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Conserved domains on  [gi|13242237|ref|NP_077327|]
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heat shock cognate 71 kDa protein [Rattus norvegicus]

Protein Classification

heat shock 70 family protein( domain architecture ID 999982)

heat shock 70 family protein similar to endoplasmic reticulum chaperone BiP that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00009 super family cl36495
heat shock 70 kDa protein; Provisional
1-613 0e+00

heat shock 70 kDa protein; Provisional


The actual alignment was detected with superfamily member PTZ00009:

Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 1169.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    1 MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDD 80
Cdd:PTZ00009   1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   81 AVVQSDMKHWPFMVVNDA-GRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATK 159
Cdd:PTZ00009  81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  160 DAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  240 HFIAEFKRKHK-KDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  319 KALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  399 LSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  479 DIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13242237  559 QGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQS 613
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQA 615
 
Name Accession Description Interval E-value
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-613 0e+00

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 1169.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    1 MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDD 80
Cdd:PTZ00009   1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   81 AVVQSDMKHWPFMVVNDA-GRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATK 159
Cdd:PTZ00009  81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  160 DAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  240 HFIAEFKRKHK-KDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  319 KALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  399 LSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  479 DIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13242237  559 QGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQS 613
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQA 615
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
6-612 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: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 951.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237     6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    86 DMKHWPFMVVNDA-GRPKVQVEYKGETksFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:pfam00012  81 DIKHLPYKVVKLPnGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   165 AGLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   245 FKRKHKKDISENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYE-GIDFYTSITRARFEELNADLFRGTLDPVEKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   323 DAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksENVQDLLLLDVTPLSLG 402
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   403 IETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   483 NGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKlqGKI 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKV 551
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13242237   563 NDEDKQKIldkcNEIISWLDKN-QTAEKEEFEHQQKELEKVCNPIITKLYQ 612
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
6-380 0e+00

nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) 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), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. 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).


Pssm-ID: 466831 [Multi-domain]  Cd Length: 375  Bit Score: 913.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:cd10233   1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 DMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd10233  81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEF 245
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 246 KRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAK 325
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13242237 326 LDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
6-612 0e+00

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: 274091 [Multi-domain]  Cd Length: 595  Bit Score: 806.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237     6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDavVQ 84
Cdd:TIGR02350   2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    85 SDMKHWPFMVVNDAGRPKVQVEykgeTKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:TIGR02350  80 EEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   165 AGLNVLRIINEPTAAAIAYGLDKKVGAERnVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   245 FKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSITRARFEELNADLFRGTLDPVEKA 320
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   321 LRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTPLS 400
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTPLS 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   401 LGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI 480
Cdd:TIGR02350 390 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDI 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   481 DANGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKlqG 560
Cdd:TIGR02350 470 DANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAG--D 546
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13242237   561 KINDEDKQKILDKCNEIISWLDKNqtaEKEEFEHQQKELEKVCNPIITKLYQ 612
Cdd:TIGR02350 547 KLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
6-519 0e+00

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 693.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDavvq 84
Cdd:COG0443   1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  85 sdmkhwpfmvvndagrpkVQVEYKGETKSfyPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:COG0443  77 ------------------EATEVGGKRYS--PEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 FKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDsLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDKSEnvqdlllLDVTPLSLGIE 404
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
                       490       500       510
                ....*....|....*....|....*....|....*
gi 13242237 485 ILNVSAVDKSTGKENKITItndkgrlsKEDIERMV 519
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
 
Name Accession Description Interval E-value
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-613 0e+00

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 1169.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    1 MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDD 80
Cdd:PTZ00009   1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   81 AVVQSDMKHWPFMVVNDA-GRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATK 159
Cdd:PTZ00009  81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  160 DAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  240 HFIAEFKRKHK-KDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  319 KALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  399 LSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  479 DIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13242237  559 QGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQS 613
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQA 615
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
6-612 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: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 951.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237     6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    86 DMKHWPFMVVNDA-GRPKVQVEYKGETksFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:pfam00012  81 DIKHLPYKVVKLPnGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   165 AGLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   245 FKRKHKKDISENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYE-GIDFYTSITRARFEELNADLFRGTLDPVEKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   323 DAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksENVQDLLLLDVTPLSLG 402
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   403 IETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   483 NGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKlqGKI 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKV 551
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13242237   563 NDEDKQKIldkcNEIISWLDKN-QTAEKEEFEHQQKELEKVCNPIITKLYQ 612
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
6-380 0e+00

nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) 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), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. 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).


Pssm-ID: 466831 [Multi-domain]  Cd Length: 375  Bit Score: 913.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:cd10233   1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 DMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd10233  81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEF 245
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 246 KRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAK 325
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13242237 326 LDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
dnaK PRK00290
molecular chaperone DnaK; Provisional
1-613 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 874.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    1 MSKgpAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFD 79
Cdd:PRK00290   1 MGK--IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   80 DavVQSDMKHWPFMVVN-DAGRPKVQVEykgeTKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQAT 158
Cdd:PRK00290  79 E--VQKDIKLVPYKIVKaDNGDAWVEID----GKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  159 KDAGTIAGLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMV 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDKK--GDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRII 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  239 NHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIeidSLyegiDFYT-----------SITRARFEELNA 307
Cdd:PRK00290 231 DYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEI---NL----PFITadasgpkhleiKLTRAKFEELTE 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  308 DLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksen 387
Cdd:PRK00290 304 DLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD---- 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  388 VQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPA 467
Cdd:PRK00290 379 VKDVLLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPA 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  468 PRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAF 547
Cdd:PRK00290 459 PRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIY 537
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13242237  548 NMKATVEDekLQGKINDEDKQKILDKCNEIISWLDKNqtaEKEEFEHQQKELEKVCNPIITKLYQS 613
Cdd:PRK00290 538 QTEKTLKE--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQ 598
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
6-612 0e+00

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: 274091 [Multi-domain]  Cd Length: 595  Bit Score: 806.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237     6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDavVQ 84
Cdd:TIGR02350   2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    85 SDMKHWPFMVVNDAGRPKVQVEykgeTKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:TIGR02350  80 EEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   165 AGLNVLRIINEPTAAAIAYGLDKKVGAERnVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   245 FKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSITRARFEELNADLFRGTLDPVEKA 320
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   321 LRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTPLS 400
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTPLS 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   401 LGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI 480
Cdd:TIGR02350 390 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDI 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   481 DANGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKlqG 560
Cdd:TIGR02350 470 DANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAG--D 546
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13242237   561 KINDEDKQKILDKCNEIISWLDKNqtaEKEEFEHQQKELEKVCNPIITKLYQ 612
Cdd:TIGR02350 547 KLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
ASKHA_NBD_HSP70_BiP cd10241
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ...
4-380 0e+00

nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. 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).


Pssm-ID: 466837 [Multi-domain]  Cd Length: 376  Bit Score: 760.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVV 83
Cdd:cd10241   1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  84 QSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGT 163
Cdd:cd10241  81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 164 IAGLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIA 243
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKK-GGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 244 EFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRD 323
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13242237 324 AKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
ASKHA_NBD_HSP70_HSPA1-like cd24028
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ...
6-380 0e+00

nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family 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), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members 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).


Pssm-ID: 466878 [Multi-domain]  Cd Length: 376  Bit Score: 756.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:cd24028   1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 DMKHWPFMVVNDA-GRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:cd24028  81 DIKHWPFKVVEDEdGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 FKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13242237 325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
4-612 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 703.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAv 82
Cdd:PRK13411   2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   83 vQSDMKHWPFMVVNdaGRPK-VQVEYKGetKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDA 161
Cdd:PRK13411  81 -EEERSRVPYTCVK--GRDDtVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  162 GTIAGLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQ-DQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  242 IAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDslyegidFYTS-----------ITRARFEELNADLF 310
Cdd:PRK13411 235 VENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLP-------FITAdetgpkhlemeLTRAKFEELTKDLV 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  311 RGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDksenVQD 390
Cdd:PRK13411 308 EATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKD 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  391 LLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRG 470
Cdd:PRK13411 384 LLLLDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRG 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  471 VPQIEVTFDIDANGILNVSAVDKSTGKENKITITNdKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMK 550
Cdd:PRK13411 464 VPQIEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYE 542
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13242237  551 ATVEDEKlqGKINDEDKQKILDKCNEIISWLDkNQTAEKEEFEHQQKELEKVCNPIITKLYQ 612
Cdd:PRK13411 543 STLKENG--ELISEELKQRAEQKVEQLEAALT-DPNISLEELKQQLEEFQQALLAIGAEVYQ 601
dnaK CHL00094
heat shock protein 70
4-613 0e+00

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 701.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDav 82
Cdd:CHL00094   2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   83 VQSDMKHWPFMVVNDaGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAG 162
Cdd:CHL00094  80 ISEEAKQVSYKVKTD-SNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  163 TIAGLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFI 242
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKK--NNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  243 AEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG-IDFYTSITRARFEELNADLFRGTLDPVE 318
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  319 KALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTP 398
Cdd:CHL00094 317 NALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTP 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  399 LSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTF 478
Cdd:CHL00094 392 LSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTF 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  479 DIDANGILNVSAVDKSTGKENKITITNdKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDekL 558
Cdd:CHL00094 472 DIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--L 548
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 13242237  559 QGKINDEDKQKIldkcNEIISWLDKN-QTAEKEEFEHQQKELEKVCNPIITKLYQS 613
Cdd:CHL00094 549 KDKISEEKKEKI----ENLIKKLRQAlQNDNYESIKSLLEELQKALMEIGKEVYSS 600
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
6-519 0e+00

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 693.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDavvq 84
Cdd:COG0443   1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  85 sdmkhwpfmvvndagrpkVQVEYKGETKSfyPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:COG0443  77 ------------------EATEVGGKRYS--PEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 FKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDsLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDKSEnvqdlllLDVTPLSLGIE 404
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
                       490       500       510
                ....*....|....*....|....*....|....*
gi 13242237 485 ILNVSAVDKSTGKENKITItndkgrlsKEDIERMV 519
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
4-613 0e+00

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 686.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAV 82
Cdd:PTZ00400  41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   83 VQSDMKHWPFMVV----NDAgrpkvQVEYKGetKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQAT 158
Cdd:PTZ00400 121 TKKEQKILPYKIVrasnGDA-----WIEAQG--KKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQAT 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  159 KDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGaeRNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMV 238
Cdd:PTZ00400 194 KDAGKIAGLDVLRIINEPTAAALAFGMDKNDG--KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRIL 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  239 NHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDslyegidFYTS-----------ITRARFEELNA 307
Cdd:PTZ00400 272 NYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLP-------FITAdqsgpkhlqikLSRAKLEELTH 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  308 DLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksen 387
Cdd:PTZ00400 345 DLLKKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE---- 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  388 VQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPA 467
Cdd:PTZ00400 420 IKDLLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPA 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  468 PRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAF 547
Cdd:PTZ00400 500 PRGVPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIY 578
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13242237  548 NMKATVEDekLQGKINDEDKQKILDKCNEIISWLdknQTAEKEEFEHQQKELEKVCNPIITKLYQS 613
Cdd:PTZ00400 579 SVEKQLSD--LKDKISDADKDELKQKITKLRSTL---SSEDVDSIKDKTKQLQEASWKISQQAYKQ 639
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
4-544 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 663.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDav 82
Cdd:PRK13410   2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   83 VQSDMKHWPFMV-VNDAGrpKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDA 161
Cdd:PRK13410  80 LDPESKRVPYTIrRNEQG--NVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  162 GTIAGLNVLRIINEPTAAAIAYGLDKkvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  242 IAEFKRKHKKDISENKRAVRRLRTACERAKRTLS--SSTQASIE-IDSLYEG---IDfyTSITRARFEELNADLFRGTLD 315
Cdd:PRK13410 236 AEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLR 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  316 PVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLD 395
Cdd:PRK13410 314 PVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLD 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  396 VTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIE 475
Cdd:PRK13410 389 VTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQ 468
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13242237  476 VTFDIDANGILNVSAVDKSTGKENKITITNdKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLES 544
Cdd:PRK13410 469 VAFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALT 536
ASKHA_NBD_HSP70_Ssb cd24093
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ...
6-380 0e+00

nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily 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).


Pssm-ID: 466943 [Multi-domain]  Cd Length: 375  Bit Score: 645.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:cd24093   1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 DMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd24093  80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLD-KKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 FKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13242237 325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
PLN03184 PLN03184
chloroplast Hsp70; Provisional
7-599 0e+00

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 629.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDavVQS 85
Cdd:PLN03184  42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   86 DMKHWPFMVVNDAGrPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:PLN03184 120 ESKQVSYRVVRDEN-GNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  166 GLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEF 245
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEKK--SNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  246 KRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG---IDfyTSITRARFEELNADLFRGTLDPVEK 319
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVEN 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  320 ALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFfNGKELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTPL 399
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPL 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  400 SLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFD 479
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  480 IDANGILNVSAVDKSTGKENKITITNdKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDekLQ 559
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--LG 586
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|.
gi 13242237  560 GKINDEDKQKILDKCNEIISWLDKNQTAE-KEEFEHQQKEL 599
Cdd:PLN03184 587 DKVPADVKEKVEAKLKELKDAIASGSTQKmKDAMAALNQEV 627
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
3-601 0e+00

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 600.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    3 KGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAV 82
Cdd:PTZ00186  26 QGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   83 VQSDMKHWPFMVVNDA-GRPKVQveyKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDA 161
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGnGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  162 GTIAGLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PTZ00186 183 GTIAGLNVIRVVNEPTAAALAYGMDKT--KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYI 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  242 IAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSITRARFEELNADLFRGTLDPV 317
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPC 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  318 EKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVT 397
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVT 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  398 PLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVT 477
Cdd:PTZ00186 416 PLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVT 495
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  478 FDIDANGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAfnmkATVEDEK 557
Cdd:PTZ00186 496 FDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQL----TTAERQL 570
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 13242237  558 LQGK-INDEDKQKILDKCNEIISWLDkNQTAEKEEFEHQQKELEK 601
Cdd:PTZ00186 571 GEWKyVSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQK 614
hscA PRK05183
chaperone protein HscA; Provisional
6-544 0e+00

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 564.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDavVQS 85
Cdd:PRK05183  21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   86 DMKHWPF-MVVNDAGRPKVQVeyKGETKSfyPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:PRK05183  99 RYPHLPYqFVASENGMPLIRT--AQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  165 AGLNVLRIINEPTAAAIAYGLDKkvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDS--GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  245 FKRKHKKDISEnkraVRRLRTACERAKRTLSSSTQASIEIdSLYEGIdfytsITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:PRK05183 253 AGLSPRLDPED----QRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRDA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDKSENvqDLLLLDVTPLSLGIE 404
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLE 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:PRK05183 400 TMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADG 479
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13242237  485 ILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQR----DKVSSKNSLES 544
Cdd:PRK05183 480 LLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA 542
ASKHA_NBD_HSP70_DnaK-like cd10234
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ...
7-381 0e+00

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins; This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all 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); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 466832 [Multi-domain]  Cd Length: 373  Bit Score: 549.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:cd10234   2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 DMKHWPfmvVNDAGRPKVQVEYKGetKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd10234  82 KQVPYP---VVSAGNGDAWVEIGG--KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEF 245
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKK--KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 246 KRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG-IDFYTSITRARFEELNADLFRGTLDPVEKAL 321
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQAL 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 322 RDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd10234 315 KDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
HscA TIGR01991
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ...
6-570 0e+00

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: 273915 [Multi-domain]  Cd Length: 599  Bit Score: 545.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237     6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQ 84
Cdd:TIGR01991   1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    85 SDMkhwPFMVVNDAGRpKVQVEYKGETKSfyPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:TIGR01991  81 SIL---PYRFVDGPGE-MVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   165 AGLNVLRIINEPTAAAIAYGLDKkvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDK--ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   245 FKRKHKKDISENKRAVRRLRTACERAkrtlssSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:TIGR01991 233 LGISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSGDKSENvqDLLLLDVTPLSLGIE 404
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGIE 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:TIGR01991 384 TMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADG 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   485 ILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEKYKAEDEKQR----DKVSSKNSLESYAfnmKATVEDEKLqg 560
Cdd:TIGR01991 464 LLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARalaeQKVEAERILEALQ---AALAADGDL-- 537
                         570
                  ....*....|
gi 13242237   561 kINDEDKQKI 570
Cdd:TIGR01991 538 -LSEDERAAI 546
ASKHA_NBD_HSP70_HSPA9 cd11733
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ...
4-380 8.83e-174

nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup 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).


Pssm-ID: 466839 [Multi-domain]  Cd Length: 377  Bit Score: 499.48  E-value: 8.83e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAV 82
Cdd:cd11733   1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  83 VQSDMKHWPFMVV----NDAgrpkvQVEYKGetKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQAT 158
Cdd:cd11733  81 VQKDIKMVPYKIVkasnGDA-----WVEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQAT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 159 KDAGTIAGLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMV 238
Cdd:cd11733 154 KDAGQIAGLNVLRIINEPTAAALAYGLDKK--DDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 239 NHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQAsiEIDSLYEGID------FYTSITRARFEELNADLFRG 312
Cdd:cd11733 232 NYLVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKR 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13242237 313 TLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11733 310 TVEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
ASKHA_NBD_HSP70_Ssc1_3 cd11734
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ...
4-382 7.03e-161

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.


Pssm-ID: 466840 [Multi-domain]  Cd Length: 378  Bit Score: 466.54  E-value: 7.03e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAV 82
Cdd:cd11734   1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  83 VQSDMKHWPFMVV----NDAgrpkvQVEYKGETKSfyPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQAT 158
Cdd:cd11734  81 VQRDIKEVPYKIVkhsnGDA-----WVEARGQKYS--PSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQAT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 159 KDAGTIAGLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMV 238
Cdd:cd11734 154 KDAGQIAGLNVLRVINEPTAAALAYGLDKS--GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 239 NHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSITRARFEELNADLFRGTL 314
Cdd:cd11734 232 RHIVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTV 311
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13242237 315 DPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSG 382
Cdd:cd11734 312 EPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
ASKHA_NBD_HSP70_HSPA13 cd10237
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ...
7-382 2.19e-152

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. 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). HSPA13 contains an NBD but lacks an SBD. It 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: 466835 [Multi-domain]  Cd Length: 409  Bit Score: 446.02  E-value: 2.19e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVV 83
Cdd:cd10237  25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  84 QSDMKHWPFMVVND-AGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAG 162
Cdd:cd10237 105 EEEAKRYPFKVVNDnIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 163 TIAGLNVLRIINEPTAAAIAYGLDKKVGAErNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFI 242
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKKSDVN-NVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 243 AEFKRKHKKDISeNKRAVRRLRTACERAKRTLSS--STQASIEIDSLYEGID---FYTSITRARFEELNADLFRGTLDPV 317
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEPI 342
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13242237 318 EKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSG 382
Cdd:cd10237 343 RQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
ASKHA_NBD_HSP70_HSPA14 cd10238
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ...
5-380 1.37e-147

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. 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.


Pssm-ID: 466836 [Multi-domain]  Cd Length: 377  Bit Score: 432.44  E-value: 1.37e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   5 PAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQ 84
Cdd:cd10238   1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  85 SDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:cd10238  81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKVGAE-RNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIA 243
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTEnSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 244 EFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRD 323
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNS 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13242237 324 AKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10238 321 AGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
6-382 2.83e-147

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily 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). 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: 466834 [Multi-domain]  Cd Length: 367  Bit Score: 431.25  E-value: 2.83e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVAMNPTNTVFDAKRLIGRRFDDavVQ 84
Cdd:cd10236   4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  85 SDMKHWPFMVVNDagrPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:cd10236  82 EELPLLPYRLVGD---ENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKvgAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQK--KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQ 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 FkrkhKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSlyEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:cd10236 237 I----GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13242237 325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILSG 382
Cdd:cd10236 311 GLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
ASKHA_NBD_HSP70_HSP105-110-like cd11732
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ...
7-378 1.32e-144

nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all 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).


Pssm-ID: 466838 [Multi-domain]  Cd Length: 377  Bit Score: 425.05  E-value: 1.32e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSD 86
Cdd:cd11732   1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPF-MVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd11732  81 IKLLPFkLVELEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKKVGAE-----RNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLEseekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 241 FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKA 320
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13242237 321 LRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
7-381 2.92e-143

nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all 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); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 466879 [Multi-domain]  Cd Length: 351  Bit Score: 420.44  E-value: 2.92e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFddavvq 84
Cdd:cd24029   1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  85 sdmkhWPFMVVNDagrpkvqveykgetKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:cd24029  75 -----KDKEEIGG--------------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKVGAErNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAE 244
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDG-TILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 FKRKH-KKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRD 323
Cdd:cd24029 215 IGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13242237 324 AKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
ASKHA_NBD_HSP70_AtHsp70-14-like cd24095
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ...
6-381 3.05e-140

nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and similar proteins; The subgroup includes Arabidopsis thaliana Hsp70-14, also known as heat shock 70 kDa protein 14; heat shock protein 91), Hsp70-15 (also known as heat shock 70 kDa protein 15), and Hsp70-16 (also known as heat shock 70 kDa protein 16). In cooperation with other chaperones, they are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. Members in this subgroup belong 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: 466945 [Multi-domain]  Cd Length: 389  Bit Score: 414.02  E-value: 3.05e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQS 85
Cdd:cd24095   3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 DMKHWPFMVVNDA-GRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTI 164
Cdd:cd24095  83 DLKLFPFKVTEGPdGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGL---DKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIyktDLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 242 IAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKAL 321
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 322 RDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
ASKHA_NBD_HSP70_HSPA4_like cd10228
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ...
7-378 1.86e-132

nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong 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: 466826 [Multi-domain]  Cd Length: 378  Bit Score: 393.95  E-value: 1.86e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSD 86
Cdd:cd10228   1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPFMVVNDA-GRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd10228  81 LKHLPYKVVKLPnGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYG-----LDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGiykqdLPAEEEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 241 FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEK 319
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13242237 320 ALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
ASKHA_NBD_HSP70_HscC cd10235
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ...
7-379 4.05e-127

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily 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). 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: 466833 [Multi-domain]  Cd Length: 343  Bit Score: 378.90  E-value: 4.05e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPTNTVFDAKRLIGrrfddavvqs 85
Cdd:cd10235   1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 dmkhwpfmvvNDAgrpkvqvEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd10235  71 ----------TDK-------QYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKKvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIaef 245
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKR-EDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFL--- 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 246 kRKHKKDISENKRAVR-RLRTACERAKRTLSSstQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDA 324
Cdd:cd10235 210 -KKHRLDFTSLSPSELaALRKRAEQAKRQLSS--QDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13242237 325 KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAI 379
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
ASKHA_NBD_HSP70_ScSse cd24094
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ...
7-381 7.98e-122

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong 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: 466944 [Multi-domain]  Cd Length: 385  Bit Score: 366.70  E-value: 7.98e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSD 86
Cdd:cd24094   1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAG 166
Cdd:cd24094  81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 167 LNVLRIINEPTAAAIAYG---LDKKVGAE--RNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGitkTDLPEPEEkpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 242 IAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKAL 321
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 322 RDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
ASKHA_NBD_HSP70_HYOU1 cd10230
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ...
7-378 4.40e-115

nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act 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. Members in this subgroup 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).


Pssm-ID: 466828 [Multi-domain]  Cd Length: 353  Bit Score: 348.33  E-value: 4.40e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGrrfddavvqs 85
Cdd:cd10230   3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  86 dmkhwpfmvvndagrpkvqveykgetksFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd10230  73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKKVGAE--RNVLIFDLGGGTFDVSILTI------EDGI------FEVKSTAGDTHLGGE 231
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNepQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 232 DFDNRMVNHFIAEFKRKHKK--DISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADL 309
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13242237 310 FRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
ASKHA_NBD_HSP70_ScSsz1p-like cd10232
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ...
5-380 4.33e-104

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily 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.


Pssm-ID: 466830 [Multi-domain]  Cd Length: 349  Bit Score: 319.69  E-value: 4.33e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   5 PAVGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGrrfddavv 83
Cdd:cd10232   1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  84 qsdmkhwpfmvvndagrpkvqveykgeTKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGT 163
Cdd:cd10232  73 ---------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 164 IAGLNVLRIINEPTAAAIAYGLDKK----VGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAEtsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 240 HFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEK 319
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13242237 320 ALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNG---KELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
hscA PRK01433
chaperone protein HscA; Provisional
6-524 3.47e-103

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 325.66  E-value: 3.47e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvamnpTNTVFDAKRLIGRRFDD----A 81
Cdd:PRK01433  21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEilntP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   82 VVQSDMKHwpFMVVNDAgrpkvQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDA 161
Cdd:PRK01433  91 ALFSLVKD--YLDVNSS-----ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  162 GTIAGLNVLRIINEPTAAAIAYGLDKkvGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNK--NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  242 IAEFKRKHKKDISEnkravrrlrtACERAKRTLSSstQASIEIDSLyegidfytSITRARFEELNADLFRGTLDPVEKAL 321
Cdd:PRK01433 242 CNKFDLPNSIDTLQ----------LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  322 RDAKldKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNkSINPDEAVAYGAAVQAAILSGDKsenvQDLLLLDVTPLSL 401
Cdd:PRK01433 302 EQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLSL 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  402 GIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDID 481
Cdd:PRK01433 375 GMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAID 454
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 13242237  482 ANGILNVSAVDKSTGKENKITITNDKGrLSKEDIERMVQEAEK 524
Cdd:PRK01433 455 ADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYK 496
ASKHA_NBD_HSP70_HSPA4 cd11737
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ...
7-379 6.87e-98

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, 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: 466843 [Multi-domain]  Cd Length: 381  Bit Score: 304.94  E-value: 6.87e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSD 86
Cdd:cd11737   3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPFMVVN-DAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd11737  83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKK-----VGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQdlpapEEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 241 FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEK 319
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 320 ALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAI 379
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
7-381 1.17e-93

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It 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: 466844 [Multi-domain]  Cd Length: 383  Bit Score: 294.13  E-value: 1.17e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSD 86
Cdd:cd11738   3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPFMVVN-DAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd11738  83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKK-----VGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQdlpalEEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 241 FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEK 319
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13242237 320 ALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
ASKHA_NBD_HSP70_HSPH1 cd11739
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ...
7-378 9.69e-93

nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. 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: 466845 [Multi-domain]  Cd Length: 380  Bit Score: 291.76  E-value: 9.69e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSD 86
Cdd:cd11739   3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPF-MVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIA 165
Cdd:cd11739  83 KENLSYdLVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 166 GLNVLRIINEPTAAAIAYGLDKK--VGAERN---VLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQdlPAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 241 FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEK 319
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13242237 320 ALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
7-375 5.69e-63

nucleotide-binding domain (NBD) 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. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 211.58  E-value: 5.69e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVgvfqhgkveiiandqgnrttpsyvAFTDTERligdaaknqvamnptntvfdakrligrrfDDAVVQSD 86
Cdd:cd10170   1 VGIDFGTTYSGV------------------------AYALLGP-----------------------------GEPPLVVL 27
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  87 MKHWPFmvvNDAGRPKVQVEYkgetksfypeEVSSMVLTKMKEIAEAYLG-------KTVTNAVVTVPAYFNDSQRQATK 159
Cdd:cd10170  28 QLPWPG---GDGGSSKVPSVL----------EVVADFLRALLEHAKAELGdriweleKAPIEVVITVPAGWSDAAREALR 94
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 160 DAGTIAGL----NVLRIINEPTAAAIAYGLDK----KVGAERNVLIFDLGGGTFDVSILTIEDGIFEVK---STAGDTHL 228
Cdd:cd10170  95 EAARAAGFgsdsDNVRLVSEPEAAALYALEDKgdllPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALL 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 229 GGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID---FYTSITRARFEEL 305
Cdd:cd10170 175 GGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEE 254
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13242237 306 NADLFRGTLDPVEKALRDA--KLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN---KSINPDEAVAYGAAV 375
Cdd:cd10170 255 IRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
ASKHA_NBD_HSP70_YegD-like cd10231
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ...
7-354 2.79e-33

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 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: 466829 [Multi-domain]  Cd Length: 409  Bit Score: 132.40  E-value: 2.79e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE------RLIGDAAKNQVAMNPTNTVF--DAKRLIG-RR 77
Cdd:cd10231   1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGsSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  78 FDDAVVQSdmKHWPFmvvndagrpkvqveykgetksfypEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQA 157
Cdd:cd10231  81 FDETTIFG--RRYPF------------------------EDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAED 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 158 T-------KDAGTIAGLNVLRIINEPTAAAIAYglDKKVGAERNVLIFDLGGGTFDVSIL----TIEDGIFEVKSTAGDt 226
Cdd:cd10231 135 DaqaesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLrlgpNRTDRRADILATSGV- 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 227 HLGGEDFDNRMVNHFIA-----------------------------------------EFKRKHKKDISENKRAVR---- 261
Cdd:cd10231 212 GIGGDDFDRELALKKVMphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktlRLLLDLRRDAADPEKIERllsl 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 262 -------RLRTACERAKRTLSSSTQASIEIDSLYEGIDfyTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDI 334
Cdd:cd10231 292 vedqlghRLFRAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
                       410       420
                ....*....|....*....|
gi 13242237 335 VLVGGSTRIPKIQKLLQDFF 354
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF 389
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
7-374 4.71e-21

nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, 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. Both HSPA12A and HSPA12B 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 and HSPA12B.


Pssm-ID: 466827 [Multi-domain]  Cd Length: 372  Bit Score: 95.42  E-value: 4.71e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVAMNPTNtvfDAKRLI 74
Cdd:cd10229   3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDE---EHQWLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  75 GRRFDDAVVQSDMKHWPFMVVNDAGrpkvqveykgetKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNA--------VVTV 146
Cdd:cd10229  80 FFKFKMMLLSEKELTRDTKVKAVNG------------KSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 147 PAYFNDSQRQATKDAGTIAGL------NVLRIINEPTAAAIAYGLDKKVGAE------RNVLIFDLGGGTFDVSILTI-E 213
Cdd:cd10229 148 PAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGEEkelkpgDKYLVVDCGGGTVDITVHEVlE 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 214 DGIFEVKSTAGDTHLGGEDFDNRMVN--------HFIAEFKRKHKKDISENKRAVrrlrtacERAKRTlssstqasieiD 285
Cdd:cd10229 228 DGKLEELLKASGGPWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLDLLQAF-------ERKKRS-----------F 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 286 SLYegidfytsITRARFEELNADLFRGTLDPVEKALRDAKLDKsqIHDIVLVGGSTRIPKIQKLLQDFFNGKelNKSI-- 363
Cdd:cd10229 290 KLR--------LSPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTK--VKIIip 357
                       410
                ....*....|..
gi 13242237 364 -NPDEAVAYGAA 374
Cdd:cd10229 358 pEPGLAVVKGAV 369
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
7-375 5.33e-17

nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 82.52  E-value: 5.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCVgvFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntvfDAKRLIGRRFDDAVV 83
Cdd:cd10225   2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  84 qsdmkHWPFM--VVNDagrpkvqveykgetksfypEEVSSMVLTKMkeIAEAYLGKTVTN--AVVTVPAYFNDSQRQATK 159
Cdd:cd10225  58 -----IRPLRdgVIAD-------------------FEATEAMLRYF--IRKAHRRRGFLRprVVIGVPSGITEVERRAVK 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 160 DAGTIAGLNVLRIINEPTAAAIAYGLDkkVGAERNVLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGEDFDNRMVN 239
Cdd:cd10225 112 EAAEHAGAREVYLIEEPMAAAIGAGLP--IEEPRGSMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAGDEMDEAIIN 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 240 HfiaeFKRKHKKDISEnkravrrlRTAcERAKRTLSSstqASIEIDSL---YEGIDFYTSITRARfeELNADLFR----G 312
Cdd:cd10225 185 Y----VRRKYNLLIGE--------RTA-ERIKIEIGS---AYPLDEELsmeVRGRDLVTGLPRTI--EITSEEVRealeE 246
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13242237 313 TLDPVEKALRDAkLDK------SQIHD--IVLVGGSTRIPKIQKLLQdffngKELNKSI----NPDEAVAYGAAV 375
Cdd:cd10225 247 PVNAIVEAVRST-LERtppelaADIVDrgIVLTGGGALLRGLDELLR-----EETGLPVhvadDPLTCVAKGAGK 315
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
7-374 6.75e-14

Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 440695 [Multi-domain]  Cd Length: 339  Bit Score: 73.19  E-value: 6.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntvfDAKRLIGRRFDDAVV 83
Cdd:COG1077  10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGE---------------EAKEMLGRTPGNIVA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  84 QSDMKHwpfmvvndagrpkvqveykGETKSFypeevssmvltkmkEIAEAYL---------GKTVTNA--VVTVPAYFND 152
Cdd:COG1077  66 IRPLKD-------------------GVIADF--------------EVTEAMLkyfikkvhgRRSFFRPrvVICVPSGITE 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 153 SQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDkkVGAERNVLIFDLGGGTFDVSILTIeDGIfeVKSTAgdTHLGGED 232
Cdd:COG1077 113 VERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP--IEEPTGNMVVDIGGGTTEVAVISL-GGI--VVSRS--IRVAGDE 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 233 FDNRMVNHfiaeFKRKHKKDISEnkravrrlRTAcERAKRTLSS----STQASIEIdslyEGIDFYTSITRARF---EEL 305
Cdd:COG1077 186 LDEAIIQY----VRKKYNLLIGE--------RTA-EEIKIEIGSayplEEELTMEV----RGRDLVTGLPKTITitsEEI 248
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13242237 306 nADLFRGTLDPVEKALRDAkLDK------SQIHD--IVLVGGSTRIPKIQKLLQDFFNgkeLNKSI--NPDEAVAYGAA 374
Cdd:COG1077 249 -REALEEPLNAIVEAIKSV-LEKtppelaADIVDrgIVLTGGGALLRGLDKLLSEETG---LPVHVaeDPLTCVARGTG 322
PRK13930 PRK13930
rod shape-determining protein MreB; Provisional
141-374 1.24e-12

rod shape-determining protein MreB; Provisional


Pssm-ID: 237564 [Multi-domain]  Cd Length: 335  Bit Score: 69.39  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  141 NAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLD--KKVGAernvLIFDLGGGTFDVSILTIeDGIFE 218
Cdd:PRK13930 102 RIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPvtEPVGN----MVVDIGGGTTEVAVISL-GGIVY 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  219 VKSTAgdthLGGEDFDNRMVNHfiaeFKRKHKKDISEnkravrrlRTAcERAKRTLSSSTQA----SIEIdslyEGIDFY 294
Cdd:PRK13930 177 SESIR----VAGDEMDEAIVQY----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLV 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  295 TSITRARfeELNADLFRGTL-DPVEK---ALRDAkLDK------SQIHD--IVLVGGSTRIPKIQKLLQDFFnGKELNKS 362
Cdd:PRK13930 236 TGLPKTI--EISSEEVREALaEPLQQiveAVKSV-LEKtppelaADIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIA 311
                        250
                 ....*....|..
gi 13242237  363 INPDEAVAYGAA 374
Cdd:PRK13930 312 EDPLTCVARGTG 323
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
7-373 1.55e-10

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 62.96  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237     7 VGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPTNTVfdAKRLI--GRRFDDA 81
Cdd:pfam06723   4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGNEAKKMLGRTPGNIV--AVRPLkdGVIADFE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    82 VVQSDMKHWPFMVVNDAGRPKVQVeykgetksfypeevssmvltkmkeiaeaylgktvtnaVVTVPAYFNDSQRQATKDA 161
Cdd:pfam06723  73 VTEAMLKYFIKKVHGRRSFSKPRV-------------------------------------VICVPSGITEVERRAVKEA 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   162 GTIAGLNVLRIINEPTAAAIAYGLDkkVGAERNVLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGEDFDNRMVNHf 241
Cdd:pfam06723 116 AKNAGAREVFLIEEPMAAAIGAGLP--VEEPTGNMVVDIGGGTTEVAVISL-GGIVTSKS----VRVAGDEFDEAIIKY- 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   242 iaeFKRKHKKDISEnkravrrlRTAcERAKrtlssstqasIEIDSLYEGIDFYTSITRAR----------------FEEL 305
Cdd:pfam06723 188 ---IRKKYNLLIGE--------RTA-ERIK----------IEIGSAYPTEEEEKMEIRGRdlvtglpktieisseeVREA 245
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13242237   306 NADLFRGTLDPVEKALRDAKLD-KSQIHD--IVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGA 373
Cdd:pfam06723 246 LKEPVSAIVEAVKEVLEKTPPElAADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
PRK11678 PRK11678
putative chaperone; Provisional
7-351 2.63e-07

putative chaperone; Provisional


Pssm-ID: 236954 [Multi-domain]  Cd Length: 450  Bit Score: 53.33  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTErLIGDAAKNQVAMNPTNTVFDA--KRLI-GRRFDDAVV 83
Cdd:PRK11678   3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTRE-AVSEWLYRHLDVPAYDDERQAllRRAIrYNREEDIDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   84 QSD--------MKH---WP---FMVVNdagrPK----------VQVeykgetkSFYPEEVSSMVLtKMKEIAEAYLGKTV 139
Cdd:PRK11678  82 TAQsvffglaaLAQyleDPeevYFVKS----PKsflgasglkpQQV-------ALFEDLVCAMML-HIKQQAEAQLQAAI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  140 TNAVVTVPAYFN-----DSQRQAT---KDAGTIAGLNVLRIINEPTAAAIAY--GLDKkvgaERNVLIFDLGGGTFDVSI 209
Cdd:PRK11678 150 TQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE----EKRVLVVDIGGGTTDCSM 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  210 LTIedGIFEVKSTAGDTHL--------GGEDFD-----NRMVNHF----------------------------IAEF-KR 247
Cdd:PRK11678 226 LLM--GPSWRGRADRSASLlghsgqriGGNDLDialafKQLMPLLgmgsetekgialpslpfwnavaindvpaQSDFySL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  248 KHKKDISENKR------AVRRL-------------RTAcERAKRTLSSSTQASIEIDSLYEGIDfyTSITRARFEELNAd 308
Cdd:PRK11678 304 ANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EEAKIALSDQAETRASLDFISDGLA--TEISQQGLEEAIS- 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 13242237  309 lfrgtlDPVEK--ALRDAKLDKSQIH-DIV-LVGGSTRIPKIQKLLQ 351
Cdd:PRK11678 380 ------QPLARilELVQLALDQAQVKpDVIyLTGGSARSPLIRAALA 420
ASKHA_NBD_EutJ cd24047
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ...
123-228 2.69e-07

nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.


Pssm-ID: 466897 [Multi-domain]  Cd Length: 241  Bit Score: 52.27  E-value: 2.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 123 VLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLdkkvgaeRNVLIFDLGG 202
Cdd:cd24047  48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI-------RDGAVVDIGG 120
                        90       100       110
                ....*....|....*....|....*....|
gi 13242237 203 GTFDVSIltIEDGifEVKSTA----GDTHL 228
Cdd:cd24047 121 GTTGIAV--LKDG--KVVYTAdeptGGTHL 146
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
116-355 6.26e-07

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 51.52  E-value: 6.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 116 PEEVSsMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKdagtiAGLNVLRIINEPTAAAiaYGLDKKVGAERNV 195
Cdd:cd24004  45 ISKVA-ESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAA--NLLIPYDMRDLNI 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 196 LIFDLGGGTFDVSIltIEDGifEVKSTaGDTHLGGEDFDNRMVNHFiaefkrkhkkDISENKravrrlrtaCERAKRTLS 275
Cdd:cd24004 117 ALVDIGAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGF----------LISFEE---------AEKIKRTYG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 276 SST--QASIEIDSLYEGIDFYTSITRArFEELNADLFrgtldpveKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF 353
Cdd:cd24004 173 IFLliEAKDQLGFTINKKEVYDIIKPV-LEELASGIA--------NAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEK 243

                ..
gi 13242237 354 FN 355
Cdd:cd24004 244 LG 245
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
143-268 9.69e-07

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 51.06  E-value: 9.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  143 VVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLD--KKVGAernvLIFDLGGGTFDVSILTIEdGIFEVK 220
Cdd:PRK13928  99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGN----MVVDIGGGTTDIAVLSLG-GIVTSS 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 13242237  221 StagdTHLGGEDFDNRMVNHfiaeFKRKHKKDISEnkravrrlRTACE 268
Cdd:PRK13928 174 S----IKVAGDKFDEAIIRY----IRKKYKLLIGE--------RTAEE 205
PRK15080 PRK15080
ethanolamine utilization protein EutJ; Provisional
123-228 1.21e-06

ethanolamine utilization protein EutJ; Provisional


Pssm-ID: 237904 [Multi-domain]  Cd Length: 267  Bit Score: 50.21  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  123 VLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKkvGAernvlIFDLGG 202
Cdd:PRK15080  72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDN--GA-----VVDIGG 144
                         90       100       110
                 ....*....|....*....|....*....|
gi 13242237  203 GTFDVSILtiEDGifEVKSTA----GDTHL 228
Cdd:PRK15080 145 GTTGISIL--KDG--KVVYSAdeptGGTHM 170
ASKHA_NBD_HSP70_HSPA12A cd11735
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ...
143-357 2.81e-06

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A 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). No co-chaperones have yet been identified for HSPA12A.


Pssm-ID: 466841 [Multi-domain]  Cd Length: 413  Bit Score: 50.00  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 143 VVTVPAYFNDSQRQATKDAGTIAGLNV------LRIINEPTAAAIaYGLDKKVGAERNVLIFDLGGGTFDVSILTI---E 213
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASI-YCRKLRLHQMDRYVVVDCGGGTVDLTVHQIrlpE 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 214 DGIFEV-KSTAGDTHLGGEDFDNRMV------NHFIAEFKRKHKKdisenkrAVRRLRTACERAKRTLSSSTQASIEIDS 286
Cdd:cd11735 223 GHLKELyKASGGPYGSLGVDYEFEKLlckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDRTNPLNITL 295
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 287 LYEGIDFYTS------------------------ITRARFEELNAdLFRGTLDPVEKALRD--AKLDKSQIHDIVLVGGS 340
Cdd:cd11735 296 PFSFIDYYKKfrghsvehalrksnvdfvkwssqgMLRMSPDAMNA-LFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGF 374
                       250
                ....*....|....*..
gi 13242237 341 TRIPKIQKLLQDFFNGK 357
Cdd:cd11735 375 AESPLLQQAVQNAFGDQ 391
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
143-301 9.47e-06

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 48.16  E-value: 9.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  143 VVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDkkVGAERNVLIFDLGGGTFDVSILTIeDGIFEVKSt 222
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLP--VTEPTGSMVVDIGGGTTEVAVISL-GGIVYSKS- 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13242237  223 agdTHLGGEDFDNRMVNHfiaeFKRKHKKDISEnkravrrlRTAcERAKrtlssstqasIEIDSLYEGIDFYTSITRAR 301
Cdd:PRK13927 176 ---VRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIK----------IEIGSAYPGDEVLEMEVRGR 228
ASKHA_NBD_HSP70_HSPA12B cd11736
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ...
124-354 1.17e-05

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, 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 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). No co-chaperones have yet been identified for HSPA12B.


Pssm-ID: 466842 [Multi-domain]  Cd Length: 361  Bit Score: 48.04  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 124 LTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGL------NVLRIINEPTAAAI-AYGLDKKVGAernvl 196
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDRYIVA----- 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 197 ifDLGGGTFDVSILTIED--GIFE--VKSTAGDTHLGGEDFD-NRMVNH-----FIAEFKRKHKKdisenkrAVRRLRTA 266
Cdd:cd11736 200 --DCGGGTVDLTVHQIEQpqGTLKelYKASGGPYGAVGVDLAfEKLLCQifgedFIATFKAKRPA-------AWVDLTIA 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 267 CERAKRT--LSSSTQASIEidslyegidfytsitrarfeelnadLFRGTLDPVEKALRD--AKLDKSQIHDIVLVGGSTR 342
Cdd:cd11736 271 FEARKRTaaLRMSSEAMNE-------------------------LFQPTISQIIQHIDDlmKKPEVKGIKFLFLVGGFAE 325
                       250
                ....*....|..
gi 13242237 343 IPKIQKLLQDFF 354
Cdd:cd11736 326 SPMLQRAVQAAF 337
PRK13929 PRK13929
rod-share determining protein MreBH; Provisional
1-240 1.67e-05

rod-share determining protein MreBH; Provisional


Pssm-ID: 184403 [Multi-domain]  Cd Length: 335  Bit Score: 47.21  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    1 MSKGPAVGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFTDTER---LIGDAAKNQVAMNPTNTVfdakrlIGRR 77
Cdd:PRK13929   1 MFQSTEIGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV------AVRP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   78 FDDAVVqsdmkhwpfmvvndagrpkvqVEYkgetksfypeEVSSMVLTKMKEIAEAYLGKTV--TNAVVTVPAYFNDSQR 155
Cdd:PRK13929  66 MKDGVI---------------------ADY----------DMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVER 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  156 QATKDAGTIAGLNVLRIINEPTAAAIayGLDKKVGAERNVLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGEDFDN 235
Cdd:PRK13929 115 RAISDAVKNCGAKNVHLIEEPVAAAI--GADLPVDEPVANVVVDIGGGTTEVAIISF-GGVVSCHS----IRIGGDQLDE 187

                 ....*
gi 13242237  236 RMVNH 240
Cdd:PRK13929 188 DIVSF 192
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
167-253 2.89e-05

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 46.36  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 167 LNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTfdVSILTIEDGIFEVKStaGDTHLGGEDFDNRMVNHFIAEFK 246
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEES--SDTLPGGEEALEKYADDILNELL 212

                ....*..
gi 13242237 247 RKHKKDI 253
Cdd:cd10227 213 KKLGDEL 219
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
7-373 2.19e-04

nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 43.74  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   7 VGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFTD---------TERLIGDAA-KNQVAMNptntvfdakrlIG 75
Cdd:cd24009   4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD-----------LR 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  76 RRFDDAVVQSDMKhwpfmvvndagrpkvqveykgetKSFypeEVSSMVLTKMkeIAEAYLGKTV-TNAVVTVPAYFNDSQ 154
Cdd:cd24009  62 RPLEDGVIKEGDD-----------------------RDL---EAARELLQHL--IELALPGPDDeIYAVIGVPARASAEN 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 155 RQATKDAgTIAGLNVLRIINEPTAaaIAYGLDKKVGAernvLIFDLGGGTFDV-----SILTIEDGIfeVKSTAGDthlg 229
Cdd:cd24009 114 KQALLEI-ARELVDGVMVVSEPFA--VAYGLDRLDNS----LIVDIGAGTTDLcrmkgTIPTEEDQI--TLPKAGD---- 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 230 geDFDNRMVnhfiAEFKRKHkKDISENKRAVRRLRtacERAKRTLSSSTQASIE--IDSLYEGIDFyTSITRARFEELNA 307
Cdd:cd24009 181 --YIDEELV----DLIKERY-PEVQLTLNMARRWK---EKYGFVGDASEPVKVElpVDGKPVTYDI-TEELRIACESLVP 249
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13242237 308 DLFRGtldpVEKALRDAKLDKSQ--IHDIVLVGGSTRI----PKIQKLLQDFFNGKeLNKSINPDEAVAYGA 373
Cdd:cd24009 250 DIVEG----IKKLIASFDPEFQEelRNNIVLAGGGSRIrgldTYIEKALKEYGGGK-VTCVDDPVFAGAEGA 316
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
165-375 4.25e-04

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 42.90  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYgLDKKvgaERN--VLIFDLGGGTFDVSILtiEDGIFEvkstagDTH---LGGedfdnrmvN 239
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTED---EKElgVALIDIGGGTTDIAVF--KNGSLR------YTAvipVGG--------N 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 240 HFIaefkrkhkKDISenkRAVRRLRTACERAKRTLSSSTQASIEIDSLYE--GIDFYTS----------ITRARFEELna 307
Cdd:cd24048 232 HIT--------NDIA---IGLNTPFEEAERLKIKYGSALSEEADEDEIIEipGVGGREPrevsrrelaeIIEARVEEI-- 298
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13242237 308 dlfrgtLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFN-----GKELNKSINPDEAVAYGAAV 375
Cdd:cd24048 299 ------LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYAT 365
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
497-602 1.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237  497 KENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSK-NSLESYAFNMKATVED-EKLQGK-------INDEDK 567
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARiGELKKEIKELKKAIEElKKAKGKcpvcgreLTEEHR 450
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 13242237  568 QKILDKCNEIIswldKNQTAEKEEFEHQQKELEKV 602
Cdd:PRK03918 451 KELLEEYTAEL----KRIEKELKEIEEKERKLRKE 481
ASKHA_ATPase-like cd00012
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
331-374 2.71e-03

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


Pssm-ID: 466786 [Multi-domain]  Cd Length: 135  Bit Score: 38.60  E-value: 2.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 13242237 331 IHDIVLVGGSTRIPKIQKLLQDFF---NGKELNKSINPDEAVAYGAA 374
Cdd:cd00012  89 SANVVLVGGGARNNGLAKRLKELLlfrGGLKVVKAVDPDEAVALGAA 135
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
165-355 2.95e-03

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 40.34  E-value: 2.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 165 AGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSIltIEDGIFEVKSTAGdthLGGEDFDNRMVNHFiae 244
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLPDEEEETVALLDIGASSTTLVI--VKNGKLLFTRSIP---VGGNDITEAIAKAL--- 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 245 fkrkhkkDISENKravrrlrtaCERAKRtlssstQASIEIDSLYEGIDFYTSITRARFEELNADLFRgTLDPVEKALRDA 324
Cdd:cd24049 220 -------GLSFEE---------AEELKR------EYGLLLEGEEGELKKVAEALRPVLERLVSEIRR-SLDYYRSQNGGE 276
                       170       180       190
                ....*....|....*....|....*....|.
gi 13242237 325 KLDKsqihdIVLVGGSTRIPKIQKLLQDFFN 355
Cdd:cd24049 277 PIDK-----IYLTGGGSLLPGLDEYLSERLG 302
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
195-372 4.92e-03

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 38.47  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   195 VLIfDLGGGTFDVSIltIEDGIFEVKSTAGdthLGGedfdnrmvNHFiaefkrkhKKDISenkRAVRRLRTACERAKRTL 274
Cdd:pfam14450   1 ALI-DIGGGTTDIAV--FEDGALRHTRVIP---VGG--------NGI--------TKDIA---IGLRTAVEEAERLKIKY 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237   275 SSSTQASIEIDSLYEGIDFY---------TSITRARFEELnADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPK 345
Cdd:pfam14450  56 GSALASLADEDEVPGVGGREpreisrkelAEIIEARVEEI-LELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPG 134
                         170       180       190
                  ....*....|....*....|....*....|...
gi 13242237   346 IQKLLQDFFNGK------ELNKSINPDEAVAYG 372
Cdd:pfam14450 135 LVELAERALGLPvrigspDGIGGRNPAYATALG 167
ASKHA_ATPase-like cd00012
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
142-204 5.49e-03

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


Pssm-ID: 466786 [Multi-domain]  Cd Length: 135  Bit Score: 37.45  E-value: 5.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13242237 142 AVVTVPAYFNDSQRQAT-----------KDAGTIAGLNVLRIINEPTAAAIAYGLDKKvgaERNVLIFDLGGGT 204
Cdd:cd00012  16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLG---PEGLLVVDLGGGT 86
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
307-382 8.82e-03

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 39.05  E-value: 8.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237 307 ADLFRGTLDPVEKALRDAK--LDKS--QIHDIVLVGGSTRIPKIQKLLQDFFnGKELNKSiNPDEAVAYGAAVQAAILSG 382
Cdd:COG1070 368 AHLARAVLEGVAFALRDGLeaLEEAgvKIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGLG 445
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
497-602 8.88e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.18  E-value: 8.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13242237    497 KENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRD---KVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDK 573
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
                           90       100
                   ....*....|....*....|....*....
gi 13242237    574 CNEIISWLDKNQTAEKEEFEHQQKELEKV 602
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKEL 347
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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