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Conserved domains on  [gi|332841149|ref|XP_003314151|]
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PREDICTED: heat shock protein 105 kDa isoform 2 [Pan troglodytes]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSPH1_NBD cd11739
Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa ...
2-384 0e+00

Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3) suppresses the aggregation of denatured proteins caused by heat shock in vitro, and may substitute for HSP70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress. It reduces the protein aggregation and cytotoxicity associated with Polyglutamine (PolyQ) diseases, including Huntington's disease, which are a group of inherited neurodegenerative disorders sharing the characteristic feature of having insoluble protein aggregates in neurons. The expression of HSPH1 is elevated in various malignant tumors, including malignant melanoma, and there is a direct correlation between HSPH1 expression and B-cell non-Hodgkin lymphomas (B-NHLs) aggressiveness and proliferation. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


:

Pssm-ID: 212689  Cd Length: 383  Bit Score: 800.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11739    1 SVVGFDVGFQSCYIAVARAGGIETVANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11739   81 KEKENLSYDLVPLKNGGVGVKVMYMGEEHLFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11739  161 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd11739  241 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd11739  321 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCAILS 383
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
3-708 0e+00

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


:

Pssm-ID: 249507 [Multi-domain]  Cd Length: 598  Bit Score: 612.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149    3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANDEGNRTTPSVVAFTPKERLVGQAAKRQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   83 EKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:pfam00012  81 DIKHVPYKVVKLPNGDAGVEVRYLGET--FTPEQISAMVLQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  163 VGLNCLRLMNDMTAVALNYGIYKQDlpsldeKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:pfam00012 159 AGLNVLRIINEPTAAALAYGLDKKD------KERNVLVFDLGGGTFDVSILEIGDGVFEVLATNGDTHLGGEDFDNRLVD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  243 HFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMN-DKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:pfam00012 233 HFVEEFKKKYGIDLSKDPRALQRLREAAEKAKIELSSNQTEINLPFITAMAdGKDVSGTLTRAKFEELCADLFERTLEPV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVP-- 399
Cdd:pfam00012 313 EKALKDAKLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKTVNPDEAVAIGAAVQAGVLSGTFDVKDVLLLDVTPls 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  400 FPISLIWNHDSEDtEGVHEVFSRNHaAPFSKVLTFLRRgPFELEAFYSDPQGVPYPEAkIGRFVVQNVSAQKDGEkSRVK 479
Cdd:pfam00012 393 LGIETLGGVMTKL-IPRNTTIPTKK-SQIFSTAADNQT-AVEIQVYQGEREMAPDNKL-LGSFELDGIPPAPRGV-PQIE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  480 VKVRVNTHGIFTISTASMVekvpteenemsseadmeclnqrppenpdtdknvqqdnseagtqpqvqTDAQQTSQSPPSPE 559
Cdd:pfam00012 468 VTFDIDANGILTVSAKDKG-----------------------------------------------TGKEQKITITNSSG 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  560 LTSEEnkipdadkanekkvdqppeakkpkikvvnvelpIEanlvwqlgkdllNMYIETEgKMIMQDKLEKERNDAKNAVE 639
Cdd:pfam00012 501 LSDDE---------------------------------IE------------RMVKDAE-EYAAEDKKRKERIEAKNEAE 534
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149  640 EYVYEFRDKLcGPYEKFICEQDHQNflrlLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQE 708
Cdd:pfam00012 535 EYVYSLEKSL-KEEGDKLPEADKKK----VEEAIEWLKEELEGEDKEEIEAKTEELQKVVQPIGERMYQ 598
 
Name Accession Description Interval E-value
HSPH1_NBD cd11739
Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa ...
2-384 0e+00

Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3) suppresses the aggregation of denatured proteins caused by heat shock in vitro, and may substitute for HSP70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress. It reduces the protein aggregation and cytotoxicity associated with Polyglutamine (PolyQ) diseases, including Huntington's disease, which are a group of inherited neurodegenerative disorders sharing the characteristic feature of having insoluble protein aggregates in neurons. The expression of HSPH1 is elevated in various malignant tumors, including malignant melanoma, and there is a direct correlation between HSPH1 expression and B-cell non-Hodgkin lymphomas (B-NHLs) aggressiveness and proliferation. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212689  Cd Length: 383  Bit Score: 800.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11739    1 SVVGFDVGFQSCYIAVARAGGIETVANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11739   81 KEKENLSYDLVPLKNGGVGVKVMYMGEEHLFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11739  161 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd11739  241 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd11739  321 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCAILS 383
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
3-708 0e+00

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 249507 [Multi-domain]  Cd Length: 598  Bit Score: 612.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149    3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANDEGNRTTPSVVAFTPKERLVGQAAKRQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   83 EKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:pfam00012  81 DIKHVPYKVVKLPNGDAGVEVRYLGET--FTPEQISAMVLQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  163 VGLNCLRLMNDMTAVALNYGIYKQDlpsldeKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:pfam00012 159 AGLNVLRIINEPTAAALAYGLDKKD------KERNVLVFDLGGGTFDVSILEIGDGVFEVLATNGDTHLGGEDFDNRLVD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  243 HFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMN-DKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:pfam00012 233 HFVEEFKKKYGIDLSKDPRALQRLREAAEKAKIELSSNQTEINLPFITAMAdGKDVSGTLTRAKFEELCADLFERTLEPV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVP-- 399
Cdd:pfam00012 313 EKALKDAKLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKTVNPDEAVAIGAAVQAGVLSGTFDVKDVLLLDVTPls 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  400 FPISLIWNHDSEDtEGVHEVFSRNHaAPFSKVLTFLRRgPFELEAFYSDPQGVPYPEAkIGRFVVQNVSAQKDGEkSRVK 479
Cdd:pfam00012 393 LGIETLGGVMTKL-IPRNTTIPTKK-SQIFSTAADNQT-AVEIQVYQGEREMAPDNKL-LGSFELDGIPPAPRGV-PQIE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  480 VKVRVNTHGIFTISTASMVekvpteenemsseadmeclnqrppenpdtdknvqqdnseagtqpqvqTDAQQTSQSPPSPE 559
Cdd:pfam00012 468 VTFDIDANGILTVSAKDKG-----------------------------------------------TGKEQKITITNSSG 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  560 LTSEEnkipdadkanekkvdqppeakkpkikvvnvelpIEanlvwqlgkdllNMYIETEgKMIMQDKLEKERNDAKNAVE 639
Cdd:pfam00012 501 LSDDE---------------------------------IE------------RMVKDAE-EYAAEDKKRKERIEAKNEAE 534
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149  640 EYVYEFRDKLcGPYEKFICEQDHQNflrlLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQE 708
Cdd:pfam00012 535 EYVYSLEKSL-KEEGDKLPEADKKK----VEEAIEWLKEELEGEDKEEIEAKTEELQKVVQPIGERMYQ 598
DnaK COG0443
Molecular chaperone [Posttranslational modification, protein turnover, chaperones]
1-590 2.46e-113

Molecular chaperone [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 223520 [Multi-domain]  Cd Length: 579  Bit Score: 360.50  E-value: 2.46e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   1 MSVVGLDVGSQSCYIAVARAGG-IETIANEFSDRCTPSVISFGSKNRT-IGVAAKNQQITHANNTVSNFKRFHGRafndp 78
Cdd:COG0443    5 KKAIGIDLGTTNSVVAVMRGGGlPKVIENAEGERLTPSVVAFSKNGEVlVGQAAKRQAVDNPENTIFSIKRKIGR----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  79 fiqkekenlsydlvplKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLD 158
Cdd:COG0443   80 ----------------GSNGLKISVEVDGKK--YTPEEISAMILTKLKEDAEAYLGEKVTDAVITVPAYFNDAQRQATKD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 159 AAQIVGLNCLRLMNDMTAVALNYGIYKQdlpsldeKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDE 238
Cdd:COG0443  142 AARIAGLNVLRLINEPTAAALAYGLDKG-------KEKTVLVYDLGGGTFDVSLLEIGDGVFEVLATGGDNHLGGDDFDN 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 239 KLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTdLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:COG0443  215 ALIDYLVMEFKGKGGIDLRSDKAALQRLREAAEKAKIELSSATQ-TSINLPSIGGDIDLLKELTRAKFEELILDLLERTI 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPafKVREFSVTDAV 398
Cdd:COG0443  294 EPVEQALKDAGLEKSDIDLVILVGGSTRIPAVQELVKEFFGKEPEKSINPDEAVALGAAIQAAVLSG--EVPDVLLLDVI 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISLIWNHDSedtegVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVP---YPEAKIGRFVVQNVSAQKDGEk 475
Cdd:COG0443  372 PLSLGIETLGGV-----RTPIIERNTTIPVKKSQEFSTAADGQTAVAIHVFQGERemaADNKSLGRFELDGIPPAPRGV- 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 476 SRVKVKVRVNTHGIFTIstaSMVEKVPTEENE----MSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQT 551
Cdd:COG0443  446 PQIEVTFDIDANGILNV---TAKDLGTGKEQSitikASSGLSDEEIERMVEDAEANAALDKKFRELVEARNEAESLIYSL 522
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|.
gi 332841149 552 SQSPPSPELTSEENK--IPDADKANEKKVDQPPEAKKPKIK 590
Cdd:COG0443  523 EKALKEIVKVSEEEKekIEEAITDLEEALEGEKEEIKAKIE 563
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
3-519 2.99e-82

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 279.33  E-value: 2.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:PRK13411   4 VIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGdRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--TE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:PRK13411  82 EERSRVPYTCVKGRDDTVNVQI----RGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQdlpslDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:PRK13411 158 IAGLEVLRIINEPTAAALAYGLDKQ-----DQEQLILVF-DLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS---NSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:PRK13411 232 DWLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSmltTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILSPafKVREFSVTDA 397
Cdd:PRK13411 312 EPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGG--EVKDLLLLDV 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 398 VPFPISLiwnhdsedtEGVHEVFS----RNHAAPFSKVLTF--------------------LRR-----GPFELEAFYSD 448
Cdd:PRK13411 390 TPLSLGI---------ETLGEVFTkiieRNTTIPTSKSQVFstatdgqtsveihvlqgeraMAKdnkslGKFLLTGIPPA 460
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149 449 PQGVPYPEA--KIGRFVVQNVSAQKDGEKSRVKVKVrVNTHGIftisTASMVEKVpTEENEMSSEAD------MECLNQ 519
Cdd:PRK13411 461 PRGVPQIEVsfEIDVNGILKVSAQDQGTGREQSIRI-TNTGGL----SSNEIERM-RQEAEKYAEEDrrrkqlIELKNQ 533
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
4-482 3.31e-82

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 278.99  E-value: 3.31e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKE 83
Cdd:PTZ00009   7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  84 KENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 163
Cdd:PTZ00009  87 MKHWPFKVTTGGDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 164 GLNCLRLMNDMTAVALNYGIYKQdlpslDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEH 243
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKK-----GDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 244 FCAEFKTKYK-LDAKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLY 322
Cdd:PTZ00009 242 CVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSS-STQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 323 SLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS--PAFKVREFSVTDAVP 399
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTgeQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 400 FPISL-----------------------IWNHDSEDTEGVH-EVFSRNHAapFSKVLTFLrrGPFELEAFYSDPQGVPYP 455
Cdd:PTZ00009 401 LSLGLetaggvmtkliernttiptkksqIFTTYADNQPGVLiQVFEGERA--MTKDNNLL--GKFHLDGIPPAPRGVPQI 476
                        490       500
                 ....*....|....*....|....*....
gi 332841149 456 EAK--IGRFVVQNVSAQKDGEKSRVKVKV 482
Cdd:PTZ00009 477 EVTfdIDANGILNVSAEDKSTGKSNKITI 505
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
3-384 3.60e-82

chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved [Protein fate, Protein folding and stabilization].


Pssm-ID: 233830 [Multi-domain]  Cd Length: 595  Bit Score: 277.27  E-value: 3.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149    3 VVGLDVG-SQSCyIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfI 80
Cdd:TIGR02350   2 IIGIDLGtTNSC-VAVMEGGEPVVIPNAEGARTTPSVVAFTKNGeRLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   81 QKEKENLSYDlVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAA 160
Cdd:TIGR02350  79 TEEAKRVPYK-VVGDGGDVRVKV----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  161 QIVGLNCLRLMNDMTAVALNYGIYKQDlpsLDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKL 240
Cdd:TIGR02350 154 KIAGLEVLRIINEPTAAALAYGLDKSK---KDEK--ILVF-DLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  241 VEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKK-LMSSNSTDLPLNIECFMND--KDVSGKMNRSQFEELCAELLQKI 317
Cdd:TIGR02350 228 IDWLADEFKKEEGIDLSKDKMALQRLKEAAEKAKIeLSSVLSTEINLPFITADASgpKHLEMTLTRAKFEELTADLVERT 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332841149  318 EVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:TIGR02350 308 KEPVRQALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLK 374
dnaK CHL00094
heat shock protein 70
3-578 2.12e-70

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 245.41  E-value: 2.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSK-NRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:CHL00094   4 VVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--IS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:CHL00094  82 EEAKQVSYKVKTDSNGNIKIECPALNKD--FSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpslDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:CHL00094 160 IAGLEVLRIINEPTAASLAYGLDKKN----NET--ILVF-DLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS---NSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:CHL00094 233 NWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNltqTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILspAFKVREFSVTDAV 398
Cdd:CHL00094 313 IPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVL--AGEVKDILLLDVT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISLiwnhdsEDTEGVH-EVFSRNHAAPFSK-----------------VLTFLRR--------GPFELEAFYSDPQGV 452
Cdd:CHL00094 391 PLSLGV------ETLGGVMtKIIPRNTTIPTKKsevfstavdnqtnveihVLQGERElakdnkslGTFRLDGIPPAPRGV 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 453 PYPEakigrfVVQNVSAqkDGEKSrvkVKVRVNTHGI---FTISTASMVEKvpTEENEMSSEADmeclnqrppENPDTDK 529
Cdd:CHL00094 465 PQIE------VTFDIDA--NGILS---VTAKDKGTGKeqsITIQGASTLPK--DEVERMVKEAE---------KNAAEDK 522
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 332841149 530 nVQQDNSEagTQPQVQTDAQQTSQsppspELTSEENKIPDADKANEKKV 578
Cdd:CHL00094 523 -EKREKID--LKNQAESLCYQAEK-----QLKELKDKISEEKKEKIENL 563
PLN03184 PLN03184
chloroplast Hsp70; Provisional
3-458 1.65e-69

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 243.99  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFG-SKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:PLN03184  41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTkNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:PLN03184 119 EESKQVSYRVVRDENGNVKLDCPAIGKQ--FAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGR 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpsldeKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:PLN03184 197 IAGLEVLRIINEPTAASLAYGFEKKS------NETILVF-DLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIV 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS---NSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:PLN03184 270 DWLASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSltqTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCK 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILspAFKVREFSVTDAV 398
Cdd:PLN03184 350 TPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVL--AGEVSDIVLLDVT 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISLiwnhdsEDTEGVH-EVFSRNHAAPFSK-----------------VLT----FLRR----GPFELEAFYSDPQGV 452
Cdd:PLN03184 428 PLSLGL------ETLGGVMtKIIPRNTTLPTSKsevfstaadgqtsveinVLQgereFVRDnkslGSFRLDGIPPAPRGV 501

                 ....*.
gi 332841149 453 PYPEAK 458
Cdd:PLN03184 502 PQIEVK 507
PRK03427 PRK03427
cell division protein ZipA; Provisional
519-594 8.95e-03

cell division protein ZipA; Provisional


Pssm-ID: 235124 [Multi-domain]  Cd Length: 333  Bit Score: 37.71  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 519 QRPPENPDTDKNVQQdnseaGTQPQVQTDAQQTSQSPPSPELTSEENKiPDADKANEKKVDQPPEAKKPKIK----VVNV 594
Cdd:PRK03427 130 QQPAYQPQPEQPLQQ-----PVSPQVAPAPQPVHSAPQPAQQAFQPAE-PVAAPQPEPVAEPAPVMDKPKRKeaviVMNV 203
 
Name Accession Description Interval E-value
HSPH1_NBD cd11739
Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa ...
2-384 0e+00

Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3) suppresses the aggregation of denatured proteins caused by heat shock in vitro, and may substitute for HSP70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress. It reduces the protein aggregation and cytotoxicity associated with Polyglutamine (PolyQ) diseases, including Huntington's disease, which are a group of inherited neurodegenerative disorders sharing the characteristic feature of having insoluble protein aggregates in neurons. The expression of HSPH1 is elevated in various malignant tumors, including malignant melanoma, and there is a direct correlation between HSPH1 expression and B-cell non-Hodgkin lymphomas (B-NHLs) aggressiveness and proliferation. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212689  Cd Length: 383  Bit Score: 800.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11739    1 SVVGFDVGFQSCYIAVARAGGIETVANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11739   81 KEKENLSYDLVPLKNGGVGVKVMYMGEEHLFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11739  161 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd11739  241 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd11739  321 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCAILS 383
HSPA4_like_NDB cd10228
Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4 and similar ...
2-384 0e+00

Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4 and similar proteins; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2; the human HSPA4 gene maps to 5q31.1), HSPA4L (also known as 70-kDa heat shock protein 4-like, APG-1, HSPH3, and OSP94; the human HSPA4L gene maps to 4q28), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3), Saccharomyces cerevisiae Sse1p and Sse2p, and a sea urchin sperm receptor. It belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212670  Cd Length: 381  Bit Score: 728.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd10228    1 SVVGIDFGNLNSVVAVARKGGIDVVANEYSNRETPSLVSFGEKQRLIGEAAKNQAISNFKNTVRNFKRLIGRKFDDPEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd10228   81 KELKFLPFKVVELPDGKVGIKVNYLGEEKVFSPEQVLAMLLTKLKEIAEKALKGKVTDCVISVPSYFTDAQRRALLDAAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDLPSlDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd10228  161 IAGLNCLRLMNETTATALAYGIYKTDLPE-EEKPRNVAFVDIGHSSTQVSIVAFNKGKLKVLSTAFDRNLGGRDFDEALF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNsTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd10228  240 EHFAKEFKEKYKIDVLSNPKARLRLLAACEKLKKVLSAN-TEAPLNIECLMEDKDVSGKIKREEFEELCAPLLERVEEPL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd10228  319 EKALAEAGLTKEDIHSVEIVGGSTRIPAVKELIAKVFGKELSTTLNADEAVARGCALQCAMLS 381
HSPA4_NBD cd11737
Nucleotide-binding domain of HSPA4; Human HSPA4 (also known as 70-kDa heat shock protein 4, ...
2-384 0e+00

Nucleotide-binding domain of HSPA4; Human HSPA4 (also known as 70-kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2; the human HSPA4 gene maps to 5q31.1) responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212687  Cd Length: 383  Bit Score: 689.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11737    1 SVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACISFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11737   81 AEKPSLAYDLVQLPTGSTGIKVMYMEEERNFTTEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11737  161 IAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDTTLGGRKFDEVLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd11737  241 NYFCEEFGKKYKLDIKSKIRALLRLSQECEKLKKLMSANASDLPLNIECFMNDIDVSGTMNRGKFLEMCDDLLARVEPPL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd11737  321 RSVLEQAKLKKEDIYAVEIVGGATRIPAVKEKISKFFGKEVSTTLNADEAVARGCALQCAILS 383
HSPA4L_NBD cd11738
Nucleotide-binding domain of HSPA4L; Human HSPA4L (also known as 70-kDa heat shock protein ...
2-384 0e+00

Nucleotide-binding domain of HSPA4L; Human HSPA4L (also known as 70-kDa heat shock protein 4-like, APG-1, HSPH3, and OSP94; the human HSPA4L gene maps to 4q28) is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212688  Cd Length: 383  Bit Score: 564.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11738    1 SVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRTRAIGNAAKSQIVTNVRNTIHGFKKLHGRSFDDPIVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11738   81 TERIRLPYELQKMPNGSVGVKVRYLEEERPFAIEQVTGMLLAKLKETSENALKKPVADCVISIPSFFTDAERRSVMAAAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11738  161 VAGLNCLRLMNETTAVALAYGIYKQDLPALDEKPRNVVFIDMGHSAYQVSVCAFNKGKLKVLATTFDPYLGGRNFDEALV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd11738  241 DYFCDEFKTKYKINVKENSRALLRLYQECEKLKKLMSANASDLPLNIECFMNDLDVSSKMNRAQFEQLCASLLARVEPPL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd11738  321 KAVMEQANLQREDIYSIEIVGGATRIPAVKEQITSFFLKDISTTLNADEAVARGCALQCAILS 383
HSP105-110_like_NBD cd11732
Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4, HYOU1, and ...
5-381 9.66e-120

Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4, HYOU1, and similar proteins; This subfamily include the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2; the human HSPA4 gene maps to 5q31.1), HSPA4L (also known as 70-kDa heat shock protein 4-like, APG-1, HSPH3, and OSP94; the human HSPA4L gene maps to 4q28), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3), HYOU1 (also known as human hypoxia up-regulated 1, GRP170; HSP12A; ORP150; GRP-170; ORP-150; the human HYOU1 gene maps to11q23.1-q23.3), Saccharomyces cerevisiae Sse1p, Sse2p, and Lhs1p, and a sea urchin sperm receptor. It belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212682 [Multi-domain]  Cd Length: 377  Bit Score: 370.51  E-value: 9.66e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   5 GLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEK 84
Cdd:cd11732    2 GLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQES 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  85 ENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVG 164
Cdd:cd11732   82 KHFTSKLVELDDKKTGAEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 165 LNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHF 244
Cdd:cd11732  162 LNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAFVDIGHSSYTCSIVAFKKGQLKVLGTACDKHFGGRDFDLAITEHF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 245 CAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNsTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSL 324
Cdd:cd11732  242 ADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSAN-TNAPFSVESVMNDVDVSSQLSREELEELVKPLLERVTEPVTKA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332841149 325 LEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCA 381
Cdd:cd11732  321 LAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAFGKPLSTTLNQDEAIAKGAAFICA 377
HSP70_NBD cd10170
Nucleotide-binding domain of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
4-381 7.18e-109

Nucleotide-binding domain of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs.


Pssm-ID: 212667 [Multi-domain]  Cd Length: 369  Bit Score: 341.51  E-value: 7.18e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVAR-AGGIETIANEFSDRCTPSVISFGSKNRTI-GVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd10170    1 IGIDLGTTNSAVAYVDnGGKPEIIPNGEGSRTTPSVVYFDGDGEVLvGEAAKRQALDNPENTVGDFKRLIGRKFDDPLVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDlvplkNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd10170   81 SAKKVIGVD-----RGAPIIPVPVELGGKKYSPEEVSALILKKLKEDAEAYLGEPVTEAVITVPAYFNDAQREATKEAAE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpslDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd10170  156 IAGLNVVRLINEPTAAALAYGLDKKD----EKGRTILVF-DLGGGTFDVSLVEVEGGVFEVLATGGDNHLGGDDFDNALA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKK-LMSSNSTDLplNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVP 320
Cdd:cd10170  231 DYLAEKFKEKGGIDLRLDPRALRRLKEAAEKAKIaLSSSEEATI--TLPGLGSGGDLEVELTREEFEELIRPLLERTIDL 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332841149 321 LYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCA 381
Cdd:cd10170  309 VERVLADAGLKPEDIDAVLLVGGSSRIPLVRELLEELFGKKPLRSIDPDEAVALGAAIYAA 369
HSPA5-like_NBD cd10241
Nucleotide-binding domain of human HSPA5 and similar proteins; This subfamily includes human ...
2-379 3.91e-100

Nucleotide-binding domain of human HSPA5 and similar proteins; This subfamily includes human HSPA5 (also known as 70-kDa heat shock protein 5, glucose-regulated protein 78/GRP78, and immunoglobulin heavy chain-binding protein/BIP, MIF2; the gene encoding HSPA5 maps to 9q33.3.), Sacchaormyces cerevisiae Kar2p (also known as Grp78p), and related proteins. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. HSPA5 and Kar2p are chaperones of the endoplasmic reticulum (ER). Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Multiple ER DNAJ domain proteins have been identified and may exist in distinct complexes with HSPA5 in various locations in the ER, for example DNAJC3-p58IPK in the lumen. HSPA5-NEFs include SIL1 and an atypical HSP70 family protein HYOU1/ORP150. The ATPase activity of Kar2p is stimulated by the NEFs: Sil1p and Lhs1p.


Pssm-ID: 212681  Cd Length: 374  Bit Score: 318.49  E-value: 3.91e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQ-SCyIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFI 80
Cdd:cd10241    2 TVIGIDLGTTySC-VGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTIFDVKRLIGRKFDDKEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  81 QKEKENLSYDLVPlKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAA 160
Cdd:cd10241   81 QKDIKLLPYKVVN-KDGKPYIEVDVKGEKKTFSPEEISAMVLTKMKEIAEAYLGKKVKHAVVTVPAYFNDAQRQATKDAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 161 QIVGLNCLRLMNDMTAVALNYGIYKQDlpslDEKpRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKL 240
Cdd:cd10241  160 TIAGLNVVRIINEPTAAAIAYGLDKKG----GEK-NILVF-DLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 241 VEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVP 320
Cdd:cd10241  234 MEHFIKLFKKKHGKDISKDKRALQKLRREVEKAKRALSS-QHQTRIEIESLFDGEDFSETLTRAKFEELNMDLFKKTLKP 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 321 LYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQ 379
Cdd:cd10241  313 VKKVLEDADLKKSDIDEIVLVGGSTRIPKVQQLLKEFFnGKEPSRGINPDEAVAYGAAVQ 372
HYOU1-like_NBD cd10230
Nucleotide-binding domain of human HYOU1 and similar proteins; This subgroup includes human ...
4-381 7.05e-100

Nucleotide-binding domain of human HYOU1 and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, GRP170; HSP12A; ORP150; GRP-170; ORP-150; the human HYOU1 gene maps to11q23.1-q23.3) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (alos known as BiP, Grp78 or HspA5) and may also function as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. This subgroup belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as NEFs, to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212672  Cd Length: 388  Bit Score: 318.36  E-value: 7.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVARAG-GIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:cd10230    1 LGIDLGSEWIKVALVKPGvPFEIVLNEESKRKTPSAVAFKGGERLFGSDASSLAARFPQQVYLHLKDLLGKPADDPSVSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  83 --EKENLSYDLVPLKNGGVGIKVmymGEEHLFSVEQITAMLLTKLKETAENSLK-KPVTDCVISVPSFFTDAERRSVLDA 159
Cdd:cd10230   81 yqSRHPLPYLVVDESRGTVAFKI---SDGEEYSVEELVAMILNYAKKLAEEHAKeAPVKDVVITVPPYFTQAQRQALLDA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 160 AQIVGLNCLRLMNDMTAVALNYGIykqDLPSLDEKPRIVVFVDMGHSAFQVSACAFN----------KGKLKVLGTAFDP 229
Cdd:cd10230  158 AELAGLNVLALVNDGTAAALNYAL---DRRFENNKPQYVLFYDMGAGSTTATVVEFSpveekeksktVPQIEVLGVGWDR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 230 FLGGKNFDEKLVEHFCAEFKTKYKLDAKSK--IRALLRLYQECEKLKKLMSSNStDLPLNIECFMNDKDVSGKMNRSQFE 307
Cdd:cd10230  235 TLGGREFDLRLADHLAKEFEEKHKAKVDVRtnPRAMAKLLKEANRAKEVLSANS-EAPVSIESLYDDIDFKTKITRAEFE 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332841149 308 ELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFG-KDISTTLNADEAVARGCALQCA 381
Cdd:cd10230  314 ELCADLFERAVAPIKKALESAGLTLKDIDSVELIGGATRVPKVQEELSEAVGkKKLGKHLNADEAAAMGAAYYAA 388
HSPA1-2_6-8-like_NBD cd10233
Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins; This ...
4-384 1.16e-99

Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM). The genes for these three HSPA1 proteins map in close proximity on the major histocompatibility complex (MHC) class III region on chromosome 6, 6p21.3. This subfamily also includes human HSPA8 (heat shock 70kDa protein 8, also known as LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; NIP71; HSPA10; the HSPA8 gene maps to 11q24.1), human HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3, the HSPA2 gene maps to 14q24.1), human HSPA6 (also known as heat shock 70kDa protein 6 (HSP70B') gi 94717614, the HSPA6 gene maps to 1q23.3), human HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B; the HSPA7 gene maps to 1q23.3) and Saccharmoyces cerevisiae Stress-Seventy subfamily B/Ssb1p. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Associations of polymorphisms within the MHC-III HSP70 gene locus with longevity, systemic lupus erythematosus, Meniere's disease, noise-induced hearing loss, high-altitude pulmonary edema, and coronary heart disease, have been found. HSPA2 is involved in cancer cell survival, is required for maturation of male gametophytes, and is linked to male infertility. The induction of HSPA6 is a biomarker of cellular stress. HSPA8 participates in the folding and trafficking of client proteins to different subcellular compartments, and in the signal transduction and apoptosis process; it has been shown to protect cardiomyocytes against oxidative stress partly through an interaction with alpha-enolase. S. cerevisiae Ssb1p, is part of the ribosome-associated complex (RAC), it acts as a chaperone for nascent polypeptides, and is important for translation fidelity; Ssb1p is also a [PSI+] prion-curing factor.


Pssm-ID: 212675  Cd Length: 376  Bit Score: 317.36  E-value: 1.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQ-SCyIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:cd10233    2 IGIDLGTTySC-VGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFSDPVVQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  83 EKENLSYDLVPlKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:cd10233   81 DMKHWPFKVVN-GGGKPPIIVEYKGETKTFYPEEISSMVLTKMKEIAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 163 VGLNCLRLMNDMTAVALNYGIYKQdlpslDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:cd10233  160 AGLNVLRIINEPTAAAIAYGLDKK-----GGGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 243 HFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLY 322
Cdd:cd10233  235 HFVQEFKRKHKKDISGNKRALRRLRTACERAKRTLSS-STQASIEIDSLFEGIDFYTSITRARFEELCADLFRGTLEPVE 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332841149 323 SLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 384
Cdd:cd10233  314 KVLRDAKLDKSQIHDIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILS 376
HSPA9-like_NBD cd11733
Nucleotide-binding domain of human HSPA9, Escherichia coli DnaK, and similar proteins; This ...
3-383 2.26e-88

Nucleotide-binding domain of human HSPA9, Escherichia coli DnaK, and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as 70-kDa heat shock protein 9, CSA; MOT; MOT2; GRP75; PBP74; GRP-75; HSPA9B; MTHSP75; the gene encoding HSPA9 maps to 5q31.1), Escherichia coli DnaK, and Saccharomyces cerevisiae Stress-Seventy subfamily C/Ssc1p (also called mtHSP70, Endonuclease SceI 75 kDa subunit). It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively. HSPA9 is involved in multiple processses including mitochondrial import, antigen processing, control of cellular proliferation and differentiation, and regulation of glucose responses. During glucose deprivation-induced cellular stress, HSPA9 plays an important role in the suppression of apoptosis by inhibiting a conformational change in Bax that allow the release of cytochrome c. DnaK modulates the heat shock response in Escherichia coli. It protects E. coli from protein carbonylation, an irreversible oxidative modification that increases during organism aging and bacterial growth arrest. Under severe thermal stress, it functions as part of a bi-chaperone system: the DnaK system and the ring-forming AAA+ chaperone ClpB (Hsp104) system, to promote cell survival. DnaK has also been shown to cooperate with GroEL and the ribosome-associated Escherichia coli Trigger Factor in the proper folding of cytosolic proteins. S. cerevisiae Ssc1p is the major HSP70 chaperone of the mitochondrial matrix, promoting translocation of proteins from the cytosol, across the inner membrane, to the matrix, and their subsequent folding. Ssc1p interacts with Tim44, a peripheral inner membrane protein associated with the TIM23 protein translocase. It is also a subunit of the endoSceI site-specific endoDNase and is required for full endoSceI activity. Ssc1p plays roles in the import of Yfh1p, a nucleus-encoded mitochondrial protein involved in iron homeostasis (and a homolog of human frataxin, implicated in the neurodegenerative disease, Friedreich's ataxia). Ssc1 also participates in translational regulation of cytochrome c oxidase (COX) biogenesis by interacting with Mss51 and Mss51-containing complexes.


Pssm-ID: 212683  Cd Length: 377  Bit Score: 287.35  E-value: 2.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11733    4 VIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTKDGeRLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11733   84 KDIKNVPYKIVKASNGDAWVEA----HGKKYSPSQIGAFVLMKMKETAEAYLGKPVKNAVITVPAYFNDSQRQATKDAGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpsldekPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11733  160 IAGLNVLRVINEPTAAALAYGLDKKD-------DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDNALL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLK-KLMSSNSTDLPLNiecFMNdKDVSG------KMNRSQFEELCAELL 314
Cdd:cd11733  233 RHLVKEFKKEQGIDLTKDNMALQRLREAAEKAKiELSSSLQTDINLP---YIT-ADASGpkhlnmKLTRAKFESLVGDLI 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149 315 QKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 383
Cdd:cd11733  309 KRTIEPCKKALKDAGVSKSDIGEVILVGGMTRMPKVQETVKEIFGKEPSKGVNPDEAVAIGAAIQGGVL 377
HSPA9-Ssq1-like_NBD cd10234
Nucleotide-binding domain of human HSPA9 and similar proteins; This subfamily includes human ...
3-383 4.74e-85

Nucleotide-binding domain of human HSPA9 and similar proteins; This subfamily includes human mitochondrial HSPA9 (also known as 70-kDa heat shock protein 9, CSA; MOT; MOT2; GRP75; PBP74; GRP-75; HSPA9B; MTHSP75; the gene encoding HSPA9 maps to 5q31.1), Escherichia coli DnaK, Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p, Ssh1p, mtHSP70 homolog), and S. cerevisiae Stress-Seventy subfamily C/Ssc1p (also called mtHSP70, Endonuclease SceI 75 kDa subunit). It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 212676 [Multi-domain]  Cd Length: 376  Bit Score: 278.38  E-value: 4.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPfiq 81
Cdd:cd10234    4 IIGIDLGTTNSCVAVMEGGEPTVIPNAEGSRTTPSVVAFTKKGeRLVGQPAKRQAVTNPENTIFSIKRFMGRKFDEV--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd10234   81 EEERKVPYKVVVDEGGNYKVEIDSNGKD--YTPQEISAMILQKLKEDAEAYLGEKVTEAVITVPAYFNDSQRQATKDAGK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpslDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd10234  159 IAGLEVLRIINEPTAAALAYGLDKKG----NEK--ILVY-DLGGGTFDVSILEIGDGVFEVLATNGDTHLGGDDFDQRII 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKK-LMSSNSTD--LPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:cd10234  232 DWLVEEFKKEEGIDLRKDKMALQRLKEAAEKAKIeLSSVTETEinLPFITADATGPKHLEMTLTRAKFEELTEDLVERTI 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 383
Cdd:cd10234  312 EPVKQALKDAKLSPSDIDEVILVGGSTRIPAVQELVKELFGKEPNKGVNPDEVVAIGAAIQGGVL 376
HscC_like_NBD cd10235
Nucleotide-binding domain of Escherichia coli HscC and similar proteins; This subfamily ...
4-381 2.18e-75

Nucleotide-binding domain of Escherichia coli HscC and similar proteins; This subfamily includes Escherichia coli HscC (also called heat shock cognate protein C, Hsc62, or YbeW) and the the putative DnaK-like protein Escherichia coli ECs0689. It belongs to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.


Pssm-ID: 212677 [Multi-domain]  Cd Length: 339  Bit Score: 250.88  E-value: 2.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTI-GVAAKNQQITHANNTVSNFKRFHGrafndpfiqK 82
Cdd:cd10235    1 IGIDLGTTNSLVAVWQDGKARLIPNALGEYLTPSVVSVDEDGEILvGKAARERLITHPDLTAASFKRFMG---------T 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  83 EKEnlsydlvplknggvgikvmYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:cd10235   72 DKK-------------------YRLGKREFRAEELSSLVLRSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKRAGEL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 163 VGLNCLRLMNDMTAVALNYGIYKQDlpslDEKpRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:cd10235  133 AGLKVERLINEPTAAALAYGLHDKD----EET-KFLVF-DLGGGTFDVSVLELFDGVMEVRASAGDNYLGGEDFTRALAE 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 243 HFCAEFKTKY-KLDAKSKIrallRLYQECEKLKKLMS-SNSTDLPLNIEcfmnDKDVSGKMNRSQFEELCAELLQKIEVP 320
Cdd:cd10235  207 AFLKKHGLDFeKLDPSELA----RLLRAAERAKRALSdQEEAEMSVRIE----GEELEYTLTREEFEEICQPLLERLRQP 278
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332841149 321 LYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCA 381
Cdd:cd10235  279 IERALRDARLKPSDIDEIILVGGATRMPVVRKLVSRLFGRFPLVHLNPDEVVALGAAIQAG 339
Ssq1_like_NBD cd11734
Nucleotide-binding domain of Saccharomyces cerevisiae Ssq1 and similar proteins; Ssq1p (also ...
2-383 3.32e-75

Nucleotide-binding domain of Saccharomyces cerevisiae Ssq1 and similar proteins; Ssq1p (also called Stress-seventy subfamily Q protein 1, Ssc2p, Ssh1p, mtHSP70 homolog) belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). S. cerevisiae Ssq1p is a mitochondrial chaperone that is involved in iron-sulfur (Fe/S) center biogenesis. Ssq1p plays a role in the maturation of Yfh1p, a nucleus-encoded mitochondrial protein involved in iron homeostasis (and a homolog of human frataxin, implicated in the neurodegenerative disease, Friedreich's ataxia).


Pssm-ID: 212684 [Multi-domain]  Cd Length: 373  Bit Score: 251.66  E-value: 3.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd11734    3 TIIGIDLGTTNSCVAVIDKTTPVIIENAEGKRTTPSIVSFTKTGILVGEAAKRQEALHPENTFFATKRLIGRQFKDVEVQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd11734   83 RKMKVPYYKIVEGRNGDAWIYT----NGKKYSPSQIASFVLKKLKKTAEAYLGKRVDEAVITVPAYFNDSQRQATKDAGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQdlpslDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd11734  159 LAGLKVLRIINEPTAAALAYGIDKR-----KENKNIAVY-DLGGGTFDISILNIEDGVFEVKATNGDTMLGGEDFDNAIV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLpLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd11734  233 QYIIKEFKRKYKIDLTRNKKAIQRIKEAAEKAKIELSSSEESV-IELPYLDGPKHLRITITRREFEQLRKSICKRTIYPC 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 383
Cdd:cd11734  312 KQCLKDAGLRKKDIDEVILVGGMTRMPYIQNVVQEIFGKKPSKSVNPDEAVALGAAIQGSIL 373
ScSsz1p_like_NBD cd10232
Nucleotide-binding domain of Saccharmomyces cerevisiae Ssz1pp and similar proteins; ...
2-379 2.42e-73

Nucleotide-binding domain of Saccharmomyces cerevisiae Ssz1pp and similar proteins; Saccharomyces cerevisiae Ssz1p (also known as /Pdr13p/YHR064C) belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but rather, function as NEFs for their Hsp70 partners, while other family members function as both chaperones and NEFs. Ssz1 does not function as a chaperone; it facilitates the interaction between the HSP70 Ssb protein and its partner J-domain protein Zuo1 (also known as zuotin) on the ribosome. Ssz1 is found in a stable heterodimer (called RAC, ribosome associated complex) with Zuo1. Zuo1 can only stimulate the ATPase activity of Ssb, when it is in complex with Ssz1. Ssz1 binds ATP but neither nucleotide-binding, hydrolysis, or its SBD, is needed for its in vivo function.


Pssm-ID: 212674 [Multi-domain]  Cd Length: 386  Bit Score: 246.92  E-value: 2.42e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPfiq 81
Cdd:cd10232    1 TVIGINFGNTYSSIACINQGKADVIANEDGERQIPSAISYHGEQEYHGNQAKAQLIRNAKNTITNFRDLLGKPFSEI--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGE----EHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVL 157
Cdd:cd10232   78 DVSAAAAAAPVPVAVIDVGGTVQEKEEpvpkETILTVHEVTVRFLRRLKEAAEDFLGKKVAGAVLSVPTWFSDEQTEALV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 158 DAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSldEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFD 237
Cdd:cd10232  158 KAAEAAGLPVLQLIPEPAAALLAYDAGEPTEDE--ALDRNVVVADFGGTRTDVSVIAVRGGLYTILATAHDPGLGGDTLD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 238 EKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMsSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKI 317
Cdd:cd10232  236 DALVKHFAKEFTKKTKTDPRTNARALAKLRAESEITKKTL-SASTSATCSVESLAEGIDFHSSINRLRFELLASAVFRQF 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 318 EVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGK--------DISTTLNADEAVARGCALQ 379
Cdd:cd10232  315 AAFVTSAVAKAGLDALDIDEVLLVGGTAFTPKLASNLSYLFPEtttitapiTVSKALDPSELVARGCAIQ 384
HSPA14-like_NBD cd10238
Nucleotide-binding domain of human HSPA14 and similar proteins; Human HSPA14 (also known as ...
2-381 1.74e-66

Nucleotide-binding domain of human HSPA14 and similar proteins; Human HSPA14 (also known as 70-kDa heat shock protein 14, HSP70L1, HSP70-4; the gene encoding HSPA14 maps to 10p13), is ribosome-associated and belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA14 interacts with the J-protein MPP11 to form the mammalian ribosome-associated complex (mRAC). HSPA14 participates in a pathway along with Nijmegen breakage syndrome 1 (NBS1, also known as p85 or nibrin), heat shock transcription factor 4b (HSF4b), and HSPA4 (belonging to a different subfamily), that induces tumor migration, invasion, and transformation. HSPA14 is a potent T helper cell (Th1) polarizing adjuvant that contributes to antitumor immune responses.


Pssm-ID: 212680  Cd Length: 375  Bit Score: 227.27  E-value: 1.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   2 SVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:cd10238    1 AAIGVHFGNTSACLAVYKDGRADVVANDAGDRVTPAVVAFTDTEVIVGLAAKQGRIRNAANTIVKNKQILGRSYSDPFKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPlKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:cd10238   81 KEKTESSCKIIE-KDGEPKYEIFTEEKTKHVSPKEVAKLIFKKMKEIAQSALGSDSKDVVITVPVYFSEKQKLALREAAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYkQDLPsldEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:cd10238  160 EAGFNVLRIIHEPSAAALAYGIG-QDSP---TGKSYVLVYRLGGTSTDVTILRVNSGMYRVLATSTDDNLGGESFTETLS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTdLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:cd10238  236 QYLANEFKRKWKQDVRGNARAMMKLNNAAEVAKQILSTLPS-ANCFVESLYEGIDFQCSVSRARFESLCSSLFPKCLEPI 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCA 381
Cdd:cd10238  315 EKVLEQANLTKTDINKVVLCGGSSRIPKLQQLIKDLFpSVEVLNSISPDEVIAIGAAKQAG 375
HscA_like_NBD cd10236
Nucleotide-binding domain of HscA and similar proteins; Escherichia coli HscA (heat shock ...
3-379 2.21e-66

Nucleotide-binding domain of HscA and similar proteins; Escherichia coli HscA (heat shock cognate protein A, also called Hsc66), belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF, and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.


Pssm-ID: 212678 [Multi-domain]  Cd Length: 355  Bit Score: 226.32  E-value: 2.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPfiqK 82
Cdd:cd10236    2 AIGIDLGTTNSLVASVLSGKVKILPDENGRVLLPSVVHYGDGGISVGHDALKLAISDPKNTISSVKRLMGKSIEDI---K 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  83 EKENLSYDLVPLKNGGVGIKVmymGEEHLFSVEqITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:cd10236   79 KSFPYLPILEGKNGGIILFHT---QQGTVTPVE-VSAEILKALKERAEKSLGGEIKGAVITVPAYFDDAQRQATKDAARL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 163 VGLNCLRLMNDMTAVALNYGIYKqdlpsldEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:cd10236  155 AGLNVLRLLNEPTAAALAYGLDK-------KKEGIYAVYDLGGGTFDVSILKLHKGVFEVLATGGDSALGGDDFDQLLAE 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 243 HFCAEFKTKYKLDAKSKiRALLrlyQECEKLKKLMSSNSTdlplnIEcfMNDKDVSGKMNRSQFEELCAELLQKIEVPLY 322
Cdd:cd10236  228 LLLKKYGLKSLISDEDQ-AELL---LIARKAKEALSGAEE-----VE--VRGQDFKCTITREEFEKLIDPLVKKTLNICK 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332841149 323 SLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQ 379
Cdd:cd10236  297 QALRDAGLSVKDIKGVILVGGSTRIPLVQEAVSKFFGQKPLCDINPDEVVAIGAALQ 353
HSPA13-like_NBD cd10237
Nucleotide-binding domain of human HSPA13 and similar proteins; Human HSPA13 (also called ...
3-383 1.26e-57

Nucleotide-binding domain of human HSPA13 and similar proteins; Human HSPA13 (also called 70-kDa heat shock protein 13, STCH, "stress 70 protein chaperone, microsome-associated, 60kD", "stress 70 protein chaperone, microsome-associated, 60kDa"; the gene encoding HSPA13 maps to 21q11.1) belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). STCH contains an NBD but lacks an SBD. STCH may function to regulate cell proliferation and survival, and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.


Pssm-ID: 212679 [Multi-domain]  Cd Length: 417  Bit Score: 203.47  E-value: 1.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARA--GGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFI 80
Cdd:cd10237   22 IIGIDLGTTYSSVGVYQAgtGETDIIPDENGRKSIPSVVAFTPGTVLVGYKAVEQAEHNPQNTIYDAKRFIGKIFTKEEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  81 QKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAA 160
Cdd:cd10237  102 EFESDRYRFKVKINSRNGAFFFSVLTNETKTVTPEEIGSRLILKLRKMAEKYLGTPVGKAVISVPAEFDEKQRNATVKAA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 161 QIVGLNCLRLMNDMTAVALNYGIYKQdlpsldEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKL 240
Cdd:cd10237  182 NLAGLEVLRVINEPTAAALAYGLHKK------QDVFNVLVVDLGGGTLDVSLLNKQGGMFLTRAMAGNNRLGGQDFNQRL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 241 VEHFCAEFKTKY--KLDAKSKIRallRLYQECEKLK-KLMSSNSTDLPLNIECFMNDKDVsGKMN----RSQFEELCAEL 313
Cdd:cd10237  256 LQYLYQKIYEKYgkVPDNKEDIQ---RLRQAVEAAKiNLTLHPSTTISLNLTLLSEGESI-VKFEyeltRDEFETLNEDL 331
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 314 LQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 383
Cdd:cd10237  332 FQKILLPIEAVLAEGHLDKEEVDEIVLVGGSTRIPRIRQVIGRFFGKDPNTSVDPELAVVTGVAIQAGII 401
YegD_like cd10231
Escherichia coli YegD, a putative chaperone protein, and related proteins; This bacterial ...
4-378 5.47e-14

Escherichia coli YegD, a putative chaperone protein, and related proteins; This bacterial subfamily includes the uncharacterized Escherichia coli YegD. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.


Pssm-ID: 212673 [Multi-domain]  Cd Length: 415  Bit Score: 73.72  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISF------GSKNRTIGVAAKNQQITHanntvsnfkRFHGRafnd 77
Cdd:cd10231    1 LGIDFGTSNSAVAVARDGQPRLVPLEGGSTTLPSALFFpheesaLEREVLFGRAAIAAYLEG---------PGEGR---- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  78 pFIQKEKENLSYDLvpLKNGGVGikvmymgeEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTD------- 150
Cdd:cd10231   68 -LMRSLKSFLGSSL--FRETRIF--------GRRLTFEDLVARFLAELKQRAEAALGAEIDRVVIGRPVHFVGddeaada 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 151 -AERRsVLDAAQIVGLNCLRLMNDMTAVALNYGiykQDLpsldEKPRIVVFVDMG-----HSAFQVSACAFNKGKLK--V 222
Cdd:cd10231  137 qAEAR-LRAAARAAGFKDVEFQYEPIAAALDYE---QRL----TREELVLVVDIGggtsdFSLVRLGPSRRGRADRRadI 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 223 L--------GTAFD---------PFLG----GKNFDEKL---VEHFcAEFKT------KYKLDAKSKIRALLRLYQECEK 272
Cdd:cd10231  209 LahsgvrigGTDFDrrlslhavmPLLGkgstYRSGGKGLpvpNSYF-ADLATwhkinfLYTPKTLRELRELARDAVEPEL 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 273 LKKLM-----------------------SSNSTDLPLNIEcfmnDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTH 329
Cdd:cd10231  288 LERLItvieeelghrlaraveaakialsSQDETRIDLDFV----EVGLEAPVTRAEFEGAIAPDLERIEAAVDEALAQAG 363
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 332841149 330 LKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCAL 378
Cdd:cd10231  364 VSPDAIDRVFLTGGSSLVPAVRQAFAARFPAARIVEGDAFGSVASGLAL 412
HSPA12_like_NBD cd10229
Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins; Human HSPA12A (also known ...
113-378 5.08e-06

Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins; Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway.


Pssm-ID: 212671 [Multi-domain]  Cd Length: 404  Bit Score: 48.43  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 113 SVEQITAMLLTKLKETAENSLKK----------PVtDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMT------- 175
Cdd:cd10229  107 TAVDVIADYLRYLYEHALEELKKtygngeftalDI-EWVLTVPAIWSDAAKQAMREAAIKAGLVSSREGPDRLlivlepe 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 176 AVALnYgIYKQDLPSLDEKP--RIVVfVDMGH-----SAFQVSAcaFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEF 248
Cdd:cd10229  186 AAAL-Y-CLKLLLISLNLKPgdGFLV-CDAGGgtvdlTVYEVTS--VEPLRLKELAAGSGGLCGSTFVDRAFEELLKERL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 249 KTKYKLDA-KSKIRALLRLYQEcEKLKKLMSSNSTDL--PLNIECFMNDKDVSGKMNRSQ-----------FEELCAELL 314
Cdd:cd10229  261 GELFYELPsKSPALWLILMRFF-ETIKRSFGGTDNDTniVLPGSLALSKKDPERGIRNGElkisgedmkslFDPVIEEII 339
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332841149 315 QKIEvplySLLEQTHlKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTL---NADEAVARGCAL 378
Cdd:cd10229  340 DLIE----EQLEQAE-KGDKVKYIFLVGGFGESPYLRSRLKERFSSRGIRVLrppDPQLAVVRGAVL 401
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
3-708 0e+00

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 249507 [Multi-domain]  Cd Length: 598  Bit Score: 612.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149    3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANDEGNRTTPSVVAFTPKERLVGQAAKRQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   83 EKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:pfam00012  81 DIKHVPYKVVKLPNGDAGVEVRYLGET--FTPEQISAMVLQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  163 VGLNCLRLMNDMTAVALNYGIYKQDlpsldeKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:pfam00012 159 AGLNVLRIINEPTAAALAYGLDKKD------KERNVLVFDLGGGTFDVSILEIGDGVFEVLATNGDTHLGGEDFDNRLVD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  243 HFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMN-DKDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:pfam00012 233 HFVEEFKKKYGIDLSKDPRALQRLREAAEKAKIELSSNQTEINLPFITAMAdGKDVSGTLTRAKFEELCADLFERTLEPV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVP-- 399
Cdd:pfam00012 313 EKALKDAKLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKTVNPDEAVAIGAAVQAGVLSGTFDVKDVLLLDVTPls 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  400 FPISLIWNHDSEDtEGVHEVFSRNHaAPFSKVLTFLRRgPFELEAFYSDPQGVPYPEAkIGRFVVQNVSAQKDGEkSRVK 479
Cdd:pfam00012 393 LGIETLGGVMTKL-IPRNTTIPTKK-SQIFSTAADNQT-AVEIQVYQGEREMAPDNKL-LGSFELDGIPPAPRGV-PQIE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  480 VKVRVNTHGIFTISTASMVekvpteenemsseadmeclnqrppenpdtdknvqqdnseagtqpqvqTDAQQTSQSPPSPE 559
Cdd:pfam00012 468 VTFDIDANGILTVSAKDKG-----------------------------------------------TGKEQKITITNSSG 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  560 LTSEEnkipdadkanekkvdqppeakkpkikvvnvelpIEanlvwqlgkdllNMYIETEgKMIMQDKLEKERNDAKNAVE 639
Cdd:pfam00012 501 LSDDE---------------------------------IE------------RMVKDAE-EYAAEDKKRKERIEAKNEAE 534
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149  640 EYVYEFRDKLcGPYEKFICEQDHQNflrlLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQE 708
Cdd:pfam00012 535 EYVYSLEKSL-KEEGDKLPEADKKK----VEEAIEWLKEELEGEDKEEIEAKTEELQKVVQPIGERMYQ 598
DnaK COG0443
Molecular chaperone [Posttranslational modification, protein turnover, chaperones]
1-590 2.46e-113

Molecular chaperone [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 223520 [Multi-domain]  Cd Length: 579  Bit Score: 360.50  E-value: 2.46e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   1 MSVVGLDVGSQSCYIAVARAGG-IETIANEFSDRCTPSVISFGSKNRT-IGVAAKNQQITHANNTVSNFKRFHGRafndp 78
Cdd:COG0443    5 KKAIGIDLGTTNSVVAVMRGGGlPKVIENAEGERLTPSVVAFSKNGEVlVGQAAKRQAVDNPENTIFSIKRKIGR----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  79 fiqkekenlsydlvplKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLD 158
Cdd:COG0443   80 ----------------GSNGLKISVEVDGKK--YTPEEISAMILTKLKEDAEAYLGEKVTDAVITVPAYFNDAQRQATKD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 159 AAQIVGLNCLRLMNDMTAVALNYGIYKQdlpsldeKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDE 238
Cdd:COG0443  142 AARIAGLNVLRLINEPTAAALAYGLDKG-------KEKTVLVYDLGGGTFDVSLLEIGDGVFEVLATGGDNHLGGDDFDN 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 239 KLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTdLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:COG0443  215 ALIDYLVMEFKGKGGIDLRSDKAALQRLREAAEKAKIELSSATQ-TSINLPSIGGDIDLLKELTRAKFEELILDLLERTI 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPafKVREFSVTDAV 398
Cdd:COG0443  294 EPVEQALKDAGLEKSDIDLVILVGGSTRIPAVQELVKEFFGKEPEKSINPDEAVALGAAIQAAVLSG--EVPDVLLLDVI 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISLIWNHDSedtegVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVP---YPEAKIGRFVVQNVSAQKDGEk 475
Cdd:COG0443  372 PLSLGIETLGGV-----RTPIIERNTTIPVKKSQEFSTAADGQTAVAIHVFQGERemaADNKSLGRFELDGIPPAPRGV- 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 476 SRVKVKVRVNTHGIFTIstaSMVEKVPTEENE----MSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQT 551
Cdd:COG0443  446 PQIEVTFDIDANGILNV---TAKDLGTGKEQSitikASSGLSDEEIERMVEDAEANAALDKKFRELVEARNEAESLIYSL 522
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|.
gi 332841149 552 SQSPPSPELTSEENK--IPDADKANEKKVDQPPEAKKPKIK 590
Cdd:COG0443  523 EKALKEIVKVSEEEKekIEEAITDLEEALEGEKEEIKAKIE 563
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
3-519 2.99e-82

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 279.33  E-value: 2.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:PRK13411   4 VIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGdRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--TE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:PRK13411  82 EERSRVPYTCVKGRDDTVNVQI----RGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQdlpslDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:PRK13411 158 IAGLEVLRIINEPTAAALAYGLDKQ-----DQEQLILVF-DLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS---NSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:PRK13411 232 DWLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSmltTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILSPafKVREFSVTDA 397
Cdd:PRK13411 312 EPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGG--EVKDLLLLDV 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 398 VPFPISLiwnhdsedtEGVHEVFS----RNHAAPFSKVLTF--------------------LRR-----GPFELEAFYSD 448
Cdd:PRK13411 390 TPLSLGI---------ETLGEVFTkiieRNTTIPTSKSQVFstatdgqtsveihvlqgeraMAKdnkslGKFLLTGIPPA 460
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149 449 PQGVPYPEA--KIGRFVVQNVSAQKDGEKSRVKVKVrVNTHGIftisTASMVEKVpTEENEMSSEAD------MECLNQ 519
Cdd:PRK13411 461 PRGVPQIEVsfEIDVNGILKVSAQDQGTGREQSIRI-TNTGGL----SSNEIERM-RQEAEKYAEEDrrrkqlIELKNQ 533
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
4-482 3.31e-82

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 278.99  E-value: 3.31e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKE 83
Cdd:PTZ00009   7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  84 KENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 163
Cdd:PTZ00009  87 MKHWPFKVTTGGDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 164 GLNCLRLMNDMTAVALNYGIYKQdlpslDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEH 243
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKK-----GDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 244 FCAEFKTKYK-LDAKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLY 322
Cdd:PTZ00009 242 CVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSS-STQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 323 SLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS--PAFKVREFSVTDAVP 399
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTgeQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 400 FPISL-----------------------IWNHDSEDTEGVH-EVFSRNHAapFSKVLTFLrrGPFELEAFYSDPQGVPYP 455
Cdd:PTZ00009 401 LSLGLetaggvmtkliernttiptkksqIFTTYADNQPGVLiQVFEGERA--MTKDNNLL--GKFHLDGIPPAPRGVPQI 476
                        490       500
                 ....*....|....*....|....*....
gi 332841149 456 EAK--IGRFVVQNVSAQKDGEKSRVKVKV 482
Cdd:PTZ00009 477 EVTfdIDANGILNVSAEDKSTGKSNKITI 505
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
3-384 3.60e-82

chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved [Protein fate, Protein folding and stabilization].


Pssm-ID: 233830 [Multi-domain]  Cd Length: 595  Bit Score: 277.27  E-value: 3.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149    3 VVGLDVG-SQSCyIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfI 80
Cdd:TIGR02350   2 IIGIDLGtTNSC-VAVMEGGEPVVIPNAEGARTTPSVVAFTKNGeRLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   81 QKEKENLSYDlVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAA 160
Cdd:TIGR02350  79 TEEAKRVPYK-VVGDGGDVRVKV----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  161 QIVGLNCLRLMNDMTAVALNYGIYKQDlpsLDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKL 240
Cdd:TIGR02350 154 KIAGLEVLRIINEPTAAALAYGLDKSK---KDEK--ILVF-DLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  241 VEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKK-LMSSNSTDLPLNIECFMND--KDVSGKMNRSQFEELCAELLQKI 317
Cdd:TIGR02350 228 IDWLADEFKKEEGIDLSKDKMALQRLKEAAEKAKIeLSSVLSTEINLPFITADASgpKHLEMTLTRAKFEELTADLVERT 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332841149  318 EVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 384
Cdd:TIGR02350 308 KEPVRQALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLK 374
dnaK PRK00290
molecular chaperone DnaK; Provisional
1-384 2.62e-79

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 270.43  E-value: 2.62e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   1 MS-VVGLDVG-SQSCyIAVARAGGIETIANEFSDRCTPSVISFgSKN--RTIGVAAKNQQITHANNTVSNFKRFHGRafN 76
Cdd:PRK00290   1 MGkIIGIDLGtTNSC-VAVMEGGEPKVIENAEGARTTPSVVAF-TKDgeRLVGQPAKRQAVTNPENTIFSIKRLMGR--R 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  77 DPFIQKEKENLSYDLVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSV 156
Cdd:PRK00290  77 DEEVQKDIKLVPYKIVKADNGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 157 LDAAQIVGLNCLRLMNDMTAVALNYGIYKQDlpslDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNF 236
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDKKG----DEK--ILVY-DLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 237 DEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKK-LMSSNSTD--LP-----------LNIecfmndkdvsgKMN 302
Cdd:PRK00290 226 DQRIIDYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIeLSSAQQTEinLPfitadasgpkhLEI-----------KLT 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 303 RSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAI 382
Cdd:PRK00290 295 RAKFEELTEDLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGV 374

                 ..
gi 332841149 383 LS 384
Cdd:PRK00290 375 LA 376
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
3-383 1.76e-73

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 255.13  E-value: 1.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKN-RTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQ 81
Cdd:PTZ00400  43 IVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGqRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATK 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMymGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:PTZ00400 123 KEQKILPYKIVRASNGDAWIEAQ--GKK--YSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGK 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpsldekPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:PTZ00400 199 IAGLDVLRIINEPTAAALAFGMDKND-------GKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRIL 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNS---TDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:PTZ00400 272 NYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTqteINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTI 351
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 383
Cdd:PTZ00400 352 EPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVL 416
dnaK CHL00094
heat shock protein 70
3-578 2.12e-70

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 245.41  E-value: 2.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSK-NRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:CHL00094   4 VVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--IS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:CHL00094  82 EEAKQVSYKVKTDSNGNIKIECPALNKD--FSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpslDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:CHL00094 160 IAGLEVLRIINEPTAASLAYGLDKKN----NET--ILVF-DLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS---NSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:CHL00094 233 NWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNltqTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILspAFKVREFSVTDAV 398
Cdd:CHL00094 313 IPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVL--AGEVKDILLLDVT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISLiwnhdsEDTEGVH-EVFSRNHAAPFSK-----------------VLTFLRR--------GPFELEAFYSDPQGV 452
Cdd:CHL00094 391 PLSLGV------ETLGGVMtKIIPRNTTIPTKKsevfstavdnqtnveihVLQGERElakdnkslGTFRLDGIPPAPRGV 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 453 PYPEakigrfVVQNVSAqkDGEKSrvkVKVRVNTHGI---FTISTASMVEKvpTEENEMSSEADmeclnqrppENPDTDK 529
Cdd:CHL00094 465 PQIE------VTFDIDA--NGILS---VTAKDKGTGKeqsITIQGASTLPK--DEVERMVKEAE---------KNAAEDK 522
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 332841149 530 nVQQDNSEagTQPQVQTDAQQTSQsppspELTSEENKIPDADKANEKKV 578
Cdd:CHL00094 523 -EKREKID--LKNQAESLCYQAEK-----QLKELKDKISEEKKEKIENL 563
PLN03184 PLN03184
chloroplast Hsp70; Provisional
3-458 1.65e-69

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 243.99  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFG-SKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:PLN03184  41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTkNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:PLN03184 119 EESKQVSYRVVRDENGNVKLDCPAIGKQ--FAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGR 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQDlpsldeKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:PLN03184 197 IAGLEVLRIINEPTAASLAYGFEKKS------NETILVF-DLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIV 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS---NSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIE 318
Cdd:PLN03184 270 DWLASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSltqTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCK 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILspAFKVREFSVTDAV 398
Cdd:PLN03184 350 TPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVL--AGEVSDIVLLDVT 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISLiwnhdsEDTEGVH-EVFSRNHAAPFSK-----------------VLT----FLRR----GPFELEAFYSDPQGV 452
Cdd:PLN03184 428 PLSLGL------ETLGGVMtKIIPRNTTLPTSKsevfstaadgqtsveinVLQgereFVRDnkslGSFRLDGIPPAPRGV 501

                 ....*.
gi 332841149 453 PYPEAK 458
Cdd:PLN03184 502 PQIEVK 507
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
3-404 6.97e-69

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 242.23  E-value: 6.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFG-SKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQ 81
Cdd:PRK13410   4 IVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE--LD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  82 KEKENLSYDLVPLKNGGVGIKVMYMGEEhlFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:PRK13410  82 PESKRVPYTIRRNEQGNVRIKCPRLERE--FAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 162 IVGLNCLRLMNDMTAVALNYGIYKQdlpsldEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:PRK13410 160 IAGLEVERILNEPTAAALAYGLDRS------SSQTVLVF-DLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 242 EHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSS-NSTDL-----------PLNIECfmndkdvsgKMNRSQFEEL 309
Cdd:PRK13410 233 DWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGvSVTDIslpfitatedgPKHIET---------RLDRKQFESL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 310 CAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILspAFKV 389
Cdd:PRK13410 304 CGDLLDRLLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGIL--AGEL 381
                        410
                 ....*....|....*
gi 332841149 390 REFSVTDAVPFPISL 404
Cdd:PRK13410 382 KDLLLLDVTPLSLGL 396
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
3-434 1.17e-66

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 235.74  E-value: 1.17e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:PTZ00186  29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  83 EKENLSYDLVPLKNGGVGIKvmyMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:PTZ00186 109 DIKNVPYKIVRAGNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 163 VGLNCLRLMNDMTAVALNYGIYKQdlpsldeKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDKT-------KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 243 HFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKD----VSGKMNRSQFEELCAELLQKIE 318
Cdd:PTZ00186 259 YILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSS-AMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSI 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 319 VPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPafKVREFSVTDAV 398
Cdd:PTZ00186 338 APCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRG--DVKGLVLLDVT 415
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 332841149 399 PFPISliwnhdsedTEGVHEVFSR----NHAAPFSKVLTF 434
Cdd:PTZ00186 416 PLSLG---------IETLGGVFTRmipkNTTIPTKKSQTF 446
hscA PRK05183
chaperone protein HscA; Provisional
4-383 6.56e-63

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 223.90  E-value: 6.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   4 VGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDpfIQKE 83
Cdd:PRK05183  22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  84 KENLSYDLVPLKNGGVGIKVMyMGeehLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 163
Cdd:PRK05183 100 YPHLPYQFVASENGMPLIRTA-QG---LKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 164 GLNCLRLMNDMTAVALNYGiykqdlpsLD-EKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:PRK05183 176 GLNVLRLLNEPTAAAIAYG--------LDsGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLAD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 243 HFCAEFKTKYKLDAKSKiRALLRLYQEC-EKLkklmsSNSTDLPLNIEcfmndkDVSGKMNRSQFEELCAELLQKIEVPL 321
Cdd:PRK05183 248 WILEQAGLSPRLDPEDQ-RLLLDAARAAkEAL-----SDADSVEVSVA------LWQGEITREQFNALIAPLVKRTLLAC 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332841149 322 YSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 383
Cdd:PRK05183 316 RRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADIL 377
HscA TIGR01991
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ...
3-379 1.59e-62

Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK [Protein fate, Protein folding and stabilization].


Pssm-ID: 233673 [Multi-domain]  Cd Length: 599  Bit Score: 222.14  E-value: 1.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149    3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNR-TIGVAAKNQQITHANNTVSNFKRFHGRAFNDPfiq 81
Cdd:TIGR01991   1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGvEVGKEALAAAAEDPKNTISSVKRLMGRSIEDI--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   82 KEKENLSYDLVPLKNGGVGIKVmymGEEHLFSVEqITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQ 161
Cdd:TIGR01991  78 KTFSILPYRFVDGPGEMVRLRT---VQGTVTPVE-VSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  162 IVGLNCLRLMNDMTAVALNYGIYKqdlpsldEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLV 241
Cdd:TIGR01991 154 LAGLNVLRLLNEPTAAAVAYGLDK-------ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  242 EHFCAEFKTKYKLDAKSKiRALLRLYQEC-EKLkklmsSNSTDLPLNIEcfMNDKDVSGKMNRSQFEELCAELLQKIEVP 320
Cdd:TIGR01991 227 KWILKQLGISADLNPEDQ-RLLLQAARAAkEAL-----TDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSI 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332841149  321 LYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQ 379
Cdd:TIGR01991 299 CRRALRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQ 357
hscA PRK01433
chaperone protein HscA; Provisional
3-379 1.72e-35

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 141.91  E-value: 1.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149   3 VVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGvaaknqqithANNTVSNFKRFHGRAFNDPFIQK 82
Cdd:PRK01433  21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG----------NNKGLRSIKRLFGKTLKEILNTP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149  83 EKENLSYDLVPLKNGGVGIKVmymgEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQI 162
Cdd:PRK01433  91 ALFSLVKDYLDVNSSELKLNF----ANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 163 VGLNCLRLMNDMTAVALNYGIYKqdlpslDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVE 242
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGLNK------NQKGCYLVY-DLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 243 HFCAEFKTKYKLDAkskirallrlYQECEKLKKLMSSNstdlplniECFMNDKdVSgkMNRSQFEELCAELLQKIEVPLY 322
Cdd:PRK01433 240 YLCNKFDLPNSIDT----------LQLAKKAKETLTYK--------DSFNNDN-IS--INKQTLEQLILPLVERTINIAQ 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332841149 323 SLLEQThlKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQ 379
Cdd:PRK01433 299 ECLEQA--GNPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQ 353
PRK13929 PRK13929
rod-share determining protein MreBH; Provisional
118-375 1.72e-04

rod-share determining protein MreBH; Provisional


Pssm-ID: 184403 [Multi-domain]  Cd Length: 335  Bit Score: 43.36  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 118 TAMLLTKLKETAEN---SLKKPvtDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNygiykQDLPSldEK 194
Cdd:PRK13929  78 TDLLKQIMKKAGKNigmTFRKP--NVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIG-----ADLPV--DE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 195 PRIVVFVDMGHSAFQVSACAFNKgklkvLGTAFDPFLGGKNFDEKLVEHfcaeFKTKYKLDAKSKIRALLRL---YQECE 271
Cdd:PRK13929 149 PVANVVVDIGGGTTEVAIISFGG-----VVSCHSIRIGGDQLDEDIVSF----VRKKYNLLIGERTAEQVKMeigYALIE 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 272 KLKKLMSSNSTD----LPLNIEcfMNDKDVSGKMNRSqfeelcaeLLQKIEVpLYSLLEQTHLKVE-DV--SAVEIVGGA 344
Cdd:PRK13929 220 HEPETMEVRGRDlvtgLPKTIT--LESKEIQGAMRES--------LLHILEA-IRATLEDCPPELSgDIvdRGVILTGGG 288
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332841149 345 TRIPAVKERIAKFFGKDISTTLNADEAVARG 375
Cdd:PRK13929 289 ALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
PRK03427 PRK03427
cell division protein ZipA; Provisional
519-594 8.95e-03

cell division protein ZipA; Provisional


Pssm-ID: 235124 [Multi-domain]  Cd Length: 333  Bit Score: 37.71  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332841149 519 QRPPENPDTDKNVQQdnseaGTQPQVQTDAQQTSQSPPSPELTSEENKiPDADKANEKKVDQPPEAKKPKIK----VVNV 594
Cdd:PRK03427 130 QQPAYQPQPEQPLQQ-----PVSPQVAPAPQPVHSAPQPAQQAFQPAE-PVAAPQPEPVAEPAPVMDKPKRKeaviVMNV 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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