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Conserved domains on  [gi|2168813359|gb|UHJ79913|]
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heat shock protein 70, partial [Cicer arietinum]

Protein Classification

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 ...
 1-75 1.75e-51

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: 169.13  E-value: 1.75e-51
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PRK00290  425 NQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG 499
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 1-75 1.75e-51

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 169.13  E-value: 1.75e-51
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PRK00290  425 NQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG 499
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 1-75 3.18e-44

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: 149.38  E-value: 3.18e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:TIGR02350 423 NQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSITITASSG 497
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1-75 9.68e-42

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: 142.40  E-value: 9.68e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:pfam00012 426 NQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTVSAKDKGTGKEQEITIEASEG 500
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-70 1.00e-36

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 127.63  E-value: 1.00e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITI 70
Cdd:COG0443   396 NQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITI 465
 
Name Accession Description Interval E-value
dnaK PRK00290
molecular chaperone DnaK; Provisional
 1-75 1.75e-51

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 169.13  E-value: 1.75e-51
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PRK00290  425 NQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG 499
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 1-75 3.55e-45

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 152.67  E-value: 3.55e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PTZ00400  466 NQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG 540
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
 1-75 3.18e-44

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: 149.38  E-value: 3.18e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:TIGR02350 423 NQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSITITASSG 497
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 1-75 9.68e-42

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: 142.40  E-value: 9.68e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:pfam00012 426 NQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTVSAKDKGTGKEQEITIEASEG 500
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
 1-75 7.01e-39

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 135.20  E-value: 7.01e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PTZ00186  452 NQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVTAKDKATGKTQNITITANGG 526
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
 1-70 5.97e-38

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 132.44  E-value: 5.97e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITI 70
Cdd:PRK13410  427 NQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQVSATDRTTGREQSVTI 496
dnaK CHL00094
heat shock protein 70
 1-70 1.16e-37

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 131.39  E-value: 1.16e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITI 70
Cdd:CHL00094  427 NQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILSVTAKDKGTGKEQSITI 496
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 1-70 1.00e-36

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 127.63  E-value: 1.00e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITI 70
Cdd:COG0443   396 NQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITI 465
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
 2-75 6.66e-36

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 126.79  E-value: 6.66e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168813359   2 QTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PRK13411  428 QTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILKVSAQDQGTGREQSIRITNTGG 501
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 1-75 1.31e-31

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 114.51  E-value: 1.31e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PTZ00009  436 NQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDANGILNVSAEDKSTGKSNKITITNDKG 510
PLN03184 PLN03184
chloroplast Hsp70; Provisional
 1-70 2.31e-31

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 114.18  E-value: 2.31e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITI 70
Cdd:PLN03184  464 GQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSATDKGTGKKQDITI 533
hscA PRK05183
chaperone protein HscA; Provisional
 1-75 1.45e-24

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 94.47  E-value: 1.45e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PRK05183  429 GQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTAMEKSTGVEASIQVKPSYG 503
hscA PRK01433
chaperone protein HscA; Provisional
 1-75 8.88e-20

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 81.05  E-value: 8.88e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168813359   1 NQTQVGVKVLQGEREMAADNKMLGEFELVGIPPAPRGVPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGG 75
Cdd:PRK01433  407 NQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAYEKISNTSHAIEVKPNHG 481
 
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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