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Conserved domains on  [gi|58331171|ref|NP_001009186|]
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T-complex protein 1 subunit zeta isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

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

T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


The actual alignment was detected with superfamily member TIGR02347:

Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 857.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171     3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM--------------- 67
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMqiqhptasmiaraat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ------------------------------GLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 115
Cdd:TIGR02347  81 aqdditgdgttstvlligellkqaeryileGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   116 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 195
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   196 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   275 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 354
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   355 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 434
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 58331171   435 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 485
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
 
Name Accession Description Interval E-value
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
3-485 0e+00

T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 857.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171     3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM--------------- 67
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMqiqhptasmiaraat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ------------------------------GLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 115
Cdd:TIGR02347  81 aqdditgdgttstvlligellkqaeryileGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   116 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 195
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   196 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   275 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 354
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   355 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 434
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 58331171   435 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 485
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
7-481 0e+00

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458 [Multi-domain]  Cd Length: 484  Bit Score: 819.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------- 67
Cdd:cd03342   1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMqiqhptasmiaraataqdd 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 --------------------------GLHPRIITEGFEAAKEKALQFLEEVKVSREM--DRETLIDVARTSLRTKVHAEL 119
Cdd:cd03342  81 itgdgttsnvlligellkqaeryiqeGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 120 ADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEV 199
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 NSGFFYKsaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERL 279
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 280 TLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDD 359
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 360 GCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTG 439
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 58331171 440 EPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGM 481
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-480 2.29e-178

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: 509.05  E-value: 2.29e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------------------ 67
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELeiqhpaakllveaakaqdeevgdgtttvvvlagelleeaekl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ---GLHPRIITEGFEAAKEKALQFLEEVKV--SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPID 142
Cdd:pfam00118  81 laaGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   143 LFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFI 222
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   223 EDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHA 302
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   303 GLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKP 382
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   383 SVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHS 462
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 58331171   463 CTVIATNILLVDEIMRAG 480
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
thermosome_alpha NF041082
thermosome subunit alpha;
19-480 6.37e-114

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 345.72  E-value: 6.37e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:NF041082  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMdiehpaakmivevaktqddevgdgtttavvl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   68 --------------GLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 132
Cdd:NF041082  98 agellkkaeelldqDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  133 AI--KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 210
Cdd:NF041082 178 AVaeKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQ 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  211 REKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 290
Cdd:NF041082 258 LQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  291 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 370
Cdd:NF041082 329 IDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  371 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 450
Cdd:NF041082 409 VELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVV 488
                        490       500       510
                 ....*....|....*....|....*....|
gi 58331171  451 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041082 489 EPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
thermosome_beta NF041083
thermosome subunit beta;
19-480 7.96e-114

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 345.40  E-value: 7.96e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:NF041083  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMdvqhpaakmlvevaktqddevgdgtttavvl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   68 --------------GLHPRIITEGFEAAKEKALQFLEEV--KVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 131
Cdd:NF041083  98 agellkkaeelldqNIHPTIIANGYRLAAEKAIEILDEIaeKVDPD-DRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  132 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 208
Cdd:NF041083 177 KQVAEKRDGkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDP 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  209 EEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 288
Cdd:NF041083 257 DQLQKFLDQEEKMLKEMVDKIKATGAN---------VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  289 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 368
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  369 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 448
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
                        490       500       510
                 ....*....|....*....|....*....|..
gi 58331171  449 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-479 5.44e-62

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 209.93  E-value: 5.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:COG0459  11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIeledpfenmgaqlvkevasktndeagdgttt 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 ------------------GLHPRIITEGFEAAKEKALQFLEE--VKVSremDRETLIDVARTSLRTKvhAELADVLTEAV 127
Cdd:COG0459  91 atvlagallkeglklvaaGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD--EEIGELIAEAM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 128 vdsiLAIKKQDEpidlFMIEimemKHKS-ETDTSLIRGLVLDHGARHPD-------MKKRVEDAYILTCNVSLEyektev 199
Cdd:COG0459 166 ----EKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS------ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 nsgffykSAEEREKLvkaerkfiedrVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRA-------- 271
Cdd:COG0459 228 -------SIQDLLPL-----------LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgf 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 272 -KRRN--MERLTLACGGVALN-----SFDDLSPDCLGHAGLVYEytlGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIK 343
Cdd:COG0459 281 gDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERK 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 344 DAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQA 423
Cdd:COG0459 358 RRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA 436
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 58331171 424 EHSESgqlVGVDLNTGEP--MVAAevGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:COG0459 437 AKDKG---FGFDAATGEYvdMLEA--GVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
10-479 2.87e-57

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 198.33  E-value: 2.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   10 KAEVARAQaalavNISAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLHEMGL--------------- 69
Cdd:PTZ00212  19 KGETARLQ-----SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLdnpaakilvdisktq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   70 ------------------------------HPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 115
Cdd:PTZ00212  94 deevgdgttsvvvlagellreaeklldqkiHPQTIIEGWRMALDVARKALEEIAFDHGSDeekfKEDLLNIARTTLSSKL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  116 HAELADVLTEAVVDSILAIKKQdepIDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 193
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  194 YEK-----TEVNSGFFYKSAEerekLVKAERKFIEDRVKKIIELKrkvCGdsdkgfVVINQKGIDPFSLDALSKEGIVAL 268
Cdd:PTZ00212 248 TDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKILAHG---CN------VFINRQLIYNYPEQLFAEAGIMAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  269 RRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRD 348
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHD 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  349 GLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSES 428
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKG 474
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 58331171  429 GQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
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 ...
3-485 0e+00

T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 857.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171     3 AVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM--------------- 67
Cdd:TIGR02347   1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMqiqhptasmiaraat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ------------------------------GLHPRIITEGFEAAKEKALQFLEEVKVSRE--MDRETLIDVARTSLRTKV 115
Cdd:TIGR02347  81 aqdditgdgttstvlligellkqaeryileGVHPRIITEGFEIARKEALQFLDKFKVKKEdeVDREFLLNVARTSLRTKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   116 HAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYE 195
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   196 KTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDS-DKGFVVINQKGIDPFSLDALSKEGIVALRRAKRR 274
Cdd:TIGR02347 241 KTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSpDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   275 NMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVK 354
Cdd:TIGR02347 321 NMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   355 NAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGV 434
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 58331171   435 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK 485
Cdd:TIGR02347 481 DLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
7-481 0e+00

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458 [Multi-domain]  Cd Length: 484  Bit Score: 819.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------- 67
Cdd:cd03342   1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMqiqhptasmiaraataqdd 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 --------------------------GLHPRIITEGFEAAKEKALQFLEEVKVSREM--DRETLIDVARTSLRTKVHAEL 119
Cdd:cd03342  81 itgdgttsnvlligellkqaeryiqeGVHPRIITEGFELAKNKALKFLESFKVPVEIdtDRELLLSVARTSLRTKLHADL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 120 ADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEV 199
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 NSGFFYKsaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERL 279
Cdd:cd03342 241 NSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERL 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 280 TLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDD 359
Cdd:cd03342 283 TLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 360 GCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTG 439
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 58331171 440 EPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGM 481
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
30-480 2.29e-178

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: 509.05  E-value: 2.29e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    30 LQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------------------ 67
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELeiqhpaakllveaakaqdeevgdgtttvvvlagelleeaekl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ---GLHPRIITEGFEAAKEKALQFLEEVKV--SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPID 142
Cdd:pfam00118  81 laaGVHPTTIIEGYEKALEKALEILDSIISipVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   143 LFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFI 222
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   223 EDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHA 302
Cdd:pfam00118 241 LEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   303 GLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKP 382
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   383 SVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHS 462
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 58331171   463 CTVIATNILLVDEIMRAG 480
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
11-478 2.64e-167

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: 480.00  E-value: 2.64e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  11 AEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM----------------------- 67
Cdd:cd00309   1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIevehpaakllvevaksqddevgd 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 ----------------------GLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLT 124
Cdd:cd00309  81 gtttvvvlagellkeaekllaaGIHPTEIIRGYEKAVEKALEILKEIAVPiDVEDREELLKVATTSLNSKLVSGGDDFLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 125 EAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYektevnsgff 204
Cdd:cd00309 161 ELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY---------- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 205 yksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACG 284
Cdd:cd00309 231 ----------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATG 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 285 GVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVP 364
Cdd:cd00309 271 ATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP 350
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 365 GAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVA 444
Cdd:cd00309 351 GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDM 430
                       490       500       510
                ....*....|....*....|....*....|....
gi 58331171 445 AEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 478
Cdd:cd00309 431 KEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
19-480 5.73e-115

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: 348.48  E-value: 5.73e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:cd03343  16 AQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMdiehpaakmlvevaktqdeevgdgtttavvl 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 --------------GLHPRIITEGFEAAKEKALQFLEE--VKVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 131
Cdd:cd03343  96 agellekaedlldqNIHPTVIIEGYRLAAEKALELLDEiaIKVDPD-DKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 132 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 208
Cdd:cd03343 175 LQVAEKRDGkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSP 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 EEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 288
Cdd:cd03343 255 DQLQAFLEQEEAMLKEMVDKIADTGANV---------VFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIV 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 368
Cdd:cd03343 326 TNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGA 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 369 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 448
Cdd:cd03343 406 VEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKG 485
                       490       500       510
                ....*....|....*....|....*....|..
gi 58331171 449 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:cd03343 486 VIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
thermosome_alpha NF041082
thermosome subunit alpha;
19-480 6.37e-114

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 345.72  E-value: 6.37e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:NF041082  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMdiehpaakmivevaktqddevgdgtttavvl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   68 --------------GLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 132
Cdd:NF041082  98 agellkkaeelldqDIHPTIIAEGYRLAAEKALEILDEIAIKvDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  133 AI--KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 210
Cdd:NF041082 178 AVaeKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQ 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  211 REKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 290
Cdd:NF041082 258 LQAFLDQEEKMLKEMVDKIADSGAN---------VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  291 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 370
Cdd:NF041082 329 IDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  371 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 450
Cdd:NF041082 409 VELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVV 488
                        490       500       510
                 ....*....|....*....|....*....|
gi 58331171  451 DNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041082 489 EPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
thermosome_beta NF041083
thermosome subunit beta;
19-480 7.96e-114

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 345.40  E-value: 7.96e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:NF041083  18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMdvqhpaakmlvevaktqddevgdgtttavvl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   68 --------------GLHPRIITEGFEAAKEKALQFLEEV--KVSREmDRETLIDVARTSLRTKVHAELADVLTEAVVDSI 131
Cdd:NF041083  98 agellkkaeelldqNIHPTIIANGYRLAAEKAIEILDEIaeKVDPD-DRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  132 LAIKKQDEP---IDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 208
Cdd:NF041083 177 KQVAEKRDGkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDP 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  209 EEREKLVKAERKFIEDRVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 288
Cdd:NF041083 257 DQLQKFLDQEEKMLKEMVDKIKATGAN---------VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIV 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  289 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGA 368
Cdd:NF041083 328 TNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGA 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  369 VEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVG 448
Cdd:NF041083 408 PEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELG 487
                        490       500       510
                 ....*....|....*....|....*....|..
gi 58331171  449 VWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:NF041083 488 VIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
14-476 1.32e-74

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: 244.13  E-value: 1.32e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  14 ARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM-------------------------- 67
Cdd:cd03339  19 LKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMdvdhqiakllvelsksqddeigdgtt 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 -------------------GLHPRIITEGFEAAKEKALQFLEEVKVS---REMDRETLIDVARTSLRTKVHAELADVLTE 125
Cdd:cd03339  99 gvvvlagalleqaeklldrGIHPIRIADGYEQACKIAVEHLEEIADKiefSPDNKEPLIQTAMTSLGSKIVSRCHRQFAE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 126 AVVDSILA---IKKQDepIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYI--LTCnvSLEYEKTEVN 200
Cdd:cd03339 179 IAVDAVLSvadLERKD--VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIaiLTC--PFEPPKPKTK 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 201 SGFFYKSAEEREKLVKAERKFIEDRVKKIielkrKVCGDSdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLT 280
Cdd:cd03339 255 HKLDITSVEDYKKLQEYEQKYFREMVEQV-----KDAGAN----LVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIA 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 281 LACGGVALNSFDDLSPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAID 358
Cdd:cd03339 326 IATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIR 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 359 DGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEH-SESGQLVGVDLN 437
Cdd:cd03339 406 DNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCL 485
                       490       500       510
                ....*....|....*....|....*....|....*....
gi 58331171 438 TGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 476
Cdd:cd03339 486 GRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDV 524
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
100-359 1.67e-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: 228.12  E-value: 1.67e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 100 RETLIDVARTSLRTKVhAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKR 179
Cdd:cd03333   1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 180 VEDAYILTCNVSLEYektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDA 259
Cdd:cd03333  80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 260 LSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTL 339
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
                       250       260
                ....*....|....*....|
gi 58331171 340 TQIKDAVRDGLRAVKNAIDD 359
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
15-480 1.41e-69

T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274084 [Multi-domain]  Cd Length: 532  Bit Score: 231.23  E-value: 1.41e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    15 RAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM--------------------------- 67
Cdd:TIGR02343  24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMdvdnqiaklmvelsksqddeigdgttg 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ------------------GLHPRIITEGFEAAKEKALQFLEEV--KVSREMD-RETLIDVARTSLRTKVHAELADVLTEA 126
Cdd:TIGR02343 104 vvvlagalleqaeelldkGIHPIKIADGFEEAARIAVEHLEEIsdEISADNNnREPLIQAAKTSLGSKIVSKCHRRFAEI 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   127 VVDSILAI-KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAY--ILTCnvSLEYEKTEVNSGF 203
Cdd:TIGR02343 184 AVDAVLNVaDMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKiaILTC--PFEPPKPKTKHKL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   204 FYKSAEEREKLVKAERKFIEDRVKKIielkRKVCGDsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLAC 283
Cdd:TIGR02343 262 DISSVEEYKKLQKYEQQKFKEMIDDI----KKSGAN-----LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIAT 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   284 GGVALNSFDDLSPDCLGHAGLVYEYTLG--EEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGC 361
Cdd:TIGR02343 333 GGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSR 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   362 VVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEH-SESGQLVGVDLNTGE 440
Cdd:TIGR02343 413 IVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYG 492
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 58331171   441 PMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG 480
Cdd:TIGR02343 493 TNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
8-476 1.87e-69

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: 230.39  E-value: 1.87e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171     8 NPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMGL------------------ 69
Cdd:TIGR02344   8 NTKRESGR-KAQLS-NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVahpaaksmielsrtqdee 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    70 ---------------------------HPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELAD 121
Cdd:TIGR02344  86 vgdgttsviilagemlsvaepfleqniHPTVIIRAYRKALDDALSVLEEISIPVDVnDDAAMLKLIQSCIGTKFVSRWSD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   122 VLTEAVVDSILAIKKQDEPIdlFMIEIMEMKhKSE-------TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEY 194
Cdd:TIGR02344 166 LMCDLALDAVRTVQRDENGR--KEIDIKRYA-KVEkipggdiEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   195 EKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRR 274
Cdd:TIGR02344 243 KKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDL---------VITEKGVSDLAQHYLLKANITAIRRVRKT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   275 NMERLTLACGGVALNSFDDLSPDCLG-HAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAV 353
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   354 KNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHS-ESGQLV 432
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTW 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 58331171   433 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 476
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
23-478 5.66e-69

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: 229.48  E-value: 5.66e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLL---------------------HEMG------------- 68
Cdd:cd03335  13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILkllevehpaakilvelaqlqdKEVGdgttsvviiaael 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  69 -----------LHPRIITEGFEAAKEKALQFLEE---VKVSrEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI 134
Cdd:cd03335  93 lkranelvkqkIHPTTIISGYRLACKEAVKYIKEhlsISVD-NLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 135 KKQDE------PIDlfMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSA 208
Cdd:cd03335 172 KTTNEkgktkyPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDP 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 EEREKLVKAERKFIEDRVKKIIElkrkvCGDSdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 288
Cdd:cd03335 250 EKLEKIRQRESDITKERIKKILA-----AGAN----VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSFDDL------SPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCV 362
Cdd:cd03335 321 STLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 363 VPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgQL---------VG 433
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAA-QVkpdkkhlkwYG 479
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*
gi 58331171 434 VDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 478
Cdd:cd03335 480 LDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
4-476 8.20e-69

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: 227.56  E-value: 8.20e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   4 VKTLNPKAEVARaQAALAvNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM---------------- 67
Cdd:cd03337   4 VLNQNTKRESGR-KAQLG-NIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIdvahpaaksmielsrt 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 -----------------------------GLHPRIITEGFEAAKEKALQFLEEVKVS-REMDRETLIDVARTSLRTKVHA 117
Cdd:cd03337  82 qdeevgdgttsviilageilavaepflerGIHPTVIIKAYRKALEDALKILEEISIPvDVNDRAQMLKIIKSCIGTKFVS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 118 ELADVLTEAVVDSILAIKKQDE----PIDL-FMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSL 192
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAVEENgrkkEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 193 EYektevnsgffyksaeereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAK 272
Cdd:cd03337 242 EY--------------------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVR 271
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 273 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTL-GEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLR 351
Cdd:cd03337 272 KTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMA 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 352 AVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQL 431
Cdd:cd03337 352 VARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENS 431
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*.
gi 58331171 432 V-GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEI 476
Cdd:cd03337 432 TwGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
23-478 8.97e-68

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: 226.53  E-value: 8.97e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLL---------------------HEMG------------- 68
Cdd:TIGR02340  17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILkllevehpaakilvelaqlqdREVGdgttsvviiaael 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    69 -----------LHPRIITEGFEAAKEKALQFLEE--VKVSREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIK 135
Cdd:TIGR02340  97 lkradelvknkIHPTSVISGYRLACKEAVKYIKEnlSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   136 KQDE------PIDlfMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 209
Cdd:TIGR02340 177 TTNEngetkyPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   210 EREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALN 289
Cdd:TIGR02340 255 KLEQIRQREADITKERIKKILDAGANV---------VLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   290 SFDDLS------PDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVV 363
Cdd:TIGR02340 326 TLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   364 PGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESgQL---------VGV 434
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAA-QLkpekkhlkwYGL 484
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 58331171   435 DLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR 478
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
23-479 1.61e-63

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: 214.62  E-value: 1.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM----------------------------------- 67
Cdd:TIGR02345  23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLdivhpaaktlvdiaksqdaevgdgttsvtilagel 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    68 ----------GLHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKVHAELADVLTEAVVDSILA 133
Cdd:TIGR02345 103 lkeakpfieeGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEkgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   134 IKKQDepIDLFMIEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEE 210
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   211 REKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNS 290
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANV---------VLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   291 FDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVE 370
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   371 VAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVW 450
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
                         490       500
                  ....*....|....*....|....*....
gi 58331171   451 DNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
23-441 1.94e-62

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: 211.76  E-value: 1.94e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM----------------------------------- 67
Cdd:cd03338  13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMsvlhpaakmlvelskaqdieagdgttsvvvlagal 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 ----------GLHPRIITEGFEAAKEKALQFLEEVKVSREM-DRETLIDVARTSLRTKVHAELADVLTEAVVDSILAI-- 134
Cdd:cd03338  93 lsacesllkkGIHPTVISESFQIAAKKAVEILDSMSIPVDLnDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVid 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 135 KKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARH-PDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREK 213
Cdd:cd03338 173 PATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 214 LVKAERKFIEDRVKKIielKRKVCGdsdkgfVVINQKGI-----DPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 288
Cdd:cd03338 253 ILREERKYILNMCKKI---KKSGCN------VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNP-RSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 367
Cdd:cd03338 324 ASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58331171 368 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEP 441
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-479 5.44e-62

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 209.93  E-value: 5.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  19 ALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEM------------------------------- 67
Cdd:COG0459  11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIeledpfenmgaqlvkevasktndeagdgttt 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  68 ------------------GLHPRIITEGFEAAKEKALQFLEE--VKVSremDRETLIDVARTSLRTKvhAELADVLTEAV 127
Cdd:COG0459  91 atvlagallkeglklvaaGANPTDIKRGIDKAVEKAVEELKKiaKPVD---DKEELAQVATISANGD--EEIGELIAEAM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 128 vdsiLAIKKQDEpidlFMIEimemKHKS-ETDTSLIRGLVLDHGARHPD-------MKKRVEDAYILTCNVSLEyektev 199
Cdd:COG0459 166 ----EKVGKDGV----ITVE----EGKGlETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS------ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 200 nsgffykSAEEREKLvkaerkfiedrVKKIIELKRKvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRA-------- 271
Cdd:COG0459 228 -------SIQDLLPL-----------LEKVAQSGKP---------LLIIAEDIDGEALATLVVNGIRGVLRVvavkapgf 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 272 -KRRN--MERLTLACGGVALN-----SFDDLSPDCLGHAGLVYEytlGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIK 343
Cdd:COG0459 281 gDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERK 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 344 DAVRDGLRAVKNAIDDGcVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQA 423
Cdd:COG0459 358 RRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA 436
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 58331171 424 EHSESgqlVGVDLNTGEP--MVAAevGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:COG0459 437 AKDKG---FGFDAATGEYvdMLEA--GVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
10-479 2.50e-59

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: 203.33  E-value: 2.50e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  10 KAEVARAQA---ALAVNisaarglqDVLRTNLGPKGTMKMLVSG--AGDIKLTKDGNVLL-------------------- 64
Cdd:cd03336  10 KGETARLSSfvgAIAIG--------DLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILksigvdnpaakvlvdiskvq 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  65 -HEMG------------------------LHPRIITEGFEAAKEKALQFLEE----VKVSREMDRETLIDVARTSLRTKV 115
Cdd:cd03336  82 dDEVGdgttsvtvlaaellreaeklvaqkIHPQTIIEGYRMATAAAREALLSsavdHSSDEEAFREDLLNIARTTLSSKI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 116 HAELADVLTEAVVDSILAIKKQDepiDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 193
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGSG---NLDAIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMD 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 194 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAK 272
Cdd:cd03336 236 TDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINC---------FINRQLIYNYPEQLFADAGIMAIEHAD 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 273 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRA 352
Cdd:cd03336 307 FDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCV 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 353 VKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLV 432
Cdd:cd03336 387 LAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA 466
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*..
gi 58331171 433 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:cd03336 467 GLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
23-479 1.16e-58

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: 201.75  E-value: 1.16e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLL------H------------------------------- 65
Cdd:cd03340  21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILklldivHpaaktlvdiaksqdaevgdgttsvvvlagef 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  66 --------EMGLHPRIITEGFEAAKEKALQFLEEVKV-----SREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSIL 132
Cdd:cd03340 101 lkeakpfiEDGVHPQIIIRGYRKALQLAIEKIKEIAVnidkeDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 133 AIkkqDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHG---ARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAE 209
Cdd:cd03340 181 SL---DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 210 EREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALN 289
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANV---------VLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 290 SFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAV 369
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAI 408
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 370 EVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQL-VGVDLNTGEPMVAAEVG 448
Cdd:cd03340 409 EMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAF 488
                       490       500       510
                ....*....|....*....|....*....|.
gi 58331171 449 VWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:cd03340 489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
10-479 2.87e-57

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 198.33  E-value: 2.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   10 KAEVARAQaalavNISAARGLQDVLRTNLGPKGTMKMLVS-----GAGDIKLTKDGNVLLHEMGL--------------- 69
Cdd:PTZ00212  19 KGETARLQ-----SFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLdnpaakilvdisktq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   70 ------------------------------HPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 115
Cdd:PTZ00212  94 deevgdgttsvvvlagellreaeklldqkiHPQTIIEGWRMALDVARKALEEIAFDHGSDeekfKEDLLNIARTTLSSKL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  116 HAELADVLTEAVVDSILAIKKQdepIDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 193
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGS---GNLDYIQIIKKPGGTLRDSYLEDGFILEKkiGVGQP---KRLENCKILVANTPMD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  194 YEK-----TEVNSGFFYKSAEerekLVKAERKFIEDRVKKIIELKrkvCGdsdkgfVVINQKGIDPFSLDALSKEGIVAL 268
Cdd:PTZ00212 248 TDKikiygAKVKVDSMEKVAE----IEAAEKEKMKNKVDKILAHG---CN------VFINRQLIYNYPEQLFAEAGIMAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  269 RRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRD 348
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHD 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  349 GLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSES 428
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKG 474
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 58331171  429 GQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
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 ...
16-479 1.87e-56

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: 196.09  E-value: 1.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    16 AQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHE----------------------------- 66
Cdd:TIGR02346  16 LEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRElevqhpaakllvmasemqeneigdgtnlv 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    67 ----------------MGLHPRIITEGFEAAKEKALQFLEEVKVSREMD---RETLIDVARTSLRTKVHAElADVLTEAV 127
Cdd:TIGR02346  96 lvlagellnkaeelirMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDlrdKDELIKALKASISSKQYGN-EDFLAQLV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   128 VDSILAIK-KQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYILTCNVSLEYEKTEVNSGFFY 205
Cdd:TIGR02346 175 AQACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   206 KSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGG 285
Cdd:TIGR02346 252 HNAEELLNYSKGEENQIEAMIKAIADSGVNV---------IVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   286 VALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVP 364
Cdd:TIGR02346 323 TPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLP 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   365 GAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMV- 443
Cdd:TIGR02346 403 GAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGVk 482
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 58331171   444 -AAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:TIGR02346 483 dASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
23-479 1.83e-48

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: 173.18  E-value: 1.83e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  23 NISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHE------------------------------------ 66
Cdd:cd03341  13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRElevqhpaakllvmasqmqeeeigdgtnlvvvlagel 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171  67 ---------MGLHPRIITEGFEAAKEKALQFLEEV---KVSREMDRETLIDVARTSLRTKVhAELADVLTEAVVDSILAI 134
Cdd:cd03341  93 lekaeellrMGLHPSEIIEGYEKALKKALEILEELvvyKIEDLRNKEEVSKALKTAIASKQ-YGNEDFLSPLVAEACISV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 135 KKQDepIDLFMIE---IMEMKHKSETDTSLIRGLVLdhgARHPDMK-KRVEDAYI--LTCNVSleyekTEVNsgffyksa 208
Cdd:cd03341 172 LPEN--IGNFNVDnirVVKILGGSLEDSKVVRGMVF---KREPEGSvKRVKKAKVavFSCPFD-----IGVN-------- 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 209 eereklvkaerkfiedrvkkiielkrkvcgdsdkgfVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVAL 288
Cdd:cd03341 234 ------------------------------------VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 289 NSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSV-TLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG 367
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 368 AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMV--AA 445
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGTkdAK 437
                       490       500       510
                ....*....|....*....|....*....|....
gi 58331171 446 EVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
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 ...
7-479 2.22e-46

T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274082  Cd Length: 519  Bit Score: 168.50  E-value: 2.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171     7 LNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA--GDIKLTKDGNVLL-------------------- 64
Cdd:TIGR02341   3 FKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILksigvdnpaakvlvdmskvq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171    65 -HEMG------------------------LHPRIITEGFEAAKEKALQFLEEVKVSREMD----RETLIDVARTSLRTKV 115
Cdd:TIGR02341  83 dDEVGdgttsvtvlaaellreaeklinqkIHPQTIIAGYREATKAARDALLKSAVDNGSDevkfRQDLMNIARTTLSSKI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   116 HAELADVLTEAVVDSILAIKKQDepiDLFMIEIMEMKHKSETDTSLIRGLVLDH--GARHPdmkKRVEDAYILTCNVSLE 193
Cdd:TIGR02341 163 LSQHKDHFAQLAVDAVLRLKGSG---NLEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   194 YEKTEV-NSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVcgdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAK 272
Cdd:TIGR02341 237 TDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINC---------FINRQLIYNYPEQLFADAGVMAIEHAD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   273 RRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRA 352
Cdd:TIGR02341 308 FEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171   353 VKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLV 432
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 58331171   433 GVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRA 479
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
158-346 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 58331171 158 DTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKteVNSGFFYksaeeREKLVKAERKFIEDRVKKIIELKRKVc 237
Cdd:cd03334  62 DSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR--VENKLLS-----LDPVILQEKEYLKNLVSRIVALRPDV- 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331171 238 gdsdkgfvVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLS-PDCLGHAGLVYEYTLGEEK-- 314
Cdd:cd03334 134 --------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLtSPKLGTCESFRVRTYVEEHgr 205
                       170       180       190
                ....*....|....*....|....*....|....*
gi 58331171 315 ---FTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAV 346
Cdd:cd03334 206 sktLMFFEGCPKELGCTILLRGGDLEELKKVKRVV 240
 
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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