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Conserved domains on  [gi|442798775|gb|AGC75094|]
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heat shock protein 70, partial [Sphaeroforma gastrica]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

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 ...
 2-168 1.03e-134

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 cd10233:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 375  Bit Score: 380.44  E-value: 1.03e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd10233   45 LIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSDMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTFDVSI 161
Cdd:cd10233  125 IAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSL 204


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:cd10233  205 LTIEDGI 211
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
 2-168 1.03e-134

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: 380.44  E-value: 1.03e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd10233   45 LIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSDMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTFDVSI 161
Cdd:cd10233  125 IAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSL 204


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:cd10233  205 LTIEDGI 211
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 2-168 1.49e-107

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 320.59  E-value: 1.49e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDK-DNKPMIQVEYKGETKTFAPEEISSMILVKMK 80
Cdd:PTZ00009  50 LIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSDMKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMK 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTFDVS 160
Cdd:PTZ00009 130 EIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVS 209


                 ....*...
gi 442798775 161 ILTIEDGI 168
Cdd:PTZ00009 210 LLTIEDGI 217
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 3-168 2.52e-95

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: 287.62  E-value: 2.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775    3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDN-KPMIQVEYKGETktFAPEEISSMILVKMKE 81
Cdd:pfam00012  46 VGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQRDIKHLPYKVVKLPNgDAGVEVRYLGET--FTPEQISAMILQKLKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVSI 161
Cdd:pfam00012 124 TAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSI 202


                  ....*..
gi 442798775  162 LTIEDGI 168
Cdd:pfam00012 203 LEIGRGV 209
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 4-168 1.81e-76

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: 238.75  E-value: 1.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775    4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIVDKDNKPMIQVEykgeTKTFAPEEISSMILVKMKETA 83
Cdd:TIGR02350  49 GQPAKRQAVTNPENTIYSIKRFMGRRFDE--VTEEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQnVLIFDLGGGTFDVSILT 163
Cdd:TIGR02350 123 EAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILE 201


                  ....*
gi 442798775  164 IEDGI 168
Cdd:TIGR02350 202 IGDGV 206
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 4-168 4.43e-68

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 213.92  E-value: 4.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKhfpfkivdkdnkpmiqveykgetkTFAPEEISSMILVKMKETA 83
Cdd:COG0443   48 GEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATEVGGK------------------------RYSPEEISALILRKLKADA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVSILT 163
Cdd:COG0443  104 EAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILR 182


                 ....*
gi 442798775 164 IEDGI 168
Cdd:COG0443  183 LGDGV 187
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
 2-168 1.03e-134

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: 380.44  E-value: 1.03e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd10233   45 LIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSDMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTFDVSI 161
Cdd:cd10233  125 IAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSL 204


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:cd10233  205 LTIEDGI 211
ASKHA_NBD_HSP70_BiP cd10241
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ...
 4-168 8.23e-120

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: 342.65  E-value: 8.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKETA 83
Cdd:cd10241   49 GDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVSILT 163
Cdd:cd10241  129 EAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKK-GGEKNILVFDLGGGTFDVSLLT 207


                 ....*
gi 442798775 164 IEDGI 168
Cdd:cd10241  208 IDNGV 212
ASKHA_NBD_HSP70_HSPA1-like cd24028
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ...
 4-168 2.41e-108

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: 313.68  E-value: 2.41e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIV-DKDNKPMIQVEYKGETKTFAPEEISSMILVKMKET 82
Cdd:cd24028   47 GEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQSDIKHWPFKVVeDEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  83 AEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTFDVSIL 162
Cdd:cd24028  127 AEAYLGRPVTKAVITVPAYFNDAQRQATKDAATIAGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLL 206


                 ....*.
gi 442798775 163 TIEDGI 168
Cdd:cd24028  207 SIDNGV 212
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 2-168 1.49e-107

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 320.59  E-value: 1.49e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDK-DNKPMIQVEYKGETKTFAPEEISSMILVKMK 80
Cdd:PTZ00009  50 LIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSDMKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMK 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTFDVS 160
Cdd:PTZ00009 130 EIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVS 209


                 ....*...
gi 442798775 161 ILTIEDGI 168
Cdd:PTZ00009 210 LLTIEDGI 217
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 3-168 2.52e-95

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: 287.62  E-value: 2.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775    3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDN-KPMIQVEYKGETktFAPEEISSMILVKMKE 81
Cdd:pfam00012  46 VGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQRDIKHLPYKVVKLPNgDAGVEVRYLGET--FTPEQISAMILQKLKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVSI 161
Cdd:pfam00012 124 TAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSI 202


                  ....*..
gi 442798775  162 LTIEDGI 168
Cdd:pfam00012 203 LEIGRGV 209
ASKHA_NBD_HSP70_Ssb cd24093
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ...
 2-168 8.26e-94

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: 276.86  E-value: 8.26e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd24093   44 LIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKE 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGD-EQNVLIFDLGGGTFDVS 160
Cdd:cd24093  124 IAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLGAGKSEkERHVLIFDLGGGTFDVS 203


                 ....*...
gi 442798775 161 ILTIEDGI 168
Cdd:cd24093  204 LLHIAGGV 211
dnaK PRK00290
molecular chaperone DnaK; Provisional
 4-167 1.22e-84

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 260.80  E-value: 1.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRfnDPSVSADAKHFPFKIVDKDNKPmIQVEYKGetKTFAPEEISSMILVKMKETA 83
Cdd:PRK00290  51 GQPAKRQAVTNPENTIFSIKRLMGRR--DEEVQKDIKLVPYKIVKADNGD-AWVEIDG--KKYTPQEISAMILQKLKKDA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSILT 163
Cdd:PRK00290 126 EDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKK--GDEKILVYDLGGGTFDVSILE 203


                 ....
gi 442798775 164 IEDG 167
Cdd:PRK00290 204 IGDG 207
ASKHA_NBD_HSP70_DnaK-like cd10234
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ...
 4-168 2.76e-84

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: 252.40  E-value: 2.76e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPfkiVDKDNKPMIQVEYKGetKTFAPEEISSMILVKMKETA 83
Cdd:cd10234   48 GQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVERKQVPYP---VVSAGNGDAWVEIGG--KEYTPEEISAFILQKLKKDA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSILT 163
Cdd:cd10234  123 EAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKK--KDEKILVYDLGGGTFDVSILE 200


                 ....*
gi 442798775 164 IEDGI 168
Cdd:cd10234  201 IGDGV 205
ASKHA_NBD_HSP70_HSPA9 cd11733
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ...
 4-168 3.15e-81

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: 244.87  E-value: 3.15e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMiQVEYKGetKTFAPEEISSMILVKMKETA 83
Cdd:cd11733   50 GMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQKDIKMVPYKIVKASNGDA-WVEAHG--KKYSPSQIGAFVLTKMKETA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSILT 163
Cdd:cd11733  127 ESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIAGLNVLRIINEPTAAALAYGLDKK--DDKIIAVYDLGGGTFDISILE 204


                 ....*
gi 442798775 164 IEDGI 168
Cdd:cd11733  205 IQKGV 209
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 4-168 1.81e-76

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: 238.75  E-value: 1.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775    4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIVDKDNKPMIQVEykgeTKTFAPEEISSMILVKMKETA 83
Cdd:TIGR02350  49 GQPAKRQAVTNPENTIYSIKRFMGRRFDE--VTEEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQnVLIFDLGGGTFDVSILT 163
Cdd:TIGR02350 123 EAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILE 201


                  ....*
gi 442798775  164 IEDGI 168
Cdd:TIGR02350 202 IGDGV 206
ASKHA_NBD_HSP70_Ssc1_3 cd11734
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ...
 2-168 7.33e-74

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: 226.17  E-value: 7.33e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMiQVEYKGetKTFAPEEISSMILVKMKE 81
Cdd:cd11734   48 LVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEVQRDIKEVPYKIVKHSNGDA-WVEARG--QKYSPSQIGAFVLGKMKE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSI 161
Cdd:cd11734  125 TAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGLNVLRVINEPTAAALAYGLDKS--GDKVIAVYDLGGGTFDISI 202


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:cd11734  203 LEIQKGV 209
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
 4-168 1.77e-71

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: 219.39  E-value: 1.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIVDKDNK-PMIQVEykgeTKTFAPEEISSMILVKMKET 82
Cdd:cd10236   51 GEKAKENAITDPENTISSVKRLMGRSLAD--VKEELPLLPYRLVGDENElPRFRTG----AGNLTPVEISAEILKELKQR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  83 AEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSIL 162
Cdd:cd10236  125 AEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAALAYGLDQK--KEGTIAVYDLGGGTFDISIL 202


                 ....*.
gi 442798775 163 TIEDGI 168
Cdd:cd10236  203 RLSDGV 208
dnaK CHL00094
heat shock protein 70
 2-168 8.73e-70

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 221.91  E-value: 8.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKiVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:CHL00094  49 LVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISEEAKQVSYK-VKTDSNGNIKIECPALNKDFSPEEISAQVLRKLVE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSI 161
Cdd:CHL00094 126 DASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAASLAYGLDKK--NNETILVFDLGGGTFDVSI 203


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:CHL00094 204 LEVGDGV 210
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 4-168 4.43e-68

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 213.92  E-value: 4.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKhfpfkivdkdnkpmiqveykgetkTFAPEEISSMILVKMKETA 83
Cdd:COG0443   48 GEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATEVGGK------------------------RYSPEEISALILRKLKADA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVSILT 163
Cdd:COG0443  104 EAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILR 182


                 ....*
gi 442798775 164 IEDGI 168
Cdd:COG0443  183 LGDGV 187
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
 4-168 5.80e-68

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 217.96  E-value: 5.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIvDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKETA 83
Cdd:PRK13410  51 GQLARRQLVLNPQNTFYNLKRFIGRRYDE--LDPESKRVPYTI-RRNEQGNVRIKCPRLEREFAPEELSAMILRKLADDA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKkvGDEQNVLIFDLGGGTFDVSILT 163
Cdd:PRK13410 128 SRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIAGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLE 205


                 ....*
gi 442798775 164 IEDGI 168
Cdd:PRK13410 206 VGNGV 210
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 2-168 1.40e-67

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 217.00  E-value: 1.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMiQVEYKGetKTFAPEEISSMILVKMKE 81
Cdd:PTZ00400  88 LVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKKEQKILPYKIVRASNGDA-WIEAQG--KKYSPSQIGAFVLEKMKE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSI 161
Cdd:PTZ00400 165 TAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGLDVLRIINEPTAAALAFGMDKN--DGKTIAVYDLGGGTFDISI 242


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:PTZ00400 243 LEILGGV 249
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
 2-168 3.91e-66

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 213.08  E-value: 3.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIVD-KDNkpMIQVEYKGetKTFAPEEISSMILVKMK 80
Cdd:PRK13411  49 LVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--TEEERSRVPYTCVKgRDD--TVNVQIRG--RNYTPQEISAMILQKLK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVS 160
Cdd:PRK13411 123 QDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGLEVLRIINEPTAAALAYGLDKQ-DQEQLILVFDLGGGTFDVS 201


                 ....*...
gi 442798775 161 ILTIEDGI 168
Cdd:PRK13411 202 ILQLGDGV 209
ASKHA_NBD_HSP70_HSPA13 cd10237
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ...
 4-168 7.80e-66

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: 206.42  E-value: 7.80e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDkDNKPMIQ--VEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd10237   73 GYDALAQAEHNPSNTIYDAKRFIGKTFTKEELEEEAKRYPFKVVN-DNIGSAFfeVPLNGSTLVVSPEDIGSLILLKLKK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTFDVSI 161
Cdd:cd10237  152 AAEAYLGVPVAKAVISVPAEFDEKQRNATRKAANLAGLEVLRVINEPTAAAMAYGLHKK-SDVNNVLVVDLGGGTLDVSL 230


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:cd10237  231 LNVQGGM 237
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 4-168 2.69e-62

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: 195.49  E-value: 2.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADakhfpfkivdkdnkpmiqveykgetKTFAPEEISSMILVKMKETA 83
Cdd:cd24029   48 GEEAKNQALLDPENTIYSVKRLMGRDTKDKEEIGG-------------------------KEYTPEEISAEILKKLKEDA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDkKVGDEQNVLIFDLGGGTFDVSILT 163
Cdd:cd24029  103 EEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLD-KEGKDGTILVYDLGGGTFDVSILE 181


                 ....*
gi 442798775 164 IEDGI 168
Cdd:cd24029  182 IENGK 186
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
 2-168 4.14e-61

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 199.91  E-value: 4.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDN-KPMIQveyKGETKTFAPEEISSMILVKMK 80
Cdd:PTZ00186  73 LVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKDIKNVPYKIVRAGNgDAWVQ---DGNGKQYSPSQIGAFVLEKMK 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVS 160
Cdd:PTZ00186 150 ETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKT--KDSLIAVYDLGGGTFDIS 227


                 ....*...
gi 442798775 161 ILTIEDGI 168
Cdd:PTZ00186 228 VLEIAGGV 235
hscA PRK05183
chaperone protein HscA; Provisional
 4-168 2.04e-58

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 191.93  E-value: 2.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIVDKDNKpMIQVEYKGETKTfaPEEISSMILVKMKETA 83
Cdd:PRK05183  67 GYEARANAAQDPKNTISSVKRFMGRSLAD--IQQRYPHLPYQFVASENG-MPLIRTAQGLKS--PVEVSAEILKALRQRA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKkvGDEQNVLIFDLGGGTFDVSILT 163
Cdd:PRK05183 142 EETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDS--GQEGVIAVYDLGGGTFDISILR 219


                 ....*
gi 442798775 164 IEDGI 168
Cdd:PRK05183 220 LSKGV 224
HscA TIGR01991
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ...
 4-168 4.44e-57

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: 187.86  E-value: 4.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775    4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPsvsADAKHFPFKIVDKDNKpMIQVEYKGETKTfaPEEISSMILVKMKETA 83
Cdd:TIGR01991  48 GKEALAAAAEDPKNTISSVKRLMGRSIEDI---KTFSILPYRFVDGPGE-MVRLRTVQGTVT--PVEVSAEILKKLKQRA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKkvGDEQNVLIFDLGGGTFDVSILT 163
Cdd:TIGR01991 122 EESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAVAYGLDK--ASEGIYAVYDLGGGTFDVSILK 199


                  ....*
gi 442798775  164 IEDGI 168
Cdd:TIGR01991 200 LTKGV 204
PLN03184 PLN03184
chloroplast Hsp70; Provisional
 2-168 6.04e-57

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 188.91  E-value: 6.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDpsVSADAKHFPFKIVDKDNKPmIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:PLN03184  86 LVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDEESKQVSYRVVRDENGN-VKLDCPAIGKQFAAEEISAQVLRKLVD 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvgDEQNVLIFDLGGGTFDVSI 161
Cdd:PLN03184 163 DASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFEKK--SNETILVFDLGGGTFDVSV 240


                 ....*..
gi 442798775 162 LTIEDGI 168
Cdd:PLN03184 241 LEVGDGV 247
ASKHA_NBD_HSP70_HscC cd10235
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ...
 2-168 7.81e-57

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: 181.29  E-value: 7.81e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIG----RRFNDpsvsadakhfpfkivdkdnkpmiqveykgetKTFAPEEISSMILV 77
Cdd:cd10235   45 LVGRAAKERLVTHPDRTAASFKRFMGtdkqYRLGN-------------------------------HTFRAEELSALVLK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  78 KMKETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKvGDEQNVLIFDLGGGTF 157
Cdd:cd10235   94 SLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKR-EDETRFLVFDLGGGTF 172

                        170
                 ....*....|.
gi 442798775 158 DVSILTIEDGI 168
Cdd:cd10235  173 DVSVLELFEGV 183
ASKHA_NBD_HSP70_HSP105-110-like cd11732
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ...
 3-161 8.35e-57

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: 182.37  E-value: 8.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVD-KDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd11732   45 IGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKEIKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKV----GDE-QNVLIFDLGGGT 156
Cdd:cd11732  125 IAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIAGLNCLRLINETTAAALDYGIYKSDllesEEKpRIVAFVDMGHSS 204


                 ....*
gi 442798775 157 FDVSI 161
Cdd:cd11732  205 TQVSI 209
ASKHA_NBD_HSP70_AtHsp70-14-like cd24095
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ...
 2-167 1.80e-56

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: 181.74  E-value: 1.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIV-DKDNKPMIQVEYKGETKTFAPEEISSMILVKMK 80
Cdd:cd24095   47 FLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQRDLKLFPFKVTeGPDGEIGINVNYLGEQKVFTPEQILAMLLSNLK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGL---DKKVGDEQNVLIFDLGGGTF 157
Cdd:cd24095  127 RIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQIAGLNCLRLMNETTATALAYGIyktDLPETDPTNVVFVDVGHSST 206

                        170
                 ....*....|
gi 442798775 158 DVSILTIEDG 167
Cdd:cd24095  207 QVCVVAFKKG 216
ASKHA_NBD_HSP70_HSPA14 cd10238
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ...
 4-168 5.76e-56

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: 180.13  E-value: 5.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKETA 83
Cdd:cd10238   48 GLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVGDEQ-NVLIFDLGGGTFDVSIL 162
Cdd:cd10238  128 QSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKAGFNVLRVISEPSAAALAYGIGQDDPTENsNVLVYRLGGTSLDVTVL 207


                 ....*.
gi 442798775 163 TIEDGI 168
Cdd:cd10238  208 SVNNGM 213
ASKHA_NBD_HSP70_HSPA4_like cd10228
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ...
 2-161 2.33e-55

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: 178.62  E-value: 2.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   2 MMGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVD-KDNKPMIQVEYKGETKTFAPEEISSMILVKMK 80
Cdd:cd10228   44 SMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKELKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK---VGDE--QNVLIFDLGGG 155
Cdd:cd10228  124 ETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIAGLNCLRLLNDTTAVALAYGIYKQdlpAEEEkpRNVVFVDMGHS 203


                 ....*.
gi 442798775 156 TFDVSI 161
Cdd:cd10228  204 SLQVSV 209
ASKHA_NBD_HSP70_ScSse cd24094
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ...
 3-167 8.24e-42

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: 143.67  E-value: 8.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPMIQVEYKGETKTFAPEEISSMILVKMKET 82
Cdd:cd24094   45 LGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEEEKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDT 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  83 AEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK--VGDEQ---NVLIFDLGGGTF 157
Cdd:cd24094  125 TQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAGLNPLRLMNDTTAAALGYGITKTdlPEPEEkprIVAFVDIGHSSY 204

                        170
                 ....*....|
gi 442798775 158 DVSILTIEDG 167
Cdd:cd24094  205 TVSIVAFKKG 214
ASKHA_NBD_HSP70_HSPH1 cd11739
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ...
 3-167 6.23e-38

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: 133.45  E-value: 6.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVD-KDNKPMIQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd11739   47 IGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKEKENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK---VGDEQN--VLIFDLGGGT 156
Cdd:cd11739  127 TAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQdlpAPDEKPriVVFVDMGHSA 206

                        170
                 ....*....|.
gi 442798775 157 FDVSILTIEDG 167
Cdd:cd11739  207 FQVSACAFNKG 217
ASKHA_NBD_HSP70_HSPA4 cd11737
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ...
 3-167 3.32e-37

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: 131.60  E-value: 3.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPM-IQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd11737   47 IGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAEKPSLAYELVQLPTGTTgIKVMYMEEERNFTIEQVTAMLLTKLKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK---VGDEQ--NVLIFDLGGGT 156
Cdd:cd11737  127 TAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQdlpAPEEKprNVVFVDMGHSA 206

                        170
                 ....*....|.
gi 442798775 157 FDVSILTIEDG 167
Cdd:cd11737  207 YQVSVCAFNKG 217
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
 3-167 5.43e-36

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: 128.11  E-value: 5.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   3 MGDAAKNQVAMNPHNTVFDAKRLIGRRFNDPSVSADAKHFPFKIVDKDNKPM-IQVEYKGETKTFAPEEISSMILVKMKE 81
Cdd:cd11738   47 IGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAEKIKLPYELQKMPNGSTgVKVRYLDEERVFAIEQVTGMLLTKLKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  82 TAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK---VGDEQ--NVLIFDLGGGT 156
Cdd:cd11738  127 TSENALKKPVADCVISVPSFFTDAERRSVMDAAQIAGLNCLRLMNETTAVALAYGIYKQdlpALEEKprNVVFVDMGHSA 206

                        170
                 ....*....|.
gi 442798775 157 FDVSILTIEDG 167
Cdd:cd11738  207 YQVSICAFNKG 217
ASKHA_NBD_HSP70_HYOU1 cd10230
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ...
 4-164 5.84e-32

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: 116.83  E-value: 5.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGrrfndpsvsadakhfpfkivdkdnkpmiqveykgetktFAPEEISSMILVKMKETA 83
Cdd:cd10230   49 GDDALALATRFPENTFSYLKDLLG--------------------------------------YSVEELVAMILEYAKSLA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK--VGDEQNVLIFDLGGGTFDVSI 161
Cdd:cd10230   91 ESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRRfeNNEPQNVLFYDMGASSTSATV 170


                 ...
gi 442798775 162 LTI 164
Cdd:cd10230  171 VEF 173
hscA PRK01433
chaperone protein HscA; Provisional
 64-168 1.47e-30

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 116.11  E-value: 1.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  64 KTFAPEEISSMILVKMKETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKkvGD 143
Cdd:PRK01433 114 KQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNK--NQ 191

                         90       100
                 ....*....|....*....|....*
gi 442798775 144 EQNVLIFDLGGGTFDVSILTIEDGI 168
Cdd:PRK01433 192 KGCYLVYDLGGGTFDVSILNIQEGI 216
ASKHA_NBD_HSP70_ScSsz1p-like cd10232
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ...
 4-168 4.18e-27

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: 103.98  E-value: 4.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   4 GDAAKNQVAMNPHNTVFDAKRLIGrrfndpsvsadakhfpfkivdkdnkpmiqveykgeTKTFAPEEISSMILVKMKETA 83
Cdd:cd10232   49 GSQAKAQLVRNPKNTVANFRDLLG-----------------------------------TTTLTVSEVTTRYLRRLKESA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  84 EAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKK----VGDEQNVLIFDLGGGTFDV 159
Cdd:cd10232   94 EDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLRAEtsgdTIKDKTVVVADLGGTRSDV 173


                 ....*....
gi 442798775 160 SILTIEDGI 168
Cdd:cd10232  174 TVVAVRGGL 182
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 70-169 3.11e-23

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: 93.32  E-value: 3.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  70 EISSMILVKMKETAEAYLGYDIKNA-------VITVPAYFNDSQRQATKD----AGAICGMNVLRIINEPTAAAIAYGLD 138
Cdd:cd10170   46 EVVADFLRALLEHAKAELGDRIWELekapievVITVPAGWSDAAREALREaaraAGFGSDSDNVRLVSEPEAAALYALED 125

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 442798775 139 KKVGDE----QNVLIFDLGGGTFDVSILTIEDGIS 169
Cdd:cd10170  126 KGDLLPlkpgDVVLVCDAGGGTVDLSLYEVTSGSP 160
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
 95-167 1.01e-11

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: 61.91  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  95 VITVPAYFNDSQ----RQATKDAGAICGMN--VLRIINEPTAAAIAYGLDKKVGDEQN------VLIFDLGGGTFDVSIL 162
Cdd:cd10229  144 VLTVPAIWSDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEGEEKElkpgdkYLVVDCGGGTVDITVH 223


                 ....*
gi 442798775 163 TIEDG 167
Cdd:cd10229  224 EVLED 228
ASKHA_NBD_HSP70_YegD-like cd10231
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ...
 63-164 1.20e-11

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: 61.52  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  63 TKTFAPEEISSMILVKMKETAEAYLGYDIKNAVITVPAYFNDSQRQAT-------KDAGAICGMNVLRIINEPTAAAIAY 135
Cdd:cd10231   88 GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqaesrlRDAARRAGFRNVEFQYEPIAAALDY 167

                         90       100
                 ....*....|....*....|....*....
gi 442798775 136 glDKKVGDEQNVLIFDLGGGTFDVSILTI 164
Cdd:cd10231  168 --EQRLDREELVLVVDFGGGTSDFSVLRL 194
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
 81-162 1.96e-09

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


Pssm-ID: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 55.17  E-value: 1.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNA-----------VITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDkkVGDEQNVLI 149
Cdd:cd10225   70 EATEAMLRYFIRKAhrrrgflrprvVIGVPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLP--IEEPRGSMV 147

                         90
                 ....*....|...
gi 442798775 150 FDLGGGTFDVSIL 162
Cdd:cd10225  148 VDIGGGTTEIAVI 160
ASKHA_NBD_EutJ cd24047
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ...
 46-167 1.27e-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: 49.57  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  46 IVDKDNKPM-------------IQVEYKGETKtfapeeissmILVKMKETAEAYLGYDIKNAVITVPAYFNDSQRQATKD 112
Cdd:cd24047   16 VVDEEGQPVagaleradvvrdgIVVDYIGAIR----------IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRN 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442798775 113 AGAICGMNVLRIINEPTAAAIAYGLDkkvgdeqNVLIFDLGGGTFDVSIltIEDG 167
Cdd:cd24047   86 VLEGAGLEVSNVVDEPTAANAVLGIR-------DGAVVDIGGGTTGIAV--LKDG 131
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
 81-162 2.70e-07

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


Pssm-ID: 440695 [Multi-domain]  Cd Length: 339  Bit Score: 48.92  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNA-----------VITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDkkVGDEQNVLI 149
Cdd:COG1077   78 EVTEAMLKYFIKKVhgrrsffrprvVICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP--IEEPTGNMV 155

                         90
                 ....*....|...
gi 442798775 150 FDLGGGTFDVSIL 162
Cdd:COG1077  156 VDIGGGTTEVAVI 168
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
 81-163 1.32e-06

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


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 46.78  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775   81 ETAEAYLGYDIK-----------NAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDkkVGDEQNVLI 149
Cdd:pfam06723  72 EVTEAMLKYFIKkvhgrrsfskpRVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP--VEEPTGNMV 149

                          90
                  ....*....|....
gi 442798775  150 FDLGGGTFDVSILT 163
Cdd:pfam06723 150 VDIGGGTTEVAVIS 163
PRK13929 PRK13929
rod-share determining protein MreBH; Provisional
 70-163 2.59e-06

rod-share determining protein MreBH; Provisional


Pssm-ID: 184403 [Multi-domain]  Cd Length: 335  Bit Score: 46.05  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  70 EISSMILVKMKETAEAYLGYDIK--NAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIayGLDKKVGDEQNV 147
Cdd:PRK13929  75 DMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAI--GADLPVDEPVAN 152

                         90
                 ....*....|....*.
gi 442798775 148 LIFDLGGGTFDVSILT 163
Cdd:PRK13929 153 VVVDIGGGTTEVAIIS 168
PRK15080 PRK15080
ethanolamine utilization protein EutJ; Provisional
 75-167 1.19e-05

ethanolamine utilization protein EutJ; Provisional


Pssm-ID: 237904 [Multi-domain]  Cd Length: 267  Bit Score: 44.05  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  75 ILVKMKETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDKKVgdeqnvlIFDLGG 154
Cdd:PRK15080  72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNGA-------VVDIGG 144

                         90
                 ....*....|...
gi 442798775 155 GTFDVSILtiEDG 167
Cdd:PRK15080 145 GTTGISIL--KDG 155
PRK11678 PRK11678
putative chaperone; Provisional
 69-162 1.99e-05

putative chaperone; Provisional


Pssm-ID: 236954 [Multi-domain]  Cd Length: 450  Bit Score: 43.70  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  69 EEISSMILVKMKETAEAYLGYDIKNAVITVPAYFN-----DSQRQAT---KDAGAICGMNVLRIINEPTAAaiayGLD-- 138
Cdd:PRK11678 127 EDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfe 202

                         90       100
                 ....*....|....*....|....
gi 442798775 139 KKVGDEQNVLIFDLGGGTFDVSIL 162
Cdd:PRK11678 203 ATLTEEKRVLVVDIGGGTTDCSML 226
PRK13930 PRK13930
rod shape-determining protein MreB; Provisional
 81-162 2.20e-05

rod shape-determining protein MreB; Provisional


Pssm-ID: 237564 [Multi-domain]  Cd Length: 335  Bit Score: 43.20  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIK-----------NAVITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDkkVGDEQNVLI 149
Cdd:PRK13930  79 EATEAMLRYFIKkargrrffrkpRIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLP--VTEPVGNMV 156

                         90
                 ....*....|...
gi 442798775 150 FDLGGGTFDVSIL 162
Cdd:PRK13930 157 VDIGGGTTEVAVI 169
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
 81-166 1.50e-04

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 41.04  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNA-----------VITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLD--KKVGDeqnv 147
Cdd:PRK13928  74 DVTEKMLKYFINKAcgkrffskpriMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGN---- 149

                         90
                 ....*....|....*....
gi 442798775 148 LIFDLGGGTFDVSILTIED 166
Cdd:PRK13928 150 MVVDIGGGTTDIAVLSLGG 168
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
 81-162 9.19e-04

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 38.53  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  81 ETAEAYLGYDIKNA----------VITVPAYFNDSQRQATKDAGAICGMNVLRIINEPTAAAIAYGLDkkVGDEQNVLIF 150
Cdd:PRK13927  76 DVTEKMLKYFIKKVhknfrpsprvVICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLP--VTEPTGSMVV 153

                         90
                 ....*....|..
gi 442798775 151 DLGGGTFDVSIL 162
Cdd:PRK13927 154 DIGGGTTEVAVI 165
ASKHA_NBD_HSP70_HSPA12B cd11736
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ...
 76-165 1.21e-03

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: 38.41  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798775  76 LVKMKETAEAYLGYDIKNAVITVPAYFNDSQRQATKDAGAICGM------NVLRIINEPTAAAI-AYGLDKKVgdeqnvl 148
Cdd:cd11736  125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDRYI------- 197

                         90
                 ....*....|....*..
gi 442798775 149 IFDLGGGTFDVSILTIE 165
Cdd:cd11736  198 VADCGGGTVDLTVHQIE 214
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
 120-167 1.99e-03

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


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 37.50  E-value: 1.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 442798775 120 NVLRIINEPTAAAIAYGLDKKVGDEQNVLIFDLGGGTfdVSILTIEDG 167
Cdd:cd10227  138 NDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENG 183
 
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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