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Conserved domains on  [gi|4502643|ref|NP_001753|]
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T-complex protein 1 subunit zeta isoform a [Homo sapiens]

Protein Classification

T-complex protein 1 subunit zeta( domain architecture ID 11494171)

T-complex protein 1 subunit zeta is a component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis

Graphical summary

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List of domain hits

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 ...
3-530 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: 962.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643      3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     83 AQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 160
Cdd:TIGR02347  81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    161 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    241 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    320 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    400 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 4502643    480 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 530
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 ...
3-530 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: 962.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643      3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     83 AQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 160
Cdd:TIGR02347  81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    161 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    241 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    320 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    400 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 4502643    480 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 530
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
7-526 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: 935.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDD 86
Cdd:cd03342   1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   87 ITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM--DRETLIDVARTSLRTKVHAEL 164
Cdd:cd03342  81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  165 ADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEV 244
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  245 NSGFFYKsaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERL 324
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  325 TLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDD 404
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  405 GCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTG 484
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 4502643  485 EPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGM 526
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-525 0e+00

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: 589.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLY 109
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    110 ISEGLHPRIITEGFEAAKEKALQFLEEVKV--SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPID 187
Cdd:pfam00118  81 LAAGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    188 LFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFI 267
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    268 EDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHA 347
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    348 GLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKP 427
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    428 SVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHS 507
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 4502643    508 CTVIATNILLVDEIMRAG 525
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
thermosome_alpha NF041082
thermosome subunit alpha;
19-525 6.19e-142

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 419.29  E-value: 6.19e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041082  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:NF041082  98 AGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   178 AI--KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:NF041082 178 AVaeKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQ 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   256 REKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 335
Cdd:NF041082 258 LQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   336 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:NF041082 329 IDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   416 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 495
Cdd:NF041082 409 VELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVV 488
                        490       500       510
                 ....*....|....*....|....*....|
gi 4502643   496 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041082 489 EPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
thermosome_beta NF041083
thermosome subunit beta;
19-525 2.19e-141

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 417.81  E-value: 2.19e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041083  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV--KVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 176
Cdd:NF041083  98 AGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIaeKVDPD-DRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   177 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:NF041083 177 KQVAEKRDGkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDP 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   254 EEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:NF041083 257 DQLQKFLDQEEKMLKEMVDKIKATGAN---------VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 413
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   414 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 493
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
                        490       500       510
                 ....*....|....*....|....*....|..
gi 4502643   494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-524 1.94e-84

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 270.41  E-value: 1.94e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAK----VATAQDDITGDGTTS 94
Cdd:COG0459  11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSremDRETLIDVARTSLRTKvhAELADVLTEAV 172
Cdd:COG0459  91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD--EEIGELIAEAM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  173 vdsiLAIKKQDEpidlFMIEimemKHKS-ETDTSLIRGLVLDHGARHPD-------MKKRVEDAYILTCNVSLEyektev 244
Cdd:COG0459 166 ----EKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS------ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  245 nsgffykSAEEREKLvkaerkfiedrVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRA-------- 316
Cdd:COG0459 228 -------SIQDLLPL-----------LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgf 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  317 -KRRN--MERLTLACGGVALN-----SFDDLSPDCLGHAGLVYEytlGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIK 388
Cdd:COG0459 281 gDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERK 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  389 DAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQA 468
Cdd:COG0459 358 RRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA 436
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4502643  469 EHSESgqlVGVDLNTGEP--MVAAevGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:COG0459 437 AKDKG---FGFDAATGEYvdMLEA--GVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
10-524 6.91e-78

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 254.18  E-value: 6.91e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    10 KAEVARAQaalavNISAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:PTZ00212  19 KGETARLQ-----SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 160
Cdd:PTZ00212  94 DEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDeekfKEDLLNIARTTLSSKL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   161 HAELADVLTEAVVDSILAIKKQdepIDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   239 YEK-----TEVNSGFFYKSAEerekLVKAERKFIEDRVKKIIELKrkvCGdsdkgfVVINQKGIDPFSLDALSKEGIVAL 313
Cdd:PTZ00212 248 TDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKILAHG---CN------VFINRQLIYNYPEQLFAEAGIMAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   314 RRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRD 393
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHD 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   394 GLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSES 473
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKG 474
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4502643   474 GQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:PTZ00212 475 NKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 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 ...
3-530 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: 962.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643      3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVAT 82
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     83 AQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 160
Cdd:TIGR02347  81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    161 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 240
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    241 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 319
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    320 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 399
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    400 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 479
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 4502643    480 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 530
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
7-526 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: 935.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDD 86
Cdd:cd03342   1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   87 ITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM--DRETLIDVARTSLRTKVHAEL 164
Cdd:cd03342  81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  165 ADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEV 244
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  245 NSGFFYKsaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERL 324
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  325 TLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDD 404
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  405 GCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTG 484
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 4502643  485 EPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGM 526
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-525 0e+00

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: 589.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLY 109
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    110 ISEGLHPRIITEGFEAAKEKALQFLEEVKV--SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPID 187
Cdd:pfam00118  81 LAAGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    188 LFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFI 267
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    268 EDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHA 347
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    348 GLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKP 427
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    428 SVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHS 507
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 4502643    508 CTVIATNILLVDEIMRAG 525
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
11-523 0e+00

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: 565.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   11 AEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGD 90
Cdd:cd00309   1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   91 GTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLT 169
Cdd:cd00309  81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPiDVEDREELLKVATTSLNSKLVSGGDDFLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  170 EAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYektevnsgff 249
Cdd:cd00309 161 ELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  250 yksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACG 329
Cdd:cd00309 231 ----------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATG 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  330 GVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVP 409
Cdd:cd00309 271 ATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP 350
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  410 GAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVA 489
Cdd:cd00309 351 GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDM 430
                       490       500       510
                ....*....|....*....|....*....|....
gi 4502643  490 AEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd00309 431 KEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
19-525 1.44e-142

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: 420.90  E-value: 1.44e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:cd03343  16 AQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 176
Cdd:cd03343  96 AGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  177 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:cd03343 175 LQVAEKRDGkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSP 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  254 EEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03343 255 DQLQAFLEQEEAMLKEMVDKIADTGANV---------VFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIV 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 413
Cdd:cd03343 326 TNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGA 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  414 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 493
Cdd:cd03343 406 VEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKG 485
                       490       500       510
                ....*....|....*....|....*....|..
gi 4502643  494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:cd03343 486 VIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
thermosome_alpha NF041082
thermosome subunit alpha;
19-525 6.19e-142

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 419.29  E-value: 6.19e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041082  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:NF041082  98 AGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   178 AI--KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:NF041082 178 AVaeKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQ 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   256 REKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 335
Cdd:NF041082 258 LQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   336 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:NF041082 329 IDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   416 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 495
Cdd:NF041082 409 VELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVV 488
                        490       500       510
                 ....*....|....*....|....*....|
gi 4502643   496 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041082 489 EPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
thermosome_beta NF041083
thermosome subunit beta;
19-525 2.19e-141

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 417.81  E-value: 2.19e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:NF041083  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV--KVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 176
Cdd:NF041083  98 AGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIaeKVDPD-DRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   177 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:NF041083 177 KQVAEKRDGkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDP 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   254 EEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:NF041083 257 DQLQKFLDQEEKMLKEMVDKIKATGAN---------VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 413
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   414 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 493
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
                        490       500       510
                 ....*....|....*....|....*....|..
gi 4502643   494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
thermosome_arch TIGR02339
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
19-524 2.98e-137

thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274080  Cd Length: 519  Bit Score: 407.15  E-value: 2.98e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLI 98
Cdd:TIGR02339  17 AQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     99 IGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSREmDRETLIDVARTSLRTKVHAELA-DVLTEAVVDS 175
Cdd:TIGR02339  97 AGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEiaTKISPE-DRDLLKKIAYTSLTSKASAEVAkDKLADLVVEA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    176 ILAIKKQDE----PIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK 251
Cdd:TIGR02339 176 VKQVAELRGdgkyYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRIT 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    252 SAEEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGV 331
Cdd:TIGR02339 256 DPDQIKKFLDQEEAMLKEMVDKIASAGAN---------VVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGAR 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    332 ALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGA 411
Cdd:TIGR02339 327 IVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    412 GAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAE 491
Cdd:TIGR02339 407 GAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLE 486
                         490       500       510
                  ....*....|....*....|....*....|...
gi 4502643    492 VGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02339 487 LGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
14-521 3.50e-96

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: 301.91  E-value: 3.50e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   14 ARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTT 93
Cdd:cd03339  19 LKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTT 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   94 SNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS---REMDRETLIDVARTSLRTKVHAELADVLTE 170
Cdd:cd03339  99 GVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKiefSPDNKEPLIQTAMTSLGSKIVSRCHRQFAE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  171 AVVDSILA---IKKQDepIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYI--LTCnvSLEYEKTEVN 245
Cdd:cd03339 179 IAVDAVLSvadLERKD--VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIaiLTC--PFEPPKPKTK 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  246 SGFFYKSAEEREKLVKAERKFIEDRVKKIielkrKVCGDSdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLT 325
Cdd:cd03339 255 HKLDITSVEDYKKLQEYEQKYFREMVEQV-----KDAGAN----LVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIA 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  326 LACGGVALNSFDDLSPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAID 403
Cdd:cd03339 326 IATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIR 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  404 DGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEH-SESGQLVGVDLN 482
Cdd:cd03339 406 DNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCL 485
                       490       500       510
                ....*....|....*....|....*....|....*....
gi 4502643  483 TGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03339 486 GRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDV 524
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
23-523 1.57e-92

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: 292.27  E-value: 1.57e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03335  13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEE---VKVSrEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI 179
Cdd:cd03335  93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhlsISVD-NLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  180 KKQDE------PIDlfMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 253
Cdd:cd03335 172 KTTNEkgktkyPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDP 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  254 EEREKLVKAERKFIEDRVKKIIElkrkvCGDSdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03335 250 EKLEKIRQRESDITKERIKKILA-----AGAN----VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  334 NSFDDL------SPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCV 407
Cdd:cd03335 321 STLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  408 VPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgQL---------VG 478
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAA-QVkpdkkhlkwYG 479
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*
gi 4502643  479 VDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:cd03335 480 LDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
4-521 5.67e-92

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: 289.20  E-value: 5.67e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    4 VKTLNPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATA 83
Cdd:cd03337   4 VLNQNTKRESGR-KAQLG-NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   84 QDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHA 162
Cdd:cd03337  82 QDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  163 ELADVLTEAVVDSILAIKKQDE----PIDL-FMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSL 237
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAVEENgrkkEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  238 EYektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAK 317
Cdd:cd03337 242 EY--------------------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVR 271
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  318 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTL-GEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLR 396
Cdd:cd03337 272 KTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMA 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  397 AVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQL 476
Cdd:cd03337 352 VARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENS 431
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*.
gi 4502643  477 V-GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:cd03337 432 TwGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
8-521 1.42e-91

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: 289.72  E-value: 1.42e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643      8 NPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDI 87
Cdd:TIGR02344   8 NTKRESGR-KAQLS-NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELAD 166
Cdd:TIGR02344  86 VGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVnDDAAMLKLIQSCIGTKFVSRWSD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    167 VLTEAVVDSILAIKKQDEPIdlFMIEIMEMKhKSE-------TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEY 239
Cdd:TIGR02344 166 LMCDLALDAVRTVQRDENGR--KEIDIKRYA-KVEkipggdiEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    240 EKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRR 319
Cdd:TIGR02344 243 KKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPD---------LVITEKGVSDLAQHYLLKANITAIRRVRKT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    320 NMERLTLACGGVALNSFDDLSPDCLG-HAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAV 398
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    399 KNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHS-ESGQLV 477
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTW 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 4502643    478 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 521
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
23-523 1.53e-91

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: 290.08  E-value: 1.53e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02340  17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIK 180
Cdd:TIGR02340  97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnlSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    181 KQDE------PIDlfMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:TIGR02340 177 TTNEngetkyPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    255 EREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALN 334
Cdd:TIGR02340 255 KLEQIRQREADITKERIKKILDAGAN---------VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    335 SFDDLS------PDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVV 408
Cdd:TIGR02340 326 TLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    409 PGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgQL---------VGV 479
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAA-QLkpekkhlkwYGL 484
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 4502643    480 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 523
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
15-525 2.90e-91

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: 289.39  E-value: 2.90e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     15 RAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTS 94
Cdd:TIGR02343  24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV--KVSREMD-RETLIDVARTSLRTKVHAELADVLTEA 171
Cdd:TIGR02343 104 VVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEI 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    172 VVDSILAI-KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAY--ILTCnvSLEYEKTEVNSGF 248
Cdd:TIGR02343 184 AVDAVLNVaDMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKiaILTC--PFEPPKPKTKHKL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    249 FYKSAEEREKLVKAERKFIEDRVKKIielkRKVCGDsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLAC 328
Cdd:TIGR02343 262 DISSVEEYKKLQKYEQQKFKEMIDDI----KKSGAN-----LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIAT 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    329 GGVALNSFDDLSPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGC 406
Cdd:TIGR02343 333 GGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSR 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    407 VVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEH-SESGQLVGVDLNTGE 485
Cdd:TIGR02343 413 IVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYG 492
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 4502643    486 PMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 525
Cdd:TIGR02343 493 TNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
23-524 5.90e-88

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: 280.49  E-value: 5.90e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02345  23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKVHAELADVLTEAVVDSILA 178
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEkgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    179 IKKQDepIDLFMIEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 255
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    256 REKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 335
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANV---------VLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    336 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 415
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    416 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 495
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
                         490       500
                  ....*....|....*....|....*....
gi 4502643    496 DNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-524 1.94e-84

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 270.41  E-value: 1.94e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAK----VATAQDDITGDGTTS 94
Cdd:COG0459  11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   95 NVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE--VKVSremDRETLIDVARTSLRTKvhAELADVLTEAV 172
Cdd:COG0459  91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD--EEIGELIAEAM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  173 vdsiLAIKKQDEpidlFMIEimemKHKS-ETDTSLIRGLVLDHGARHPD-------MKKRVEDAYILTCNVSLEyektev 244
Cdd:COG0459 166 ----EKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS------ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  245 nsgffykSAEEREKLvkaerkfiedrVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRA-------- 316
Cdd:COG0459 228 -------SIQDLLPL-----------LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgf 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  317 -KRRN--MERLTLACGGVALN-----SFDDLSPDCLGHAGLVYEytlGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIK 388
Cdd:COG0459 281 gDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERK 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  389 DAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQA 468
Cdd:COG0459 358 RRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA 436
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4502643  469 EHSESgqlVGVDLNTGEP--MVAAevGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:COG0459 437 AKDKG---FGFDAATGEYvdMLEA--GVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
23-524 2.37e-84

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: 270.70  E-value: 2.37e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03340  21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKV-----SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 177
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVnidkeDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  178 AIkkqDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 254
Cdd:cd03340 181 SL---DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  255 EREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALN 334
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANV---------VLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  335 SFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAV 414
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAI 408
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  415 EVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQL-VGVDLNTGEPMVAAEVG 493
Cdd:cd03340 409 EMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAF 488
                       490       500       510
                ....*....|....*....|....*....|.
gi 4502643  494 VWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03340 489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
23-486 1.26e-83

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: 268.77  E-value: 1.26e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03338  13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 179
Cdd:cd03338  93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLnDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVid 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  180 KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARH-PDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 258
Cdd:cd03338 173 PATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  259 LVKAERKFIEDRVKKIielKRKVCGdsdkgfVVINQKGI-----DPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03338 253 ILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNP-RSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 412
Cdd:cd03338 324 ASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4502643  413 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEP 486
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
23-522 6.09e-80

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: 259.33  E-value: 6.09e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:TIGR02342  14 NIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 179
Cdd:TIGR02342  94 LGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLsDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVid 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    180 KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPD-MKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 258
Cdd:TIGR02342 174 PENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    259 LVKAERKFIEDRVKKIielKRKVCGdsdkgfVVINQKGI-----DPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:TIGR02342 254 VLKEERAYILNIVKKI---KKTGCN------VLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPR-SVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 412
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    413 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEV 492
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
                         490       500       510
                  ....*....|....*....|....*....|
gi 4502643    493 GVWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
10-524 1.42e-78

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: 255.72  E-value: 1.42e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   10 KAEVARAQA---ALAVNisaarglqDVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:cd03336  10 KGETARLSSfvgAIAIG--------DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEE----VKVSREMDRETLIDVARTSLRTKV 160
Cdd:cd03336  82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  161 HAELADVLTEAVVDSILAIKKQDepiDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGSG---NLDAIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMD 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  239 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAK 317
Cdd:cd03336 236 TDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINC---------FINRQLIYNYPEQLFADAGIMAIEHAD 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  318 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRA 397
Cdd:cd03336 307 FDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCV 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  398 VKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLV 477
Cdd:cd03336 387 LAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA 466
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*..
gi 4502643  478 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03336 467 GLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
10-524 6.91e-78

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 254.18  E-value: 6.91e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    10 KAEVARAQaalavNISAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:PTZ00212  19 KGETARLQ-----SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 160
Cdd:PTZ00212  94 DEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDeekfKEDLLNIARTTLSSKL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   161 HAELADVLTEAVVDSILAIKKQdepIDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   239 YEK-----TEVNSGFFYKSAEerekLVKAERKFIEDRVKKIIELKrkvCGdsdkgfVVINQKGIDPFSLDALSKEGIVAL 313
Cdd:PTZ00212 248 TDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKILAHG---CN------VFINRQLIYNYPEQLFAEAGIMAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   314 RRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRD 393
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHD 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   394 GLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSES 473
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKG 474
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4502643   474 GQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:PTZ00212 475 NKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
16-524 6.87e-77

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: 251.56  E-value: 6.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     16 AQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSN 95
Cdd:TIGR02346  16 LEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     96 VLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD---RETLIDVARTSLRTKVHAElADVLTEAV 172
Cdd:TIGR02346  96 LVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDlrdKDELIKALKASISSKQYGN-EDFLAQLV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    173 VDSILAIK-KQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYILTCNVSLEYEKTEVNSGFFY 250
Cdd:TIGR02346 175 AQACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    251 KSAEEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGG 330
Cdd:TIGR02346 252 HNAEELLNYSKGEENQIEAMIKAIADSGVN---------VIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    331 VALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVP 409
Cdd:TIGR02346 323 TPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLP 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    410 GAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMV- 488
Cdd:TIGR02346 403 GAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVk 482
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 4502643    489 -AAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02346 483 dASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
145-404 4.20e-72

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: 228.50  E-value: 4.20e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  145 RETLIDVARTSLRTKVhAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKR 224
Cdd:cd03333   1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  225 VEDAYILTCNVSLEYektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDA 304
Cdd:cd03333  80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  305 LSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTL 384
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
                       250       260
                ....*....|....*....|
gi 4502643  385 TQIKDAVRDGLRAVKNAIDD 404
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
23-524 3.47e-67

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: 224.41  E-value: 3.47e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGEL 102
Cdd:cd03341  13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  103 LKQADLYISEGLHPRIITEGFEAAKEKALQFLEEV---KVSREMDRETLIDVARTSLRTKVhAELADVLTEAVVDSILAI 179
Cdd:cd03341  93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELvvyKIEDLRNKEEVSKALKTAIASKQ-YGNEDFLSPLVAEACISV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  180 KKQDepIDLFMIE---IMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYI--LTCNVSleyekTEVNsgffyksa 253
Cdd:cd03341 172 LPEN--IGNFNVDnirVVKILGGSLEDSKVVRGMVF---KREPEGSvKRVKKAKVavFSCPFD-----IGVN-------- 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  254 eereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 333
Cdd:cd03341 234 ------------------------------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  334 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 412
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  413 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMV--AA 490
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAK 437
                       490       500       510
                ....*....|....*....|....*....|....
gi 4502643  491 EVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
7-524 3.70e-64

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: 217.80  E-value: 3.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643      7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQ 84
Cdd:TIGR02341   3 FKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643     85 DDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 160
Cdd:TIGR02341  83 DDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDevkfRQDLMNIARTTLSSKI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    161 HAELADVLTEAVVDSILAIKKQDepiDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 238
Cdd:TIGR02341 163 LSQHKDHFAQLAVDAVLRLKGSG---NLEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    239 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAK 317
Cdd:TIGR02341 237 TDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINC---------FINRQLIYNYPEQLFADAGVMAIEHAD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    318 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRA 397
Cdd:TIGR02341 308 FEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    398 VKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLV 477
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 4502643    478 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 524
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
203-391 1.95e-13

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: 70.33  E-value: 1.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  203 DTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKteVNSGFFYksaeeREKLVKAERKFIEDRVKKIIELKRKVc 282
Cdd:cd03334  62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLS-----LDPVILQEKEYLKNLVSRIVALRPDV- 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  283 gdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLS-PDCLGHAGLVYEYTLGEEK-- 359
Cdd:cd03334 134 --------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLtSPKLGTCESFRVRTYVEEHgr 205
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4502643  360 ---FTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAV 391
Cdd:cd03334 206 sktLMFFEGCPKELGCTILLRGGDLEELKKVKRVV 240
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
30-510 2.73e-11

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 66.09  E-value: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDG-----NVLLHEmQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLK 104
Cdd:PTZ00114  34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvakAIEFSD-RFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   105 QADLYISEGLHPRIITEGFEAAKEKALQFLEEvkVSREM-DRETLIDVARTSLRTKVhaELADVLTEAV----VDSILAI 179
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLKE--QSRPVkTKEDILNVATISANGDV--EIGSLIADAMdkvgKDGTITV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   180 kkQDEPIDLFMIEIMEmkhksetdtslirGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVNS-GFFYK 251
Cdd:PTZ00114 189 --EDGKTLEDELEVVE-------------GMSFDRGYISPyfvtnekTQKVELENPLILVTDKKISSIQSILPIlEHAVK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   252 S-------AEEREKLVKAerKFIEDRVKKIIelkrKVC-------GDSDK----------GFVVINQKG----IDPFSLD 303
Cdd:PTZ00114 254 NkrplliiAEDVEGEALQ--TLIINKLRGGL----KVCavkapgfGDNRKdilqdiavltGATVVSEDNvglkLDDFDPS 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   304 ALS------------------------KEGIVALRRAKRRNM---------ERLTLACGGVALnsfddlspdclghaglv 350
Cdd:PTZ00114 328 MLGsakkvtvtkdetviltgggdkaeiKERVELLRSQIERTTseydkeklkERLAKLSGGVAV----------------- 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   351 yeytlgeekftfiekcnnprsvtLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEAL--IKHKPS 428
Cdd:PTZ00114 391 -----------------------IKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLdkLEEDNE 446
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   429 VKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgqlVGVDLNTGEPMVAAEVGVWDNY-CVKKQLLHS 507
Cdd:PTZ00114 447 LTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPS---FGYDAQTGEYVNMFEAGIIDPTkVVRSALVDA 523

                 ...
gi 4502643   508 CTV 510
Cdd:PTZ00114 524 ASV 526
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
12-496 2.71e-09

GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239460  Cd Length: 520  Bit Score: 59.39  E-value: 2.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDI 87
Cdd:cd03344   7 EEARKALLRGVNK-----LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEevKVSREM-DRETLIDVARTSlrTKVHAELAD 166
Cdd:cd03344  82 AGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELK--KLSKPVkTKEEIAQVATIS--ANGDEEIGE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  167 VLTEavvdsilAIKK--QDEPIDLfmieimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSL 237
Cdd:cd03344 158 LIAE-------AMEKvgKDGVITV------EEGKTLETELEVVEGMQFDRGYLSPyfvtdpeKMEVELENPYILLTDKKI 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  238 EYEKTEVNSgffyksaeeREKLVKAERKFI---EDrvkkiielkrkVCGDSDKGFVVINQKGIDPfsldalskegIVALR 314
Cdd:cd03344 225 SSIQELLPI---------LELVAKAGRPLLiiaED-----------VEGEALATLVVNKLRGGLK----------VCAVK 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  315 ----RAKRRNM-ERLTLACGGVALN-----SFDDLSPDCLGHAGLVyeyTLGEEKFTFIEKCNNPRSV------------ 372
Cdd:cd03344 275 apgfGDRRKAMlEDIAILTGGTVISeelglKLEDVTLEDLGRAKKV---VVTKDDTTIIGGAGDKAAIkariaqirkqie 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643  373 -----------------------TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSv 429
Cdd:cd03344 352 ettsdydkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKAL- 429
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4502643  430 KGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQaehsESGQLVGVDLNTGE--PMVAAevGVWD 496
Cdd:cd03344 430 NGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEyvDMIEA--GIID 492
groEL PRK12851
chaperonin GroEL; Reviewed
30-522 8.84e-09

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 57.83  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHP----TASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PRK12851  23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVRE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   106 ADLYISEGLHPRIITEGFEAAKEKALQFLEevKVSREMDRETliDVART-SLRTKVHAELADVLTEAVVdsilaiKKQDE 184
Cdd:PRK12851 103 GAKAVAAGANPMDLKRGIDRAVAAVVEELK--ANARPVTTNA--EIAQVaTISANGDAEIGRLVAEAME------KVGNE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   185 PIdlfmIEIMEMKhKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYILTCNVSLEYEKTEVnsgffyksaEERE 257
Cdd:PRK12851 173 GV----ITVEESK-TAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEKKISNLQDLL---------PVLE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   258 KLVKAERKFI---EDrvkkiielkrkVCGDSDKGFVVINQKGIdpFSLDALSKEGIVALRRAKRRNMERLTlacGGVALN 334
Cdd:PRK12851 239 AVVQSGKPLLiiaED-----------VEGEALATLVVNKLRGG--LKVAAVKAPGFGDRRKAMLEDIAILT---GGTVIS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   335 -----SFDDLSPDCLGHAGLVyeyTLGEEKFTF--------------------IEKCNNP--------RSVTL-----LI 376
Cdd:PRK12851 303 edlgiKLENVTLEQLGRAKKV---VVEKENTTIidgagskteiegrvaqiraqIEETTSDydreklqeRLAKLaggvaVI 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   377 K--GPNKHTLTQIKDAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKpSVKGRAQLGVQAFADALLIIPKVLAQN 454
Cdd:PRK12851 380 RvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLE-TANGDQRTGVEIVRRALEAPVRQIAEN 457
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4502643   455 SGFDLQETLVKIqAEHSESgqlVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIM 522
Cdd:PRK12851 458 AGAEGSVVVGKL-REKPGG---YGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
PRK14104 PRK14104
chaperonin GroEL; Provisional
30-524 2.69e-08

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 56.58  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQI----QHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQ 105
Cdd:PRK14104  23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   106 ADLYISEGLHPRIITEGFEAAKEKALQFLeeVKVSREM-DRETLIDVARTSLR--TKVHAELADVLTEAVVDSILAIkkq 182
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADL--VKNSKKVtSNDEIAQVGTISANgdAEIGKFLADAMKKVGNEGVITV--- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   183 depidlfmieimEMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYIL-------TCNVSLEYEKTEVNSGF 248
Cdd:PRK14104 178 ------------EEAKSLETELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYILinekklsSLNELLPLLEAVVQTGK 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   249 -FYKSAEEREKlvKAERKFIEDRVK---KIIELKRKVCGDSDKGFV--VINQKGIDPFSLD---ALSKEGIVALRRAKRR 319
Cdd:PRK14104 246 pLVIVAEDVEG--EALATLVVNRLRgglKVAAVKAPGFGDRRKAMLqdIAILTGGQAISEDlgiKLENVTLQMLGRAKKV 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   320 --NMERLTLACGGvalNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIK--GPNKHTLTQIKDAVRDGL 395
Cdd:PRK14104 324 miDKENTTIVNGA---GKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKERKDRVDDAM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   396 RAVKNAIDDGcVVPGAGAVEVAMAEALiKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgq 475
Cdd:PRK14104 401 HATRAAVEEG-IVPGGGVALLRASEQL-KGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYS-- 476
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 4502643   476 lVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATnILLVDEIMRA 524
Cdd:PRK14104 477 -YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAA-LLITTEAMVA 523
groEL PRK12852
chaperonin GroEL; Reviewed
14-231 6.39e-07

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 52.15  E-value: 6.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    14 ARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQI----QHPTASLIAKVATAQDDITG 89
Cdd:PRK12852  12 ARDRMLRGVDI-----LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    90 DGTTSNVLIIGELLKQADLYISEGLHPriitegfeaakekalqfleevkvsreMDRETLIDVARTSLRTKVHAELADVLT 169
Cdd:PRK12852  87 DGTTTATVLAQAIVREGAKAVAAGMNP--------------------------MDLKRGIDIAVAAVVKDIEKRAKPVAS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   170 EAVVDSILAIKKQ-DEPIDLFMIEIM-----------EMKHKSETDTSLIRGLVLDHGARHP-------DMKKRVEDAYI 230
Cdd:PRK12852 141 SAEIAQVGTISANgDAAIGKMIAQAMqkvgnegvitvEENKSLETEVDIVEGMKFDRGYLSPyfvtnaeKMTVELDDAYI 220

                 .
gi 4502643   231 L 231
Cdd:PRK12852 221 L 221
groEL PRK12850
chaperonin GroEL; Reviewed
12-231 2.37e-06

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 50.10  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHP----TASLIAKVATAQDDI 87
Cdd:PRK12850  10 TDARDRLLRGVNI-----LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    88 TGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQfleevkvsremdretliDVARTSLRTKVHAELADV 167
Cdd:PRK12850  85 AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVD-----------------ELKKIAKKVTSSKEIAQV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643   168 LTEAVVDsilaikkqDEPIDLFMIEIMEMKHKS-----------ETDTSLIRGLVLDHGARHPDM-----KKRV--EDAY 229
Cdd:PRK12850 148 ATISANG--------DESIGEMIAEAMDKVGKEgvitveeaktlGTELDVVEGMQFDRGYLSPYFvtnpeKMRAelEDPY 219

                 ..
gi 4502643   230 IL 231
Cdd:PRK12850 220 IL 221
groEL CHL00093
chaperonin GroEL
38-134 6.67e-04

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 42.40  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    38 LGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQ----IQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEG 113
Cdd:CHL00093  30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
                         90       100
                 ....*....|....*....|.
gi 4502643   114 LHPRIITEGFeaakEKALQFL 134
Cdd:CHL00093 110 ANPISLKRGI----EKATQYV 126
groEL PRK00013
chaperonin GroEL; Reviewed
12-136 4.45e-03

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 39.72  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502643    12 EVARAQAALAVNIsaargLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPT----ASLIAKVATAQDDI 87
Cdd:PRK00013   9 EDARRKLLRGVNK-----LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDV 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4502643    88 TGDG-TTSNVL---IIGELLKqadlYISEGLHPRIITEGFEAAKEKALQFLEE 136
Cdd:PRK00013  84 AGDGtTTATVLaqaIVREGLK----NVAAGANPMDLKRGIDKAVEAAVEELKK 132
 
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.
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