NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|302058292|ref|NP_001180459|]
View 

T-complex protein 1 subunit zeta-2 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
chap_CCT_zeta super family cl28957
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485 0e+00

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.


The actual alignment was detected with superfamily member TIGR02347:

Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 780.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292    3 AIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM--------------- 67
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMqiqhptasmiaraat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ------------------------------GLHPRIIAEGFEAAKIKALEVLEEVKVTKE--MKRKILLDVARTSLQTKV 115
Cdd:TIGR02347  81 aqdditgdgttstvlligellkqaeryileGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  116 HAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYE 195
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  196 KTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQS-NKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  275 NMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIK 354
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  355 NAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGV 434
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 302058292  435 DLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 485
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
 
Name Accession Description Interval E-value
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485 0e+00

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: 780.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292    3 AIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM--------------- 67
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMqiqhptasmiaraat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ------------------------------GLHPRIIAEGFEAAKIKALEVLEEVKVTKE--MKRKILLDVARTSLQTKV 115
Cdd:TIGR02347  81 aqdditgdgttstvlligellkqaeryileGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  116 HAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYE 195
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  196 KTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQS-NKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  275 NMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIK 354
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  355 NAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGV 434
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 302058292  435 DLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 485
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
23-481 0e+00

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: 756.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd03342   17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMqiqhptasmiaraataqdditgdgttsnvlligel 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK--RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 135
Cdd:cd03342   97 lkqaeryiqeGVHPRIITEGFELAKNKALKFLESFKVPVEIDtdRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 RPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKtaeekeklv 215
Cdd:cd03342  177 KPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSGFFYS--------- 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 216 kaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLT 295
Cdd:cd03342  248 -----------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLS 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 296 VDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAE 375
Cdd:cd03342  299 PECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 376 ALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCV 455
Cdd:cd03342  379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
                        490       500
                 ....*....|....*....|....*.
gi 302058292 456 KKQLLHSCTVIATNILLVDEIMRAGM 481
Cdd:cd03342  459 KRQILHSATVIASQLLLVDEIIRAGR 484
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-480 6.84e-172

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: 492.49  E-value: 6.84e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM------------------------------------------ 67
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELeiqhpaakllveaakaqdeevgdgtttvvvlagelleeaekl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ---GLHPRIIAEGFEAAKIKALEVLEEVKV--TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPID 142
Cdd:pfam00118  81 laaGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  143 LFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEKLVKAERKFI 222
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  223 EDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHA 302
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  303 GLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKN 382
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  383 SIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHS 462
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 302058292  463 CTVIATNILLVDEIMRAG 480
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
thermosome_alpha NF041082
thermosome subunit alpha;
23-480 8.17e-114

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 345.33  E-value: 8.17e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:NF041082  22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMdiehpaakmivevaktqddevgdgtttavvlagel 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:NF041082 102 lkkaeelldqDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P--GYPIDLFMVEImeMKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKE 212
Cdd:NF041082 182 KdgGYNVDLDNIKV--EKKVGGSieDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQ 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 213 KLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFE 292
Cdd:NF041082 260 AFLDQEEKMLKEMVDKIAD------SGAN---VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSID 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 293 DLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVA 372
Cdd:NF041082 331 DLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVE 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 373 MAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDN 452
Cdd:NF041082 411 LALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEP 490
                        490       500
                 ....*....|....*....|....*...
gi 302058292 453 YCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041082 491 LRVKTQAIKSATEAAVMILRIDDVIAAA 518
thermosome_beta NF041083
thermosome subunit beta;
23-480 1.46e-112

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 342.31  E-value: 1.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:NF041083  22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMdvqhpaakmlvevaktqddevgdgtttavvlagel 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV-- 134
Cdd:NF041083 102 lkkaeelldqNIHPTIIANGYRLAAEKAIEILDEIAEKvDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVae 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 -RRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEK 213
Cdd:NF041083 182 kRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQK 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 214 LVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFED 293
Cdd:NF041083 262 FLDQEEKMLKEMVDKIKA------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDD 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 294 LTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAM 373
Cdd:NF041083 333 LTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVEL 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 374 AEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNY 453
Cdd:NF041083 413 AKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPL 492
                        490       500
                 ....*....|....*....|....*..
gi 302058292 454 CVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041083 493 RVKTQAIKSATEAATMILRIDDVIAAK 519
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
23-479 3.68e-65

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 218.41  E-value: 3.68e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:COG0459   15 NIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIeledpfenmgaqlvkevasktndeagdgtttatvl 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 --------------GLHPRIIAEGFEAAKIKALEVLEE--VKVTKemkRKILLDVARTSLQTKvhaelaDVLTEVVVDSV 131
Cdd:COG0459   95 agallkeglklvaaGANPTDIKRGIDKAVEKAVEELKKiaKPVDD---KEELAQVATISANGD------EEIGELIAEAM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 132 LAVRRPGYpidlFMVEimemKHK-LGTDTKLIQGLVLDHGARHPD-------MKKRVEDAFILICNVSLEyektevnsgf 203
Cdd:COG0459  166 EKVGKDGV----ITVE----EGKgLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS---------- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 204 fyktaeekeklvkaerkfiedRVQKIIDLKDKVcAQSNKGfVVINQKGIDPFSLDSLAKHGIVALRRA---------KRR 274
Cdd:COG0459  228 ---------------------SIQDLLPLLEKV-AQSGKP-LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgDRR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 N--MERLSLACGGMAVN-----SFEDLTVDCLGHAGLVYEytlGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIR 347
Cdd:COG0459  285 KamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVE 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 348 DGLRAIKNAIEDGCmVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEhve 427
Cdd:COG0459  362 DALHATRAAVEEGI-VPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA--- 437
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 302058292 428 SKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:COG0459  438 KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
23-479 2.29e-55

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 193.32  E-value: 2.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLL---------------------DEMG-------- 68
Cdd:PTZ00212  27 SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILksvwldnpaakilvdisktqdEEVGdgttsvvv 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  69 ----------------LHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVV 128
Cdd:PTZ00212 107 lagellreaeklldqkIHPQTIIEGWRMALDVARKALEEIAFDhgsdEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAV 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 129 DSVLAVRRPGypiDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEK-----TE 198
Cdd:PTZ00212 187 DAVLRLKGSG---NLDYIQIIK---KPGgtlRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMDTDKikiygAK 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 199 VNSGFFYKTAEekekLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMER 278
Cdd:PTZ00212 258 VKVDSMEKVAE----IEAAEKEKMKNKVDKILA------HGCN---VFINRQLIYNYPEQLFAEAGIMAIEHADFDGMER 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 279 LSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIE 358
Cdd:PTZ00212 325 LAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVK 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 359 DGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNT 438
Cdd:PTZ00212 405 DTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEK 484
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 302058292 439 GEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
 
Name Accession Description Interval E-value
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485 0e+00

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: 780.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292    3 AIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM--------------- 67
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMqiqhptasmiaraat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ------------------------------GLHPRIIAEGFEAAKIKALEVLEEVKVTKE--MKRKILLDVARTSLQTKV 115
Cdd:TIGR02347  81 aqdditgdgttstvlligellkqaeryileGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  116 HAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYE 195
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  196 KTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQS-NKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  275 NMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIK 354
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  355 NAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGV 434
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 302058292  435 DLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 485
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
23-481 0e+00

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: 756.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd03342   17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMqiqhptasmiaraataqdditgdgttsnvlligel 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK--RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 135
Cdd:cd03342   97 lkqaeryiqeGVHPRIITEGFELAKNKALKFLESFKVPVEIDtdRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 RPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKtaeekeklv 215
Cdd:cd03342  177 KPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSGFFYS--------- 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 216 kaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLT 295
Cdd:cd03342  248 -----------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLS 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 296 VDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAE 375
Cdd:cd03342  299 PECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 376 ALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCV 455
Cdd:cd03342  379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
                        490       500
                 ....*....|....*....|....*.
gi 302058292 456 KKQLLHSCTVIATNILLVDEIMRAGM 481
Cdd:cd03342  459 KRQILHSATVIASQLLLVDEIIRAGR 484
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-480 6.84e-172

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: 492.49  E-value: 6.84e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM------------------------------------------ 67
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELeiqhpaakllveaakaqdeevgdgtttvvvlagelleeaekl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ---GLHPRIIAEGFEAAKIKALEVLEEVKV--TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPID 142
Cdd:pfam00118  81 laaGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  143 LFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEKLVKAERKFI 222
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  223 EDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHA 302
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  303 GLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKN 382
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  383 SIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHS 462
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 302058292  463 CTVIATNILLVDEIMRAG 480
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
23-478 1.47e-158

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: 457.66  E-value: 1.47e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd00309   13 NINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIevehpaakllvevaksqddevgdgtttvvvlagel 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:cd00309   93 lkeaekllaaGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEdREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 PGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYektevnsgffyktaeekeklvk 216
Cdd:cd00309  173 ENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------------------- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 217 aerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTV 296
Cdd:cd00309  231 ----------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTP 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 297 DCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEA 376
Cdd:cd00309  283 EDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKA 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 377 LVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVK 456
Cdd:cd00309  363 LEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVK 442
                        490       500
                 ....*....|....*....|..
gi 302058292 457 KQLLHSCTVIATNILLVDEIMR 478
Cdd:cd00309  443 RQALKSATEAASLILTIDDIIV 464
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
23-480 7.71e-114

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: 345.40  E-value: 7.71e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd03343   20 NIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMdiehpaakmlvevaktqdeevgdgtttavvlagel 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEE--VKVTKEmKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV- 134
Cdd:cd03343  100 lekaedlldqNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVa 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 --RRPGYPIDLFMVEIMemKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 210
Cdd:cd03343  179 ekRDGKYVVDLDNIKIE--KKTGGSvdDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQ 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 KEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 290
Cdd:cd03343  257 LQAFLEQEEAMLKEMVDKIAD------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTN 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 370
Cdd:cd03343  328 IDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVE 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 371 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 450
Cdd:cd03343  408 IELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVI 487
                        490       500       510
                 ....*....|....*....|....*....|
gi 302058292 451 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:cd03343  488 EPLRVKKQAIKSATEAATMILRIDDVIAAK 517
thermosome_alpha NF041082
thermosome subunit alpha;
23-480 8.17e-114

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 345.33  E-value: 8.17e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:NF041082  22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMdiehpaakmivevaktqddevgdgtttavvlagel 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:NF041082 102 lkkaeelldqDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P--GYPIDLFMVEImeMKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKE 212
Cdd:NF041082 182 KdgGYNVDLDNIKV--EKKVGGSieDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQ 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 213 KLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFE 292
Cdd:NF041082 260 AFLDQEEKMLKEMVDKIAD------SGAN---VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSID 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 293 DLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVA 372
Cdd:NF041082 331 DLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVE 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 373 MAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDN 452
Cdd:NF041082 411 LALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEP 490
                        490       500
                 ....*....|....*....|....*...
gi 302058292 453 YCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041082 491 LRVKTQAIKSATEAAVMILRIDDVIAAA 518
thermosome_beta NF041083
thermosome subunit beta;
23-480 1.46e-112

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 342.31  E-value: 1.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:NF041083  22 NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMdvqhpaakmlvevaktqddevgdgtttavvlagel 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV-- 134
Cdd:NF041083 102 lkkaeelldqNIHPTIIANGYRLAAEKAIEILDEIAEKvDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVae 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 -RRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEK 213
Cdd:NF041083 182 kRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQK 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 214 LVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFED 293
Cdd:NF041083 262 FLDQEEKMLKEMVDKIKA------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDD 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 294 LTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAM 373
Cdd:NF041083 333 LTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVEL 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 374 AEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNY 453
Cdd:NF041083 413 AKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPL 492
                        490       500
                 ....*....|....*....|....*..
gi 302058292 454 CVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041083 493 RVKTQAIKSATEAATMILRIDDVIAAK 519
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
23-476 1.72e-76

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: 249.14  E-value: 1.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd03339   28 HILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMdvdhqiakllvelsksqddeigdgttgvvvlagal 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTKE---MKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV 134
Cdd:cd03339  108 leqaeklldrGIHPIRIADGYEQACKIAVEHLEEIADKIEfspDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSV 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 ----RRPgypIDLfmvEIMEMKHKLG---TDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKT 207
Cdd:cd03339  188 adleRKD---VNF---ELIKVEGKVGgrlEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITS 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 208 AEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 287
Cdd:cd03339  262 VEDYKKLQEYEQKYFREMVEQVKD------AGAN---LVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRI 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 288 VNSFEDLTVDCLGHAGLVYEYTLG--EEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPG 365
Cdd:cd03339  333 VPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYG 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 366 AGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQ-LVGVDLNTGEPMVA 444
Cdd:cd03339  413 GGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNpHLGIDCLGRGTNDM 492
                        490       500       510
                 ....*....|....*....|....*....|..
gi 302058292 445 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEI 476
Cdd:cd03339  493 KEQKVFETLISKKQQILLATQVVKMILKIDDV 524
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
23-480 8.75e-70

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: 231.62  E-value: 8.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:TIGR02343  32 NIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMdvdnqiaklmvelsksqddeigdgttgvvvlagal 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ----------GLHPRIIAEGFEAAKIKALEVLEEV--KVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAV 134
Cdd:TIGR02343 112 leqaeelldkGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  135 ----RRPgypIDLfmvEIMEMKHKLG---TDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKT 207
Cdd:TIGR02343 192 admeRRD---VDF---DLIKVEGKVGgslEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISS 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  208 AEEKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 287
Cdd:TIGR02343 266 VEEYKKLQKYEQQKFKEMIDDIKK------SGAN---LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRI 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  288 VNSFEDLTVDCLGHAGLVYEYTLG--EEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPG 365
Cdd:TIGR02343 337 VPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYG 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  366 AGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQ-LVGVDLNTGEPMVA 444
Cdd:TIGR02343 417 GGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNpNLGVDCLGYGTNDM 496
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 302058292  445 ADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:TIGR02343 497 KEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
100-359 7.63e-69

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: 218.87  E-value: 7.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 100 RKILLDVARTSLQTKVhAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKR 179
Cdd:cd03333    1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 180 VEDAFILICNVSLEYektevnsgffyktaeekeklvkaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDS 259
Cdd:cd03333   80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 260 LAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTL 339
Cdd:cd03333  110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
                        250       260
                 ....*....|....*....|
gi 302058292 340 TQVKDAIRDGLRAIKNAIED 359
Cdd:cd03333  190 DEVKRSLHDALCAVRAAVEE 209
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
23-476 6.29e-67

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: 223.85  E-value: 6.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMGL--------------------------------- 69
Cdd:TIGR02344  21 NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVahpaaksmielsrtqdeevgdgttsviilagem 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   70 ------------HPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:TIGR02344 101 lsvaepfleqniHPTVIIRAYRKALDDALSVLEEISIPVDVNdDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQR 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  137 PGYPIdlFMVEIMEM----KHKLG--TDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 210
Cdd:TIGR02344 181 DENGR--KEIDIKRYakveKIPGGdiEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEED 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  211 KEKLVKAERKFIEDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 290
Cdd:TIGR02344 259 WNRILQMEEEYVQLMCEDIIAVKPDL---------VITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNR 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  291 FEDLTVDCLG-HAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAI 369
Cdd:TIGR02344 330 PEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGAT 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  370 EVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHV-ESKQLVGVDLNTGEPMVAADAG 448
Cdd:TIGR02344 410 EMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDGETGKIVDMKEKG 489
                         490       500
                  ....*....|....*....|....*...
gi 302058292  449 VWDNYCVKKQLLHSCTVIATNILLVDEI 476
Cdd:TIGR02344 490 IWEPLAVKLQTYKTAIESACLLLRIDDI 517
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
23-476 2.51e-65

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: 218.32  E-value: 2.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd03337   21 NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIdvahpaaksmielsrtqdeevgdgttsviilagei 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVT-KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:cd03337  101 lavaepflerGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 P----GYPIDL--FM-VEimemKHKLGT--DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYektevnsgffykt 207
Cdd:cd03337  181 EengrKKEIDIkrYAkVE----KIPGGEieDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY------------- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 208 aeekeklvkaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMA 287
Cdd:cd03337  244 -------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATI 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 288 VNSFEDLTVDCLGHAGLVYEYTL-GEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGA 366
Cdd:cd03337  287 VNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGG 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 367 GAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVES-KQLVGVDLNTGEPMVAA 445
Cdd:cd03337  367 GATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGeNSTWGIDGETGDIVDMK 446
                        490       500       510
                 ....*....|....*....|....*....|.
gi 302058292 446 DAGVWDNYCVKKQLLHSCTVIATNILLVDEI 476
Cdd:cd03337  447 ELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
23-479 3.68e-65

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 218.41  E-value: 3.68e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:COG0459   15 NIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIeledpfenmgaqlvkevasktndeagdgtttatvl 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 --------------GLHPRIIAEGFEAAKIKALEVLEE--VKVTKemkRKILLDVARTSLQTKvhaelaDVLTEVVVDSV 131
Cdd:COG0459   95 agallkeglklvaaGANPTDIKRGIDKAVEKAVEELKKiaKPVDD---KEELAQVATISANGD------EEIGELIAEAM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 132 LAVRRPGYpidlFMVEimemKHK-LGTDTKLIQGLVLDHGARHPD-------MKKRVEDAFILICNVSLEyektevnsgf 203
Cdd:COG0459  166 EKVGKDGV----ITVE----EGKgLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS---------- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 204 fyktaeekeklvkaerkfiedRVQKIIDLKDKVcAQSNKGfVVINQKGIDPFSLDSLAKHGIVALRRA---------KRR 274
Cdd:COG0459  228 ---------------------SIQDLLPLLEKV-AQSGKP-LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgDRR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 275 N--MERLSLACGGMAVN-----SFEDLTVDCLGHAGLVYEytlGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIR 347
Cdd:COG0459  285 KamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVE 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 348 DGLRAIKNAIEDGCmVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEhve 427
Cdd:COG0459  362 DALHATRAAVEEGI-VPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA--- 437
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 302058292 428 SKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:COG0459  438 KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
23-478 9.48e-63

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: 212.91  E-value: 9.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLL-------------------------------------- 64
Cdd:cd03335   13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILkllevehpaakilvelaqlqdkevgdgttsvviiaael 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  65 ----DE---MGLHPRIIAEGFEAAKIKALEVLEEVKVTK--EMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 135
Cdd:cd03335   93 lkraNElvkQKIHPTTIISGYRLACKEAVKYIKEHLSISvdNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 136 R------PGYPIDlfMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAE 209
Cdd:cd03335  173 TtnekgkTKYPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPE 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 210 EKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVN 289
Cdd:cd03335  251 KLEKIRQRESDITKERIKKILA------AGAN---VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 290 SFEDLTVD------CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMV 363
Cdd:cd03335  322 TLANLEGEetfdpsYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 364 PGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQL--------VGVD 435
Cdd:cd03335  402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKpdkkhlkwYGLD 481
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 302058292 436 LNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 478
Cdd:cd03335  482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
23-441 9.57e-63

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: 212.53  E-value: 9.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:cd03338   13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMsvlhpaakmlvelskaqdieagdgttsvvvlagal 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:cd03338   93 lsacesllkkGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 137 PGYP--IDLFMVEIMEmkhKLG---TDTKLIQGLVLDHGARH-PDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 210
Cdd:cd03338  173 PATAtnVDLKDIRIVK---KLGgtiEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 KEKLVKAERKFIEDRVQKIidlKDKVCAqsnkgfVVINQKGI-----DPFSLDSLAKHGIVALRRAKRRNMERLSLACGG 285
Cdd:cd03338  250 MDRILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 286 MAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPC-SVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVP 364
Cdd:cd03338  321 KPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGkTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIP 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302058292 365 GAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEP 441
Cdd:cd03338  401 GGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
23-478 9.67e-63

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: 213.04  E-value: 9.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:TIGR02340  17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLevehpaakilvelaqlqdrevgdgttsvviiaael 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTK--EMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVR 135
Cdd:TIGR02340  97 lkradelvknKIHPTSVISGYRLACKEAVKYIKENLSVSvdELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  136 ------RPGYPIDlfMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAE 209
Cdd:TIGR02340 177 ttnengETKYPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  210 EKEKLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVN 289
Cdd:TIGR02340 255 KLEQIRQREADITKERIKKILD------AGAN---VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  290 SFEDLTVD------CLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMV 363
Cdd:TIGR02340 326 TLADLEGEetfeasYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  364 PGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVES------KQL--VGVD 435
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAqlkpekKHLkwYGLD 485
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 302058292  436 LNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 478
Cdd:TIGR02340 486 LVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
32-479 7.39e-60

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: 204.87  E-value: 7.39e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  32 DVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLL---------------------DEMG-------------------- 68
Cdd:cd03336   27 DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILksigvdnpaakvlvdiskvqdDEVGdgttsvtvlaaellreaekl 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  69 ----LHPRIIAEGFEAAKIKALEVLEE----VKVTKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGyp 140
Cdd:cd03336  107 vaqkIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSG-- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 141 iDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEK-----TEVNSGFFYKTAEe 210
Cdd:cd03336  185 -NLDAIQIIK---KLGgslKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMDTDKikifgAKVRVDSTAKVAE- 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 211 kekLVKAERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 290
Cdd:cd03336  257 ---IEEAEKEKMKNKVEKIL---------KHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIAST 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 291 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 370
Cdd:cd03336  325 FDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSE 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 371 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 450
Cdd:cd03336  405 MLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGIT 484
                        490       500
                 ....*....|....*....|....*....
gi 302058292 451 DNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:cd03336  485 ESFKVKRQVLLSASEAAEMILRVDDIIKC 513
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
23-477 1.40e-59

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: 204.25  E-value: 1.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:TIGR02342  14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMavlhpaakmlvelskaqdieagdgttsvvilagal 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVTKEMK-RKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRR 136
Cdd:TIGR02342  94 lgacerllnkGIHPTIISESFQSAADEAIKILDEMSIPVDLSdREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVID 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  137 PGYPIDLFMVEIMEMKHKLGT--DTKLIQGLVLDHGARHPD-MKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEK 213
Cdd:TIGR02342 174 PENAKNVDLNDIKVVKKLGGTidDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  214 LVKAERKFIEDRVQKIidlkdkvcaQSNKGFVVINQKGI-----DPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAV 288
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---------KKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  289 NSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPC-SVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAG 367
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  368 AIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADA 447
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
                         490       500       510
                  ....*....|....*....|....*....|
gi 302058292  448 GVWDNYCVKKQLLHSCTVIATNILLVDEIM 477
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
23-479 1.23e-56

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: 196.52  E-value: 1.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEM----------------------------------- 67
Cdd:TIGR02345  23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLdivhpaaktlvdiaksqdaevgdgttsvtilagel 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   68 ----------GLHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLA 133
Cdd:TIGR02345 103 lkeakpfieeGVHPQLIIRCYREALSLAVEKIKEIAVTideeKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  134 VRRPGypIDLFMVEIMEMKHKLGTDTKLIQGLVLDHG---ARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 210
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  211 KEKLVKAERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 290
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIV---------ESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  291 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIE 370
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  371 VAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVW 450
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
                         490       500
                  ....*....|....*....|....*....
gi 302058292  451 DNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
23-479 8.81e-56

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: 194.04  E-value: 8.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNV---LLD---------------------------------- 65
Cdd:cd03340   21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATilkLLDivhpaaktlvdiaksqdaevgdgttsvvvlagef 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  66 --------EMGLHPRIIAEGFEAAKIKALEVLEEVKVT-----KEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVL 132
Cdd:cd03340  101 lkeakpfiEDGVHPQIIIRGYRKALQLAIEKIKEIAVNidkedKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 133 AVRRPgypIDLFMVEIMEMKHKLGTDTKLIQGLVLDHG---ARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAE 209
Cdd:cd03340  181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 210 EKEKLVKAERKFIEDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVN 289
Cdd:cd03340  258 EYQAIVDAEWKIIYDKLEKIVKSGANV---------VLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 290 SFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAI 369
Cdd:cd03340  329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAI 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 370 EVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQL-VGVDLNTGEPMVAADAG 448
Cdd:cd03340  409 EMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAF 488
                        490       500       510
                 ....*....|....*....|....*....|.
gi 302058292 449 VWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:cd03340  489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
23-479 2.29e-55

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 193.32  E-value: 2.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLL---------------------DEMG-------- 68
Cdd:PTZ00212  27 SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILksvwldnpaakilvdisktqdEEVGdgttsvvv 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  69 ----------------LHPRIIAEGFEAAKIKALEVLEEVKVT----KEMKRKILLDVARTSLQTKVHAELADVLTEVVV 128
Cdd:PTZ00212 107 lagellreaeklldqkIHPQTIIEGWRMALDVARKALEEIAFDhgsdEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAV 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 129 DSVLAVRRPGypiDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEK-----TE 198
Cdd:PTZ00212 187 DAVLRLKGSG---NLDYIQIIK---KPGgtlRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMDTDKikiygAK 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 199 VNSGFFYKTAEekekLVKAERKFIEDRVQKIIDlkdkvcAQSNkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMER 278
Cdd:PTZ00212 258 VKVDSMEKVAE----IEAAEKEKMKNKVDKILA------HGCN---VFINRQLIYNYPEQLFAEAGIMAIEHADFDGMER 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 279 LSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIE 358
Cdd:PTZ00212 325 LAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVK 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 359 DGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNT 438
Cdd:PTZ00212 405 DTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEK 484
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 302058292 439 GEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
23-479 1.35e-51

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: 182.99  E-value: 1.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDE------------------------------------ 66
Cdd:TIGR02346  23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRElevqhpaakllvmasemqeneigdgtnlvlvlagel 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   67 ---------MGLHPRIIAEGFEAAKIKALEVLEEVKVTKEM---KRKILLDVARTSLQTKVHAElADVLTEVVVDSVLAV 134
Cdd:TIGR02346 103 lnkaeelirMGLHPSEIIKGYEMALKKAMEILEELVVWEVKdlrDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  135 RrPGYPIDlFMVEIMEMKHKLGT---DTKLIQGLVLdhgARHPDMK-KRVEDAFILICNVSLEYEKTEVNSGFFYKTAEE 210
Cdd:TIGR02346 182 L-PKNPQN-FNVDNIRVCKILGGslsNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  211 KEKLVKAERKFIEDRVQKIIDLKDKVcaqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNS 290
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVNV---------IVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPR 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  291 FEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSV-TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAI 369
Cdd:TIGR02346 328 LGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGAT 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  370 EVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMV--AADA 447
Cdd:TIGR02346 408 EIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVkdASEA 487
                         490       500       510
                  ....*....|....*....|....*....|..
gi 302058292  448 GVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:TIGR02346 488 GIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
32-479 7.41e-46

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: 167.34  E-value: 7.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   32 DVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLL---------------------DEMG-------------------- 68
Cdd:TIGR02341  28 DLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILksigvdnpaakvlvdmskvqdDEVGdgttsvtvlaaellreaekl 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292   69 ----LHPRIIAEGFEAAKIKALEVLEEVKV----TKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGyp 140
Cdd:TIGR02341 108 inqkIHPQTIIAGYREATKAARDALLKSAVdngsDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSG-- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  141 iDLFMVEIMEmkhKLG---TDTKLIQGLVLDH--GARHPdmkKRVEDAFILICNVSLEYEKTEV-NSGFFYKTAEEKEKL 214
Cdd:TIGR02341 186 -NLEAIQIIK---KLGgslADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMDTDKVKIfGSRVRVDSTAKVAEL 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  215 VKAERKFIEDRVQKIIdlkdkvcaqSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDL 294
Cdd:TIGR02341 259 EHAEKEKMKEKVEKIL---------KHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHP 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  295 TVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMA 374
Cdd:TIGR02341 330 ELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMS 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  375 EALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYC 454
Cdd:TIGR02341 410 KAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYK 489
                         490       500
                  ....*....|....*....|....*
gi 302058292  455 VKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:TIGR02341 490 VKRAVVSSAAEAAEVILRVDNIIKA 514
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
23-479 7.43e-45

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: 163.55  E-value: 7.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  23 NICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDE------------------------------------ 66
Cdd:cd03341   13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRElevqhpaakllvmasqmqeeeigdgtnlvvvlagel 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292  67 ---------MGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKILLDVA---RTSLQTKVhAELADVLTEVVVDSVLAV 134
Cdd:cd03341   93 lekaeellrMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSkalKTAIASKQ-YGNEDFLSPLVAEACISV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 135 rrpgYPIDL--FMVEIMEMKHKLG---TDTKLIQGLVLdhgARHPDMK-KRVEDAFILICNVSLEyekTEVNsgffykta 208
Cdd:cd03341  172 ----LPENIgnFNVDNIRVVKILGgslEDSKVVRGMVF---KREPEGSvKRVKKAKVAVFSCPFD---IGVN-------- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 209 eekeklvkaerkfiedrvqkiidlkdkvcaqsnkgfVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAV 288
Cdd:cd03341  234 ------------------------------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 289 NSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSV-TLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAG 367
Cdd:cd03341  278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 368 AIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMV--AA 445
Cdd:cd03341  358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAK 437
                        490       500       510
                 ....*....|....*....|....*....|....
gi 302058292 446 DAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:cd03341  438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
158-343 1.53e-12

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 67.63  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 158 DTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKteVNSGFFYKtaeekEKLVKAERKFIEDRVQKIIDLKDKVc 237
Cdd:cd03334   62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLSL-----DPVILQEKEYLKNLVSRIVALRPDV- 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302058292 238 aqsnkgfvVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLtVDC--LGHAGLVYEYTLGEEK- 314
Cdd:cd03334  134 --------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDL-LTSpkLGTCESFRVRTYVEEHg 204
                        170       180       190
                 ....*....|....*....|....*....|...
gi 302058292 315 ----FTFIEECVNPCSVTLLVKGPNKHTLTQVK 343
Cdd:cd03334  205 rsktLMFFEGCPKELGCTILLRGGDLEELKKVK 237
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
343-413 6.94e-04

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 42.21  E-value: 6.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302058292 343 KDAIRDGLRAIKNAIEDGcMVPGAGAIEVAMAEAL--VTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYD 413
Cdd:PTZ00114 405 KDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLdkLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH