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Conserved domains on  [gi|515597205|ref|WP_017029811|]
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Hsp20 family protein [Vibrio breoganii]

Protein Classification

alpha-crystallin domain-containing protein( domain architecture ID 129)

alpha-crystallin domain-containing protein similar to alpha-crystallin-type small heat shock proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
alpha-crystallin-Hsps_p23-like super family cl00175
alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a ...
 1-137 2.07e-66

alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.; The alpha-crystallin-Hsps_p23-like superfamily 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 superfamily 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).


The actual alignment was detected with superfamily member PRK10743:

Pssm-ID: 469641  Cd Length: 137  Bit Score: 198.11  E-value: 2.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205   1 MRTVDFTPLYRNAIGFDRLFNMMEtSNAKNTSGGYPPYNIEQQDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLE-NNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515597205  81 EG-KTYVYQGIAERDFERKFQLADYVKVIGATMENGLLHVDLEREIPEAMKPRKIAIN 137
Cdd:PRK10743  80 QKeRTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 2.07e-66

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 198.11  E-value: 2.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205   1 MRTVDFTPLYRNAIGFDRLFNMMEtSNAKNTSGGYPPYNIEQQDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLE-NNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515597205  81 EG-KTYVYQGIAERDFERKFQLADYVKVIGATMENGLLHVDLEREIPEAMKPRKIAIN 137
Cdd:PRK10743  80 QKeRTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 36-123 5.24e-45

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: 142.29  E-value: 5.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  36 PPYNIEQQDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE--EGKTYVYQGIAERDFERKFQLADYVKVIGATME 113
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEenEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 515597205 114 NGLLHVDLER 123
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 38-139 1.35e-32

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 111.40  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  38 YNIEQqDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE---EGKTYVYQGIAERDFERKFQLADYVKV--IGATM 112
Cdd:COG0071    2 VDIEE-TDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEeeeEGENYLRRERRYGSFERSFTLPDDVDVdkIEASY 80

                         90       100
                 ....*....|....*....|....*..
gi 515597205 113 ENGLLHVDLEREipEAMKPRKIAINGS 139
Cdd:COG0071   81 ENGVLTITLPKA--EEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 43-137 8.51e-22

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: 83.43  E-value: 8.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205   43 QDENKYRITMAVAGFSDDQMDITQKENVLIVRGERK-AEEGKTYVYQGIAERDFERKFQLADYVKV--IGATMENGLLHV 119
Cdd:pfam00011   4 EDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEeEKEDDHGLRSERSYGSFSRKFTLPENADPdkVKASLKDGVLTV 83

                          90
                  ....*....|....*...
gi 515597205  120 DLEREIPEAmKPRKIAIN 137
Cdd:pfam00011  84 TVPKLEPEP-KERRIQIQ 100
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 2.07e-66

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 198.11  E-value: 2.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205   1 MRTVDFTPLYRNAIGFDRLFNMMEtSNAKNTSGGYPPYNIEQQDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLE-NNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515597205  81 EG-KTYVYQGIAERDFERKFQLADYVKVIGATMENGLLHVDLEREIPEAMKPRKIAIN 137
Cdd:PRK10743  80 QKeRTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN 137
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 36-123 5.24e-45

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: 142.29  E-value: 5.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  36 PPYNIEQQDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE--EGKTYVYQGIAERDFERKFQLADYVKVIGATME 113
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEenEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 515597205 114 NGLLHVDLER 123
Cdd:cd06470   81 NGLLTIDLER 90
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-144 7.33e-45

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 143.73  E-value: 7.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205   1 MRTVDFTPLYRNAIGFDRLFNMMETSNaknTSGGYPPYNIEQQDENKYRITMAVAGFSDDQMDITQKENVLIVRGE-RKA 79
Cdd:PRK11597   1 MRNYDLSPLLRQWIGFDKLANALQNAG---ESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTpEQP 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515597205  80 EEGKTYVYQGIAERDFERKFQLADYVKVIGATMENGLLHVDLEREIPEAMKPRKIAINGSNLIES 144
Cdd:PRK11597  78 EKEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPALNS 142
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 38-139 1.35e-32

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 111.40  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  38 YNIEQqDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAE---EGKTYVYQGIAERDFERKFQLADYVKV--IGATM 112
Cdd:COG0071    2 VDIEE-TDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEeeeEGENYLRRERRYGSFERSFTLPDDVDVdkIEASY 80

                         90       100
                 ....*....|....*....|....*..
gi 515597205 113 ENGLLHVDLEREipEAMKPRKIAINGS 139
Cdd:COG0071   81 ENGVLTITLPKA--EEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 43-137 8.51e-22

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: 83.43  E-value: 8.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205   43 QDENKYRITMAVAGFSDDQMDITQKENVLIVRGERK-AEEGKTYVYQGIAERDFERKFQLADYVKV--IGATMENGLLHV 119
Cdd:pfam00011   4 EDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEeEKEDDHGLRSERSYGSFSRKFTLPENADPdkVKASLKDGVLTV 83

                          90
                  ....*....|....*...
gi 515597205  120 DLEREIPEAmKPRKIAIN 137
Cdd:pfam00011  84 TVPKLEPEP-KERRIQIQ 100
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 43-123 6.55e-19

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: 75.67  E-value: 6.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  43 QDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKA--EEGKTYVYQGIAERDFERKFQLADYVKV--IGATMENGLLH 118
Cdd:cd06464    4 ETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEeeEEEENYLRRERSYGSFSRSFRLPEDVDPdkIKASLENGVLT 83


                 ....*
gi 515597205 119 VDLER 123
Cdd:cd06464   84 ITLPK 88
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 43-123 6.68e-14

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: 62.61  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  43 QDENKYRITMAVAGFSDDQMDITQKENVLIVRGERKAEEGKTYVYqgiaeRDFERKFQLADYVKV--IGATMENGLLHVD 120
Cdd:cd00298    3 QTDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEERERSY-----GEFERSFELPEDVDPekSKASLENGVLEIT 77


                 ...
gi 515597205 121 LER 123
Cdd:cd00298   78 LPK 80
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 43-119 3.36e-05

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: 40.20  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  43 QDENKYRITMAVAGFSDDQMDITQKENVLIVRGERK-AEEGKTYVYqgiaeRDFERKFQLADYVKV--IGATM-ENGLLH 118
Cdd:cd06526    4 DDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEeREDEHGYVS-----REFTRRYQLPEGVDPdsVTSSLsSDGVLT 78


                 .
gi 515597205 119 V 119
Cdd:cd06526   79 I 79
ACD_HspB1_like cd06475
Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also ...
 42-120 4.47e-05

Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also denoted HspB1 in human) 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. Hsp27 shows enhanced synthesis in response to stress. It is a molecular chaperone which interacts with a large number of different proteins. It is found in many types of human cells including breast, uterus, cervix, platelets and cancer cells. Hsp27 has diverse cellular functions including, chaperoning, regulation of actin polymerization, keratinocyte differentiation, regulation of inflammatory pathways in keratinocytes, and protection from oxidative stress through modulating glutathione levels. It is also a subunit of AUF1-containing protein complexes. It has been linked to several transduction pathways regulating cellular functions including differentiation, cell growth, development, and apoptosis. Its activity can be regulated by phosphorylation. Its unphosphorylated state is a high molecular weight aggregated form (100-800kDa) composed of up to 24 subunits, which forms as a result of multiple interactions within the ACD, and is required for chaperone function and resistance to oxidative stress. Upon phosphorylation these large aggregates rapidly disassociate to smaller oligomers and chaperone activity is modified. High constitutive levels of Hsp27 have been detected in various cancer cells, in particular those of carcinoma origin. Over-expression of Hsp27 has a protective effect against various diseases-processes, including Huntington's disease. Mutations in Hsp27 have been associated with a form of distal hereditary motor neuropathy type II and Charcot-Marie-Tooth disease type 2.


Pssm-ID: 107230  Cd Length: 86  Bit Score: 39.83  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  42 QQDENKYRITMAVAGFSDDQMDITQKENVLIVRGerKAEEGKTyvYQGIAERDFERKFQL---ADYVKVIGATMENGLLH 118
Cdd:cd06475    6 RQTADRWKVSLDVNHFAPEELVVKTKDGVVEITG--KHEEKQD--EHGFVSRCFTRKYTLppgVDPTAVTSSLSPDGILT 81


                 ..
gi 515597205 119 VD 120
Cdd:cd06475   82 VE 83
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 42-121 4.33e-03

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: 34.38  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515597205  42 QQDENKYRITMAVAGFSDDQMDITQKENVLIVRGERK-----AEEGKTYVYQgiaER---DFERKFQLADyVKV--IGAT 111
Cdd:cd06471    6 KETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDeskdeKDKKGNYIRR---ERyygSFSRSFYLPN-VDEeeIKAK 81

                         90
                 ....*....|
gi 515597205 112 MENGLLHVDL 121
Cdd:cd06471   82 YENGVLKITL 91
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 69-119 9.83e-03

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: 33.43  E-value: 9.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515597205  69 NVLIVRGERKAEEGKTYVYQGIAERD---FERKFQL-----ADYVKvigATMENGLLHV 119
Cdd:cd06472   33 RVLRISGERKKEEEKKGDDWHRVERSsgrFVRRFRLpenadADEVK---AFLENGVLTV 88
 
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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