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Conserved domains on  [gi|308517320|emb|CBM06411|]
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molecular chaperone, partial [Marichromatium litoris]

Protein Classification

Hsp70 family protein( domain architecture ID 1000525)

Hsp70 family protein such as Hsp70 chaperone DnaK, which is involved in DNA replication, protein folding and the stress response; it cooperates with the Hsp40 co-chaperone DnaJ and the nucleotide exchange factor GrpE

CATH:  3.30.420.40
Gene Ontology:  GO:0005524|GO:0140662|GO:0051082
PubMed:  9476895|30338057|15770419
SCOP:  4000313

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 2-208 1.80e-139

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.


The actual alignment was detected with superfamily member PRK00290:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 627  Bit Score: 403.33  E-value: 1.80e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:PRK00290  64 NTIFSIKRLMGRRDEE--VQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVP 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDisiiEIAEIEGEHQFEVLSTNG 161
Cdd:PRK00290 142 AYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKK-GDEKILVYDLGGGTFD----VSILEIGDGVFEVLSTNG 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PRK00290 217 DTHLGGDDFDQRIIDYLADEFKKENGIDLRKDKMALQRLKEAAEKAK 263
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 2-208 1.80e-139

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 403.33  E-value: 1.80e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:PRK00290  64 NTIFSIKRLMGRRDEE--VQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVP 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDisiiEIAEIEGEHQFEVLSTNG 161
Cdd:PRK00290 142 AYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKK-GDEKILVYDLGGGTFD----VSILEIGDGVFEVLSTNG 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PRK00290 217 DTHLGGDDFDQRIIDYLADEFKKENGIDLRKDKMALQRLKEAAEKAK 263
ASKHA_NBD_HSP70_HSPA9 cd11733
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ...
 1-208 7.58e-127

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: 362.35  E-value: 7.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:cd11733   62 ENTLYATKRLIGRRFDDPEVQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTN 160
Cdd:cd11733  142 PAYFNDSQRQATKDAGQIAGLNVLRIINEPTAAALAYGLDKK-DDKIIAVYDLGGGTFDISILEIQKGV----FEVKATN 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 161 GDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11733  217 GDTFLGGEDFDNALLNYLVAEFKKEQGIDLSKDNLALQRLREAAEKAK 264
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 2-208 1.54e-115

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: 341.16  E-value: 1.54e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320    2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS--GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVIT 79
Cdd:pfam00012  60 NTVFSVKRLIGRKFSDPVVQRDIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVIT 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   80 VPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIegehQFEVLST 159
Cdd:pfam00012 140 VPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRG----VFEVKAT 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 308517320  160 NGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:pfam00012 216 NGDTHLGGEDFDLRLVDHLAEEFKKKYGIDLSKDKRALQRLREAAEKAK 264
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 2-208 2.52e-113

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: 335.43  E-value: 2.52e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320    2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVkADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:TIGR02350  62 NTIYSIKRFMGRRFDE--VTEEAKRVPYKVV-GDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNG 161
Cdd:TIGR02350 139 AYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGV----FEVLSTAG 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 308517320  162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:TIGR02350 215 DTHLGGDDFDQRIIDWLADEFKKEEGIDLSKDKMALQRLKEAAEKAK 261
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-208 2.33e-94

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 282.87  E-value: 2.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDtvvskdkdmvpykivkadngdAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:COG0443   60 GRTIRSIKRLLGRSLFD---------------------EATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDisiiEIAEIEGEHQFEVLSTN 160
Cdd:COG0443  119 PAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFD----VSILRLGDGVFEVLATG 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 161 GDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:COG0443  195 GDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLREAAEKAK 242
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 2-208 1.80e-139

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 403.33  E-value: 1.80e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:PRK00290  64 NTIFSIKRLMGRRDEE--VQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVP 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDisiiEIAEIEGEHQFEVLSTNG 161
Cdd:PRK00290 142 AYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKK-GDEKILVYDLGGGTFD----VSILEIGDGVFEVLSTNG 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PRK00290 217 DTHLGGDDFDQRIIDYLADEFKKENGIDLRKDKMALQRLKEAAEKAK 263
ASKHA_NBD_HSP70_HSPA9 cd11733
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ...
 1-208 7.58e-127

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: 362.35  E-value: 7.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:cd11733   62 ENTLYATKRLIGRRFDDPEVQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTN 160
Cdd:cd11733  142 PAYFNDSQRQATKDAGQIAGLNVLRIINEPTAAALAYGLDKK-DDKIIAVYDLGGGTFDISILEIQKGV----FEVKATN 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 161 GDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11733  217 GDTFLGGEDFDNALLNYLVAEFKKEQGIDLSKDNLALQRLREAAEKAK 264
ASKHA_NBD_HSP70_DnaK-like cd10234
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ...
 2-208 7.73e-127

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: 362.18  E-value: 7.73e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:cd10234   61 NTIFSIKRFMGRRYKE--VEVERKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDISIIEIAEIegehQFEVLSTNG 161
Cdd:cd10234  139 AYFNDSQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKK-KDEKILVYDLGGGTFDVSILEIGDG----VFEVLSTNG 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10234  214 DTHLGGDDFDQRIIDYLADEFKKEEGIDLSKDKMALQRLKEAAEKAK 260
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 2-208 1.54e-115

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: 341.16  E-value: 1.54e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320    2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS--GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVIT 79
Cdd:pfam00012  60 NTVFSVKRLIGRKFSDPVVQRDIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVIT 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   80 VPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIegehQFEVLST 159
Cdd:pfam00012 140 VPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRG----VFEVKAT 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 308517320  160 NGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:pfam00012 216 NGDTHLGGEDFDLRLVDHLAEEFKKKYGIDLSKDKRALQRLREAAEKAK 264
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 2-208 2.52e-113

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: 335.43  E-value: 2.52e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320    2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVkADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:TIGR02350  62 NTIYSIKRFMGRRFDE--VTEEAKRVPYKVV-GDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNG 161
Cdd:TIGR02350 139 AYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGV----FEVLSTAG 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 308517320  162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:TIGR02350 215 DTHLGGDDFDQRIIDWLADEFKKEEGIDLSKDKMALQRLKEAAEKAK 261
ASKHA_NBD_HSP70_Ssc1_3 cd11734
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ...
 2-208 3.18e-105

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: 307.84  E-value: 3.18e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:cd11734   63 NTLFATKRLIGRKFDDAEVQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVP 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNG 161
Cdd:cd11734  143 AYFNDSQRQATKDAGQIAGLNVLRVINEPTAAALAYGLDKS-GDKVIAVYDLGGGTFDISILEIQKGV----FEVKSTNG 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11734  218 DTHLGGEDFDIALVRHIVSEFKKESGIDLSKDRMAIQRIREAAEKAK 264
ASKHA_NBD_HSP70_BiP cd10241
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ...
 1-208 7.62e-105

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: 306.44  E-value: 7.62e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKaDNGDAWVEVSG----KKMAPPEISAKVLQKMKKTAEDYLGAEVTEA 76
Cdd:cd10241   61 ENTVFDVKRLIGRKFDDKEVQKDIKLLPFKIVN-KNGKPYIQVEVkgekKTFAPEEISAMVLTKMKETAEAYLGKKVTHA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEV 156
Cdd:cd10241  140 VVTVPAYFNDAQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGV----FEV 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 308517320 157 LSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10241  216 LATNGDTHLGGEDFDQRVMDHFIKLFKKKTGKDISKDKRAVQKLRREVEKAK 267
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 2-208 1.07e-104

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 315.23  E-value: 1.07e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:PTZ00400 103 NTVFATKRLIGRRYDEDATKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVP 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGdQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNG 161
Cdd:PTZ00400 183 AYFNDSQRQATKDAGKIAGLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEILGGV----FEVKATNG 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PTZ00400 258 NTSLGGEDFDQRILNYLIAEFKKQQGIDLKKDKLALQRLREAAETAK 304
ASKHA_NBD_HSP70_HSPA1-like cd24028
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ...
 1-208 1.33e-99

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: 293.26  E-value: 1.33e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSG----KKMAPPEISAKVLQKMKKTAEDYLGAEVTEA 76
Cdd:cd24028   59 ENTIFDVKRLIGRKFDDPSVQSDIKHWPFKVVEDEDGKPKIEVTYkgeeKTFSPEEISAMILKKLKEIAEAYLGRPVTKA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQR-GDQKIAVYDLGGGTFDisiiEIAEIEGEHQFE 155
Cdd:cd24028  139 VITVPAYFNDAQRQATKDAATIAGLNVLRIINEPTAAALAYGLDKKSsGERNVLVFDLGGGTFD----VSLLSIDNGVFE 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308517320 156 VLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd24028  215 VKATAGDTHLGGEDFDNRLVEYLVEEFKKKHGKDLRENPRAMRRLRSACERAK 267
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-208 2.33e-94

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 282.87  E-value: 2.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDtvvskdkdmvpykivkadngdAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:COG0443   60 GRTIRSIKRLLGRSLFD---------------------EATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDisiiEIAEIEGEHQFEVLSTN 160
Cdd:COG0443  119 PAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFD----VSILRLGDGVFEVLATG 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 161 GDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:COG0443  195 GDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLREAAEKAK 242
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
 1-208 1.28e-92

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: 275.28  E-value: 1.28e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVkADNGDAWVEVS----GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEA 76
Cdd:cd10233   59 TNTVFDAKRLIGRKFDDPVVQSDMKHWPFKVV-SGGDKPKIQVEykgeTKTFTPEEISSMVLTKMKEIAEAYLGKKVKNA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ-RGDQKIAVYDLGGGTFDISIIEIAEIEgehqFE 155
Cdd:cd10233  138 VITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKgKGERNVLIFDLGGGTFDVSLLTIEDGI----FE 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308517320 156 VLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10233  214 VKATAGDTHLGGEDFDNRLVNHFVQEFKRKHKKDISGNPRALRRLRTACERAK 266
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
 2-208 3.15e-91

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 280.10  E-value: 3.15e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKdmVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:PRK13411  64 NTVYSIKRFIGRRWDDTEEERSR--VPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVP 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNG 161
Cdd:PRK13411 142 AYFTDAQRQATKDAGTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGV----FEVKATAG 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PRK13411 218 NNHLGGDDFDNCIVDWLVENFQQQEGIDLSQDKMALQRLREAAEKAK 264
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
 2-208 1.08e-90

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 278.88  E-value: 1.08e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVE-VSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:PTZ00186  88 STFYAVKRLIGRRFEDEHIQKDIKNVPYKIVRAGNGDAWVQdGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTC 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRgDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTN 160
Cdd:PTZ00186 168 PAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEIAGGV----FEVKATN 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 161 GDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PTZ00186 243 GDTHLGGEDFDLALSDYILEEFRKTSGIDLSKERMALQRVREAAEKAK 290
dnaK CHL00094
heat shock protein 70
 1-208 7.35e-90

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 275.84  E-value: 7.35e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVS--GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVI 78
Cdd:CHL00094  63 ENTFYSVKRFIGRKFSE--ISEEAKQVSYKVKTDSNGNIKIECPalNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  79 TVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRgDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLS 158
Cdd:CHL00094 141 TVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAASLAYGLDKKN-NETILVFDLGGGTFDVSILEVGDGV----FEVLS 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 308517320 159 TNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:CHL00094 216 TSGDTHLGGDDFDKKIVNWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAK 265
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
 2-208 3.73e-88

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 272.66  E-value: 3.73e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVE--VSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVIT 79
Cdd:PRK13410  64 NTFYNLKRFIGRRYDE--LDPESKRVPYTIRRNEQGNVRIKcpRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVIT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  80 VPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRgDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLST 159
Cdd:PRK13410 142 VPAYFNDSQRQATRDAGRIAGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGV----FEVKAT 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 308517320 160 NGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PRK13410 217 SGDTQLGGNDFDKRIVDWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAK 265
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
 1-208 2.31e-81

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: 246.36  E-value: 2.31e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:cd10236   63 ENTISSVKRLMGRSLAD--VKEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTN 160
Cdd:cd10236  141 PAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAALAYGLDQK-KEGTIAVYDLGGGTFDISILRLSDGV----FEVLATG 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 161 GDTFLGGEDFDLRIIDHlvesFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10236  216 GDTALGGDDFDHLLADW----ILKQIGIDARLDPAVQQALLQAARRAK 259
PLN03184 PLN03184
chloroplast Hsp70; Provisional
 1-208 5.32e-78

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 246.30  E-value: 5.32e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVE--VSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVI 78
Cdd:PLN03184 100 ENTFFSVKRFIGRKMSE--VDEESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVI 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  79 TVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKqRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLS 158
Cdd:PLN03184 178 TVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFEK-KSNETILVFDLGGGTFDVSVLEVGDGV----FEVLS 252

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 308517320 159 TNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PLN03184 253 TSGDTHLGGDDFDKRIVDWLASNFKKDEGIDLLKDKQALQRLTEAAEKAK 302
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 1-208 3.80e-77

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 243.55  E-value: 3.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS----GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEA 76
Cdd:PTZ00009  64 ENTVFDAKRLIGRKFDDSVVQSDMKHWPFKVTTGGDDKPMIEVTyqgeKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ-RGDQKIAVYDLGGGTFDISIIEIAEIEgehqFE 155
Cdd:PTZ00009 144 VVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKgDGEKNVLIFDLGGGTFDVSLLTIEDGI----FE 219

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308517320 156 VLSTNGDTFLGGEDFDLRIIDHLVESFK-KEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PTZ00009 220 VKATAGDTHLGGEDFDNRLVEFCVQDFKrKNRGKDLSSNQRALRRLRTQCERAK 273
ASKHA_NBD_HSP70_Ssb cd24093
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ...
 2-208 2.43e-75

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: 231.41  E-value: 2.43e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKaDNGDAWVEVS----GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd24093   59 NTVFDAKRLIGRRFDDESVQKDMKTWPFKVID-VNGNPVIEVQylgeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQK--IAVYDLGGGTFDISIIEIAEIEgehqFE 155
Cdd:cd24093  138 ITVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLGAGKSEKErhVLIFDLGGGTFDVSLLHIAGGV----YT 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308517320 156 VLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd24093  214 VKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAK 266
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 2-208 8.88e-75

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: 229.00  E-value: 8.88e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVvskdkdmvpykivkadngdawvEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVP 81
Cdd:cd24029   61 NTIYSVKRLMGRDTKDKE----------------------EIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  82 AYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDisiiEIAEIEGEHQFEVLSTNG 161
Cdd:cd24029  119 AYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFD----VSILEIENGKFEVLATGG 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 308517320 162 DTFLGGEDFDLRIIDHLVESFKKEQGV-DLRNDPLALQRLKEAAEKAK 208
Cdd:cd24029  195 DNFLGGDDFDEAIAELILEKIGIETGIlDDKEDERARARLREAAEEAK 242
hscA PRK05183
chaperone protein HscA; Provisional
 1-208 1.76e-61

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 201.56  E-value: 1.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDtvVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:PRK05183  79 KNTISSVKRFMGRSLAD--IQQRYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDK-QRGdqKIAVYDLGGGTFDISIIEIAEIEgehqFEVLST 159
Cdd:PRK05183 157 PAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDSgQEG--VIAVYDLGGGTFDISILRLSKGV----FEVLAT 230

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 308517320 160 NGDTFLGGEDFDLRIIDHLVEsfkkEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:PRK05183 231 GGDSALGGDDFDHLLADWILE----QAGLSPRLDPEDQRLLLDAARAAK 275
ASKHA_NBD_HSP70_HscC cd10235
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ...
 45-208 8.36e-60

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: 190.53  E-value: 8.36e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  45 GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRG 124
Cdd:cd10235   79 NHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKRED 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320 125 DQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDlrnDPLALQRLKEAA 204
Cdd:cd10235  159 ETRFLVFDLGGGTFDVSVLELFEGV----IEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTSL---SPSELAALRKRA 231


                 ....
gi 308517320 205 EKAK 208
Cdd:cd10235  232 EQAK 235
HscA TIGR01991
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ...
 1-208 2.90e-58

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: 192.87  E-value: 2.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320    1 TNTLFAVKRLIGRRFDDTvvsKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITV 80
Cdd:TIGR01991  60 KNTISSVKRLMGRSIEDI---KTFSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   81 PAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKqrGDQKI-AVYDLGGGTFDISIIEIAEIEgehqFEVLST 159
Cdd:TIGR01991 137 PAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAVAYGLDK--ASEGIyAVYDLGGGTFDVSILKLTKGV----FEVLAT 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 308517320  160 NGDTFLGGEDFDLRIIDHLVesfkKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:TIGR01991 211 GGDSALGGDDFDHALAKWIL----KQLGISADLNPEDQRLLLQAARAAK 255
ASKHA_NBD_HSP70_HSPA13 cd10237
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ...
 2-208 3.49e-58

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: 188.32  E-value: 3.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSG----KKMAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd10237   86 NTIYDAKRFIGKTFTKEELEEEAKRYPFKVVNDNIGSAFFEVPLngstLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAV 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFEVL 157
Cdd:cd10237  166 ISVPAEFDEKQRNATRKAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGM----FLTR 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308517320 158 STNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLrNDPLALQRLKEAAEKAK 208
Cdd:cd10237  242 AMAGNNHLGGQDFNQRLFQYLIDRIAKKFGKTL-TDKEDIQRLRQAVEEVK 291
ASKHA_NBD_HSP70_HSP105-110-like cd11732
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ...
 2-208 3.13e-55

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: 179.68  E-value: 3.13e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS--GKKM--APPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd11732   59 NTIRNFKRLIGLKFDDPEVQKEIKLLPFKLVELEDGKVGIEVSynGEEVvfSPEQVLAMLLGKLKEIAEAANKGEVKDCV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ---RGDQK---IAVYDLGGGTFdisiIEIAEIEGE 151
Cdd:cd11732  139 ISVPGYYTDAQRRALLDAAEIAGLNCLRLINETTAAALDYGIYKSdllESEEKpriVAFVDMGHSST----QVSIAAFTK 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308517320 152 HQFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11732  215 GKLKVLSTAFDRNLGGRDFDRALVEHFAEEFKKKYKIDPLENPKARLRLLDACEKLK 271
ASKHA_NBD_HSP70_HSPA4_like cd10228
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ...
 1-208 5.42e-52

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: 171.30  E-value: 5.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS--GKKM--APPEISAKVLQKMKKTAEDYLGAEVTEA 76
Cdd:cd10228   58 KNTVSGFKRLLGRKFDDPFVQKELKHLPYKVVKLPNGSVGIKVQylGEEHvfTPEQVTAMLLTKLKETAETALKTKVVDC 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ---RGDQK---IAVYDLGGGTFDISIIEIAEIeg 150
Cdd:cd10228  138 VISVPSYFTDAERRAVLDAAQIAGLNCLRLLNDTTAVALAYGIYKQdlpAEEEKprnVVFVDMGHSSLQVSVCAFNKG-- 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 308517320 151 ehQFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10228  216 --KLKVLATAADPNLGGRDFDELLVEHFAEEFKTKYKIDVKSKPRALLRLLTECEKLK 271
ASKHA_NBD_HSP70_AtHsp70-14-like cd24095
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ...
 1-208 5.39e-48

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: 161.32  E-value: 5.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS--GKKMA--PPEISAKVLQKMKKTAEDYLGAEVTEA 76
Cdd:cd24095   61 KNTISQLKRLIGRKFDDPEVQRDLKLFPFKVTEGPDGEIGINVNylGEQKVftPEQILAMLLSNLKRIAEKNLKTPVTDC 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGM---DKQRGDQ-KIAVYDLGggtfDISIIEIAEIEGEH 152
Cdd:cd24095  141 VISVPVYFTDAQRRAMLDAAQIAGLNCLRLMNETTATALAYGIyktDLPETDPtNVVFVDVG----HSSTQVCVVAFKKG 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 308517320 153 QFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd24095  217 QLKVLSHAFDRNLGGRDFDEVLFDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVK 272
ASKHA_NBD_HSP70_HSPA14 cd10238
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ...
 1-208 1.22e-47

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: 160.10  E-value: 1.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   1 TNTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAW-VEVSGKK--MAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd10238   60 SNTVVRVKQLLGRSFDDPAVQELKKESKCKIIEKDGKPGYeIELEEKKklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVV 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGM--DKQRGDQKIAVYDLGGGTFDISIIEIAEIEgehqFE 155
Cdd:cd10238  140 LTVPLDFDEDQRNALKEAAEKAGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGM----YR 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308517320 156 VLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10238  216 VLATRTDDNLGGDDFTEALAEHLASEFKRQWKQDVRENKRAMAKLMNAAEVCK 268
ASKHA_NBD_HSP70_HYOU1 cd10230
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ...
 48-208 1.81e-41

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: 143.40  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  48 MAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDK---QRG 124
Cdd:cd10230   73 YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRrfeNNE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320 125 DQKIAVYDLGGG-------TFDISIIEIAEIEGEH-QFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQG--VDLRNDP 194
Cdd:cd10230  153 PQNVLFYDMGASstsatvvEFSSVKEKDKGKNKTVpQVEVLGVGWDRTLGGLEFDLRLADHLADEFNEKHKkdKDVRTNP 232

                        170
                 ....*....|....
gi 308517320 195 LALQRLKEAAEKAK 208
Cdd:cd10230  233 RAMAKLLKEANRVK 246
hscA PRK01433
chaperone protein HscA; Provisional
 4-205 5.27e-41

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 146.54  E-value: 5.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   4 LFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVPAY 83
Cdd:PRK01433  72 LRSIKRLFGKTLKEILNTPALFSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAH 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  84 FNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDK-QRGdqKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNGD 162
Cdd:PRK01433 152 FNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKnQKG--CYLVYDLGGGTFDVSILNIQEGI----FQVIATNGD 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 308517320 163 TFLGGEDFDLRIIDHLVESFkkeqgvDLRNDPLALQRLKEAAE 205
Cdd:PRK01433 226 NMLGGNDIDVVITQYLCNKF------DLPNSIDTLQLAKKAKE 262
ASKHA_NBD_HSP70_ScSse cd24094
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ...
 2-208 9.94e-41

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: 142.13  E-value: 9.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKAdNGDAWVEVS----GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd24094   59 NTVGSLKRLIGRTFSDPEVAEEEKYFTAKLVDA-NGEVGAEVNylgeKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDK------QRGDQKIAVYDLGGGTFDISIIEIAEIege 151
Cdd:cd24094  138 ISVPGWFTDEQRRAILDAAEIAGLNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFVDIGHSSYTVSIVAFKKG--- 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308517320 152 hQFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd24094  215 -QLTVKGTAYDRHFGGRDFDKALTDHFADEFKEKYKIDVRSNPKAYFRLLAAAEKLK 270
ASKHA_NBD_HSP70_HSPA4 cd11737
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ...
 2-208 7.53e-38

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: 134.68  E-value: 7.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEVS----GKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd11737   61 NTVQGFKRFHGRAFSDPFVQAEKPSLAYELVQLPTGTTGIKVMymeeERNFTIEQVTAMLLTKLKETAESALKKPVVDCV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ------RGDQKIAVYDLGGGTFDISIIEIAEIege 151
Cdd:cd11737  141 VSVPCFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFVDMGHSAYQVSVCAFNKG--- 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308517320 152 hQFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11737  218 -KLKVLATAFDPTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLK 273
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
 2-208 1.17e-37

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: 134.27  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEV----SGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd11738   61 NTIHGFKKFHGRAFDDPFVQAEKIKLPYELQKMPNGSTGVKVryldEERVFAIEQVTGMLLTKLKETSENALKKPVADCV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ------RGDQKIAVYDLGGGTFDISIIEIAEIege 151
Cdd:cd11738  141 ISVPSFFTDAERRSVMDAAQIAGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFVDMGHSAYQVSICAFNKG--- 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308517320 152 hQFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11738  218 -KLKVLATTFDPYLGGRNFDEVLVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLK 273
ASKHA_NBD_HSP70_HSPH1 cd11739
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ...
 2-208 5.63e-37

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: 132.29  E-value: 5.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320   2 NTLFAVKRLIGRRFDDTVVSKDKDMVPYKIVKADNGDAWVEV----SGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAV 77
Cdd:cd11739   61 NTVSNFKRFHGRAFNDPFVQKEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  78 ITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQ---RGDQK---IAVYDLGGGTFDISIIEIAEIege 151
Cdd:cd11739  141 ISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQdlpAPDEKpriVVFVDMGHSAFQVSACAFNKG--- 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308517320 152 hQFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd11739  218 -KLKVLGTAFDPYLGGRNFDEKLVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK 273
ASKHA_NBD_HSP70_ScSsz1p-like cd10232
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ...
 46-208 1.53e-33

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: 122.47  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  46 KKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQRG- 124
Cdd:cd10232   74 TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLRAETSg 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320 125 ----DQKIAVYDLGGGTFDISIIEIAEIEgehqFEVLSTNGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRL 200
Cdd:cd10232  154 dtikDKTVVVADLGGTRSDVTVVAVRGGL----YTILATVHDYELGGVALDDVLVGHFAKEFKKKTKTDPRKNARSLAKL 229


                 ....*...
gi 308517320 201 KEAAEKAK 208
Cdd:cd10232  230 RNAAEITK 237
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 18-208 4.33e-31

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: 115.66  E-value: 4.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  18 TVVSKDKDMVPYKIVKADNGDAWVEVSGKKMAPP--EISAKVLQKMKKTAEDYLGAEV-------TEAVITVPAYFNDSQ 88
Cdd:cd10170   10 SGVAYALLGPGEPPLVVLQLPWPGGDGGSSKVPSvlEVVADFLRALLEHAKAELGDRIwelekapIEVVITVPAGWSDAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  89 RQATKDAGRIAGL----DVKRIINEPTAAALAYGMDKQRG-----DQKIAVYDLGGGTFDISIIEIAEIEGEHQFEVlST 159
Cdd:cd10170   90 REALREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLlplkpGDVVLVCDAGGGTVDLSLYEVTSGSPLLLEEV-AP 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 308517320 160 NGDTFLGGEDFDLRIIDHLVESFKKEQGVDLRNDPLALQRLKEAAEKAK 208
Cdd:cd10170  169 GGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAK 217
ASKHA_NBD_HSP70_YegD-like cd10231
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ...
 43-179 2.05e-14

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: 70.77  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  43 VSGKKMAPPEISAKVLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQAT-------KDAGRIAGLDVKRIINEPTAAAL 115
Cdd:cd10231   86 IFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqaesrlRDAARRAGFRNVEFQYEPIAAAL 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308517320 116 AYGMDKQRgDQKIAVYDLGGGTFDISIIEIAEIEGEHQFEVLSTNGDtFLGGEDFDLRIIDHLV 179
Cdd:cd10231  166 DYEQRLDR-EELVLVVDFGGGTSDFSVLRLGPNRTDRRADILATSGV-GIGGDDFDRELALKKV 227
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
 22-208 1.71e-09

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: 56.52  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  22 KDKDMVPYKIVKADNGdawvevsgKKMAPPEISAKVLQKMKKTAEDYL----GAEVTEA----VITVPAYFNDSQRQATK 93
Cdd:cd10229   89 SEKELTRDTKVKAVNG--------KSMPALEVFAEALRYLKDHALKELrdrsGSSLDEDdirwVLTVPAIWSDAAKQFMR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  94 DAGRIAGLDVK------RIINEPTAAALAYG-------MDKQRGDQKIAVYDLGGGTFDisIIEIAEIEGEHQFEVLSTN 160
Cdd:cd10229  161 EAAVKAGLISEenseqlIIALEPEAAALYCQkllaegeEKELKPGDKYLVVDCGGGTVD--ITVHEVLEDGKLEELLKAS 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 308517320 161 GDTFlGGEDFDLRIIDHLVESFKKEQGVDLR-NDPLALQRLKEAAEKAK 208
Cdd:cd10229  239 GGPW-GSTSVDEEFEELLEEIFGDDFMEAFKqKYPSDYLDLLQAFERKK 286
ASKHA_NBD_EutJ cd24047
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ...
 57-137 1.56e-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: 49.96  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  57 VLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrgdqkiAVYDLGGG 136
Cdd:cd24047   48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121


                 .
gi 308517320 137 T 137
Cdd:cd24047  122 T 122
PRK15080 PRK15080
ethanolamine utilization protein EutJ; Provisional
 54-137 7.76e-07

ethanolamine utilization protein EutJ; Provisional


Pssm-ID: 237904 [Multi-domain]  Cd Length: 267  Bit Score: 48.29  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  54 SAKVLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMDKQrgdqkiAVYDL 133
Cdd:PRK15080  69 AVTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDI 142


                 ....
gi 308517320 134 GGGT 137
Cdd:PRK15080 143 GGGT 146
PRK11678 PRK11678
putative chaperone; Provisional
 58-139 3.14e-05

putative chaperone; Provisional


Pssm-ID: 236954 [Multi-domain]  Cd Length: 450  Bit Score: 43.70  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  58 LQKMKKTAEDYLGAEVTEAVITVPAYFN-----DSQRQA----TKDAGRiAGL-DVkRIINEPTAAALAY--GMDKqrgD 125
Cdd:PRK11678 134 MLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAegilERAAKR-AGFkDV-EFQFEPVAAGLDFeaTLTE---E 208

                         90
                 ....*....|....
gi 308517320 126 QKIAVYDLGGGTFD 139
Cdd:PRK11678 209 KRVLVVDIGGGTTD 222
ASKHA_NBD_HSP70_HSPA12B cd11736
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ...
 43-139 3.25e-04

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: 40.72  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  43 VSGKKMAPPEISAKVL--------QKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKDAGRIAGLdVKR-------II 107
Cdd:cd11736  102 VNGKKVQALEVFAHALrffkehalQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGL-VSPenpeqllIA 180

                         90       100       110
                 ....*....|....*....|....*....|..
gi 308517320 108 NEPTAAALAYgmdkqRGDQKIAVYDLGGGTFD 139
Cdd:cd11736  181 LEPEAASIYC-----RKLDRYIVADCGGGTVD 207
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
 77-139 8.18e-04

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 39.50  E-value: 8.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308517320  77 VITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGMD--KQRGDQkiaVYDLGGGTFD 139
Cdd:PRK13928  99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGNM---VVDIGGGTTD 160
ASKHA_NBD_HSP70_HSPA12A cd11735
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ...
 44-139 9.24e-04

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: 39.60  E-value: 9.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  44 SGKKMAPPEISAKVLQKMKKTA----EDYLGAEVTEA----VITVPAYFNDSQRQATKDAGRIAGLDVKR------IINE 109
Cdd:cd11735  103 NGKKVKALEIFAYALQFFKEQAlkelSDQAGSEFDNSdvrwVITVPAIWKQPAKQFMRQAAYKAGLASPEnpeqliIALE 182

                         90       100       110
                 ....*....|....*....|....*....|
gi 308517320 110 PTAAALAYGMDKQRGDQKIAVYDLGGGTFD 139
Cdd:cd11735  183 PEAASIYCRKLRLHQMDRYVVVDCGGGTVD 212
ASKHA_ATPase-like cd00012
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 76-137 1.08e-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: 37.83  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308517320  76 AVITVPAYFNDSQRQAT-----------KDAGRIAGLDVKRIINEPTAAALAYGMDkqRGDQKIAVYDLGGGT 137
Cdd:cd00012   16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLT--LGPEGLLVVDLGGGT 86
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
 55-184 5.81e-03

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: 36.89  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308517320  55 AKVLQKMKKTAEDYLGAEVTEAVITVPAYFNDSQRQATKdagriAGLDVKRIINEPTAAALAYGMDKQRgDQKIAVYDLG 134
Cdd:cd24004   49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDMR-DLNIALVDIG 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 308517320 135 GGTFDIsiieiaeiegehqfeVLSTNGDTF------LGGEDFDLRIIDHLVESFKK 184
Cdd:cd24004  123 AGTTDI---------------ALIRNGGIEayrmvpLGGDDFTKAIAEGFLISFEE 163
 
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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