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Conserved domains on  [gi|1002302348|ref|XP_015614562|]
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17.7 kDa class II heat shock protein [Oryza sativa Japonica Group]

Protein Classification

Hsp20/alpha crystallin family protein( domain architecture ID 10157978)

Hsp20/alpha crystallin family protein is a small, stress-induced protein, between 12-43 kDa, which functions as an ATP-independent chaperone that prevents aggregation and protects against cell stress, induced by heat, osmotic, or acid shock

CATH:  2.60.40.790
Gene Ontology:  GO:0006950
PubMed:  10950306|11875128|16165157|11908065|7723051
SCOP:  4002439

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 26-99 6.43e-14

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: 63.34  E-value: 6.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  26 TLTIDLsaKGYKKEHIKVQLvrSRRRLVVSGECPVAGETN--------RWSRFRLQFPVPDGCDLKAIQARLHDGVIRVT 97
Cdd:cd06464    10 VVEADL--PGFKKEDIKVEV--EDGVLTISGEREEEEEEEenylrrerSYGSFSRSFRLPEDVDPDKIKASLENGVLTIT 85


                  ..
gi 1002302348  98 LP 99
Cdd:cd06464    86 LP 87
 
Name Accession Description Interval E-value
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 26-99 6.43e-14

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: 63.34  E-value: 6.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  26 TLTIDLsaKGYKKEHIKVQLvrSRRRLVVSGECPVAGETN--------RWSRFRLQFPVPDGCDLKAIQARLHDGVIRVT 97
Cdd:cd06464    10 VVEADL--PGFKKEDIKVEV--EDGVLTISGEREEEEEEEenylrrerSYGSFSRSFRLPEDVDPDKIKASLENGVLTIT 85


                  ..
gi 1002302348  98 LP 99
Cdd:cd06464    86 LP 87
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 18-106 1.10e-10

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: 55.31  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  18 MVREPPTHTLTIDLSakGYKKEHIKVQLVRsrRRLVVSGECPVAGETNRWSR-------FRLQFPVPDGCDLKAIQARLH 90
Cdd:pfam00011   2 IKEDEDAFEVRLDVP--GFKPEELKVKVED--NRLLVKGEHEEEKEDDHGLRsersygsFSRKFTLPENADPDKVKASLK 77

                          90
                  ....*....|....*.
gi 1002302348  91 DGVIRVTLPGVKPQQQ 106
Cdd:pfam00011  78 DGVLTVTVPKLEPEPK 93
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 26-99 7.90e-10

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 53.23  E-value: 7.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  26 TLTIDLSakGYKKEHIKVQLvrSRRRLVVSGECPVAGETN---------RWSRFRLQFPVPDGCDLKAIQARLHDGVIRV 96
Cdd:COG0071    12 VITADLP--GVDKEDIDVTV--EGNVLTISGERKEEEEEEgenylrrerRYGSFERSFTLPDDVDVDKIEASYENGVLTI 87


                  ...
gi 1002302348  97 TLP 99
Cdd:COG0071    88 TLP 90
 
Name Accession Description Interval E-value
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 26-99 6.43e-14

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: 63.34  E-value: 6.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  26 TLTIDLsaKGYKKEHIKVQLvrSRRRLVVSGECPVAGETN--------RWSRFRLQFPVPDGCDLKAIQARLHDGVIRVT 97
Cdd:cd06464    10 VVEADL--PGFKKEDIKVEV--EDGVLTISGEREEEEEEEenylrrerSYGSFSRSFRLPEDVDPDKIKASLENGVLTIT 85


                  ..
gi 1002302348  98 LP 99
Cdd:cd06464    86 LP 87
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 26-99 3.23e-13

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: 61.45  E-value: 3.23e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002302348  26 TLTIDLsaKGYKKEHIKVQLvrSRRRLVVSGECPVAGETNRWSR-FRLQFPVPDGCDLKAIQARLHDGVIRVTLP 99
Cdd:cd00298     9 VVTVDL--PGVKKEDIKVEV--EDNVLTISGKREEEEERERSYGeFERSFELPEDVDPEKSKASLENGVLEITLP 79
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 18-106 1.10e-10

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: 55.31  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  18 MVREPPTHTLTIDLSakGYKKEHIKVQLVRsrRRLVVSGECPVAGETNRWSR-------FRLQFPVPDGCDLKAIQARLH 90
Cdd:pfam00011   2 IKEDEDAFEVRLDVP--GFKPEELKVKVED--NRLLVKGEHEEEKEDDHGLRsersygsFSRKFTLPENADPDKVKASLK 77

                          90
                  ....*....|....*.
gi 1002302348  91 DGVIRVTLPGVKPQQQ 106
Cdd:pfam00011  78 DGVLTVTVPKLEPEPK 93
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 26-99 7.90e-10

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


Pssm-ID: 439841  Cd Length: 105  Bit Score: 53.23  E-value: 7.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  26 TLTIDLSakGYKKEHIKVQLvrSRRRLVVSGECPVAGETN---------RWSRFRLQFPVPDGCDLKAIQARLHDGVIRV 96
Cdd:COG0071    12 VITADLP--GVDKEDIDVTV--EGNVLTISGERKEEEEEEgenylrrerRYGSFERSFTLPDDVDVDKIEASYENGVLTI 87


                  ...
gi 1002302348  97 TLP 99
Cdd:COG0071    88 TLP 90
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 22-99 8.65e-07

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: 44.60  E-value: 8.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  22 PPTHTLTIDLSakGYKKEHIKVQlVRSRRRLVVSGECPVAGET--------NRWS-RFRLQFPVPDGCDLKAIQARLHDG 92
Cdd:cd06472     8 PEAHVFKADVP--GVKKEDVKVE-VEDGRVLRISGERKKEEEKkgddwhrvERSSgRFVRRFRLPENADADEVKAFLENG 84


                  ....*..
gi 1002302348  93 VIRVTLP 99
Cdd:cd06472    85 VLTVTVP 91
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 26-99 3.30e-04

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: 37.84  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302348  26 TLTIDLSakGYKKEHIKVQL------------------------VRSRRRlvvSGECpvagetnrwSRfrlQFPVPDgCD 81
Cdd:cd06471    13 IVEADLP--GFKKEDIKLDYkdgyltisakrdeskdekdkkgnyIRRERY---YGSF---------SR---SFYLPN-VD 74

                          90
                  ....*....|....*...
gi 1002302348  82 LKAIQARLHDGVIRVTLP 99
Cdd:cd06471    75 EEEIKAKYENGVLKITLP 92
 
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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