putative protein PTGES3L isoform 4 [Homo sapiens]
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
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 ... |
4-72 | 1.27e-39 | ||
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 cd00237: Pssm-ID: 469641 Cd Length: 106 Bit Score: 128.00 E-value: 1.27e-39
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| 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 ... |
4-72 | 1.27e-39 | ||
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: 128.00 E-value: 1.27e-39
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| 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 ... |
4-72 | 1.27e-39 | ||
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: 128.00 E-value: 1.27e-39
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| p23_hB-ind1_like | cd06465 | p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ... |
3-71 | 2.25e-14 | ||
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: 63.77 E-value: 2.25e-14
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| p23_like | cd06463 | Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ... |
3-53 | 4.22e-05 | ||
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: 39.19 E-value: 4.22e-05
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