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Conserved domains on  [gi|33414505|ref|NP_877966|]
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T-complex protein 1 subunit delta [Rattus norvegicus]

Protein Classification

T-complex protein 1 subunit delta( domain architecture ID 10129587)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
25-538 0e+00

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: 980.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:cd03338   1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03338  81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANS--GITRVEKAKIGLIQFCLSAPKTDMDN 262
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 263 QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGT 342
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 343 KPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISN 502
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
                       490       500       510
                ....*....|....*....|....*....|....*.
gi 33414505 503 ILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNT 538
Cdd:cd03338 480 ILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
 
Name Accession Description Interval E-value
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
25-538 0e+00

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: 980.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:cd03338   1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03338  81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANS--GITRVEKAKIGLIQFCLSAPKTDMDN 262
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 263 QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGT 342
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 343 KPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISN 502
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
                       490       500       510
                ....*....|....*....|....*....|....*.
gi 33414505 503 ILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNT 538
Cdd:cd03338 480 ILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
24-539 0e+00

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


Pssm-ID: 274083  Cd Length: 517  Bit Score: 923.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    24 YQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAG 103
Cdd:TIGR02342   1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   104 DGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLL 183
Cdd:TIGR02342  81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   184 SPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKV--ANSGITRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02342 161 APLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKAskSAGGPTRIEKAKIGLIQFQISPPKTDME 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   342 TKPVAHIDQFTPDMLGSAELAEEVSLNGsGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDG-GKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGIS 501
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGIT 479
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 33414505   502 NILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
44-539 0e+00

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 562.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKL 123
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   124 LQKGIHPTIISESFQKALEKGLEILTDM-SRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVidPATATS 202
Cdd:pfam00118  81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   203 VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERA 281
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   282 YILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAEL 361
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   362 AEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSR 441
Cdd:pfam00118 314 VEEEKI-GDEKYTFIEGCKSP-KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   442 TLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTL 521
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 33414505   522 ATETVRSILKIDDVVNTR 539
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
thermosome_alpha NF041082
thermosome subunit alpha;
36-536 0e+00

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 550.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:NF041082  21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  196 DPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:NF041082 181 EKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMpKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:NF041082 261 FLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  355 MLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:NF041082 336 DLGYAGLVEERKVGGDKMIF-VEGCKNP-KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
                        490       500
                 ....*....|....*....|..
gi 33414505  515 SVSALTLATETVRSILKIDDVV 536
Cdd:NF041082 494 KTQAIKSATEAAVMILRIDDVI 515
thermosome_beta NF041083
thermosome subunit beta;
22-539 0e+00

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 521.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   22 GAYQDRDKPAQirFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIE 101
Cdd:NF041083   9 GTQRTKGRDAQ--RNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSS 181
Cdd:NF041083  87 VGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  182 LLSPMSVNAVMKVIDPATAT-SVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTD 259
Cdd:NF041083 167 YLAEIAVKAVKQVAEKRDGKyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  260 MDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKT 339
Cdd:NF041083 247 IDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  340 IGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKR 419
Cdd:NF041083 322 TGARIVTNIDDLTPEDLGYAELVEERKV-GDDKMVFVEGCKNP-KAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  420 ALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGG 499
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGE 479
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 33414505  500 ISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:NF041083 480 VVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
34-536 1.02e-112

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 343.60  E-value: 1.02e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSV 109
Cdd:COG0459  12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 110 VIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvsqysSLLSPMSVN 189
Cdd:COG0459  92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANGD------EEIGELIAE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 190 AVMKVIDPATATsvdlrdikiVKKLGGTIDDCELVEGLVLTQKVANSGItrvekakigliqfclsapktdmdnqivVSDY 269
Cdd:COG0459 164 AMEKVGKDGVIT---------VEEGKGLETELEVVEGMQFDKGYLSPYF---------------------------VTDP 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 270 AQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSIlrdalSDLALHFL--NKM----KIMVVK---- 326
Cdd:COG0459 208 EKMPAEL--ENAYILltdkkissiqdllPLLEKVAQSGKPLLIIAEDI-----DGEALATLvvNGIrgvlRVVAVKapgf 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 327 -DIEREDIEFICKTIGTKPVAH-----IDQFTPDMLGSAELAEEvslnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEE 400
Cdd:COG0459 281 gDRRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEV----DKDNTTIVEGAGNP-KAIVILVGAATEVEVKE 355
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 401 AERSIHDALCVIRCLVKKRaLIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTEL 480
Cdd:COG0459 356 RKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33414505 481 RnrhAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:COG0459 435 R---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
22-536 4.68e-112

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 343.16  E-value: 4.68e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   22 GAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQ-----DGKGDVTITNDGATILKQMQVLHPAARMLVELSK 96
Cdd:PTZ00212  14 GAQEEKGETA--RLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   97 AQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNS 173
Cdd:PTZ00212  92 TQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  174 KVVSQYSSLLSPMSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgliqfcL 253
Cdd:PTZ00212 172 KLLTVEKDHFAKLAVDAVLRLKG-----SGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKI------L 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  254 SApKTDMDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVV 325
Cdd:PTZ00212 241 VA-NTPMDTdkikiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  326 KDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSI 405
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMI-GEDKLIRFSGCAK-GEACTIVLRGASTHILDEAERSL 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  406 HDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA 485
Cdd:PTZ00212 393 HDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY 472
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 33414505  486 QGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:PTZ00212 473 KGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
 
Name Accession Description Interval E-value
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
25-538 0e+00

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: 980.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:cd03338   1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03338  81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANS--GITRVEKAKIGLIQFCLSAPKTDMDN 262
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 263 QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGT 342
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 343 KPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISN 502
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
                       490       500       510
                ....*....|....*....|....*....|....*.
gi 33414505 503 ILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNT 538
Cdd:cd03338 480 ILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
24-539 0e+00

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


Pssm-ID: 274083  Cd Length: 517  Bit Score: 923.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    24 YQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAG 103
Cdd:TIGR02342   1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   104 DGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLL 183
Cdd:TIGR02342  81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   184 SPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKV--ANSGITRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02342 161 APLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKAskSAGGPTRIEKAKIGLIQFQISPPKTDME 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   342 TKPVAHIDQFTPDMLGSAELAEEVSLNGsGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDG-GKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGIS 501
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGIT 479
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 33414505   502 NILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
26-536 0e+00

chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 238189  Cd Length: 464  Bit Score: 588.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd00309   2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSP 185
Cdd:cd00309  82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 186 MSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSapktdmdnqi 264
Cdd:cd00309 162 LVVDAVLKVGKENG--DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLE---------- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 265 vvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKP 344
Cdd:cd00309 230 -------------------------------YVVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 345 VAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKI-GDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPG 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNIL 504
Cdd:cd00309 352 GGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMK 431
                       490       500       510
                ....*....|....*....|....*....|..
gi 33414505 505 EEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd00309 432 EAGIIDPLKVKRQALKSATEAASLILTIDDII 463
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
44-539 0e+00

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 562.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKL 123
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   124 LQKGIHPTIISESFQKALEKGLEILTDM-SRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVidPATATS 202
Cdd:pfam00118  81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   203 VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERA 281
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   282 YILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAEL 361
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   362 AEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSR 441
Cdd:pfam00118 314 VEEEKI-GDEKYTFIEGCKSP-KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   442 TLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTL 521
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
                         490
                  ....*....|....*...
gi 33414505   522 ATETVRSILKIDDVVNTR 539
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
thermosome_alpha NF041082
thermosome subunit alpha;
36-536 0e+00

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 550.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:NF041082  21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  196 DPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:NF041082 181 EKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMpKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:NF041082 261 FLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  355 MLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:NF041082 336 DLGYAGLVEERKVGGDKMIF-VEGCKNP-KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
                        490       500
                 ....*....|....*....|..
gi 33414505  515 SVSALTLATETVRSILKIDDVV 536
Cdd:NF041082 494 KTQAIKSATEAAVMILRIDDVI 515
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
36-536 0e+00

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: 538.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03343  19 MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03343  99 LLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVA 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPAT-ATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMD 273
Cdd:cd03343 179 EKRDgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQ 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTP 353
Cdd:cd03343 259 AFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTP 333
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 354 DMLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELA 433
Cdd:cd03343 334 EDLGEAELVEERKVGDDKMVF-VEGCKNP-KAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELA 411
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 434 LRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLL 513
Cdd:cd03343 412 KRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLR 491
                       490       500
                ....*....|....*....|...
gi 33414505 514 VSVSALTLATETVRSILKIDDVV 536
Cdd:cd03343 492 VKKQAIKSATEAATMILRIDDVI 514
thermosome_beta NF041083
thermosome subunit beta;
22-539 0e+00

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 521.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   22 GAYQDRDKPAQirFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIE 101
Cdd:NF041083   9 GTQRTKGRDAQ--RNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSS 181
Cdd:NF041083  87 VGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  182 LLSPMSVNAVMKVIDPATAT-SVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTD 259
Cdd:NF041083 167 YLAEIAVKAVKQVAEKRDGKyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  260 MDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKT 339
Cdd:NF041083 247 IDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  340 IGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKR 419
Cdd:NF041083 322 TGARIVTNIDDLTPEDLGYAELVEERKV-GDDKMVFVEGCKNP-KAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  420 ALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGG 499
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGE 479
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 33414505  500 ISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:NF041083 480 VVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
thermosome_arch TIGR02339
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
36-536 3.43e-177

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


Pssm-ID: 274080  Cd Length: 519  Bit Score: 509.61  E-value: 3.43e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02339  20 NNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYS-SLLSPMSVNAVMKV 194
Cdd:TIGR02339 100 LLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   195 IDPATATS--VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQ 271
Cdd:TIGR02339 180 AELRGDGKyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMpKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQ 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   272 MDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQF 351
Cdd:TIGR02339 260 IKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEI 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   352 TPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:TIGR02339 335 TESDLGYAELVEERKV-GEDKMVFVEGCKNP-KAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIE 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQP 511
Cdd:TIGR02339 413 LALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEP 492
                         490       500
                  ....*....|....*....|....*
gi 33414505   512 LLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02339 493 LRVKEQAIKSATEAATMILRIDDVI 517
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
36-536 4.47e-148

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: 435.57  E-value: 4.47e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03339  27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSR--PVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMK 193
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADkiEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 194 VIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQM 272
Cdd:cd03339 187 VAD-LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKeVKDAKIAILTCPFEPPKPKTKHKLDITSVEDY 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 273 DRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03339 266 KKLQEYEQKYFREMVEQVKDAGANLVICQW-----GFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLS 340
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 353 PDMLGSAELAEEVSLNGS-GKLFKITGCtSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:cd03339 341 PEKLGKAGLVREISFGTTkDKMLVIEGC-PNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEIS 419
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTTGINVRKGGISNILEEMVVQ 510
Cdd:cd03339 420 CSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQKVFE 499
                       490       500
                ....*....|....*....|....*.
gi 33414505 511 PLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03339 500 TLISKKQQILLATQVVKMILKIDDVI 525
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
27-536 2.02e-129

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: 388.01  E-value: 2.02e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:TIGR02343  22 RLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPV--QLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02343 102 TGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsaDNNNREPLIQAAKTSLGSKIVSKCHRRFA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   185 PMSVNAVMKVIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMDNQ 263
Cdd:TIGR02343 182 EIAVDAVLNVAD-MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKeVEDAKIAILTCPFEPPKPKTKHK 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   264 IVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTK 343
Cdd:TIGR02343 261 LDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQW-----GFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGR 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   344 PVAHIDQFTPDMLGSAELAEEVSLNGSG-KLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:TIGR02343 336 IVPRFQELSKDKLGKAGLVREISFGTTKdRMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIV 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTTGINVRKGGIS 501
Cdd:TIGR02343 415 YGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYGTN 494
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 33414505   502 NILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02343 495 DMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
36-536 7.91e-129

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: 385.87  E-value: 7.91e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03340  20 SNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD----RETLLNSATTSLNSKVVSQYSSLLSPMSVNAV 191
Cdd:cd03340 100 FLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKMVVDAV 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 192 MKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVV 266
Cdd:cd03340 180 LSLDD-----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFeqqpKKFKNPKILLLNVELEL-KAEKDNaEVRV 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 267 SDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVA 346
Cdd:cd03340 254 EDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 347 HIDQFTPDMLGSAELAEEVSLngSGKLFKI-TGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGG 425
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQV--GGERYNIfTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGG 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 426 GAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKT-TGINVRKGGISNIL 504
Cdd:cd03340 406 GAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNF 485
                       490       500       510
                ....*....|....*....|....*....|..
gi 33414505 505 EEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03340 486 EAFVWEPSLVKINALTAATEAACLILSVDETI 517
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
26-536 1.08e-123

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: 373.16  E-value: 1.08e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd03335   2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTD-MSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03335  82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:cd03335 162 NMVVDAILavKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMpTRVKNAKIACLDFNLQKTKMKLG 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 342 TKPVAHI------DQFTPDMLGSAELAEEVSLnGSGKLFKITGCtSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:cd03335 317 ATLVSTLanlegeETFDPSYLGEAEEVVQERI-GDDELILIKGT-KKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*....
gi 33414505 488 EKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03335 475 LKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
27-536 4.16e-122

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: 367.39  E-value: 4.16e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:cd03337  11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPM 186
Cdd:cd03337  91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 187 SVNAVMKVI--DPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLtqkvansgitrvekakigliqfclsapktdmdNQ 263
Cdd:cd03337 171 ALDAVKTVAveENGRKKEIDIkRYAKVEKIPGGEIEDSRVLDGVML--------------------------------NK 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 264 IVVsdYAQMDRVLREERAYILNlvkqikktgCNVLLIqkSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTK 343
Cdd:cd03337 219 DVT--HPKMRRRIENPRIVLLD---------CPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGAT 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 344 PVAHIDQFTPDMLGSAELAEEVSLNGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIA 423
Cdd:cd03337 286 IVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVP 364
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 424 GGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TTGINVRKGGISN 502
Cdd:cd03337 365 GGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWGIDGETGDIVD 444
                       490       500       510
                ....*....|....*....|....*....|....
gi 33414505 503 ILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03337 445 MKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
26-536 2.16e-120

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: 364.81  E-value: 2.16e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:TIGR02340   6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTD-MSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02340  86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02340 166 NIVVDAVLavKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMpKRIKNAKIACLDFNLQKAKMALG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02340 246 VQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   342 TKPVAHI------DQFTPDMLGSAELAEEVSLnGSGKLFKITGcTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:TIGR02340 321 ATLVSTLadlegeETFEASYLGFADEVVQERI-ADDECILIKG-TKKRKSASIILRGANDFMLDEMERSLHDALCVVKRT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:TIGR02340 399 LESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKH 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 33414505   488 EKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02340 479 LKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
36-536 8.36e-119

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: 360.23  E-value: 8.36e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02345  22 SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSKVVSQYSSLLSPMSVNAVM 192
Cdd:TIGR02345 102 LLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   193 KVIDPAtatsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVVS 267
Cdd:TIGR02345 182 SLDRDD----LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFeqqpKKFANPKILLLNVELEL-KAEKDNaEIRVE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   268 DYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAH 347
Cdd:TIGR02345 257 DVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   348 IDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGA 427
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQI-GSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   428 PEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEM 507
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAF 489
                         490       500
                  ....*....|....*....|....*....
gi 33414505   508 VVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02345 490 VWEPALVKINALKAAFEAACTILSVDETI 518
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
35-536 2.47e-115

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: 349.60  E-value: 2.47e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  35 FSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAG 114
Cdd:cd03341  11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 115 SLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMS--RPVQLSDRETLLNSATTSLNSKVVSqYSSLLSPMSVNAVM 192
Cdd:cd03341  91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvyKIEDLRNKEEVSKALKTAIASKQYG-NEDFLSPLVAEACI 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 193 KVIdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSgITRVEKAKIGLiqfclsapktdmdnqivvsdyaqm 272
Cdd:cd03341 170 SVL-PENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGS-VKRVKKAKVAV------------------------ 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 273 drvlreeraYILNLvkqikKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03341 224 ---------FSCPF-----DIGVNVIVAGGSV-----GDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPT 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 353 PDMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIEL 432
Cdd:cd03341 285 PEEIGYCDSVYVEEI-GDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 433 ALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKG--GISNILEEMVVQ 510
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKEAGIFD 443
                       490       500
                ....*....|....*....|....*.
gi 33414505 511 PLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03341 444 HLATKKWAIKLATEAAVTVLRVDQII 469
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
22-536 2.77e-115

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: 351.25  E-value: 2.77e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  22 GAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKAQD 99
Cdd:cd03336   5 GAQEEKGETA--RLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 100 IEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSKVV 176
Cdd:cd03336  83 DEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKIL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 177 SQYSSLLSPMSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgLIQfclsap 256
Cdd:cd03336 163 TQDKEHFAELAVDAVLRLKG-----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKI-LIA------ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 257 KTDMDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVKDI 328
Cdd:cd03336 231 NTPMDTdkikifgaKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHA 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 329 EREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDA 408
Cdd:cd03336 306 DFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMI-GEDKLIRFSGVAA-GEACTIVLRGASQQILDEAERSLHDA 383
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 409 LCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGE 488
Cdd:cd03336 384 LCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN 463
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*...
gi 33414505 489 KTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03336 464 TTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
34-536 1.02e-112

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 343.60  E-value: 1.02e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSV 109
Cdd:COG0459  12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 110 VIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvsqysSLLSPMSVN 189
Cdd:COG0459  92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANGD------EEIGELIAE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 190 AVMKVIDPATATsvdlrdikiVKKLGGTIDDCELVEGLVLTQKVANSGItrvekakigliqfclsapktdmdnqivVSDY 269
Cdd:COG0459 164 AMEKVGKDGVIT---------VEEGKGLETELEVVEGMQFDKGYLSPYF---------------------------VTDP 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 270 AQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSIlrdalSDLALHFL--NKM----KIMVVK---- 326
Cdd:COG0459 208 EKMPAEL--ENAYILltdkkissiqdllPLLEKVAQSGKPLLIIAEDI-----DGEALATLvvNGIrgvlRVVAVKapgf 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 327 -DIEREDIEFICKTIGTKPVAH-----IDQFTPDMLGSAELAEEvslnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEE 400
Cdd:COG0459 281 gDRRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEV----DKDNTTIVEGAGNP-KAIVILVGAATEVEVKE 355
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 401 AERSIHDALCVIRCLVKKRaLIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTEL 480
Cdd:COG0459 356 RKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33414505 481 RnrhAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:COG0459 435 R---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
37-536 2.76e-112

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: 344.01  E-value: 2.76e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02346  23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMS--RPVQLSDRETLLNSATTSLNSKVVSQYSsLLSPMSVNAVMKV 194
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGNED-FLAQLVAQACSTV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   195 IdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKvANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02346 182 L-PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLN 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNVIVTGGSV-----GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   355 MLGSAELAEeVSLNGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:TIGR02346 335 EIGYVDSVY-VSEIGGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELAS 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKG--GISNILEEMVVQPL 512
Cdd:TIGR02346 414 RLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsdGVKDASEAGIYDML 493
                         490       500
                  ....*....|....*....|....
gi 33414505   513 LVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02346 494 ATKKWAIKLATEAAVTVLRVDQII 517
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
22-536 4.68e-112

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 343.16  E-value: 4.68e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   22 GAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQ-----DGKGDVTITNDGATILKQMQVLHPAARMLVELSK 96
Cdd:PTZ00212  14 GAQEEKGETA--RLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   97 AQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNS 173
Cdd:PTZ00212  92 TQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  174 KVVSQYSSLLSPMSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgliqfcL 253
Cdd:PTZ00212 172 KLLTVEKDHFAKLAVDAVLRLKG-----SGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKI------L 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  254 SApKTDMDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVV 325
Cdd:PTZ00212 241 VA-NTPMDTdkikiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  326 KDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSI 405
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMI-GEDKLIRFSGCAK-GEACTIVLRGASTHILDEAERSL 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  406 HDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA 485
Cdd:PTZ00212 393 HDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY 472
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 33414505  486 QGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:PTZ00212 473 KGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
25-536 2.36e-111

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: 341.33  E-value: 2.36e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:TIGR02344   9 TKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02344  89 GTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   185 PMSVNAVMKV-IDPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02344 169 DLALDAVRTVqRDENGRKEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRyIENPRIVLLDCPLEYKKGESQ 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02344 249 TNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGV-----SDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   342 TKPVAHIDQFTPDMLGSAELAEEVSLNGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02344 324 ATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKL 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TTGINVRKGGI 500
Cdd:TIGR02344 403 VPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETGKI 482
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 33414505   501 SNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02344 483 VDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
37-536 1.40e-88

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: 281.07  E-value: 1.40e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03342  17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQ-LSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03342  97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSdyaqmdr 274
Cdd:cd03342 177 KP--DEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMpKRVENAYILTCNVSLEYEKTEVNSGFFYS------- 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 275 vlreerayilnlvkqikktgcnVLLIQKSIlrDALSdlaLHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:cd03342 248 ----------------------VVINQKGI--DPPS---LDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 355 MLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:cd03342 301 CLGYAGLVYERTL-GEEKYTFIEGVKNP-KSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
                       490       500
                ....*....|....*....|..
gi 33414505 515 SVSALTLATETVRSILKIDDVV 536
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEII 480
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
20-539 4.70e-88

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: 280.59  E-value: 4.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    20 GKGAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKA 97
Cdd:TIGR02341   4 KDGADEERAENA--RLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    98 QDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSrpVQLSD-----RETLLNSATTSLN 172
Cdd:TIGR02341  82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSdevkfRQDLMNIARTTLS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   173 SKVVSQYSSLLSPMSVNAVMKVidpatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFC 252
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL-----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   253 LSAPKTDM-DNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVKDIERE 331
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   332 DIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCV 411
Cdd:TIGR02341 310 GVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMI-GEDKLLKFSGVKL-GEACTIVLRGATQQILDEAERSLHDALCV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   412 IRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTT 491
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 33414505   492 GINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
37-536 2.71e-83

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: 268.53  E-value: 2.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02347  21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLS-DRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   196 DPATAtsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02347 181 KDGED--IDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMpRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREK 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   275 VLREERAYILNLVKQI---KKTGCN-------VLLIQKSIlrDALSdlaLHFLNKMKIMVVKDIEREDIEFICKTIGTKP 344
Cdd:TIGR02347 259 LVKAERKFVDDRVKKIielKKKVCGkspdkgfVVINQKGI--DPPS---LDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   345 VAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTI-GEEKYTFIEECKNP-KSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPG 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNIL 504
Cdd:TIGR02347 412 AGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPE 491
                         490       500       510
                  ....*....|....*....|....*....|..
gi 33414505   505 EEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
160-417 1.87e-64

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: 208.86  E-value: 1.87e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 160 RETLLNSATTSLNSKVvSQYSSLLSPMSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-I 238
Cdd:cd03333   1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR--MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 239 TRVEKAKIGLIQFCLSapktdmdnqivvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLN 318
Cdd:cd03333  78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHYLA 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 319 KMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVI 398
Cdd:cd03333 112 KAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKI-GEEKLTFIEGCKG-GKAATILLRGATEVEL 189
                       250
                ....*....|....*....
gi 33414505 399 EEAERSIHDALCVIRCLVK 417
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVE 208
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
33-523 6.43e-23

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 102.30  E-value: 6.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   33 IRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQM----QVLHPAARMLVELSKAQDIEA 102
Cdd:PTZ00114  17 IRFGDearqslLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  103 GDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKVVsqyssl 182
Cdd:PTZ00114  97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANGDVE------ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  183 LSPMSVNAVMKVIDPATATSVDlrdikivkklGGTIDD-CELVEGLVLTQK------VANSGITRVEkakigliqfcLSA 255
Cdd:PTZ00114 169 IGSLIADAMDKVGKDGTITVED----------GKTLEDeLEVVEGMSFDRGyispyfVTNEKTQKVE----------LEN 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  256 PktdmdnQIVVSDY--AQMDRVLReerayILNLVKQIKKtgcNVLLIQKSILRDALSDLAlhfLNKMKIMV--------- 324
Cdd:PTZ00114 229 P------LILVTDKkiSSIQSILP-----ILEHAVKNKR---PLLIIAEDVEGEALQTLI---INKLRGGLkvcavkapg 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  325 ---VKDIEREDIEFIC--KTIGTKPV-AHIDQFTPDMLGSAELA-----EEVSLNGSG--KLFK---------ITGCTS- 381
Cdd:PTZ00114 292 fgdNRKDILQDIAVLTgaTVVSEDNVgLKLDDFDPSMLGSAKKVtvtkdETVILTGGGdkAEIKervellrsqIERTTSe 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  382 -------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL--TEYSRTLSGM 446
Cdd:PTZ00114 372 ydkeklkerlaklSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLLdkLEEDNELTPD 450
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33414505  447 ESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLAT 523
Cdd:PTZ00114 451 QRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAA 524
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
41-526 5.11e-18

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


Pssm-ID: 239460  Cd Length: 520  Bit Score: 87.13  E-value: 5.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  41 AKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03344  17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSkvvsqySSLLSPMSVNAVMKVID 196
Cdd:cd03344  97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAEAMEKVGK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 197 PATATsvdlrdikiVKKLGGTIDDCELVEGlvltqkvansgitrvekakiglIQF---CLSaPK--TDMDNQIVVSdyaq 271
Cdd:cd03344 169 DGVIT---------VEEGKTLETELEVVEG----------------------MQFdrgYLS-PYfvTDPEKMEVEL---- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 272 mdrvlreERAYIL------NLVKQI-------KKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DiER-- 330
Cdd:cd03344 213 -------ENPYILltdkkiSSIQELlpilelvAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAVKapgfgD-RRka 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 331 --EDI------EFICKTIGTKpvahIDQFTPDMLGSAELAeEVS------LNGSGKLFKITG-----------CTSP--- 382
Cdd:cd03344 285 mlEDIailtggTVISEELGLK----LEDVTLEDLGRAKKV-VVTkddttiIGGAGDKAAIKAriaqirkqieeTTSDydk 359
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 383 -----------GKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLtEYSRTLSGMESYCV 451
Cdd:cd03344 360 eklqerlaklsGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEE-GIVPGGGVALLRASPAL-DKLKALNGDEKLGI 437
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 452 RAFADAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTTGINVRKGGISNILEEMVVQPLLV---------SVSALTLA 522
Cdd:cd03344 438 EIVRRALEAPLRQIAENAGVDGSVVVEKVLE----SPDGFGYDAATGEYVDMIEAGIIDPTKVvrsalqnaaSVASLLLT 513

                ....
gi 33414505 523 TETV 526
Cdd:cd03344 514 TEAL 517
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
196-394 9.47e-17

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: 80.34  E-value: 9.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPATATSVDLRD-IKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLsapktdmDNQIVVSDYAQMD 273
Cdd:cd03334  37 DVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMpSKIKNPRILLLQGPL-------EYQRVENKLLSLD 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHID-QFT 352
Cdd:cd03334 110 PVILQEKEYLKNLVSRIVALRPDVILVEKSV-----SRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDdLLT 184
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33414505 353 PDMLGSAELAEE---VSLNGSGK-LFKITGCTSPGKTvTIVVRGSN 394
Cdd:cd03334 185 SPKLGTCESFRVrtyVEEHGRSKtLMFFEGCPKELGC-TILLRGGD 229
groEL PRK12851
chaperonin GroEL; Reviewed
32-526 4.15e-15

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 77.86  E-value: 4.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   32 QIRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIE 101
Cdd:PRK12851   5 EVKFHVearekmLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSkvvsqyss 181
Cdd:PRK12851  85 AGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV--TTNAEIAQVATISANG-------- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  182 llspmsvnavmkvidpatatsvdlrDIKIVKKLGGTIDdcelveglvltqKVANSGITRVEKAKIGLIQFCLsAPKTDMD 261
Cdd:PRK12851 155 -------------------------DAEIGRLVAEAME------------KVGNEGVITVEESKTAETELEV-VEGMQFD 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  262 NQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLAlhfLNKM---- 320
Cdd:PRK12851 197 RGYLspyfVTDADKMEAEL--EDPYILihekkisnlqdllPVLEAVVQSGKPLLIIAEDVEGEALATLV---VNKLrggl 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  321 KIMVVK--------DIEREDI------EFICKTIGTKpvahIDQFTPDMLGSAELA----EEVSL-NGSGKLFKITG--- 378
Cdd:PRK12851 272 KVAAVKapgfgdrrKAMLEDIailtggTVISEDLGIK----LENVTLEQLGRAKKVvvekENTTIiDGAGSKTEIEGrva 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  379 --------CTSP--------------GKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL 436
Cdd:PRK12851 348 qiraqieeTTSDydreklqerlaklaGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALLRAVKAL 426
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  437 TEySRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTTGINVRKGGISNILEEMVVQPLLV-- 514
Cdd:PRK12851 427 DK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLRE----KPGGYGFNAATNEYGDLYAQGVIDPVKVvr 501
                        570
                 ....*....|....*....
gi 33414505  515 -------SVSALTLATETV 526
Cdd:PRK12851 502 talqnaaSVAGLLLTTEAM 520
groEL PRK12849
chaperonin GroEL; Reviewed
43-526 8.90e-15

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 76.77  E-value: 8.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVE-LSKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK12849  21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEvASKTNDV-AGDGTTTATVLAQALV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  118 DSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIdp 197
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANGDE--------------EIGELI-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  198 ATA-TSVDLRDIKIVKKLGGTIDDCELVEGLVLtqkvaNSG------ITRVEKakigliqfclsapktdmdnqivvsdya 270
Cdd:PRK12849 162 AEAmEKVGKDGVITVEESKTLETELEVTEGMQF-----DRGylspyfVTDPER--------------------------- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  271 qMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLalhFLNKM----KIMVVKDI---ER 330
Cdd:PRK12849 210 -MEAVL--EDPLILltdkkisslqdllPLLEKVAQSGKPLLIIAEDVEGEALATL---VVNKLrgglKVAAVKAPgfgDR 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  331 -----EDI------EFICKTIGTKpvahIDQFTPDMLGSAElaeevslngsgklfKITgctsPGKTVTIVVRGSN----- 394
Cdd:PRK12849 284 rkamlEDIailtggTVISEDLGLK----LEEVTLDDLGRAK--------------RVT----ITKDNTTIVDGAGdkeai 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  395 -------KLVIEEA----------ER--------------------------SIHDALCVIRCLVKKrALIAGGGAPEIE 431
Cdd:PRK12849 342 earvaqiRRQIEETtsdydreklqERlaklaggvavikvgaatevelkerkdRVEDALNATRAAVEE-GIVPGGGVALLR 420
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  432 LALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgekttGINVRKGGISNILEEMV 508
Cdd:PRK12849 421 AAKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGsvvVAKVLELEDGF-------GFNAATGEYGDLIAAGI 492
                        570       580
                 ....*....|....*....|....*..
gi 33414505  509 VQPLLV---------SVSALTLATETV 526
Cdd:PRK12849 493 IDPVKVtrsalqnaaSVAGLLLTTEAL 519
groEL PRK12850
chaperonin GroEL; Reviewed
32-526 3.11e-14

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 75.14  E-value: 3.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   32 QIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDI 100
Cdd:PRK12850   5 EIRFSTDARDRllrgvnILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  101 eAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQlsDRETLLNSATTSLNSKvvsqys 180
Cdd:PRK12850  85 -AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT--SSKEIAQVATISANGD------ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  181 sllspmsvNAVMKVIdpatATSVDlrdikivkklggtiddcelveglvltqKVANSGITRVEKAK-IGL-------IQFc 252
Cdd:PRK12850 156 --------ESIGEMI----AEAMD---------------------------KVGKEGVITVEEAKtLGTeldvvegMQF- 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  253 lsapktdmDNQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALH 315
Cdd:PRK12850 196 --------DRGYLspyfVTNPEKMRAEL--EDPYILlhekkisnlqdllPILEAVVQSGRPLLIIAEDVEGEALATLVVN 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  316 FLNK-MKIMVVK--------DIEREDI------EFICKTIGTKpvahIDQFTPDMLGSA-----ELAEEVSLNGSGKLFK 375
Cdd:PRK12850 266 KLRGgLKSVAVKapgfgdrrKAMLEDIavltggQVISEDLGIK----LENVTLDMLGRAkrvliTKENTTIIDGAGDKKN 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  376 ITGCTS-------------------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEI 430
Cdd:PRK12850 342 IEARVKqiraqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALL 420
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  431 ElALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgekttGINVRKGGISNILEEM 507
Cdd:PRK12850 421 R-ARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGsvvVGKVAELPGNF-------GFNAQTGEYGDMVEAG 492
                        570       580
                 ....*....|....*....|....*...
gi 33414505  508 VVQPLLV---------SVSALTLATETV 526
Cdd:PRK12850 493 IIDPAKVtrtalqdaaSIAALLITTEAM 520
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
30-173 4.83e-14

chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274089  Cd Length: 524  Bit Score: 74.64  E-value: 4.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505    30 PAQIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:TIGR02348   1 AKQIKFDEEARKAllrgvdKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLvkevaSKTN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33414505    99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNS 173
Cdd:TIGR02348  81 DV-AGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPV--KGKKEIAQVATISANN 152
groEL CHL00093
chaperonin GroEL
24-530 1.55e-11

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 66.67  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   24 YQDRDKPAQIRFSNIsaakaVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:CHL00093   7 YQDNARRALERGMDI-----LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQlsDRETLLNSATTSL-NSKVVS 177
Cdd:CHL00093  82 DV-AGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgNDEEVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  178 QyssllspMSVNAVMKVidpatatsvdLRDIKIVKKLG-GTIDDCELVEGLvltqkvansgitRVEKAKIgliqfclsap 256
Cdd:CHL00093 159 S-------MIADAIEKV----------GREGVISLEEGkSTVTELEITEGM------------RFEKGFI---------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  257 ktdmdNQIVVSDYAQMDRVLreERAYIL------NLVKQ--------IKKTGCNVLLIQKSILRDALSDLalhFLNKMK- 321
Cdd:CHL00093 200 -----SPYFVTDTERMEVVQ--ENPYILltdkkiTLVQQdllpileqVTKTKRPLLIIAEDVEKEALATL---VLNKLRg 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  322 -IMVVK-------DIEREDIEFICKTIGTKPVAH-----IDQFTPDMLGSA--------------------------ELA 362
Cdd:CHL00093 270 iVNVVAvrapgfgDRRKAMLEDIAILTGGQVITEdaglsLETIQLDLLGQArriivtkdsttiiadgneeqvkarceQLR 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  363 EEVSLNGSG--------KLFKITGctspGKTVtIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELAL 434
Cdd:CHL00093 350 KQIEIADSSyekeklqeRLAKLSG----GVAV-IKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGATLVHLSE 423
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  435 RLTEYSRT-LSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqgEKTTGINVRKGGISNILEEMVVQPLL 513
Cdd:CHL00093 424 NLKTWAKNnLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGIIDPAK 499
                        570
                 ....*....|....*..
gi 33414505  514 VSVSALTLATETVRSIL 530
Cdd:CHL00093 500 VTRSALQNAASIASMIL 516
groEL PRK00013
chaperonin GroEL; Reviewed
43-173 6.69e-11

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 64.76  E-value: 6.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK00013  21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLAQAIV 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 33414505  118 DSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNS 173
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV--EDKEEIAQVATISANG 153
groEL PRK12852
chaperonin GroEL; Reviewed
44-524 8.15e-11

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 64.48  E-value: 8.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVL----HPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK12852  23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKTNDL-AGDGTTTATVLAQAIVR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSdrETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIDPA 198
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASS--AEIAQVGTISANGDA--------------AIGKMIAQA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  199 tatsvdlrdikivkklggtiddcelveglvlTQKVANSGITRVEKAKigliqfclsapktDMDNQIVVSDYAQMDR---- 274
Cdd:PRK12852 166 -------------------------------MQKVGNEGVITVEENK-------------SLETEVDIVEGMKFDRgyls 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  275 ----------VLREERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNK-MKIMVVK---- 326
Cdd:PRK12852 202 pyfvtnaekmTVELDDAYILlhekklsglqamlPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGgLKVAAVKapgf 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  327 -DIER---EDI------EFICKTIGTKpvahIDQFTPDMLGSAELAE-----EVSLNGSGKLFKITG-----------CT 380
Cdd:PRK12852 282 gDRRKamlEDIailtggQLISEDLGIK----LENVTLKMLGRAKKVVidkenTTIVNGAGKKADIEArvgqikaqieeTT 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  381 S--------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPeielALRLTEYSRTLSGM 446
Cdd:PRK12852 358 SdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQE-GIVPGGGVA----LLRAKKAVGRINND 432
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  447 ES---YCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQgekTTGINVRKGGISNILEEMVVQPLLV--------- 514
Cdd:PRK12852 433 NAdvqAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVvrtalqdaa 509
                        570
                 ....*....|
gi 33414505  515 SVSALTLATE 524
Cdd:PRK12852 510 SVAGLLVTTE 519
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
44-159 1.76e-09

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 60.32  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PLN03167  78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLvrqaaAKTNDL-AGDGTTTSVVLAQGLIA 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 33414505  119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD 159
Cdd:PLN03167 157 EGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE 197
PRK14104 PRK14104
chaperonin GroEL; Provisional
44-526 1.47e-08

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 57.35  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505   44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQV----LHPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK14104  23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGTTTATVLAQAIVR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvSQYSSLLSpmsvNAVMKVIDPA 198
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKV--TSNDEIAQVGTISANGD--AEIGKFLA----DAMKKVGNEG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  199 TATSVDLRDIKIvkklggtidDCELVEGLVLTQK-VANSGITRVEKAKIgliqfclsapktDMDNQIVVSDYAQMDRvLR 277
Cdd:PRK14104 174 VITVEEAKSLET---------ELDVVEGMQFDRGyISPYFVTNADKMRV------------EMDDAYILINEKKLSS-LN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  278 EerayILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DIEREDIEFICKTIGTKPVAH---- 347
Cdd:PRK14104 232 E----LLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLrGGLKVAAVKapgfgDRRKAMLQDIAILTGGQAISEdlgi 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  348 -IDQFTPDMLGSA-----ELAEEVSLNGSGKLFKITG-----------CTS--------------PGKTVTIVVRGSNKL 396
Cdd:PRK14104 308 kLENVTLQMLGRAkkvmiDKENTTIVNGAGKKADIEArvaqikaqieeTTSdydreklqerlaklAGGVAVIRVGGATEV 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505  397 VIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPIST 476
Cdd:PRK14104 388 EVKERKDRVDDAMHATRAAVEE-GIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVI 465
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 33414505  477 VTELRNRHaqgEKTTGINVRKGGISNILEEMVVQPLLV---------SVSALTLATETV 526
Cdd:PRK14104 466 VGKILEKE---QYSYGFDSQTGEYGNLVSKGIIDPTKVvrtaiqnaaSVAALLITTEAM 521
 
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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