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Conserved domains on  [gi|1892084087|gb|QNG40335|]
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chaperone protein, partial [Pseudochrobactrum kiredjianiae]

Protein Classification

Hsp70 family protein( domain architecture ID 1000525)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 1-156 5.47e-120

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


The actual alignment was detected with superfamily member PRK00290:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 627  Bit Score: 350.94  E-value: 5.47e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:PRK00290  235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCK 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PRK00290  315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPL 390
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 1-156 5.47e-120

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 350.94  E-value: 5.47e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:PRK00290  235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCK 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PRK00290  315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPL 390
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 1-156 3.67e-101

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: 301.92  E-value: 3.67e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:TIGR02350 233 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVR 312

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPL 388
ASKHA_NBD_HSP70_DnaK-like cd10234
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ...
 1-142 3.80e-100

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: 292.07  E-value: 3.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd10234   232 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVE 311

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQ 142
Cdd:cd10234   312 QALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1-156 9.92e-86

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: 262.20  E-value: 9.92e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQqTEINLPFITADATGpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNQ-TNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVE 313

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQG--DVKDVLLLDVTPL 156
Cdd:pfam00012 314 KALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPL 391
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-156 2.12e-77

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 237.41  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFitadaTGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:COG0443   214 PEFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVR 288

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDvllLDVTPL 156
Cdd:COG0443   289 QALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPL 361
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 1-156 5.47e-120

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 350.94  E-value: 5.47e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:PRK00290  235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCK 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PRK00290  315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPL 390
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 1-156 3.67e-101

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: 301.92  E-value: 3.67e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:TIGR02350 233 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVR 312

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPL 388
ASKHA_NBD_HSP70_DnaK-like cd10234
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ...
 1-142 3.80e-100

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: 292.07  E-value: 3.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd10234   232 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVE 311

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQ 142
Cdd:cd10234   312 QALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
ASKHA_NBD_HSP70_HSPA9 cd11733
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ...
 1-141 5.92e-97

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: 284.16  E-value: 5.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd11733   236 AEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCK 315

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd11733   316 KCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 1-156 7.66e-91

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 277.09  E-value: 7.66e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:PTZ00400  276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCE 355

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PTZ00400  356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPL 431
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1-156 9.92e-86

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: 262.20  E-value: 9.92e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQqTEINLPFITADATGpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNQ-TNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVE 313

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQG--DVKDVLLLDVTPL 156
Cdd:pfam00012 314 KALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPL 391
ASKHA_NBD_HSP70_Ssc1_3 cd11734
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ...
 1-143 1.02e-82

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: 248.13  E-value: 1.02e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd11734   236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCK 315

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQG 143
Cdd:cd11734   316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
 2-156 5.90e-80

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 248.77  E-value: 5.90e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCKA 81
Cdd:PRK13410  238 QFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKR 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1892084087  82 ALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PRK13410  318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPL 392
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
 3-156 5.23e-79

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 246.20  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   3 FKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCKAA 82
Cdd:PRK13411  238 FQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQA 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1892084087  83 LKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PRK13411  318 LKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPL 392
dnaK CHL00094
heat shock protein 70
 2-156 9.37e-79

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 244.64  E-value: 9.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCKA 81
Cdd:CHL00094  238 EFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVEN 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1892084087  82 ALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:CHL00094  318 ALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPL 392
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-156 2.12e-77

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 237.41  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFitadaTGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:COG0443   214 PEFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVR 288

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDvllLDVTPL 156
Cdd:COG0443   289 QALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPL 361
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
 2-156 9.00e-72

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 227.26  E-value: 9.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCKA 81
Cdd:PTZ00186  263 EFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQ 342

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1892084087  82 ALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PTZ00186  343 CMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPL 417
PLN03184 PLN03184
chloroplast Hsp70; Provisional
 1-156 4.72e-67

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 215.10  E-value: 4.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:PLN03184  274 SNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVE 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVLLLDVTPL 156
Cdd:PLN03184  354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPL 429
ASKHA_NBD_HSP70_HSPA1-like cd24028
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ...
 1-141 1.71e-52

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: 170.39  E-value: 1.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADatgpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd24028   239 EEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDG----IDFETTITRAKFEELCEDLFKKCLEPVE 314

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd24028   315 KVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
ASKHA_NBD_HSP70_BiP cd10241
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ...
 3-141 4.96e-51

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: 166.62  E-value: 4.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   3 FKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINlpfITADATGpKHLAIKLSRAKLESLVDDLVQRTVGPCKAA 82
Cdd:cd10241   241 FKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIE---IESLFDG-EDFSETLTRAKFEELNMDLFRKTLKPVQKV 316

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  83 LKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd10241   317 LEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
 3-143 1.38e-47

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: 157.76  E-value: 1.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   3 FKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPkhlaikLSRAKLESLVDDLVQRTVGPCKAA 82
Cdd:cd10236   233 ILKQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWERE------ITREEFEELIQPLVKRTLEPCRRA 306

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  83 LKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQG 143
Cdd:cd10236   307 LKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
hscA PRK05183
chaperone protein HscA; Provisional
 1-156 4.84e-46

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 158.03  E-value: 4.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQ-GIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLpfitADATGpkhlaiKLSRAKLESLVDDLVQRTVGPC 79
Cdd:PRK05183  246 ADWILEQaGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLAC 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1892084087  80 KAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDV--KDVLLLDVTPL 156
Cdd:PRK05183  316 RRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKpdSDMLLLDVIPL 394
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 2-141 5.78e-42

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: 142.71  E-value: 5.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFKKEQGI-DLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITadatGPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd24029   214 KIGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILDDG----KGGELEIEITREEFEELIAPLIERTIDLLE 289

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd24029   290 KALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
 1-141 7.86e-42

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: 142.77  E-value: 7.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQT--EINLPFITADatgpkhLAIKLSRAKLESLVDDLVQRTVGP 78
Cdd:cd10233   238 QEFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQAsiEIDSLFEGID------FYTSITRARFEELCADLFRSTLEP 311

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1892084087  79 CKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd10233   312 VEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 2-156 3.21e-39

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 139.93  E-value: 3.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFK-KEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQT--EINLPFITADatgpkhLAIKLSRAKLESLVDDLVQRTVGP 78
Cdd:PTZ00009  245 DFKrKNRGKDLSSNQRALRRLRTQCERAKRTLSSSTQAtiEIDSLFEGID------YNVTISRARFEELCGDYFRNTLQP 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  79 CKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVLQGD----VKDVLLLDV 153
Cdd:PTZ00009  319 VEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDV 398


                  ...
gi 1892084087 154 TPL 156
Cdd:PTZ00009  399 TPL 401
ASKHA_NBD_HSP70_HSPA13 cd10237
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ...
 13-143 1.15e-35

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: 127.46  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  13 NDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHL-AIKLSRAKLESLVDDLVQRTVGPCKAALKDAGLKAG 91
Cdd:cd10237   275 TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLFETLNEDLFQRVLEPIRQVLAEVELGKE 354

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  92 EIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQG 143
Cdd:cd10237   355 DVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
ASKHA_NBD_HSP70_Ssb cd24093
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ...
 1-141 1.28e-35

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: 126.64  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQT--EINLPFITADatgpkhLAIKLSRAKLESLVDDLVQRTVGP 78
Cdd:cd24093   238 AEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTtvEVDSLFDGED------FESSITRARFEDLNAALFKSTLEP 311

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1892084087  79 CKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd24093   312 VEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
ASKHA_NBD_HSP70_HSP105-110-like cd11732
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ...
 1-138 2.39e-32

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: 118.05  E-value: 2.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADatgpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd11732   243 EEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMED----IDFSGQIKREEFEELIQPLLARLEAPIK 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQA 138
Cdd:cd11732   319 KALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQA 376
ASKHA_NBD_HSP70_HscC cd10235
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ...
 18-143 4.66e-32

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: 116.57  E-value: 4.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  18 LQRLKEAAEKAKIELSSAQQTEINLPFitadatGPKHLAIKLSRAKLESLVDDLVQRTVGPCKAALKDAGLKAGEIDEVV 97
Cdd:cd10235   224 LAALRKRAEQAKRQLSSQDSAEIRLTY------RGEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVI 297

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1892084087  98 LVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQG 143
Cdd:cd10235   298 LVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
ASKHA_NBD_HSP70_AtHsp70-14-like cd24095
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ...
 1-142 2.87e-30

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: 112.79  E-value: 2.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADatgpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd24095   244 AEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMED----KDVKGMITREEFEELAAPLLERLLEPLE 319

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVLQ 142
Cdd:cd24095   320 KALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAMLS 381
ASKHA_NBD_HSP70_HYOU1 cd10230
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ...
 1-138 8.36e-30

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: 110.66  E-value: 8.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGI--DLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADatgpKHLAIKLSRAKLESLVDDLVQRTVGP 78
Cdd:cd10230   216 DEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEELCADLFERVVAP 291

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  79 CKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEP-HKGVNPDEVVAMGAAIQA 138
Cdd:cd10230   292 IEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
ASKHA_NBD_HSP70_HSPA14 cd10238
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ...
 1-141 5.31e-29

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: 108.87  E-value: 5.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSaQQTEINlpFITADATGpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd10238   240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLST-LNTATC--SVESLYDG-MDFQCNVSRARFESLCSSLFQQCLEPIQ 315

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFF-GKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd10238   316 EVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
ASKHA_NBD_HSP70_HSPA4_like cd10228
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ...
 1-138 6.40e-29

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: 108.90  E-value: 6.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKiELSSAQQTEI--NLPFITADatgpKHLAIKLSRAKLESLVDDLVQRTVGP 78
Cdd:cd10228   243 EEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMDD----KDVSGKMKRAEFEELCAPLFARVEVP 317

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  79 CKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQA 138
Cdd:cd10228   318 LRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQC 377
ASKHA_NBD_HSP70_ScSse cd24094
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ...
 1-141 1.41e-26

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: 102.84  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADatgpKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd24094   242 DEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMND----IDVSSMLKREEFEELIAPLLERVTAPLE 317

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd24094   318 KALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAIL 378
ASKHA_NBD_HSP70_HSPA4 cd11737
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ...
 2-140 6.28e-21

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: 87.30  E-value: 6.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFKKEQGIDLKNDKLALQRLKEAAEKAKIELSS-AQQTEINLPFITADATgpkhLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd11737   246 EFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDID----VSGTMNRGQFEEMCADLLARVEPPLR 321

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  81 AALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGV 140
Cdd:cd11737   322 SVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
ASKHA_NBD_HSP70_YegD-like cd10231
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ...
 4-135 4.35e-20

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: 85.02  E-value: 4.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   4 KKEQGIDLKNDKLAlQRLKEAAEKAKIELSSAQQTEINLPFItadatgPKHLAIKLSRAKLESLVDDLVQRTVGPCKAAL 83
Cdd:cd10231   284 KIERLLSLVEDQLG-HRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTL 356

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  84 KDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAA 135
Cdd:cd10231   357 NDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
ASKHA_NBD_HSP70_HSPH1 cd11739
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ...
 1-137 4.63e-20

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: 84.91  E-value: 4.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKiELSSAQQTEINLP---FIT-ADATGpkhlaiKLSRAKLESLVDDLVQRTV 76
Cdd:cd11739   245 AEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLPLNiecFMNdKDVSG------KMNRSQFEELCADLLQRIE 317

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  77 GPCKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQ 137
Cdd:cd11739   318 VPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
 2-141 5.06e-19

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: 81.89  E-value: 5.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   2 EFKKEQGIDLKNDKLALQRLKEAAEKAKiELSSAQQTEinLPFITADATGPKHLAIKLSRAKLESLVDDLVQRTVGPCKA 81
Cdd:cd11738   246 EFKTKYKLNVKENIRALLRLYQECEKLK-KLMSANASD--LPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  82 ALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQAGVL 141
Cdd:cd11738   323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 382
ASKHA_NBD_HSP70_ScSsz1p-like cd10232
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ...
 1-141 1.71e-18

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: 80.10  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEInlpFITADATGPK-HLAIklSRAKLESLVDDLVQRTVGPC 79
Cdd:cd10232   209 KEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPC---SVESLADGIDfHSSI--NRTRYELLASKVFQQFADLV 283

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1892084087  80 KAALKDAGLKAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHK----GVNPDEVVAMGAAIQAGVL 141
Cdd:cd10232   284 TDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 1-136 8.15e-18

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: 78.30  E-value: 8.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   1 AEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSAQQTEINLPFITADATgPKHLAIKLSRAKLESLVDDLVQRTVGPCK 80
Cdd:cd10170   189 EKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGL-PELGLEKGTLLLTEEEIRDLFDPVIDKIL 267

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892084087  81 AALKDAGL--KAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGV----NPDEVVAMGAAI 136
Cdd:cd10170   268 ELIEEQLEakSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
hscA PRK01433
chaperone protein HscA; Provisional
 57-156 1.42e-13

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 66.80  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  57 IKLSRAKLESLVDDLVQRTVGPCKAALKDAGlkAGEIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAI 136
Cdd:PRK01433  275 ISINKQTLEQLILPLVERTINIAQECLEQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAAL 352

                          90       100
                  ....*....|....*....|
gi 1892084087 137 QAGVLQGDVKDVLLLDVTPL 156
Cdd:PRK01433  353 QAENLIAPHTNSLLIDVVPL 372
PRK11678 PRK11678
putative chaperone; Provisional
 20-110 1.47e-09

putative chaperone; Provisional


Pssm-ID: 236954 [Multi-domain]  Cd Length: 450  Bit Score: 55.25  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  20 RLKEAAEKAKIELSSAQQTEINLPFITADatgpkhLAIKLSRAKLESLVDDLVQRTVGPCKAALKDAGLKAgeiDEVVLV 99
Cdd:PRK11678  336 RLVRSAEEAKIALSDQAETRASLDFISDG------LATEISQQGLEEAISQPLARILELVQLALDQAQVKP---DVIYLT 406

                          90
                  ....*....|.
gi 1892084087 100 GGMTRMPKIQE 110
Cdd:PRK11678  407 GGSARSPLIRA 417
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 49-148 5.16e-06

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


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 44.82  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  49 ATGPKHLAiklsRAKLE----SLVDdlvqrtvgpCKAALKDAGLKageIDEVVLVGGMTRMPKIQEVVKAFFGKEPHKgV 124
Cdd:COG1070   364 SHTRAHLA----RAVLEgvafALRD---------GLEALEEAGVK---IDRIRATGGGARSPLWRQILADVLGRPVEV-P 426

                          90       100
                  ....*....|....*....|....
gi 1892084087 125 NPDEVVAMGAAIQAGVLQGDVKDV 148
Cdd:COG1070   427 EAEEGGALGAALLAAVGLGLYDDL 450
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 8-140 1.16e-05

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


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 43.09  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087   8 GIDLKND-KLALQRLKEAAEKAKIELSSAQQTEINLPFITADATGPKHlaiKLSRAKLESLVDDLVQRTVGPCKAALKDA 86
Cdd:pfam14450  30 GNGITKDiAIGLRTAVEEAERLKIKYGSALASLADEDEVPGVGGREPR---EISRKELAEIIEARVEEILELVRAELEDR 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892084087  87 GLKAGEIDE-------VVLVGGMTRMPKIQEVVKAFFGKEPHKGvNPDEVVAMGAAIQAGV 140
Cdd:pfam14450 107 EVLPGEYVRlevdvhgIVLTGGGSALPGLVELAERALGLPVRIG-SPDGIGGRNPAYATAL 166
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
 45-143 4.94e-04

nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466809 [Multi-domain]  Cd Length: 443  Bit Score: 39.07  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  45 ITADATGPKHLAiklsRAKLESLVddlvqrtvgpckAALKDaGLKA-----GEIDEVVLVGGMTRMPKIQEVVKAFFGkE 119
Cdd:cd07809   358 LTLSNFTRANLA----RAALEGAT------------FGLRY-GLDIlrelgVEIDEIRLIGGGSKSPVWRQILADVFG-V 419

                          90       100
                  ....*....|....*....|....
gi 1892084087 120 PHKGVNPDEVVAMGAAIQAGVLQG 143
Cdd:cd07809   420 PVVVPETGEGGALGAALQAAWGAG 443
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
 57-136 1.09e-03

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: 38.03  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892084087  57 IKLSRAKLESLVDDLVQRTVGPCKAALKDAGLKagEIDEVVLVGGMTRMPKIQEVVKAFFGKE-----PHkgvNPDEVVA 131
Cdd:cd10229   291 LRLSPELMKSLFDPVVKKIIEHIKELLEKPELK--GVDYIFLVGGFAESPYLQKAVKEAFSTKvkiiiPP---EPGLAVV 365


                  ....*
gi 1892084087 132 MGAAI 136
Cdd:cd10229   366 KGAVL 370
ASKHA_NBD_benz_CoA_BzdP cd24107
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ...
 94-138 8.28e-03

nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar proteins; bzd-type benzoyl-CoA reductase BzdP is encoded by the gene bzdP from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdP may function the same as the D subunit of benzoyl-CoA reductase BcrD from Thauera aromatica and benzoyl-CoA reductase BadG from Rhodopseudomonas palustris.


Pssm-ID: 466957 [Multi-domain]  Cd Length: 250  Bit Score: 35.21  E-value: 8.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1892084087  94 DEVVLVGGMTRMPKIQEVVKAFFGKEPHKGVNPDEVVAMGAAIQA 138
Cdd:cd24107   206 DDVALIGGVAKNPGFVESLKELLGKEVLVPEDPEYVGALGAALIA 250
 
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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