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Conserved domains on  [gi|75279027|sp|O82012|]
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RecName: Full=17.6 kDa class I heat shock protein; AltName: Full=Hsp20.0

Protein Classification

Hsp26/alpha crystallin family protein( domain architecture ID 10158136)

Hsp26/alpha crystallin family protein, most likely a small heat shock protein that suppresses protein aggregation and protects against cell stress, induced by heat, osmotic, or acid shock

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 48-139 1.14e-49

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.


:

Pssm-ID: 107229  Cd Length: 92  Bit Score: 154.39  E-value: 1.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  48 RIDWKETPEAHVFKADLPGLKKEEVKVEVEEDRVLQISGERNVEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKAS 127
Cdd:cd06472   1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPENADADEVKAF 80

                        90
                ....*....|..
gi 75279027 128 MENGVLTVTVPK 139
Cdd:cd06472  81 LENGVLTVTVPK 92
 
Name Accession Description Interval E-value
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 48-139 1.14e-49

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.


Pssm-ID: 107229  Cd Length: 92  Bit Score: 154.39  E-value: 1.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  48 RIDWKETPEAHVFKADLPGLKKEEVKVEVEEDRVLQISGERNVEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKAS 127
Cdd:cd06472   1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPENADADEVKAF 80

                        90
                ....*....|..
gi 75279027 128 MENGVLTVTVPK 139
Cdd:cd06472  81 LENGVLTVTVPK 92
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 50-153 1.28e-30

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


Pssm-ID: 459629  Cd Length: 100  Bit Score: 106.15  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027    50 DWKETPEAHVFKADLPGLKKEEVKVEVEEDRVLQISGErnvEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKASME 129
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEH---EEEKEDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|....
gi 75279027   130 NGVLTVTVPKEEvNNPDVKSIEIS 153
Cdd:pfam00011  78 DGVLTVTVPKLE-PEPKERRIQIQ 100
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 49-153 1.90e-27

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439841  Cd Length: 105  Bit Score: 98.30  E-value: 1.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  49 IDWKETPEAHVFKADLPGLKKEEVKVEVEeDRVLQISGERNVEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKASM 128
Cdd:COG0071   2 VDIEETDDAYVITADLPGVDKEDIDVTVE-GNVLTISGERKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKIEASY 80

                        90       100
                ....*....|....*....|....*
gi 75279027 129 ENGVLTVTVPKEEVNNPdvKSIEIS 153
Cdd:COG0071  81 ENGVLTITLPKAEEAKP--RKIEIK 103
 
Name Accession Description Interval E-value
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 48-139 1.14e-49

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.


Pssm-ID: 107229  Cd Length: 92  Bit Score: 154.39  E-value: 1.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  48 RIDWKETPEAHVFKADLPGLKKEEVKVEVEEDRVLQISGERNVEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKAS 127
Cdd:cd06472   1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPENADADEVKAF 80

                        90
                ....*....|..
gi 75279027 128 MENGVLTVTVPK 139
Cdd:cd06472  81 LENGVLTVTVPK 92
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 50-153 1.28e-30

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


Pssm-ID: 459629  Cd Length: 100  Bit Score: 106.15  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027    50 DWKETPEAHVFKADLPGLKKEEVKVEVEEDRVLQISGErnvEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKASME 129
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEH---EEEKEDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|....
gi 75279027   130 NGVLTVTVPKEEvNNPDVKSIEIS 153
Cdd:pfam00011  78 DGVLTVTVPKLE-PEPKERRIQIQ 100
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 49-153 1.90e-27

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439841  Cd Length: 105  Bit Score: 98.30  E-value: 1.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  49 IDWKETPEAHVFKADLPGLKKEEVKVEVEeDRVLQISGERNVEKEDKNDTWHRVERSSGKFMRRFRLPENAKMDQVKASM 128
Cdd:COG0071   2 VDIEETDDAYVITADLPGVDKEDIDVTVE-GNVLTISGERKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKIEASY 80

                        90       100
                ....*....|....*....|....*
gi 75279027 129 ENGVLTVTVPKEEVNNPdvKSIEIS 153
Cdd:COG0071  81 ENGVLTITLPKAEEAKP--RKIEIK 103
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 50-139 2.01e-25

Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107221  Cd Length: 88  Bit Score: 92.62  E-value: 2.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  50 DWKETPEAHVFKADLPGLKKEEVKVEVEeDRVLQISGERNVEKEDKnDTWHRVERSSGKFMRRFRLPENAKMDQVKASME 129
Cdd:cd06464   1 DVYETDDAYVVEADLPGFKKEDIKVEVE-DGVLTISGEREEEEEEE-ENYLRRERSYGSFSRSFRLPEDVDPDKIKASLE 78

                        90
                ....*....|
gi 75279027 130 NGVLTVTVPK 139
Cdd:cd06464  79 NGVLTITLPK 88
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 51-139 4.65e-16

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 68.38  E-value: 4.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  51 WKETPEAHVFKADLPGLKKEEVKVEVEeDRVLQISGERNVEKEdkndtwhrVERSSGKFMRRFRLPENAKMDQVKASMEN 130
Cdd:cd00298   1 WYQTDDEVVVTVDLPGVKKEDIKVEVE-DNVLTISGKREEEEE--------RERSYGEFERSFELPEDVDPEKSKASLEN 71


                ....*....
gi 75279027 131 GVLTVTVPK 139
Cdd:cd00298  72 GVLEITLPK 80
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 48-139 3.05e-15

Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to Lactobacillus plantarum (Lp) small heat shock proteins (sHsp) HSP 18.5, HSP 18.55 and HSP 19.3. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Transcription of the genes encoding Lp HSP 18.5, 18.55 and 19.3 is regulated by a variety of stresses including heat, cold and ethanol. Early growing L. plantarum cells contain elevated levels of these mRNAs which rapidly fall of as the cells enter stationary phase. Also belonging to this group is Bifidobacterium breve (Bb) HSP20 and Oenococcus oenis (syn. Leuconostoc oenos) (Oo) HSP18. Transcription of the gene encoding BbHSP20 is strongly induced following heat or osmotic shock, and that of the gene encoding OoHSP18 following heat, ethanol or acid shock. OoHSP18 is peripherally associated with the cytoplasmic membrane.


Pssm-ID: 107228  Cd Length: 93  Bit Score: 66.73  E-value: 3.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  48 RIDWKETPEAHVFKADLPGLkKEEVKVEVEEDRVLQISGERNVEKE--DKNDTWHRVERSSGKFMRRFRLPeNAKMDQVK 125
Cdd:cd06471   2 KTDIKETDDEYIVEADLPGF-KKEDIKLDYKDGYLTISAKRDESKDekDKKGNYIRRERYYGSFSRSFYLP-NVDEEEIK 79

                        90
                ....*....|....
gi 75279027 126 ASMENGVLTVTVPK 139
Cdd:cd06471  80 AKYENGVLKITLPK 93
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 79-139 2.29e-08

Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107247  Cd Length: 83  Bit Score: 48.67  E-value: 2.29e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75279027  79 DRVLQISGERnvekEDKNDTWHRVERSsgkFMRRFRLPENAKMDQVKASM-ENGVLTVTVPK 139
Cdd:cd06526  29 DNKLVVEGKH----EEREDEHGYVSRE---FTRRYQLPEGVDPDSVTSSLsSDGVLTIEAPK 83
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 77-135 2.77e-04

Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. IbpA and IbpB are 16 kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600-kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal. IbpA also forms multimers.


Pssm-ID: 107227  Cd Length: 90  Bit Score: 37.90  E-value: 2.77e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75279027  77 EEDRVLQISGERNvEKEDKNDTW-HRvERSSGKFMRRFRLPENAKMdqVKASMENGVLTV 135
Cdd:cd06470  31 VENNQLTVTGKKA-DEENEEREYlHR-GIAKRAFERSFNLADHVKV--KGAELENGLLTI 86
 
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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