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Conserved domains on  [gi|1373918076|ref|XP_024383634|]
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17.4 kDa class I heat shock protein-like [Physcomitrium patens]

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 9.30e-54

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: 164.79  E-value: 9.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  48 RIDWRETPEAHIFKADLPGLKKEEVKVRVVEGRTLEISGERKKEEVQKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQ 127
Cdd:cd06472     1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPENADADEVKAF 80

                          90
                  ....*....|..
gi 1373918076 128 VQDGVLTVTVPK 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 9.30e-54

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: 164.79  E-value: 9.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  48 RIDWRETPEAHIFKADLPGLKKEEVKVRVVEGRTLEISGERKKEEVQKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQ 127
Cdd:cd06472     1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPENADADEVKAF 80

                          90
                  ....*....|..
gi 1373918076 128 VQDGVLTVTVPK 139
Cdd:cd06472    81 LENGVLTVTVPK 92
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 50-152 1.03e-36

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: 121.56  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  50 DWRETPEAHIFKADLPGLKKEEVKVRVvEGRTLEISGERKKEEvqKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQVQ 129
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKV-EDNRLLVKGEHEEEK--EDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|...
gi 1373918076 130 DGVLTVTVPKLqEPKPQVRQIEI 152
Cdd:pfam00011  78 DGVLTVTVPKL-EPEPKERRIQI 99
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 49-152 1.05e-35

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 119.10  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  49 IDWRETPEAHIFKADLPGLKKEEVKVRVvEGRTLEISGERKKEEVQKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQV 128
Cdd:COG0071     2 VDIEETDDAYVITADLPGVDKEDIDVTV-EGNVLTISGERKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKIEASY 80

                          90       100
                  ....*....|....*....|....
gi 1373918076 129 QDGVLTVTVPKLQEPKPqvRQIEI 152
Cdd:COG0071    81 ENGVLTITLPKAEEAKP--RKIEI 102
 
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 9.30e-54

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: 164.79  E-value: 9.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  48 RIDWRETPEAHIFKADLPGLKKEEVKVRVVEGRTLEISGERKKEEVQKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQ 127
Cdd:cd06472     1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKKGDDWHRVERSSGRFVRRFRLPENADADEVKAF 80

                          90
                  ....*....|..
gi 1373918076 128 VQDGVLTVTVPK 139
Cdd:cd06472    81 LENGVLTVTVPK 92
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 50-152 1.03e-36

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: 121.56  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  50 DWRETPEAHIFKADLPGLKKEEVKVRVvEGRTLEISGERKKEEvqKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQVQ 129
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKV-EDNRLLVKGEHEEEK--EDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|...
gi 1373918076 130 DGVLTVTVPKLqEPKPQVRQIEI 152
Cdd:pfam00011  78 DGVLTVTVPKL-EPEPKERRIQI 99
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 49-152 1.05e-35

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 119.10  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  49 IDWRETPEAHIFKADLPGLKKEEVKVRVvEGRTLEISGERKKEEVQKGDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQV 128
Cdd:COG0071     2 VDIEETDDAYVITADLPGVDKEDIDVTV-EGNVLTISGERKEEEEEEGENYLRRERRYGSFERSFTLPDDVDVDKIEASY 80

                          90       100
                  ....*....|....*....|....
gi 1373918076 129 QDGVLTVTVPKLQEPKPqvRQIEI 152
Cdd:COG0071    81 ENGVLTITLPKAEEAKP--RKIEI 102
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 50-139 3.62e-33

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: 112.26  E-value: 3.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  50 DWRETPEAHIFKADLPGLKKEEVKVRVvEGRTLEISGERKKEEVQKgDTWHRVERAQGSFMRRFRLPEGTNTDEVKAQVQ 129
Cdd:cd06464     1 DVYETDDAYVVEADLPGFKKEDIKVEV-EDGVLTISGEREEEEEEE-ENYLRRERSYGSFSRSFRLPEDVDPDKIKASLE 78

                          90
                  ....*....|
gi 1373918076 130 DGVLTVTVPK 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 1.13e-23

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: 88.03  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  51 WRETPEAHIFKADLPGLKKEEVKVRVvEGRTLEISGERKKEEVQkgdtwhrvERAQGSFMRRFRLPEGTNTDEVKAQVQD 130
Cdd:cd00298     1 WYQTDDEVVVTVDLPGVKKEDIKVEV-EDNVLTISGKREEEEER--------ERSYGEFERSFELPEDVDPEKSKASLEN 71


                  ....*....
gi 1373918076 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 7.54e-21

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: 80.99  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373918076  48 RIDWRETPEAHIFKADLPGLKKEEVKVRVVEGrTLEISGERK--KEEVQKGDTWHRVERAQGSFMRRFRLPeGTNTDEVK 125
Cdd:cd06471     2 KTDIKETDDEYIVEADLPGFKKEDIKLDYKDG-YLTISAKRDesKDEKDKKGNYIRRERYYGSFSRSFYLP-NVDEEEIK 79

                          90
                  ....*....|....
gi 1373918076 126 AQVQDGVLTVTVPK 139
Cdd:cd06471    80 AKYENGVLKITLPK 93
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 63-139 5.56e-12

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: 57.92  E-value: 5.56e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1373918076  63 DLPGLKKEEVKVRVVeGRTLEISGERKKEEVQKGdtwhRVERaqgSFMRRFRLPEGTNTDEVKAQVQ-DGVLTVTVPK 139
Cdd:cd06526    14 DVKGFKPEELKVKVS-DNKLVVEGKHEEREDEHG----YVSR---EFTRRYQLPEGVDPDSVTSSLSsDGVLTIEAPK 83
ACD_HspB4-5-6 cd06478
Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the ...
 70-139 7.13e-04

Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the small heat shock protein (sHsp) HspB6, also known as Hsp20. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 on the other hand is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. HspB5's functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy. Mutations in HspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). HspB6 (Hsp20) is ubiquitous and is involved in diverse functions including regulation of glucose transport and contraction of smooth muscle, in platelet aggregation, in cardioprotection, and in the prevention of apoptosis. It interacts with the universal scaffolding and adaptor protein 14-3-3, and also with the proapoptotic protein Bax.


Pssm-ID: 107233  Cd Length: 83  Bit Score: 36.66  E-value: 7.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373918076  70 EEVKVRVVeGRTLEISGerKKEEVQkgDTWHRVERaqgSFMRRFRLPEGTNTDEVKAQVQ-DGVLTVTVPK 139
Cdd:cd06478    21 EELSVKVL-GDFVEIHG--KHEERQ--DEHGFISR---EFHRRYRLPPGVDPAAITSSLSaDGVLTISGPR 83
 
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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