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Conserved domains on  [gi|12840608|dbj|BAB24896|]
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unnamed protein product [Mus musculus]

Protein Classification

Hsp20/alpha crystallin family protein; p23/wos2 family protein( domain architecture ID 10083256)

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| p23/wos2 family protein similar to Arabidopsis thaliana co-chaperone protein p23, Saccharomyces cerevisiae Sba1 and Schizosaccharomyces pombe protein wos2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 5-110 5.07e-63

p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.


:

Pssm-ID: 107218  Cd Length: 106  Bit Score: 187.71  E-value: 5.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12840608   5 PARTLWYDRPKYVFMEFCVEDSTDVSVLIEDHRVVFSCRNGDGVELYNEIEFYAKVNSKDSQDKRSGRSITCFVRKWKEK 84
Cdd:cd00237   1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKGKEG 80

                        90       100
                ....*....|....*....|....*.
gi 12840608  85 VAWPRLTKEDIKPVWLSVDFDNWRDW 110
Cdd:cd00237  81 VAWPRLTKEKAKPNWLSVDFDNWRDW 106
 
Name Accession Description Interval E-value
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 5-110 5.07e-63

p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.


Pssm-ID: 107218  Cd Length: 106  Bit Score: 187.71  E-value: 5.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12840608   5 PARTLWYDRPKYVFMEFCVEDSTDVSVLIEDHRVVFSCRNGDGVELYNEIEFYAKVNSKDSQDKRSGRSITCFVRKWKEK 84
Cdd:cd00237   1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKGKEG 80

                        90       100
                ....*....|....*....|....*.
gi 12840608  85 VAWPRLTKEDIKPVWLSVDFDNWRDW 110
Cdd:cd00237  81 VAWPRLTKEKAKPNWLSVDFDNWRDW 106
 
Name Accession Description Interval E-value
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 5-110 5.07e-63

p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.


Pssm-ID: 107218  Cd Length: 106  Bit Score: 187.71  E-value: 5.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12840608   5 PARTLWYDRPKYVFMEFCVEDSTDVSVLIEDHRVVFSCRNGDGVELYNEIEFYAKVNSKDSQDKRSGRSITCFVRKWKEK 84
Cdd:cd00237   1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKGKEG 80

                        90       100
                ....*....|....*....|....*.
gi 12840608  85 VAWPRLTKEDIKPVWLSVDFDNWRDW 110
Cdd:cd00237  81 VAWPRLTKEKAKPNWLSVDFDNWRDW 106
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 9-109 9.70e-23

p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity.


Pssm-ID: 107222 [Multi-domain]  Cd Length: 108  Bit Score: 85.72  E-value: 9.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12840608   9 LWYDRPKYVFMEFCVEDSTDVSVLIEDHRVVFSCRNGDGVELYN-EIEFYAKVNSKDSQDKRSGRSITCFVRKWKEKVAW 87
Cdd:cd06465   4 LWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGGGGKKYEfDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAGEYW 83

                        90       100
                ....*....|....*....|..
gi 12840608  88 PRLTKEDIKPVWLSVDFDNWRD 109
Cdd:cd06465  84 PRLTKEKGKLPWLKVDFDKWVD 105
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 10-91 9.29e-14

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes 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). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 61.92  E-value: 9.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12840608  10 WYDRPKYVFMEFCVEDST--DVSVLIEDHRVVFSCRNGDGVELYNEIEFYAKVNSKDSQDKRSGRSITCFVRKWKEKVAW 87
Cdd:cd06463   1 WYQTLDEVTITIPLKDVTkkDVKVEFTPKSLTVSVKGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEWW 80


                ....
gi 12840608  88 PRLT 91
Cdd:cd06463  81 PRLE 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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