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Conserved domains on  [gi|2472930855|ref|NP_001406291|]
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23.2 kDa heat shock protein precursor [Oryza sativa Japonica Group]

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 ...
 77-172 5.17e-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: 155.16  E-value: 5.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  77 RVDWRETGDAHEVVVDVPGMRKEDLRVEVEDNRVLRISGERRREETTEqkggGDHWHREERSYGRFWRQLRLPDNADLDS 156
Cdd:cd06472     1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKK----GDDWHRVERSSGRFVRRFRLPENADADE 76

                          90
                  ....*....|....*.
gi 2472930855 157 IAASLDNGVLTVRFRK 172
Cdd:cd06472    77 VKAFLENGVLTVTVPK 92
 
Name Accession Description Interval E-value
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 77-172 5.17e-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: 155.16  E-value: 5.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  77 RVDWRETGDAHEVVVDVPGMRKEDLRVEVEDNRVLRISGERRREETTEqkggGDHWHREERSYGRFWRQLRLPDNADLDS 156
Cdd:cd06472     1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKK----GDDWHRVERSSGRFVRRFRLPENADADE 76

                          90
                  ....*....|....*.
gi 2472930855 157 IAASLDNGVLTVRFRK 172
Cdd:cd06472    77 VKAFLENGVLTVTVPK 92
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 78-189 7.93e-33

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 114.09  E-value: 7.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  78 VDWRETGDAHEVVVDVPGMRKEDLRVEVEDNrVLRISGERRREETTEqkggGDHWHREERSYGRFWRQLRLPDNADLDSI 157
Cdd:COG0071     2 VDIEETDDAYVITADLPGVDKEDIDVTVEGN-VLTISGERKEEEEEE----GENYLRRERRYGSFERSFTLPDDVDVDKI 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2472930855 158 AASLDNGVLTVRFRKLAPDQikgPRVVGIASA 189
Cdd:COG0071    77 EASYENGVLTITLPKAEEAK---PRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 79-186 8.09e-33

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: 113.86  E-value: 8.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  79 DWRETGDAHEVVVDVPGMRKEDLRVEVEDNRVLRISGERRREEtteqkggGDHWHREERSYGRFWRQLRLPDNADLDSIA 158
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKE-------DDHGLRSERSYGSFSRKFTLPENADPDKVK 73

                          90       100
                  ....*....|....*....|....*...
gi 2472930855 159 ASLDNGVLTVRFRKLAPDqiKGPRVVGI 186
Cdd:pfam00011  74 ASLKDGVLTVTVPKLEPE--PKERRIQI 99
 
Name Accession Description Interval E-value
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 77-172 5.17e-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: 155.16  E-value: 5.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  77 RVDWRETGDAHEVVVDVPGMRKEDLRVEVEDNRVLRISGERRREETTEqkggGDHWHREERSYGRFWRQLRLPDNADLDS 156
Cdd:cd06472     1 RVDWKETPEAHVFKADVPGVKKEDVKVEVEDGRVLRISGERKKEEEKK----GDDWHRVERSSGRFVRRFRLPENADADE 76

                          90
                  ....*....|....*.
gi 2472930855 157 IAASLDNGVLTVRFRK 172
Cdd:cd06472    77 VKAFLENGVLTVTVPK 92
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 79-172 9.29e-34

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: 116.11  E-value: 9.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  79 DWRETGDAHEVVVDVPGMRKEDLRVEVEDNrVLRISGERRREETTEqkgggDHWHREERSYGRFWRQLRLPDNADLDSIA 158
Cdd:cd06464     1 DVYETDDAYVVEADLPGFKKEDIKVEVEDG-VLTISGEREEEEEEE-----ENYLRRERSYGSFSRSFRLPEDVDPDKIK 74

                          90
                  ....*....|....
gi 2472930855 159 ASLDNGVLTVRFRK 172
Cdd:cd06464    75 ASLENGVLTITLPK 88
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 78-189 7.93e-33

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 114.09  E-value: 7.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  78 VDWRETGDAHEVVVDVPGMRKEDLRVEVEDNrVLRISGERRREETTEqkggGDHWHREERSYGRFWRQLRLPDNADLDSI 157
Cdd:COG0071     2 VDIEETDDAYVITADLPGVDKEDIDVTVEGN-VLTISGERKEEEEEE----GENYLRRERRYGSFERSFTLPDDVDVDKI 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2472930855 158 AASLDNGVLTVRFRKLAPDQikgPRVVGIASA 189
Cdd:COG0071    77 EASYENGVLTITLPKAEEAK---PRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 79-186 8.09e-33

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: 113.86  E-value: 8.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  79 DWRETGDAHEVVVDVPGMRKEDLRVEVEDNRVLRISGERRREEtteqkggGDHWHREERSYGRFWRQLRLPDNADLDSIA 158
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKE-------DDHGLRSERSYGSFSRKFTLPENADPDKVK 73

                          90       100
                  ....*....|....*....|....*...
gi 2472930855 159 ASLDNGVLTVRFRKLAPDqiKGPRVVGI 186
Cdd:pfam00011  74 ASLKDGVLTVTVPKLEPE--PKERRIQI 99
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 80-172 1.19e-24

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: 92.27  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  80 WRETGDAHEVVVDVPGMRKEDLRVEVEDNRvLRISGERRREETteqkgggdhwhrEERSYGRFWRQLRLPDNADLDSIAA 159
Cdd:cd00298     1 WYQTDDEVVVTVDLPGVKKEDIKVEVEDNV-LTISGKREEEEE------------RERSYGEFERSFELPEDVDPEKSKA 67

                          90
                  ....*....|...
gi 2472930855 160 SLDNGVLTVRFRK 172
Cdd:cd00298    68 SLENGVLEITLPK 80
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 77-172 2.39e-23

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: 89.46  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  77 RVDWRETGDAHEVVVDVPGMRKEDLRVEVEDNrVLRISGErrREETTEQKGGGDHWHREERSYGRFWRQLRLPdNADLDS 156
Cdd:cd06471     2 KTDIKETDDEYIVEADLPGFKKEDIKLDYKDG-YLTISAK--RDESKDEKDKKGNYIRRERYYGSFSRSFYLP-NVDEEE 77

                          90
                  ....*....|....*.
gi 2472930855 157 IAASLDNGVLTVRFRK 172
Cdd:cd06471    78 IKAKYENGVLKITLPK 93
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 88-169 2.46e-09

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: 52.14  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  88 EVVVDVPGMRKEDLRVEVEDNRVLrISGErrREETTEQKGggdhwhreeRSYGRFWRQLRLPDNADLDSIAASL-DNGVL 166
Cdd:cd06526    10 QVTLDVKGFKPEELKVKVSDNKLV-VEGK--HEEREDEHG---------YVSREFTRRYQLPEGVDPDSVTSSLsSDGVL 77


                  ...
gi 2472930855 167 TVR 169
Cdd:cd06526    78 TIE 80
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 85-172 3.60e-09

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: 52.15  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  85 DAHEVVVDVPGMRKEDLRVEVEDNrVLRISGeRRREETTEQKgggdHW-HReERSYGRFWRQLRLPDNADLDSiaASLDN 163
Cdd:cd06470    11 NNYRITLAVAGFSEDDLEIEVENN-QLTVTG-KKADEENEER----EYlHR-GIAKRAFERSFNLADHVKVKG--AELEN 81


                  ....*....
gi 2472930855 164 GVLTVRFRK 172
Cdd:cd06470    82 GLLTIDLER 90
ACD_HspB7_like cd06479
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also ...
 81-172 7.13e-04

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), 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. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies.


Pssm-ID: 107234  Cd Length: 81  Bit Score: 37.21  E-value: 7.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  81 RETGDAHEVVVDVPGMRKEDLRVEVEDNRVlrisgerrreETTEQKGGGDhwhreERSYGRFWRQLRLPDNADLDSIAAS 160
Cdd:cd06479     4 KTLGDTYQFAVDVSDFSPEDIIVTTSNNQI----------EVHAEKLASD-----GTVMNTFTHKCQLPEDVDPTSVSSS 68

                          90
                  ....*....|...
gi 2472930855 161 L-DNGVLTVRFRK 172
Cdd:cd06479    69 LgEDGTLTIKARR 81
ACD_HspB1_like cd06475
Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also ...
 81-168 1.49e-03

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: 36.36  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  81 RETGDAHEVVVDVPGMRKEDLRVEVEDNrVLRISGerRREETTEQKGggdhwhREERSygrFWRQLRLPDNADLDSIAAS 160
Cdd:cd06475     6 RQTADRWKVSLDVNHFAPEELVVKTKDG-VVEITG--KHEEKQDEHG------FVSRC---FTRKYTLPPGVDPTAVTSS 73


                  ....*....
gi 2472930855 161 LD-NGVLTV 168
Cdd:cd06475    74 LSpDGILTV 82
ACD_HspB9_like cd06481
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 and ...
 88-169 1.56e-03

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 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. Human (h) HspB9 is expressed exclusively in the normal testis and in various tumor samples and is a cancer/testis antigen. hHspB9 interacts with TCTEL1 (T-complex testis expressed protein -1), a subunit of dynein. hHspB9 and TCTEL1 are co-expressed in similar cells within the testis and in tumor cells. Included in this group is Xenopus Hsp30, a developmentally-regulated heat-inducible molecular chaperone.


Pssm-ID: 107236  Cd Length: 87  Bit Score: 36.61  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2472930855  88 EVVVDVPGMRKEDLRVEVeDNRVLRISGERRREETTEQKGggdhwhrEERSYGRFWRQLRLPDNADLDSIAASL-DNGVL 166
Cdd:cd06481    10 SLKLDVRGFSPEDLSVRV-DGRKLVVTGKREKKNEDEKGS-------FSYEYQEFVREAQLPEHVDPEAVTCSLsPSGHL 81


                  ...
gi 2472930855 167 TVR 169
Cdd:cd06481    82 HIR 84
 
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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