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Conserved domains on  [gi|689199087|gb|AIQ85676|]
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molecular chaperone protein, partial [Bradyrhizobium sp. hnkt1]

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 ...
 1-186 2.54e-125

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: 366.73  E-value: 2.54e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PRK00290 416 SQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITIT 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:PRK00290 496 ASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEAAIKELKEALKGEDKE 575

                        170       180
                 ....*....|....*....|....*.
gi 689199087 161 AIKAKTNTLAQASMKLGEAMYKQQAE 186
Cdd:PRK00290 576 AIKAKTEELTQASQKLGEAMYQQAQA 601
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 1-186 2.54e-125

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 366.73  E-value: 2.54e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PRK00290 416 SQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITIT 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:PRK00290 496 ASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEAAIKELKEALKGEDKE 575

                        170       180
                 ....*....|....*....|....*.
gi 689199087 161 AIKAKTNTLAQASMKLGEAMYKQQAE 186
Cdd:PRK00290 576 AIKAKTEELTQASQKLGEAMYQQAQA 601
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 1-182 6.13e-99

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: 298.07  E-value: 6.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087    1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:TIGR02350 414 SQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSITIT 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:TIGR02350 494 ASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAVAELKEALKGEDVE 573

                         170       180
                  ....*....|....*....|..
gi 689199087  161 AIKAKTNTLAQASMKLGEAMYK 182
Cdd:TIGR02350 574 EIKAKTEELQQALQKLAEAMYQ 595
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1-182 9.05e-89

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: 272.21  E-value: 9.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087    1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:pfam00012 417 SQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTVSAKDKGTGKEQEITIE 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:pfam00012 497 ASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDELEGDDKE 576

                         170       180
                  ....*....|....*....|..
gi 689199087  161 AIKAKTNTLAQASMKLGEAMYK 182
Cdd:pfam00012 577 EIEAKTEELAQVSQKIGERMYQ 598
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-94 8.39e-42

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 146.51  E-value: 8.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:COG0443  387 SQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIK 466

                         90
                 ....*....|....
gi 689199087  81 asgglseADIDKMV 94
Cdd:COG0443  467 -------EEIERML 473
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 1-186 2.54e-125

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 366.73  E-value: 2.54e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PRK00290 416 SQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITIT 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:PRK00290 496 ASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEAAIKELKEALKGEDKE 575

                        170       180
                 ....*....|....*....|....*.
gi 689199087 161 AIKAKTNTLAQASMKLGEAMYKQQAE 186
Cdd:PRK00290 576 AIKAKTEELTQASQKLGEAMYQQAQA 601
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 1-182 6.13e-99

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: 298.07  E-value: 6.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087    1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:TIGR02350 414 SQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSITIT 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:TIGR02350 494 ASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAVAELKEALKGEDVE 573

                         170       180
                  ....*....|....*....|..
gi 689199087  161 AIKAKTNTLAQASMKLGEAMYK 182
Cdd:TIGR02350 574 EIKAKTEELQQALQKLAEAMYQ 595
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1-182 9.05e-89

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: 272.21  E-value: 9.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087    1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:pfam00012 417 SQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTVSAKDKGTGKEQEITIE 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:pfam00012 497 ASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDELEGDDKE 576

                         170       180
                  ....*....|....*....|..
gi 689199087  161 AIKAKTNTLAQASMKLGEAMYK 182
Cdd:pfam00012 577 EIEAKTEELAQVSQKIGERMYQ 598
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 1-183 5.79e-80

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 250.90  E-value: 5.79e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PTZ00400 457 SQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQ 536

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:PTZ00400 537 SSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELKQKITKLRSTLSSEDVD 616

                        170       180
                 ....*....|....*....|...
gi 689199087 161 AIKAKTNTLAQASMKLGEAMYKQ 183
Cdd:PTZ00400 617 SIKDKTKQLQEASWKISQQAYKQ 639
dnaK CHL00094
heat shock protein 70
 1-186 7.35e-71

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 226.15  E-value: 7.35e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:CHL00094 418 SEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILSVTAKDKGTGKEQSITIQ 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:CHL00094 498 GASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEKIENLIKKLRQALQNDNYE 577

                        170       180
                 ....*....|....*....|....*.
gi 689199087 161 AIKAKTNTLAQASMKLGEAMYKQQAE 186
Cdd:CHL00094 578 SIKSLLEELQKALMEIGKEVYSSTST 603
PLN03184 PLN03184
chloroplast Hsp70; Provisional
 1-185 1.85e-68

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 220.88  E-value: 1.85e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PLN03184 455 SEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSATDKGTGKKQDITIT 534

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAE 160
Cdd:PLN03184 535 GASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVEAKLKELKDAIASGSTQ 614

                        170       180
                 ....*....|....*....|....*
gi 689199087 161 AIKAKTNTLAQASMKLGEAMYKQQA 185
Cdd:PLN03184 615 KMKDAMAALNQEVMQIGQSLYNQPG 639
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
 1-183 4.61e-65

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 211.54  E-value: 4.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PRK13411 418 SQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILKVSAQDQGTGREQSIRIT 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDD-- 158
Cdd:PRK13411 498 NTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRAEQKVEQLEAALTDPNis 577

                        170       180
                 ....*....|....*....|....*
gi 689199087 159 AEAIKAKTNTLAQASMKLGEAMYKQ 183
Cdd:PRK13411 578 LEELKQQLEEFQQALLAIGAEVYQQ 602
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
 1-181 1.20e-62

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 205.25  E-value: 1.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PRK13410 418 SDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQVSATDRTTGREQSVTIQ 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALA----EHGSKIPDTDRRAIEDAVSDLKEALKG 156
Cdd:PRK13410 498 GASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRdaalEFGPYFAERQRRAVESAMRDVQDSLEQ 577

                        170       180
                 ....*....|....*....|....*
gi 689199087 157 DDAEAIKaktntLAQASmkLGEAMY 181
Cdd:PRK13410 578 DDDRELD-----LAVAD--LQEALY 595
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
 1-185 3.66e-59

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 196.06  E-value: 3.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PTZ00186 443 SQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVTAKDKATGKTQNITIT 522

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  81 ASGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHgSKIPDTDRRAIEDAVSDLKEALKGDDA- 159
Cdd:PTZ00186 523 ANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEW-KYVSDAEKENVKTLVAELRKAMENPNVa 601

                        170       180
                 ....*....|....*....|....*..
gi 689199087 160 -EAIKAKTNTLAQASMKLGEAMYKQQA 185
Cdd:PTZ00186 602 kDDLAAATDKLQKAVMECGRTEYQQAA 628
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 1-155 2.14e-50

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 172.29  E-value: 2.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:PTZ00009 427 SQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDANGILNVSAEDKSTGKSNKITIT 506

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 689199087  81 ASGG-LSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEH--GSKIPDTDRRAIEDAVsdlKEALK 155
Cdd:PTZ00009 507 NDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEkvKGKLSDSDKATIEKAI---DEALE 581
hscA PRK05183
chaperone protein HscA; Provisional
 2-173 6.23e-49

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 167.66  E-value: 6.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   2 QVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQA 81
Cdd:PRK05183 421 QEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTAMEKSTGVEASIQVKP 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  82 SGGLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAEA 161
Cdd:PRK05183 501 SYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAIDAAMAALREVAQGDDADA 580

                        170
                 ....*....|..
gi 689199087 162 IKAKTNTLAQAS 173
Cdd:PRK05183 581 IEAAIKALDKAT 592
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-94 8.39e-42

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 146.51  E-value: 8.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   1 SQVFSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQ 80
Cdd:COG0443  387 SQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIK 466

                         90
                 ....*....|....
gi 689199087  81 asgglseADIDKMV 94
Cdd:COG0443  467 -------EEIERML 473
hscA PRK01433
chaperone protein HscA; Provisional
 4-163 1.68e-29

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 114.18  E-value: 1.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087   4 FSTAEDNQGAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQASG 83
Cdd:PRK01433 401 FTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAYEKISNTSHAIEVKPNH 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689199087  84 GLSEADIDKMVKDAEANAAEDKKRREAVDAKNHADGLVHSTEKALAEHGSKIPDTDRRAIEDAVSDLKEALKGDDAEAIK 163
Cdd:PRK01433 481 GIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINSLLDNIKEAVHARDIILIN 560
 
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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