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Conserved domains on  [gi|520914159|ref|WP_020333579|]
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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 ...
 1-136 7.89e-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: 196.57  E-value: 7.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159   1 MRNVDFSPLYRNAIGFDRLFNLMEaSSAKNSSGGYPPYNIEQKDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERKAE 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLE-NNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 520914159  81 EG-KNYVYQGIAERDFERKFQLADYVKVIGASMENGLLHIDLVREIPEAMQPRKIAI 136
Cdd:PRK10743  80 QKeRTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-136 7.89e-66

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 196.57  E-value: 7.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159   1 MRNVDFSPLYRNAIGFDRLFNLMEaSSAKNSSGGYPPYNIEQKDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERKAE 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLE-NNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 520914159  81 EG-KNYVYQGIAERDFERKFQLADYVKVIGASMENGLLHIDLVREIPEAMQPRKIAI 136
Cdd:PRK10743  80 QKeRTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 36-123 7.78e-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: 141.52  E-value: 7.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  36 PPYNIEQKDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERKAEEGKN--YVYQGIAERDFERKFQLADYVKVIGASME 113
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEreYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 520914159 114 NGLLHIDLVR 123
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 38-136 5.41e-34

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 114.48  E-value: 5.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  38 YNIEQKDEHnYRITMAVAGFAEEQLDLTQNENMLIVKGERKAE---EGKNYVYQGIAERDFERKFQLADYVKV--IGASM 112
Cdd:COG0071    2 VDIEETDDA-YVITADLPGVDKEDIDVTVEGNVLTISGERKEEeeeEGENYLRRERRYGSFERSFTLPDDVDVdkIEASY 80

                         90       100
                 ....*....|....*....|....
gi 520914159 113 ENGLLHIDLVREipEAMQPRKIAI 136
Cdd:COG0071   81 ENGVLTITLPKA--EEAKPRKIEI 102
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 44-136 1.32e-21

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: 83.04  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159   44 DEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERK-AEEGKNYVYQGIAERDFERKFQLADYVKV--IGASMENGLLHID 120
Cdd:pfam00011   5 DEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEeEKEDDHGLRSERSYGSFSRKFTLPENADPdkVKASLKDGVLTVT 84

                          90
                  ....*....|....*.
gi 520914159  121 LVREIPEAmQPRKIAI 136
Cdd:pfam00011  85 VPKLEPEP-KERRIQI 99
 
Name Accession Description Interval E-value
PRK10743 PRK10743
heat shock chaperone IbpA;
1-136 7.89e-66

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 196.57  E-value: 7.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159   1 MRNVDFSPLYRNAIGFDRLFNLMEaSSAKNSSGGYPPYNIEQKDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERKAE 80
Cdd:PRK10743   1 MRNFDLSPLYRSAIGFDRLFNLLE-NNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 520914159  81 EG-KNYVYQGIAERDFERKFQLADYVKVIGASMENGLLHIDLVREIPEAMQPRKIAI 136
Cdd:PRK10743  80 QKeRTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEI 136
PRK11597 PRK11597
heat shock chaperone IbpB; Provisional
 1-143 1.54e-47

heat shock chaperone IbpB; Provisional


Pssm-ID: 183223  Cd Length: 142  Bit Score: 150.28  E-value: 1.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159   1 MRNVDFSPLYRNAIGFDRLFNLMEASSaknSSGGYPPYNIEQKDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGE-RKA 79
Cdd:PRK11597   1 MRNYDLSPLLRQWIGFDKLANALQNAG---ESQSFPPYNIEKSDDNHYRITLALAGFRQEDLDIQLEGTRLTVKGTpEQP 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520914159  80 EEGKNYVYQGIAERDFERKFQLADYVKVIGASMENGLLHIDLVREIPEAMQPRKIAIGGNNLLE 143
Cdd:PRK11597  78 EKEVKWLHQGLVNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEAIAPQRIAISERPALN 141
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 36-123 7.78e-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: 141.52  E-value: 7.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  36 PPYNIEQKDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERKAEEGKN--YVYQGIAERDFERKFQLADYVKVIGASME 113
Cdd:cd06470    1 PPYNIEKTGENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEreYLHRGIAKRAFERSFNLADHVKVKGAELE 80

                         90
                 ....*....|
gi 520914159 114 NGLLHIDLVR 123
Cdd:cd06470   81 NGLLTIDLER 90
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 38-136 5.41e-34

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 114.48  E-value: 5.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  38 YNIEQKDEHnYRITMAVAGFAEEQLDLTQNENMLIVKGERKAE---EGKNYVYQGIAERDFERKFQLADYVKV--IGASM 112
Cdd:COG0071    2 VDIEETDDA-YVITADLPGVDKEDIDVTVEGNVLTISGERKEEeeeEGENYLRRERRYGSFERSFTLPDDVDVdkIEASY 80

                         90       100
                 ....*....|....*....|....
gi 520914159 113 ENGLLHIDLVREipEAMQPRKIAI 136
Cdd:COG0071   81 ENGVLTITLPKA--EEAKPRKIEI 102
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 44-136 1.32e-21

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: 83.04  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159   44 DEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERK-AEEGKNYVYQGIAERDFERKFQLADYVKV--IGASMENGLLHID 120
Cdd:pfam00011   5 DEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEeEKEDDHGLRSERSYGSFSRKFTLPENADPdkVKASLKDGVLTVT 84

                          90
                  ....*....|....*.
gi 520914159  121 LVREIPEAmQPRKIAI 136
Cdd:pfam00011  85 VPKLEPEP-KERRIQI 99
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 44-121 1.94e-20

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: 79.52  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  44 DEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERKA--EEGKNYVYQGIAERDFERKFQLADYVKV--IGASMENGLLHI 119
Cdd:cd06464    5 TDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEeeEEEENYLRRERSYGSFSRSFRLPEDVDPdkIKASLENGVLTI 84


                 ..
gi 520914159 120 DL 121
Cdd:cd06464   85 TL 86
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 40-123 1.81e-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: 64.15  E-value: 1.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  40 IEQKDEHnYRITMAVAGFAEEQLDLTQNENMLIVKGERKAEEGKNYVYqgiaeRDFERKFQLADYVKV--IGASMENGLL 117
Cdd:cd00298    1 WYQTDDE-VVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEERERSY-----GEFERSFELPEDVDPekSKASLENGVL 74


                 ....*.
gi 520914159 118 HIDLVR 123
Cdd:cd00298   75 EITLPK 80
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 43-119 2.92e-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: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  43 KDEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERK-AEEGKNYVYqgiaeRDFERKFQLADYVKV--IGASM-ENGLLH 118
Cdd:cd06526    4 DDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEeREDEHGYVS-----REFTRRYQLPEGVDPdsVTSSLsSDGVLT 78


                 .
gi 520914159 119 I 119
Cdd:cd06526   79 I 79
ACD_HspB9_like cd06481
Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 and ...
 41-119 5.91e-04

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: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  41 EQKDEHnYRITMAVAGFAEEQLDLTQNENMLIVKG--ERKAEEGK-NYVYQgiaERDFERKFQLADYV---KVIGASMEN 114
Cdd:cd06481    3 KDGKEG-FSLKLDVRGFSPEDLSVRVDGRKLVVTGkrEKKNEDEKgSFSYE---YQEFVREAQLPEHVdpeAVTCSLSPS 78


                 ....*
gi 520914159 115 GLLHI 119
Cdd:cd06481   79 GHLHI 83
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 44-121 2.60e-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: 35.15  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914159  44 DEHNYRITMAVAGFAEEQLDLTQNENMLIVKGERK-----AEEGKNYVYQgiaER---DFERKFQLADyVKV--IGASME 113
Cdd:cd06471    8 TDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDeskdeKDKKGNYIRR---ERyygSFSRSFYLPN-VDEeeIKAKYE 83


                 ....*...
gi 520914159 114 NGLLHIDL 121
Cdd:cd06471   84 NGVLKITL 91
 
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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