|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 982.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 2 AAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 82 NDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLD 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAVV 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 242 QTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKSK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 322 KVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDALN 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 402 ATRAAVQEGIVPGGGVALLRSSTKI-TAKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEDNYGYNA 480
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALeALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2495363996 481 QTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKK 528
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 935.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 2 AAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 82 NDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLD 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAVV 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 242 QTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKSK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 322 KVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDALN 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 402 ATRAAVQEGIVPGGGVALLRSSTKITA-KGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKnEDNYGYNA 480
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDElAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLEL-EDGFGFNA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2495363996 481 QTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PRK12849 480 ATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEE 527
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 920.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 1 MAAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 81 TNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGL 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 241 VQTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKS 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 321 KKVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 401 NATRAAVQEGIVPGGGVALLRSSTKITA-KGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNeDNYGYN 479
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGlKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELP-GNFGFN 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2495363996 480 AQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-523 |
0e+00 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 902.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 4 KEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKTND 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 84 IAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLDIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 164 EAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAVVQT 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 244 GKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKSKKV 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 324 SISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDALNAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 404 RAAVQEGIVPGGGVALLRSSTKI-TAKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILdKNEDNYGYNAQT 482
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALdKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL-ESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2495363996 483 GEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAE 523
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 899.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 1 MAAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 81 TNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGL 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 241 VQTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKS 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 321 KKVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 401 NATRAAVQEGIVPGGGVALLRSSTKITA-KGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEDNYGYN 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRiNNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETFGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2495363996 480 AQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKD 529
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-526 |
0e+00 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 856.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 3 AKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKTN 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 83 DIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLDI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 163 AEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAVVQ 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 243 TGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKSKK 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 323 VSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDALNA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 403 TRAAVQEGIVPGGGVALLRSSTKI-TAKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNeDNYGYNAQ 481
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALeGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELK-GNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2495363996 482 TGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPK 526
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 840.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 1 MAAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 81 TNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGL 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 241 VQTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKS 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 321 KKVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 401 NATRAAVQEGIVPGGGVALLRSSTKITA-KGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKnEDNYGYN 479
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKlETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK-PGGYGFN 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2495363996 480 AQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKE 528
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-527 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 782.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 1 MAAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 81 TNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGL 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 241 VQTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKS 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 321 KKVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 401 NATRAAVQEGIVPGGGVALLRSSTKITA-KGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEDNYGYN 479
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGiKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2495363996 480 AQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKK 527
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-528 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 781.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 2 AAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 82 NDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLD 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAVV 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 242 QTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGIKLENVTLDMLGKS 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 321 KKVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 401 NATRAAVQEGIVPGGGVALLRSSTKI----TAKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEDNY 476
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLdkleEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2495363996 477 GYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEK 544
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 778.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 2 AAKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 82 NDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLD 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEAVV 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 242 QTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKSK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 322 KVSISKENTTIVDGAGQKSDIegrvaqikaqieettsdydreklqerlaklaggvaVIRVGGSTEVEVKEKKDRIDDALN 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 402 ATRAAVQEGIVPGGGVALLRSSTKIT--AKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEDNYGYN 479
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRelAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2495363996 480 AQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 645.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 3 AKEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVASKTN 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 83 DIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLDI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 163 AEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNL-QAMLPVLEAVV 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 242 QTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGKSK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 322 KVSISKENTTIVdGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDALN 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 402 ATRAAVQEGIVPGGGVAL------LRSSTKITAKganDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEdN 475
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLvhlsenLKTWAKNNLK---EDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDF-E 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2495363996 476 YGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:CHL00093 477 IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-528 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 550.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 2 AAKEVKFGR--TAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLVREVAS 79
Cdd:PLN03167 55 AAKELHFNKdgSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 80 KTNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEeVAQVGTISANGERQIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 160 LDIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQAMLPVLEA 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 240 VVQTGKPLVIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLDMLGK 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 320 SKKVSISKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 400 LNATRAAVQEGIVPGGGVALLRSSTKITA---KGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNEDNY 476
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAikdTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2495363996 477 GYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKKE 528
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-522 |
9.95e-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: 450.34 E-value: 9.95e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 4 KEVKFGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKTND 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 84 IAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKI--NTSEEVAQVGTISAN------GE 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIdvEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 156 RQIGLDIAEAMQKVG------NEGVITVEEAKT-AETELEVVEGMQFDRGYLSPYfvtnpekMVADLEDAYILLHEKKLS 228
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 229 NlqamlpvleavvqtgkplVIIAED-VEGEALATLVVnklrggLKIAAVKApgfgdRRKAMLEDIAILTGGTVISEdlgi 307
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 308 kLENVTLDMLGKSKKVSISK----ENTTIVDGAGqksdiegrvaqikaqieettsdydreklqerlaklaGGVAVIRVGG 383
Cdd:cd00309 277 -LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 384 STEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSTKIT--AKGANDDQEAGINIVRKALQALVRQIAENAGDE 460
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495363996 461 ASIVVGKIL---DKNEDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIA 522
Cdd:cd00309 400 PIEVVTKLRakhAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-521 |
2.43e-89 |
|
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: 283.32 E-value: 2.43e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKfenmGAQLVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 103 GSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAK---KINTSEEVAQVGTISANGE------RQIGLDIAEAMQ------ 167
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIISipvEDVDREDLLKVARTSLSSKiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 168 ---KVGNEGVITVEEAKTAETELevVEGMQFDRGYLSPyfvtnpeKMVADLEDAYILLHEKKLSN--------------- 229
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYektetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 230 ---------LQAMLPVLEAVVQTGKPLVIIAEDVEGEALATLVVNKLRGGLKIaavkapgfgdrRKAMLEDIAILTGGTV 300
Cdd:pfam00118 228 qlerflkaeEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 301 ISedlgiKLENVTLDMLGKSKKV---SISKENTTIVDGagqksdiegrvaqikaqieettsdydreklqerlaKLAGGVA 377
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEG-----------------------------------CKSPKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 378 VIRVGGSTEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSTKI--TAKGANDDQEAGINIVRKALQALVRQIA 454
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALreYAKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 455 ENAGDEASIVVGKILD---KNEDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMI 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
2.14e-40 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 145.30 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 142 EEVAQVGTISANGERQIGLD-----IAEAMQKVG------NEGVITVEEAKTAE-TELEVVEGMQFDRGYLSPYfvtnpe 209
Cdd:cd03333 2 ELLLQVATTSLNSKLSSWDDflgklVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPY------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 210 kMVADLEDAYILLHEKKLSNlqamlpvleavvqtgkplVIIAED-VEGEALATLVVnklrggLKIAAVKApgfgdRRKAM 288
Cdd:cd03333 76 -MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 289 LEDIAILTGGTVISEdlgikLENVTLDMLGKSKKVSISK----ENTTIVDGAGqksdiegrvaqikaqieettsdydrek 364
Cdd:cd03333 126 LERIARATGATIVSS-----LEDLTPEDLGTAELVEETKigeeKLTFIEGCKG--------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2495363996 365 lqerlaklaGGVAVIRVGGSTEVEVKEKKDRIDDALNATRAAVQE 409
Cdd:cd03333 174 ---------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-522 |
4.82e-23 |
|
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239459 [Multi-domain] Cd Length: 517 Bit Score: 102.34 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 9 GRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKTNDIAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 89 TTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSE--------EVAQVGTISANGERQIGL 160
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDkdtlrkiaKTSLTGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 161 DIAEAMQKV--GNEGVITVE------EAKTAET--ELEVVEGMQFDRGYLSPyfvtnpeKMVADLEDAYILLHEKKL--- 227
Cdd:cd03343 169 LVVDAVLQVaeKRDGKYVVDldnikiEKKTGGSvdDTELIRGIVIDKEVVHP-------GMPKRVENAKIALLDAPLevk 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 228 -------------SNLQAMLP--------VLEAVVQTGKPLVIIAEDVEGEALATLVVNKlrgglkIAAVKapgfgDRRK 286
Cdd:cd03343 242 kteidakiritspDQLQAFLEqeeamlkeMVDKIADTGANVVFCQKGIDDLAQHYLAKAG------ILAVR-----RVKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 287 AMLEDIAILTGGTVISedlgiKLENVTLDMLGKSKKVSISKenttivDGAGQKSDIEGrvaqikaqieettsdydreklq 366
Cdd:cd03343 311 SDMEKLARATGAKIVT-----NIDDLTPEDLGEAELVEERK------VGDDKMVFVEG---------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 367 erlAKLAGGVAVIrVGGSTEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSTKIT--AKGANDDQEAGINIVR 443
Cdd:cd03343 358 ---CKNPKAVTIL-LRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLReyARSVGGREQLAVEAFA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 444 KALQALVRQIAENAGDEASIVVGKILDKNED---NYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAM 520
Cdd:cd03343 434 DALEEIPRTLAENAGLDPIDTLVELRAAHEKgnkNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
..
gi 2495363996 521 IA 522
Cdd:cd03343 514 IA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-522 |
1.47e-14 |
|
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: 76.14 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGR-NVVIDKSfGAPRITKDGVSVAKEIEledkFENMGAQLVREVASKTNDIAGDGTTTATVLAQAIVR 101
Cdd:cd03342 24 LQDVLKTNLGPKGTlKMLVSGA-GDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 102 EGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQA--KAKKINTSEEVA-QVGTISANGERQIGLdiAEAMQKVGNEGVITVE 178
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLESfkVPVEIDTDRELLlSVARTSLRTKLHADL--ADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 179 EAkTAETELEVVEGMQFD----------RGYLSPYFVTNPEkMVADLEDAYILL------HEKKLSNLQamlpVLEAVVQ 242
Cdd:cd03342 177 KP-DEPIDLHMVEIMQMQhksdsdtkliRGLVLDHGARHPD-MPKRVENAYILTcnvsleYEKTEVNSG----FFYSVVI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 243 TGKPLVIIAEDVEGEAlatlvvnklrgglKIAAVkapgfgdrRKAM---LEDIAILTGGTVISEdlgikLENVTLDMLGK 319
Cdd:cd03342 251 NQKGIDPPSLDMLAKE-------------GILAL--------RRAKrrnMERLTLACGGVAMNS-----VDDLSPECLGY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 320 SKKV---SISKENTTIvdgagqksdiegrvaqikaqIEETTsdydreklqerlaklAGGVAVIRVGGSTEVEVKEKKDRI 396
Cdd:cd03342 305 AGLVyerTLGEEKYTF--------------------IEGVK---------------NPKSCTILIKGPNDHTITQIKDAI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 397 DDALNATRAAVQEG-IVPGGGVALLRSSTKIT--AKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNE 473
Cdd:cd03342 350 RDGLRAVKNAIEDKcVVPGAGAFEVALYAHLKefKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2495363996 474 D---NYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVAS-LLITTEAMIA 522
Cdd:cd03342 430 EggqVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEIIRA 482
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-514 |
1.69e-13 |
|
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: 72.70 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLvrevaSKTNDI-AGDGTTTATVLAQAIVR 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 102 EGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEE---------------VAQVGT----ISANGERQIGlDI 162
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDResliksattslnskvVSQYSSllapIAVDAVLKVI-DP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 163 AEA----------MQKVGNegviTVEEAktaetelEVVEGMQFD-RGYLSPYFVTNPEKMV------------ADLEDAY 219
Cdd:cd03338 174 ATAtnvdlkdiriVKKLGG----TIEDT-------ELVDGLVFTqKASKKAGGPTRIEKAKigliqfclsppkTDMDNNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 220 I---------LLHEKKlsnlQAMLPVLEAVVQTGKPLVIIAEDVEGEALATLVVNKLRgGLKIAAVKAPgfgDRrkamlE 290
Cdd:cd03338 243 VvndyaqmdrILREER----KYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLA-KLKIMVVKDI---ER-----E 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 291 DIAIltggtvISEDLGIK----LENVTLDMLGKSKKVsiskenttivdgagqksdiegrvaqikaqiEETTSDYDREKLQ 366
Cdd:cd03338 310 EIEF------ICKTIGCKpvasIDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 367 ERLAKLAGGVAVIrVGGSTEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSTKITAKgANDDQEAGINIVR-- 443
Cdd:cd03338 354 TGVKNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEW-ARTLTGVEQYCVRaf 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495363996 444 -KALQALVRQIAENAGDEASIVVGKILDKN---EDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAA-SVASLL 514
Cdd:cd03338 432 aDALEVIPYTLAENAGLNPISIVTELRNRHaqgEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATeTVRMIL 507
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
5.74e-13 |
|
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: 71.30 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 103 GSKAVAAGMNPMDLKRGIDLAVAEVVKDL-QAKAKKINTSEEVAQVGTISANGERQIGLDIAEAMQKVGNEGVITVEEAK 181
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLdKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 182 TA---------------ETELEVVEGMQFDRGYLSPyfvtnpeKMVADLEDAYILLHEKKLsnlqamlpvleavvqtgkp 246
Cdd:TIGR02347 184 EDidlfmveimemkhksATDTTLIRGLVLDHGARHP-------DMPRRVKNAYILTCNVSL------------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 247 lviiaEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTG-----GTVISEDLGIKLenVTLDMLGKSK 321
Cdd:TIGR02347 238 -----EYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGkspdkGFVVINQKGIDP--PSLDLLAKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 322 KVSISK------ENTTIVDGAGQKSDIEGRVAQI---KAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGSTEVEVKEK 392
Cdd:TIGR02347 311 IMALRRakrrnmERLTLACGGEALNSVEDLTPEClgwAGLVYETTIGEEKYTFIEECKNPKSCTILIK--GPNDHTIAQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 393 KDRIDDALNATRAAVQEG-IVPGGGV--ALLRSSTKITAKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKIL 469
Cdd:TIGR02347 389 KDAVRDGLRAVKNAIEDKcVVPGAGAfeIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLE 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2495363996 470 DKNEDNY---GYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVAS-LLITTEAMIA 522
Cdd:TIGR02347 469 DEHDEGGevvGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASqLLLVDEVMRA 525
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
22-521 |
1.39e-12 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 70.17 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 22 VLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELedkfENMGAQLVREVASKTNDIAGDGTTTATVLAQAIVR 101
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 102 EGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTS--------EEVAQVGTIS---ANGERQIGLDIAEAMQKVG 170
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEkgeqrellEKCAATALSSkliSHNKEFFSKMIVDAVLSLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 171 NE-------GVITVEEAKTAETELevVEGMQFDRGYLSPYFVTNPEKmvadLEDAYILLHEKKLSnLQAMLPVLEAVVQT 243
Cdd:TIGR02345 185 RDdldlkliGIKKVQGGALEDSQL--VNGVAFKKTFSYAGFEQQPKK----FANPKILLLNVELE-LKAEKDNAEIRVED 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 244 GKPLVIIAeDVEGEalatLVVNKLR----GGLKIAAVKAPgFGDRRKAMLEDIAILTGGTVISEDLGiklenvtldmlgk 319
Cdd:TIGR02345 258 VEDYQAIV-DAEWA----IIFRKLEkiveSGANVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDLK------------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 320 skkvSISKENTTIVDGAgqKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvGGSTEVeVKEKKDRIDDA 399
Cdd:TIGR02345 319 ----RVIKACGGSIQST--TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILR-GGAEQF-IEEAERSLHDA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 400 LNATRAAVQ-EGIVPGGGVALLRSSTKI--TAKGANDDQEAGINIVRKALQALVRQIAENAGDEASIVVGKILDKNED-- 474
Cdd:TIGR02345 391 IMIVRRALKnKKIVAGGGAIEMELSKCLrdYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKgg 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2495363996 475 -NYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMI 521
Cdd:TIGR02345 471 kWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
3-143 |
4.57e-12 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 68.51 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 3 AKEVKfGRTAREKMLKGVDVLADAVKVTLGPKGRNVVI--DKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASK 80
Cdd:cd03336 6 AQEEK-GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVD----NPAAKVLVDISKV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495363996 81 TNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEE 143
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-135 |
1.22e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 66.98 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 3 AKEVKfGRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPR-----ITKDGVSVAKEIELEdkfeNMGAQLVREV 77
Cdd:PTZ00212 15 AQEEK-GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPRsgnvtVTNDGATILKSVWLD----NPAAKILVDI 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495363996 78 ASKTNDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKA 135
Cdd:PTZ00212 90 SKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-521 |
1.10e-10 |
|
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: 63.78 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGRN--VV--IDKSFgaprITKDGVSVAKEIEledkFENMGAQLVREvASKTNDI-AGDGTTTATVLAQ 97
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 98 AIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQ----AKAKKINTSEEVAQVgTISANGERQIGLD------IAEAMQ 167
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEelvvYKIEDLRNKEEVSKA-LKTAIASKQYGNEdflsplVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 168 KV--GNEGVITVEEAKTAE------TELEVVEGMQFDRgylspyfvtNPEKMVADLEDAYILlhekklsnlqamlpVLEA 239
Cdd:cd03341 170 SVlpENIGNFNVDNIRVVKilggslEDSKVVRGMVFKR---------EPEGSVKRVKKAKVA--------------VFSC 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 240 VVQTGKPLVIIAEDVEGEALATLvvNKLrgglKIAAVKAPG-FGDRRkamledIAILTGGTVIsedlgIKLENVTLDMLG 318
Cdd:cd03341 227 PFDIGVNVIVAGGSVGDLALHYC--NKY----GIMVIKINSkFELRR------LCRTVGATPL-----PRLGAPTPEEIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 319 KSKKVSISkenttivdgagqksDIEGRVAQIKAQIEETTSdydreklqerlaklaggVAVIRVGGSTEVEVKEKKDRIDD 398
Cdd:cd03341 290 YCDSVYVE--------------EIGDTKVVVFRQNKEDSK-----------------IATIVLRGATQNILDDVERAIDD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 399 ALNATRAAVQEG-IVPGGGVALLRSSTKITAKGAND---DQEAgINIVRKALQALVRQIAENAGDEASIVVGKIL---DK 471
Cdd:cd03341 339 GVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGEKTpglEQYA-IKKFAEAFEVVPRTLAENAGLDATEVLSELYaahQK 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2495363996 472 NEDNYGYNAQTGEYG--DLIQLGIVDPVKVVRTALQNAASVASLLITTEAMI 521
Cdd:cd03341 418 GNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-514 |
6.27e-10 |
|
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: 61.72 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQLvrevaSKTNDI-AGDGTTTATVLAQAIVR 101
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVILAGALLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 102 EGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISANGERQIGLDIAEAMQKVGNEGVITVEEAK 181
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVIDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 182 TAET-----------------ELEVVEGMQFDRGYLSP---------------YFVTNPEKmvADLEDAYILLHEKKLSN 229
Cdd:TIGR02342 176 NAKNvdlndikvvkklggtidDTELIEGLVFTQKASKSaggptriekakigliQFQISPPK--TDMENQIIVNDYAQMDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 230 LQA-----MLPVLEAVVQTGKPLVIIAEDVEGEALATLVVNKLrGGLKIAAVKapgfgDRRKAMLEDIAILTGGTVISEd 304
Cdd:TIGR02342 254 VLKeerayILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFL-AKMKIMVVK-----DIEREEIEFICKTIGCKPIAS- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 305 lgikLENVTLDMLGKSKKVS-ISKENTTIVDGAGQKSdiegrvaqikaqieettsdydreklqerlaklAGGVAVIRVGG 383
Cdd:TIGR02342 327 ----IDHFTADKLGSAELVEeVDSDGGKIIKITGIQN--------------------------------AGKTVTVVVRG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 384 STEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSTKITAKGandDQEAGIN--IVR---KALQALVRQIAENA 457
Cdd:TIGR02342 371 SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYA---RTMKGVEsyCVRafaDALEVIPYTLAENA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495363996 458 GDEASIVVGKILDKN---EDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAA-SVASLL 514
Cdd:TIGR02342 448 GLNPIKVVTELRNRHangEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASeTVRSIL 508
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
13-522 |
1.97e-09 |
|
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: 60.20 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 13 REKMLKGVDVL----------ADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFenmgAQLVREVASKTN 82
Cdd:TIGR02343 19 NKKRLKGLEAKksniaaaksvASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 83 DIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQ--VGTISANGERQIGL 160
Cdd:TIGR02343 95 DEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREplIQAAKTSLGSKIVS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 161 DIAEAMQKVGNEGVITVEEAKTAETELEVV----------EGMQFDRGYLSPYFVTNPEkMVADLEDAYILL-------- 222
Cdd:TIGR02343 175 KCHRRFAEIAVDAVLNVADMERRDVDFDLIkvegkvggslEDTKLIKGIIIDKDFSHPQ-MPKEVEDAKIAIltcpfepp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 223 -----HEKKLSNL-----------QAMLPVLEAVVQTGKPLVIIAEDVEGEALATLVVNKLrgglkiAAVKAPGFGDrrk 286
Cdd:TIGR02343 254 kpktkHKLDISSVeeykklqkyeqQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDL------PAVRWVGGQE--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 287 amLEDIAILTGGTVISedlgiKLENVTLDMLGKSKKV-----SISKENTTIVDGAGQKSDIegrvaqikaqieettsdyd 361
Cdd:TIGR02343 325 --LELIAIATGGRIVP-----RFQELSKDKLGKAGLVreisfGTTKDRMLVIEQCKNSKAV------------------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 362 reklqerlaklaggvaVIRVGGSTEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSS---TKITAKGANDDQEA 437
Cdd:TIGR02343 379 ----------------TIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSlavSQEADKYPGVEQYA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 438 gINIVRKALQALVRQIAENAG----DEASIVVGKILDKNEDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASL 513
Cdd:TIGR02343 443 -IRAFADALETIPMALAENSGldpiGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRM 521
|
....*....
gi 2495363996 514 LITTEAMIA 522
Cdd:TIGR02343 522 ILKIDDVIS 530
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-527 |
2.17e-09 |
|
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: 59.87 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 9 GRTAREKMLKGVDVLADAVKVTLGPKGRNVVI--DKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKTNDIAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 87 DGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKA--------------KKINTSEEVAQVGTISA 152
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsdevkfrqdlMNIARTTLSSKILSQHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 153 NGERQIGLDIAEAMQKVGNEGVITVEE---AKTAETELEvvEGMQFDR--GYLSPYFVTNPEKMVADL---EDAYILLHE 224
Cdd:TIGR02341 168 DHFAQLAVDAVLRLKGSGNLEAIQIIKklgGSLADSYLD--EGFLLDKkiGVNQPKRIENAKILIANTgmdTDKVKIFGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 225 KKLSNLQAMLPVLEAVVQ---TGKPLVIIAEDVEGEALATLVVN---KLRGGLKIAAVKAPGFGDrrkamLEDIAILTGG 298
Cdd:TIGR02341 246 RVRVDSTAKVAELEHAEKekmKEKVEKILKHGINCFINRQLIYNypeQLFADAGVMAIEHADFEG-----VERLALVTGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 299 TVISedlgiKLENVTLDMLGKSKKvsiskenttivdgagqksdiegrvaqikaqIEETTSDYDreKLQERLAKLAGGVAV 378
Cdd:TIGR02341 321 EIVS-----TFDHPELVKLGSCDL------------------------------IEEIMIGED--KLLKFSGVKLGEACT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 379 IRVGGSTEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSTKITAKGANDDQEAGINI--VRKALQALVRQIAE 455
Cdd:TIGR02341 364 IVLRGATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVeaFARALRQLPTIIAD 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495363996 456 NAGDEASIVVGKI---LDKNEDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLITTEAMIAELPKK 527
Cdd:TIGR02341 444 NAGFDSAELVAQLraaHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-129 |
4.11e-08 |
|
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: 55.88 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 9 GRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKfenmGAQLVREVASKTNDIAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2495363996 89 TTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVK 129
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVK 126
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
22-146 |
6.19e-08 |
|
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: 55.37 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 22 VLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELedkfENMGAQLVREVASKTNDIAGDGTTTATVLAQAIVR 101
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2495363996 102 EGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAkkINTSEEVAQ 146
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA--VNIDKEDKE 145
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
12-143 |
6.45e-07 |
|
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: 51.92 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 12 AREKMLKGVD----------VLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKT 81
Cdd:cd03339 14 EKKKRLKGLEahkshilaakSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQ 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495363996 82 NDIAGDGTTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEE 143
Cdd:cd03339 90 DDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD 151
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-129 |
1.46e-06 |
|
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: 50.75 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 9 GRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKfenmGAQLVREVASKTNDIAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2495363996 89 TTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVK 129
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVK 122
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-495 |
9.73e-05 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 45.09 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMgaqLVREVASKTNDIaGDGTTTATVLAQAIVRE 102
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKL---LVMASEMQENEI-GDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 103 GSKAVAAGMNPMDLKRGIDLAVAEVVKDLQA----KAKKINTSEEVAQVgTISANGERQIGLD------IAEAM-----Q 167
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEElvvwEVKDLRDKDELIKA-LKASISSKQYGNEdflaqlVAQACstvlpK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 168 KVGNEGVITVEEAKTAETEL---EVVEGMQFDRgylspyfvtNPEKMVADLEDAYILLH---------EKK----LSNLQ 231
Cdd:TIGR02346 185 NPQNFNVDNIRVCKILGGSLsnsEVLKGMVFNR---------EAEGSVKSVKNAKVAVFscpldtattETKgtvlIHNAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 232 AML-----------PVLEAVVQTGKPLVIIAEDVeGEaLATLVVNKlrggLKIAAVKAPGfgdrrKAMLEDIAILTGGTV 300
Cdd:TIGR02346 256 ELLnyskgeenqieAMIKAIADSGVNVIVTGGSV-GD-MALHYLNK----YNIMVLKIPS-----KFELRRLCKTVGATP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 301 IsedlgIKLENVTLDMLGKSKKVSISKENTTIVDGAGQKSDiEGRVAQIkaqieettsdydreklqerlaklaggvaVIR 380
Cdd:TIGR02346 325 L-----PRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENG-DSKISTI----------------------------ILR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 381 vgGSTEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSTKITAKGAND---DQEAgINIVRKALQALVRQIAEN 456
Cdd:TIGR02346 371 --GSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEKLpglDQYA-IKKFAEAFEIIPRTLAEN 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2495363996 457 AGDEASIVVGKIL---DKNEDNYGYNAQTGEYG--DLIQLGIVD 495
Cdd:TIGR02346 448 AGLNANEVIPKLYaahKKGNKSKGIDIEAESDGvkDASEAGIYD 491
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
9-515 |
9.30e-04 |
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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: 41.90 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 9 GRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKTNDIAGDG 88
Cdd:cd03337 14 GRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDG 89
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 89 TTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTS--EEVAQV-----GTISANGERQIGLD 161
Cdd:cd03337 90 TTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNdrAQMLKIiksciGTKFVSRWSDLMCN 169
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 162 IA-EAMQKVGNEGVITVEE------AKTAE------TELEVVEGMQFDRGYLSP---YFVTNPEKMVADLEDAYILLHEK 225
Cdd:cd03337 170 LAlDAVKTVAVEENGRKKEidikryAKVEKipggeiEDSRVLDGVMLNKDVTHPkmrRRIENPRIVLLDCPLEYLVITEK 249
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 226 KLSNL-QAMLpvleavvqtgkplviiaedvegealatlvvnkLRGGlkIAAVKapgfgdR-RKAMLEDIAILTGGTVISE 303
Cdd:cd03337 250 GVSDLaQHYL--------------------------------VKAG--ITALR------RvRKTDNNRIARACGATIVNR 289
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 304 DlgiklENVTLDMLGKS----KKVSISKENTTIVDGAGqksdiEGRVAQIkaqieettsdydreklqerlaklaggvaVI 379
Cdd:cd03337 290 P-----EELTESDVGTGaglfEVKKIGDEYFTFITECK-----DPKACTI----------------------------LL 331
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 380 RvGGSTEVeVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSTKITAKGANDD--QEAGINIVRKALQALVRQIAEN 456
Cdd:cd03337 332 R-GASKDV-LNEVERNLQDAMAVARNIILNPkLVPGGGATEMAVSHALSEKAKSIEgvEQWPYKAVASALEVIPRTLAQN 409
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490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495363996 457 AGDEASIVV----GKILDKNEDNYGYNAQTGEYGDLIQLGIVDPVKVVRTALQNAASVASLLI 515
Cdd:cd03337 410 CGANVIRTLtelrAKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLL 472
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| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-152 |
1.04e-03 |
|
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: 41.65 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495363996 9 GRTAREKMLKGVDVLADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEdkfeNMGAQLVREVASKTNDIAGDG 88
Cdd:TIGR02344 14 GRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDG 89
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495363996 89 TTTATVLAQAIVREGSKAVAAGMNPMDLKRGIDLAVAEVVKDLQAKAKKINTSEEVAQVGTISA 152
Cdd:TIGR02344 90 TTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQS 153
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