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Conserved domains on  [gi|515659229|ref|WP_017091829|]
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MULTISPECIES: Hsp20 family protein [Vibrio]

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 4.61e-63

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: 189.25  E-value: 4.61e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229   1 MRNVDFSPLYRHAIGFERLFNLAESSTNKpSCNGYPPYNIEQKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPV 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLENNQSQ-SNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515659229  81 ETKPNYLYQGIAERNFERKFQMADYVTVKAASMGNGLLHVDLVREVPEAMQPRQISI 137
Cdd:PRK10743  80 QKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 4.61e-63

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 189.25  E-value: 4.61e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229   1 MRNVDFSPLYRHAIGFERLFNLAESSTNKpSCNGYPPYNIEQKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPV 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLENNQSQ-SNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515659229  81 ETKPNYLYQGIAERNFERKFQMADYVTVKAASMGNGLLHVDLVREVPEAMQPRQISI 137
Cdd:PRK10743  80 QKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 36-124 7.04e-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: 136.51  E-value: 7.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229  36 PPYNIEQKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPVETKP-NYLYQGIAERNFERKFQMADYVTVKAASMG 114
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEErEYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 515659229 115 NGLLHVDLVR 124
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 38-137 1.55e-27

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 97.91  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229  38 YNIEqKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQP--VETKPNYLYQGIAERNFERKFQMADYVTVKA--ASM 113
Cdd:COG0071    2 VDIE-ETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEeeEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                         90       100
                 ....*....|....*....|....
gi 515659229 114 GNGLLHVDLVREvpEAMQPRQISI 137
Cdd:COG0071   81 ENGVLTITLPKA--EEAKPRKIEI 102
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 44-138 4.52e-17

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: 71.10  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229   44 DENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPVETKPNYLYQGIAERNFERKFQM---ADYVTVKaASMGNGLLHV 120
Cdd:pfam00011   5 DEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKDGVLTV 83

                          90
                  ....*....|....*...
gi 515659229  121 DLVREVPEAmQPRQISIH 138
Cdd:pfam00011  84 TVPKLEPEP-KERRIQIQ 100
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-137 4.61e-63

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 189.25  E-value: 4.61e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229   1 MRNVDFSPLYRHAIGFERLFNLAESSTNKpSCNGYPPYNIEQKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPV 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLENNQSQ-SNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515659229  81 ETKPNYLYQGIAERNFERKFQMADYVTVKAASMGNGLLHVDLVREVPEAMQPRQISI 137
Cdd:PRK10743  80 QKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-137 9.70e-44

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 140.27  E-value: 9.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229   1 MRNVDFSPLYRHAIGFERLfnlAESSTNKPSCNGYPPYNIEQKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPV 80
Cdd:PRK11597   1 MRNYDLSPLLRQWIGFDKL---ANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTPEQP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515659229  81 ETKPNYLYQGIAERNFERKFQMADYVTVKAASMGNGLLHVDLVREVPEAMQPRQISI 137
Cdd:PRK11597  78 EKEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAI 134
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 36-124 7.04e-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: 136.51  E-value: 7.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229  36 PPYNIEQKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPVETKP-NYLYQGIAERNFERKFQMADYVTVKAASMG 114
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEErEYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 515659229 115 NGLLHVDLVR 124
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 38-137 1.55e-27

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 97.91  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229  38 YNIEqKDENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQP--VETKPNYLYQGIAERNFERKFQMADYVTVKA--ASM 113
Cdd:COG0071    2 VDIE-ETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEeeEEEGENYLRRERRYGSFERSFTLPDDVDVDKieASY 80

                         90       100
                 ....*....|....*....|....
gi 515659229 114 GNGLLHVDLVREvpEAMQPRQISI 137
Cdd:COG0071   81 ENGVLTITLPKA--EEAKPRKIEI 102
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 44-138 4.52e-17

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: 71.10  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229   44 DENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPVETKPNYLYQGIAERNFERKFQM---ADYVTVKaASMGNGLLHV 120
Cdd:pfam00011   5 DEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEKEDDHGLRSERSYGSFSRKFTLpenADPDKVK-ASLKDGVLTV 83

                          90
                  ....*....|....*...
gi 515659229  121 DLVREVPEAmQPRQISIH 138
Cdd:pfam00011  84 TVPKLEPEP-KERRIQIQ 100
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 44-122 8.93e-17

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: 69.89  E-value: 8.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229  44 DENNYRITMAVAGFSEDALTLTQNENMLIVSGEV-QPVETKPNYLYQGIAERNFERKFQMADYVTVKA--ASMGNGLLHV 120
Cdd:cd06464    5 TDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEReEEEEEEENYLRRERSYGSFSRSFRLPEDVDPDKikASLENGVLTI 84


                 ..
gi 515659229 121 DL 122
Cdd:cd06464   85 TL 86
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 44-124 1.26e-09

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: 51.44  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515659229  44 DENNYRITMAVAGFSEDALTLTQNENMLIVSGEVQPVETKpnylyqGIAERNFERKFQMADYVTVKA--ASMGNGLLHVD 121
Cdd:cd00298    4 TDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEER------ERSYGEFERSFELPEDVDPEKskASLENGVLEIT 77


                 ...
gi 515659229 122 LVR 124
Cdd:cd00298   78 LPK 80
 
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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