFGDRR--KAMLEDIAI 292
Cdd:NF041083 260 QKFLDQEEKMLKE-------------------MVDKIKATgANVVFCqkgiddlaqhylaKAGILAVRRvkKSDMEKLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 293 LTGGTVITDdlgleLKDVTIENLGNASKVVVDK---DNTTIVEGsgekeaiearvqlIKNQIAETtsdfdreklqerlak 369
Cdd:NF041083 321 ATGARIVTN-----IDDLTPEDLGYAELVEERKvgdDKMVFVEG-------------CKNPKAVT--------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 370 laggvavVKVGAATETELKELKLRIEDALNATRAAVEEGM-VSGGGTALVNVISKVS--AVEAEGDVATGIKIVVRALEE 446
Cdd:NF041083 368 -------ILIRGGTEHVVDEAERALEDALSVVADAVEDGKiVAGGGAPEVELAKRLReyAATVGGREQLAVEAFAEALEI 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950320998 447 PIRQIAENAGYEGSVIVDKL----KNVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:NF041083 441 IPRTLAENAGLDPIDILVKLrsahEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
22-519 |
3.41e-31 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 126.92 E-value: 3.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:NF041082 29 VAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDS--KEAIAQVAA-------VSSGSDKVGHLIADA----MEKVG 168
Cdd:NF041082 105 AEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPddKETLKKIAAtamtgkgAEAAKDKLADLVVDAvkavAEKDG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 169 NDGV----ITIEESKG---IETELdvVEGMQFDRGYLsqymvtdNDKMEAVLENPYILI-----------TDKKIsNIQD 230
Cdd:NF041082 185 GYNVdldnIKVEKKVGgsiEDSEL--VEGVVIDKERV-------HPGMPKRVENAKIALldaplevkkteIDAKI-SITD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 231 ILPLLEQILQQSRpllIIADDVDgealptlvlnKIRGT-FNVVAV-------------KAPGFGDRR--KAMLEDIAILT 294
Cdd:NF041082 255 PDQLQAFLDQEEK---MLKEMVD----------KIADSgANVVFCqkgiddlaqhylaKEGILAVRRvkKSDMEKLAKAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 295 GGTVITDdlgleLKDVTIENLGNASKVV---VDKDNTTIVEGsgekeaiearvqlIKNQIAETtsdfdreklqerlakla 371
Cdd:NF041082 322 GARIVTS-----IDDLSPEDLGYAGLVEerkVGGDKMIFVEG-------------CKNPKAVT----------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 372 ggvavVKVGAATETELKELKLRIEDALNATRAAVEEGMVSGGGTA--------LVNVISKVS-----AVEAEGDvatgik 438
Cdd:NF041082 367 -----ILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGApevelalrLREYAASVGgreqlAIEAFAE------ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 439 ivvrALEEPIRQIAENAGYEGSVIVDKLKNV----ELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTT 514
Cdd:NF041082 436 ----ALEIIPRTLAENAGLDPIDALVELRSAhekgNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRI 511
|
....*
gi 1950320998 515 EAVVA 519
Cdd:NF041082 512 DDVIA 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-512 |
2.00e-19 |
|
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: 91.19 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELeDHfenMGAKLVSEVaSKTNDI-AGDGTTTATVLTQAIVR 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV-LH---PAAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 101 EGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVD--SKEAIAQVAA-------VSSGSDKVGHLIADAMEKVGNDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATtslnskvVSQYSSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 172 VITIEESKGI-----------ETELdvVEGMQFDRGYL-----------------------------SQYMVTDNDKMEA 211
Cdd:cd03338 175 TATNVDLKDIrivkklggtieDTEL--VDGLVFTQKASkkaggptriekakigliqfclsppktdmdNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 212 VL--ENPYILITDKKIS----NIqdilpLLeqiLQQSrpllIIADDVDGEALPtlVLNKIrgtfNVVAVKapgfgDRRKA 285
Cdd:cd03338 253 ILreERKYILNMCKKIKksgcNV-----LL---IQKS----ILRDAVSDLALH--FLAKL----KIMVVK-----DIERE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 286 MLEDIAILTGGTVITDdlgleLKDVTIENLGNAskvvvdkDNTTIVEGSGEKEaiearVQLIKNQIAETTsdfdreklqe 365
Cdd:cd03338 310 EIEFICKTIGCKPVAS-----IDHFTEDKLGSA-------DLVEEVSLGDGKI-----VKITGVKNPGKT---------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 366 rlaklaggVAVVkVGAATETELKELKLRIEDALNATRAAVEE-GMVSGGGTALVNVISKVS--AVEAEGDVATGIKIVVR 442
Cdd:cd03338 363 --------VTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSewARTLTGVEQYCVRAFAD 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950320998 443 ALEEPIRQIAENAGYEGSVIVDKLKNV----ELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLL 512
Cdd:cd03338 434 ALEVIPYTLAENAGLNPISIVTELRNRhaqgEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
8-518 |
1.81e-18 |
|
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: 88.54 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 8 AEDARAAMLRGVDKLADTVKVTLGPKGRNVVLE--KSYGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAG 85
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 86 DGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQV----AAVSSGSDKVGHLIA 161
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREdllnIARTTLSSKILTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 162 DAMEKVGNDGVITIEESkgieTELDVVEGMQFDRGYLSQYMVTDN---DKMEAV-----LENPYILI------TDK-KI- 225
Cdd:cd03336 167 EHFAELAVDAVLRLKGS----GNLDAIQIIKKLGGSLKDSYLDEGfllDKKIGVnqpkrIENAKILIantpmdTDKiKIf 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 226 -SNIQ-DILPLLEQILQQSRPLL------IIADDVDGEALPTLVLN---KIRGTFNVVAVKAPGFgdrrkAMLEDIAILT 294
Cdd:cd03336 243 gAKVRvDSTAKVAEIEEAEKEKMknkvekILKHGINCFINRQLIYNypeQLFADAGIMAIEHADF-----DGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 295 GGTVI-TDDLGLELKdvtienLGNASKVvvdkDNTTIvegsGEKEAIearvqliknqiaettsdfdreklqeRLAKLAGG 373
Cdd:cd03336 318 GGEIAsTFDHPELVK------LGTCKLI----EEIMI----GEDKLI-------------------------RFSGVAAG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 374 VA--VVKVGAATETeLKELKLRIEDALNATRAAVEEG-MVSGGG---TALVNVISKVsAVEAEGDVATGIKIVVRALEEP 447
Cdd:cd03336 359 EActIVLRGASQQI-LDEAERSLHDALCVLAQTVKDTrVVLGGGcseMLMAKAVEEL-AKKTPGKKSLAIEAFAKALRQL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950320998 448 IRQIAENAGYEGSVIVDKLK----NVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:cd03336 437 PTIIADNAGYDSAELVAQLRaahyNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-520 |
2.09e-18 |
|
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: 88.32 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 10 DARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFenmgAKLVSEVASKTNDIAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 90 TATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEEL----HNISTVVDSKEAIAQVAAVSSGSdKVGHLIADAME 165
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLeeisDEISADNNNREPLIQAAKTSLGS-KIVSKCHRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 166 KVGNDGVITIE--ESKGIETELDVVE---GMQFDRGYLSQYMVTDND----KMEAVLENPYILI-----------TDKK- 224
Cdd:TIGR02343 182 EIAVDAVLNVAdmERRDVDFDLIKVEgkvGGSLEDTKLIKGIIIDKDfshpQMPKEVEDAKIAIltcpfeppkpkTKHKl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 225 -ISNIQDILPL-----------LEQILQQSRPLLIIADDVDGEALPTLVLNkirgtfNVVAVKAPGFGDrrkamLEDIAI 292
Cdd:TIGR02343 262 dISSVEEYKKLqkyeqqkfkemIDDIKKSGANLVICQWGFDDEANHLLLQN------DLPAVRWVGGQE-----LELIAI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 293 LTGGTVITddlglELKDVTIENLGNASKVV-----VDKDNTTIVEGSGEKEAIEARVQLIKNQIAEttsdfdreklqerl 367
Cdd:TIGR02343 331 ATGGRIVP-----RFQELSKDKLGKAGLVReisfgTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIE-------------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 368 aklaggvavvkvgaatetelkELKLRIEDALNATRAAVEEG-MVSGGGTAlvnVISKVSAVEAEGDVATG-----IKIVV 441
Cdd:TIGR02343 392 ---------------------EAKRSIHDALCVVRNLIKDSrIVYGGGAA---EISCSLAVSQEADKYPGveqyaIRAFA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 442 RALEEPIRQIAENAGY---EGSVIVDKLKNVE---------LGTGFNaatgewvNMVEAGIVDPTKVTRSALQNAASVSA 509
Cdd:TIGR02343 448 DALETIPMALAENSGLdpiGTLSTLKSLQLKEknpnlgvdcLGYGTN-------DMKEQFVFETLIGKKQQILLATQLVR 520
|
570
....*....|.
gi 1950320998 510 LLLTTEAVVAD 520
Cdd:TIGR02343 521 MILKIDDVISP 531
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
16-521 |
1.06e-17 |
|
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: 85.97 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 16 LRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLT 95
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 96 QAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDS-----KEAIAQVAAVSSGSDKVGH-------LIADA 163
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEekgeqRELLEKCAATALSSKLISHnkeffskMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 164 MEKVGND----GVITIEESKGIETELDV-VEGMQFDR-----GYLSQYMVTDNDK---------MEAVLENPYILITDKK 224
Cdd:TIGR02345 180 VLSLDRDdldlKLIGIKKVQGGALEDSQlVNGVAFKKtfsyaGFEQQPKKFANPKilllnveleLKAEKDNAEIRVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 225 isNIQDIlplleqilqqsrplliiaddVDGE-ALPTLVLNKIRGT-FNVVAVKAPgFGDRRKAMLEDIAILTGGTVITDD 302
Cdd:TIGR02345 260 --DYQAI--------------------VDAEwAIIFRKLEKIVESgANVVLSKLP-IGDLATQYFADRDIFCAGRVSAED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 303 LGlelkdvtienlgnaskvvvdkdntTIVEGSGekEAIEARVQLIKNQIAETTSDFDREKL-QERLAKLAGGvavVKVGA 381
Cdd:TIGR02345 317 LK------------------------RVIKACG--GSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGC---PHAKT 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 382 AT-------ETELKELKLRIEDALNATRAAVEEGMVSGGGTALVNVISKV---SAVEAEGDVATGIKIVVRALEEPIRQI 451
Cdd:TIGR02345 368 CTiilrggaEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKClrdYSKTIDGKQQLIINAFAKALEIIPRQL 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950320998 452 AENAGYEGSVIVDKLK----NVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:TIGR02345 448 CENAGFDSIEILNKLRsrhaKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNP 521
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
22-190 |
2.08e-16 |
|
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: 81.96 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFenmgAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTVV----DSKEAIAQVAAVSSGSdKVGHLIADAMEKVGNDGVITIE- 176
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIefspDNKEPLIQTAMTSLGS-KIVSRCHRQFAEIAVDAVLSVAd 189
|
170
....*....|....*
gi 1950320998 177 -ESKGIETELDVVEG 190
Cdd:cd03339 190 lERKDVNFELIKVEG 204
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
9-519 |
8.37e-16 |
|
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: 80.21 E-value: 8.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 9 EDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVaSKTNDI-AGDG 87
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVEL-SKAQDIeAGDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 88 TTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVD-SKEAIAQVAAVSSGSDKVGHLIADAMEK 166
Cdd:TIGR02342 83 TTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDlSDREQLLKSATTSLSSKVVSQYSSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 167 VGNDGVITIEESK-----------------GIETELDVVEGMQFDRGYL-----------------------------SQ 200
Cdd:TIGR02342 163 LAVDAVLKVIDPEnaknvdlndikvvkklgGTIDDTELIEGLVFTQKASksaggptriekakigliqfqisppktdmeNQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 201 YMVTDNDKMEAVL--ENPYILITDKKISNIQDILPLleqiLQQSrpllIIADDVDGEALPtlVLNKIrgtfNVVAVKapg 278
Cdd:TIGR02342 243 IIVNDYAQMDRVLkeERAYILNIVKKIKKTGCNVLL----IQKS----ILRDAVNDLALH--FLAKM----KIMVVK--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 279 fgDRRKAMLEDIAILTGGTVITDdlgleLKDVTIENLGNASKVV-VDKDNTTIVEGSGekeaiearvqliknqiaettsd 357
Cdd:TIGR02342 306 --DIEREEIEFICKTIGCKPIAS-----IDHFTADKLGSAELVEeVDSDGGKIIKITG---------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 358 fdreklqerLAKLAGGVAVVKVGaATETELKELKLRIEDALNATRAAVEE-GMVSGGGTALVNVISKVS--AVEAEGDVA 434
Cdd:TIGR02342 357 ---------IQNAGKTVTVVVRG-SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSkyARTMKGVES 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 435 TGIKIVVRALEEPIRQIAENAGYEGSVIVDKLKNV----ELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSAL 510
Cdd:TIGR02342 427 YCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRhangEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRS 506
|
....*....
gi 1950320998 511 LLTTEAVVA 519
Cdd:TIGR02342 507 ILKIDDIVF 515
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-518 |
2.04e-15 |
|
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: 78.75 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 8 AEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEK--SYGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 86 DGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNIStvVDS-------KEAIAQVAAVSSGSDKVGH 158
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNgsdevkfRQDLMNIARTTLSSKILSQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 159 LiADAMEKVGNDGVITIEESkgieTELDVVEGMQFDRGYLSqymvtdndkmEAVLENPYILitDKKISNIQDILPLLEQI 238
Cdd:TIGR02341 166 H-KDHFAQLAVDAVLRLKGS----GNLEAIQIIKKLGGSLA----------DSYLDEGFLL--DKKIGVNQPKRIENAKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 239 LQQSRPLLIIADDVDGEALptlvlnKIRGTFNVVAVKAPGfGDRRKAMLEDIAILTGGTVITDDLGLELKDVTIENLGNA 318
Cdd:TIGR02341 229 LIANTGMDTDKVKIFGSRV------RVDSTAKVAELEHAE-KEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 319 SKVVVDkdnttivegsgeKEAIEaRVQLIKNqiAETTSDFDREKL---------------QERLAKL----AGGVAVVKV 379
Cdd:TIGR02341 302 AIEHAD------------FEGVE-RLALVTG--GEIVSTFDHPELvklgscdlieeimigEDKLLKFsgvkLGEACTIVL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 380 GAATETELKELKLRIEDALNATRAAVEEGMVSGGGTALVNVISKVSAVEAE---GDVATGIKIVVRALEEPIRQIAENAG 456
Cdd:TIGR02341 367 RGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQrtpGKEALAVEAFARALRQLPTIIADNAG 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1950320998 457 YEGSVIVDKLK----NVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:TIGR02341 447 FDSAELVAQLRaahyNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
8-142 |
1.28e-14 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 76.61 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 8 AEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSY-----GSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTND 82
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegprsGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 83 IAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEA 142
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEE 155
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-512 |
2.46e-13 |
|
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: 72.32 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 21 KLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVR 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 101 EGLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSK------EAIAQVAAVSSGSDKVGH-------LIADAMEKV 167
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEdkeeqrELLEKCAATALNSKLIASekeffakMVVDAVLSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 168 GND---GVITIEESKG--IETELdVVEGMQFDR-----GYLSQYMVTDNDK---------MEAVLENPYILITDkkISNI 228
Cdd:cd03340 183 DDDldlDMIGIKKVPGgsLEDSQ-LVNGVAFKKtfsyaGFEQQPKKFKNPKilllnveleLKAEKDNAEVRVED--PEEY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 229 QDIlplleqilqqsrplliiaddVDGE-ALPTLVLNKIRGT-FNVVAVKAPgFGDRRKAMLEDIAILTGGTVITDDLGle 306
Cdd:cd03340 260 QAI--------------------VDAEwKIIYDKLEKIVKSgANVVLSKLP-IGDLATQYFADRDIFCAGRVPEEDLK-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 307 lkdvtienlgnasKVVvdkdnttivegsgekEAIEARVQLIKNQIAE----TTSDFDREKL-QERLAKLAGG-----VAV 376
Cdd:cd03340 317 -------------RVA---------------QATGGSIQTTVSNITDdvlgTCGLFEERQVgGERYNIFTGCpkaktCTI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 377 VKVGAAtETELKELKLRIEDALNATRAAVEEGMVSGGGTALVNVISKV---SAVEAEGDVATGIKIVVRALEEPIRQIAE 453
Cdd:cd03340 369 ILRGGA-EQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYlrdYSRTIAGKQQLVINAFAKALEIIPRQLCD 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950320998 454 NAGYEGSVIVDKL-----KNVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLL 512
Cdd:cd03340 448 NAGFDATDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-167 |
4.12e-11 |
|
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: 65.51 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 9 EDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHfenmGAKLVSEVASKTNDIAGDGT 88
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 89 TTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEEL-HNISTVVDS--KEAIAQVAA-------VSSGSDKVGH 158
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIkENLSVSVDElgREALINVAKtsmsskiIGLDSDFFSN 166
|
....*....
gi 1950320998 159 LIADAMEKV 167
Cdd:TIGR02340 167 IVVDAVLAV 175
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-515 |
5.54e-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: 64.97 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNIST---VVDSKEAIAQVAAvSSGSDKVGHLIADAMEKVGNDGVITIEES 178
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVpveIDTDRELLLSVAR-TSLRTKLHADLADQLTEIVVDAVLAIYKP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 179 kGIETELDVVEGMQFDRGYLSQY-----MVTD----NDKMEAVLENPYILITD----------------KKISNIQDILP 233
Cdd:cd03342 179 -DEPIDLHMVEIMQMQHKSDSDTklirgLVLDhgarHPDMPKRVENAYILTCNvsleyektevnsgffySVVINQKGIDP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 234 LLEQILQQSrplliiaddvdgealptlvlnkirgtfNVVAVkapgfgdrRKAM---LEDIAILTGGTVITddlglELKDV 310
Cdd:cd03342 258 PSLDMLAKE---------------------------GILAL--------RRAKrrnMERLTLACGGVAMN-----SVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 311 TIENLGNASKV---VVDKDNTTIVEGsgekeaiearvqlIKNQIAETTsdfdreklqerLAKlaggvavvkvgAATETEL 387
Cdd:cd03342 298 SPECLGYAGLVyerTLGEEKYTFIEG-------------VKNPKSCTI-----------LIK-----------GPNDHTI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 388 KELKLRIEDALNATRAAVEEG-MVSGGGT---ALVNVISKVSAvEAEGDVATGIKIVVRALEEPIRQIAENAGYEGS--- 460
Cdd:cd03342 343 TQIKDAIRDGLRAVKNAIEDKcVVPGAGAfevALYAHLKEFKK-SVKGKAKLGVQAFADALLVIPKTLAENSGLDVQetl 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1950320998 461 -VIVDKLKNVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASV-SALLLTTE 515
Cdd:cd03342 422 vKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIaSQLLLVDE 478
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-167 |
6.87e-11 |
|
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: 64.61 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 9 EDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHfenmGAKLVSEVASKTNDIAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 89 TTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELH-NISTVVDS--KEAIAQVAA-------VSSGSDKVGH 158
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKeHLSISVDNlgKESLINVAKtsmsskiIGADSDFFAN 162
|
....*....
gi 1950320998 159 LIADAMEKV 167
Cdd:cd03335 163 MVVDAILAV 171
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-518 |
9.63e-11 |
|
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: 64.24 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDS--KEAIAQVAAVSSGSDKVGHLiADAMEKVGNDGVITIE-ES 178
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVndRAQMLKIIKSCIGTKFVSRW-SDLMCNLALDAVKTVAvEE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 179 KGIETELDVVEGMQFDR---GYLSQYMVTD---------NDKMEAVLENP----------YILITDKKISNiqdilpLLE 236
Cdd:cd03337 183 NGRKKEIDIKRYAKVEKipgGEIEDSRVLDgvmlnkdvtHPKMRRRIENPrivlldcpleYLVITEKGVSD------LAQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 237 QILQQSRpllIIAddvdgealptlvLNKIRGTFNvvavkapgfgdRRkamledIAILTGGTVITDDLGLELKDVTIeNLG 316
Cdd:cd03337 257 HYLVKAG---ITA------------LRRVRKTDN-----------NR------IARACGATIVNRPEELTESDVGT-GAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 317 NASKVVVDKDNTTIVEGSGEKEAiearvqliknqiaettsdfdreklqerlaklaggVAVVKVGAATETeLKELKLRIED 396
Cdd:cd03337 304 LFEVKKIGDEYFTFITECKDPKA----------------------------------CTILLRGASKDV-LNEVERNLQD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 397 ALNATRAAVEEGMVSGGGTALVNVIS---KVSAVEAEGDVATGIKIVVRALEEPIRQIAENAGyeGSVI--VDKLK---- 467
Cdd:cd03337 349 AMAVARNIILNPKLVPGGGATEMAVShalSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCG--ANVIrtLTELRakha 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1950320998 468 -NVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:cd03337 427 qGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-518 |
1.17e-10 |
|
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: 63.99 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDS---KEAIAQVAAVSSGS-------DKVGHLIADAMEKVGNDG 171
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDevdREFLLNVARTSLRTklpadlaDQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 172 ---------VITIEESKGIETELdvVEGMQFDRG-------------YL---------------SQYMVTDNDKMEAVLE 214
Cdd:TIGR02347 184 edidlfmveIMEMKHKSATDTTL--IRGLVLDHGarhpdmprrvknaYIltcnvsleyektevnSGFFYSSAEQREKLVK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 215 NPYILITDKkisnIQDILPLLEQILQQSRPLLIIADDVDGEALPTL-VLNKIrgtfNVVAVKAPgfgdRRKAMlEDIAIL 293
Cdd:TIGR02347 262 AERKFVDDR----VKKIIELKKKVCGKSPDKGFVVINQKGIDPPSLdLLAKE----GIMALRRA----KRRNM-ERLTLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 294 TGGTVITDdlgleLKDVTIENLGNASKV---VVDKDNTTIVEgsgEKEAIEARVQLIKnqiaettsdfdreklqerlakl 370
Cdd:TIGR02347 329 CGGEALNS-----VEDLTPECLGWAGLVyetTIGEEKYTFIE---ECKNPKSCTILIK---------------------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 371 aggvavvkvgAATETELKELKLRIEDALNATRAAVEEG-MVSGGGTALVNVISKVSAVE--AEGDVATGIKIVVRALEEP 447
Cdd:TIGR02347 379 ----------GPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKksVKGKAKLGVEAFANALLVI 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1950320998 448 IRQIAENAGYEG-----SVIVDKLKNVELGtGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:TIGR02347 449 PKTLAENSGFDAqdtlvKLEDEHDEGGEVV-GVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
14-521 |
6.64e-09 |
|
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: 58.39 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 14 AMLRGVD---KLADTVKVTLGPKGRN--VV--LEKSYgsplITNDGVTIAKEIEledhFENMGAKLVSEvASKTNDI-AG 85
Cdd:cd03341 9 AVLRNIEackELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 86 DGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHN--ISTVVD--SKEAIAQVAAVSSGSDKVGH--- 158
Cdd:cd03341 80 DGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEElvVYKIEDlrNKEEVSKALKTAIASKQYGNedf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 159 ---LIADAM-----EKVGNDGVITIEESK---GIETELDVVEGMQFDRGYLSQYMVTDNDKMeAVLENPYilitDKKISN 227
Cdd:cd03341 160 lspLVAEACisvlpENIGNFNVDNIRVVKilgGSLEDSKVVRGMVFKREPEGSVKRVKKAKV-AVFSCPF----DIGVNV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 228 IqdilplleqilqqsrpllIIADDVDGEALPtlVLNKirgtFNVVAVKAPG-FGDRRkamledIAILTGGTVITddlglE 306
Cdd:cd03341 235 I------------------VAGGSVGDLALH--YCNK----YGIMVIKINSkFELRR------LCRTVGATPLP-----R 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 307 LKDVTIENLGNASKVVVdkdnttivegsgekEAIEARVQLIKNQIAETTSdfdreklqerlaklaggVAVVKVGAATETE 386
Cdd:cd03341 280 LGAPTPEEIGYCDSVYV--------------EEIGDTKVVVFRQNKEDSK-----------------IATIVLRGATQNI 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 387 LKELKLRIEDALNATRAAVEEG-MVSGGGTALVNVISKVSAVeaeGDVATG-----IKIVVRALEEPIRQIAENAGYEGS 460
Cdd:cd03341 329 LDDVERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKKLKEY---GEKTPGleqyaIKKFAEAFEVVPRTLAENAGLDAT 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950320998 461 VIVDKL------KNVELGTGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 521
Cdd:cd03341 406 EVLSELyaahqkGNKSAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
2-518 |
1.45e-08 |
|
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: 57.42 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 2 AKELKFAEDARAAMLRGVDKLADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTN 81
Cdd:TIGR02346 10 YRHFSGLEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ----HPAAKLLVMASEMQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPLGIRRGIELATKAAVEELHNIST-----VVDSKEAIAQVAAVSSgSDKV 156
Cdd:TIGR02346 86 NEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVwevkdLRDKDELIKALKASIS-SKQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 157 GH------LIADAM-----EKVGNDGVITIEESK----GIETElDVVEGMQFDRGYLSQYMVTDNDKMeAVLENPY-ILI 220
Cdd:TIGR02346 165 GNedflaqLVAQACstvlpKNPQNFNVDNIRVCKilggSLSNS-EVLKGMVFNREAEGSVKSVKNAKV-AVFSCPLdTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 221 TDKK----ISNIQDIL-------PLLEQILQQsrplliIADD-----VDGEALPTLVLNKIRgTFNVVAVKAPGfgdrrK 284
Cdd:TIGR02346 243 TETKgtvlIHNAEELLnyskgeeNQIEAMIKA------IADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----K 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 285 AMLEDIAILTGGTVItddlgLELKDVTIENLGNASKVVVdkdnttivegsgeKEAIEARVQLIKNQiaettsdfdreklq 364
Cdd:TIGR02346 311 FELRRLCKTVGATPL-----PRLGAPTPEEIGYVDSVYV-------------SEIGGDKVTVFKQE-------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 365 erlaKLAGGVAVVKVGAATETELKELKLRIEDALNATRAAVEEG-MVSGGGTALVNVISKVSAV-EAEGDVAT-GIKIVV 441
Cdd:TIGR02346 359 ----NGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYgEKLPGLDQyAIKKFA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 442 RALEEPIRQIAENAGYEGSVIVDKL------KNVELGTGFNAATGEWVNMVEAGIVDPTkvtrsalqnAASVSALLLTTE 515
Cdd:TIGR02346 435 EAFEIIPRTLAENAGLNANEVIPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDML---------ATKKWAIKLATE 505
|
...
gi 1950320998 516 AVV 518
Cdd:TIGR02346 506 AAV 508
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-519 |
1.08e-07 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 54.36 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 22 LADTVKVTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 102 GLKNVTAGANPLGIRRGIELATKAAVEELHNISTVVDSKEAIAQVAAVSSG---------SDKVGHLIADAMEKVGND-- 170
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCigtkfvsrwSDLMCDLALDAVRTVQRDen 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 171 GVITIEESKGIETElDVVEGMQFDRGYLSQYMVTDN---DKMEAVLENPYILITD-----KKISNIQDILPLLEQILQqs 242
Cdd:TIGR02344 184 GRKEIDIKRYAKVE-KIPGGDIEDSCVLKGVMINKDvthPKMRRYIENPRIVLLDcpleyKKGESQTNIEITKEEDWN-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 243 RPLLIIADDVdgealptlvlnkirgtfnvvavkapgfgdrrKAMLEDIAILTGGTVITDDlglELKDVTIENLGNASKVV 322
Cdd:TIGR02344 261 RILQMEEEYV-------------------------------QLMCEDIIAVKPDLVITEK---GVSDLAQHYLLKANITA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 323 VDK----DNTTIVEGSGEKeaIEARVQLIKNQ-IAETTSDFDREKLQERL------AKLAGGVAVVKVGAATETeLKELK 391
Cdd:TIGR02344 307 IRRvrktDNNRIARACGAT--IVNRPEELRESdVGTGCGLFEVKKIGDEYftfiteCKDPKACTILLRGASKDI-LNEVE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950320998 392 LRIEDALNATRAAVEEGMVSGGGTAL---VNVISKVSAVEAEGDVATGIKIVVRALEEPIRQIAENAGYEGSVIVDKL-- 466
Cdd:TIGR02344 384 RNLQDAMAVARNVLLDPKLVPGGGATemaVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELra 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1950320998 467 KNVELG---TGFNAATGEWVNMVEAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:TIGR02344 464 KHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| |
