NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|517056375|ref|WP_018245193|]
View 

Hsp20 family protein [Rhizobium leguminosarum]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 8.75e-52

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: 161.52  E-value: 8.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375   1 MRNeFDFAPLYRSSIGFDRVFNLLNNAQRvQPVDTWPPYNIVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKAD 80
Cdd:PRK10743   1 MRN-FDLSPLYRSAIGFDRLFNLLENNQS-QSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHAD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517056375  81 KEDAQ-YLHHGIAGRSFERRFELADHVKVSGASLKNGLLSVELKLEIPEEMKPRRIPI 137
Cdd:PRK10743  79 EQKERtYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 8.75e-52

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 161.52  E-value: 8.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375   1 MRNeFDFAPLYRSSIGFDRVFNLLNNAQRvQPVDTWPPYNIVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKAD 80
Cdd:PRK10743   1 MRN-FDLSPLYRSAIGFDRLFNLLENNQS-QSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHAD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517056375  81 KEDAQ-YLHHGIAGRSFERRFELADHVKVSGASLKNGLLSVELKLEIPEEMKPRRIPI 137
Cdd:PRK10743  79 EQKERtYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 37-123 3.81e-43

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: 138.05  E-value: 3.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  37 PPYNIVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADK--EDAQYLHHGIAGRSFERRFELADHVKVSGASLK 114
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEenEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80


                 ....*....
gi 517056375 115 NGLLSVELK 123
Cdd:cd06470   81 NGLLTIDLE 89
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 39-140 4.02e-29

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 102.92  E-value: 4.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  39 YNIVKAgDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADK---EDAQYLHHGIAGRSFERRFELADHVKVSG--ASL 113
Cdd:COG0071    2 VDIEET-DDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEeeeEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                         90       100
                 ....*....|....*....|....*..
gi 517056375 114 KNGLLsvELKLEIPEEMKPRRIPIGAS 140
Cdd:COG0071   81 ENGVL--TITLPKAEEAKPRKIEIKAG 105
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 42-137 4.74e-18

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: 74.18  E-value: 4.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375   42 VKAGDDDYRIVIAVAGFGEEDLSITHERN-VLIIAGEKADKEDAQYLHHGIAGRSFERRFELADHVKVSG--ASLKNGLL 118
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNrLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLPENADPDKvkASLKDGVL 81

                          90
                  ....*....|....*....
gi 517056375  119 SVELKLEIPEEmKPRRIPI 137
Cdd:pfam00011  82 TVTVPKLEPEP-KERRIQI 99
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 8.75e-52

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 161.52  E-value: 8.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375   1 MRNeFDFAPLYRSSIGFDRVFNLLNNAQRvQPVDTWPPYNIVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKAD 80
Cdd:PRK10743   1 MRN-FDLSPLYRSAIGFDRLFNLLENNQS-QSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHAD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517056375  81 KEDAQ-YLHHGIAGRSFERRFELADHVKVSGASLKNGLLSVELKLEIPEEMKPRRIPI 137
Cdd:PRK10743  79 EQKERtYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 37-123 3.81e-43

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: 138.05  E-value: 3.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  37 PPYNIVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADK--EDAQYLHHGIAGRSFERRFELADHVKVSGASLK 114
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEenEEREYLHRGIAKRAFERSFNLADHVKVKGAELE 80


                 ....*....
gi 517056375 115 NGLLSVELK 123
Cdd:cd06470   81 NGLLTIDLE 89
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-142 1.44e-37

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 125.63  E-value: 1.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375   1 MRNeFDFAPLYRSSIGFDRVFNLLNNAQRVQpvdTWPPYNIVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAG--EK 78
Cdd:PRK11597   1 MRN-YDLSPLLRQWIGFDKLANALQNAGESQ---SFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGtpEQ 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517056375  79 ADKEdAQYLHHGIAGRSFERRFELADHVKVSGASLKNGLLSVELKLEIPEEMKPRRIPIGASEA 142
Cdd:PRK11597  77 PEKE-VKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPA 139
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 39-140 4.02e-29

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 102.92  E-value: 4.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  39 YNIVKAgDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADK---EDAQYLHHGIAGRSFERRFELADHVKVSG--ASL 113
Cdd:COG0071    2 VDIEET-DDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEeeeEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                         90       100
                 ....*....|....*....|....*..
gi 517056375 114 KNGLLsvELKLEIPEEMKPRRIPIGAS 140
Cdd:COG0071   81 ENGVL--TITLPKAEEAKPRKIEIKAG 105
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 42-123 3.53e-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: 76.82  E-value: 3.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  42 VKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDAQ--YLHHGIAGRSFERRFELADHVKVSG--ASLKNGL 117
Cdd:cd06464    2 VYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEEenYLRRERSYGSFSRSFRLPEDVDPDKikASLENGV 81


                 ....*.
gi 517056375 118 LSVELK 123
Cdd:cd06464   82 LTITLP 87
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 42-137 4.74e-18

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: 74.18  E-value: 4.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375   42 VKAGDDDYRIVIAVAGFGEEDLSITHERN-VLIIAGEKADKEDAQYLHHGIAGRSFERRFELADHVKVSG--ASLKNGLL 118
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNrLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLPENADPDKvkASLKDGVL 81

                          90
                  ....*....|....*....
gi 517056375  119 SVELKLEIPEEmKPRRIPI 137
Cdd:pfam00011  82 TVTVPKLEPEP-KERRIQI 99
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 46-123 1.12e-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: 64.92  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  46 DDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDaqylhHGIAGRSFERRFELADHVKVSG--ASLKNGLLSVELK 123
Cdd:cd00298    5 DDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEE-----RERSYGEFERSFELPEDVDPEKskASLENGVLEITLP 79
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 41-121 7.34e-07

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: 44.82  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  41 IVKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDaqylHHGIAGRSFERRFELADHVKVSG--ASL-KNGL 117
Cdd:cd06526    1 VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEERED----EHGYVSREFTRRYQLPEGVDPDSvtSSLsSDGV 76


                 ....
gi 517056375 118 LSVE 121
Cdd:cd06526   77 LTIE 80
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 42-122 1.45e-06

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: 44.01  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  42 VKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDAQ-----YLHHGIAGRSFERRFELADhVKVSG--ASLK 114
Cdd:cd06471    5 IKETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDESKDEKdkkgnYIRRERYYGSFSRSFYLPN-VDEEEikAKYE 83


                 ....*...
gi 517056375 115 NGLLSVEL 122
Cdd:cd06471   84 NGVLKITL 91
ACD_HspB1_like cd06475
Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also ...
 42-121 9.23e-06

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: 41.76  E-value: 9.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  42 VKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDaqylHHGIAGRSFERRFEL---ADHVKVSGASLKNGLL 118
Cdd:cd06475    5 IRQTADRWKVSLDVNHFAPEELVVKTKDGVVEITGKHEEKQD----EHGFVSRCFTRKYTLppgVDPTAVTSSLSPDGIL 80


                 ...
gi 517056375 119 SVE 121
Cdd:cd06475   81 TVE 83
ACD_HspB3_Like cd06477
Alpha crystallin domain (ACD) found in mammalian HspB3, also known as heat-shock protein ...
 45-123 1.14e-03

Alpha crystallin domain (ACD) found in mammalian HspB3, also known as heat-shock protein 27-like protein (HSPL27, 17-kDa) 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. HspB3 is expressed in adult skeletal muscle, smooth muscle, and heart, and in several other fetal tissues. In muscle cells HspB3 forms an oligomeric 150 kDa complex with myotonic dystrophy protein kinase-binding protein (MKBP/ HspB2), this complex may comprise one of two independent muscle-cell specific chaperone systems. The expression of HspB3 is induced during muscle differentiation controlled by the myogenic factor MyoD. HspB3 may also interact with Hsp22 (HspB8).


Pssm-ID: 107232  Cd Length: 83  Bit Score: 36.32  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056375  45 GDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDaqylHHGIAGRSFERRFELAD---HVKVSGASLKNGLLSVE 121
Cdd:cd06477    5 GKPMFQILLDVVQFRPEDIIIQVFEGWLLIKGQHGVRMD----EHGFISRSFTRQYQLPDgveHKDLSAMLCHDGILVVE 80


                 ..
gi 517056375 122 LK 123
Cdd:cd06477   81 TK 82
ACD_alphaA-crystallin_HspB4 cd06497
Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, ...
 42-112 1.18e-03

Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). 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 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract.


Pssm-ID: 107245  Cd Length: 86  Bit Score: 36.12  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517056375  42 VKAGDDDYRIVIAVAGFGEEDLSITHERNVLIIAGEKADKEDaqylHHGIAGRSFERRFELADHVKVSGAS 112
Cdd:cd06497    5 VRSDRDKFTIYLDVKHFSPEDLTVKVLDDYVEIHGKHSERQD----DHGYISREFHRRYRLPSNVDQSAIT 71
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH