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Conserved domains on  [gi|543583707|ref|NP_001269532|]
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prostaglandin E synthase 3 isoform d [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

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 ...
 3-76 1.36e-34

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: 115.68  E-value: 1.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583707   3 PASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGsDNFKHLNEIDLFHCIDPN-------------------- 62
Cdd:cd00237    1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNG-DNVKIYNEIELYDRVDPNdskhkrtdrsilcclrkgke 79

                         90       100
                 ....*....|....*....|....*..
gi 543583707  63 -------------LNWLSVDFNNWKDW 76
Cdd:cd00237   80 gvawprltkekakPNWLSVDFDNWRDW 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 ...
 3-76 1.36e-34

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: 115.68  E-value: 1.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583707   3 PASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGsDNFKHLNEIDLFHCIDPN-------------------- 62
Cdd:cd00237    1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNG-DNVKIYNEIELYDRVDPNdskhkrtdrsilcclrkgke 79

                         90       100
                 ....*....|....*....|....*..
gi 543583707  63 -------------LNWLSVDFNNWKDW 76
Cdd:cd00237   80 gvawprltkekakPNWLSVDFDNWRDW 106
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 7-62 5.77e-04

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 36.08  E-value: 5.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583707    7 KWYDRRDYVFIEFCVED----SKDVNVNFEKSKLTFSCLGGSDNFKHlneiDLFHCIDPN 62
Cdd:pfam04969   4 DWYQTLDEVTITIPVKGagikKKDVKVNIKPRSLKVKIKGGYELIDG----ELFHPIDPE 59
 
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 ...
 3-76 1.36e-34

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: 115.68  E-value: 1.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583707   3 PASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGsDNFKHLNEIDLFHCIDPN-------------------- 62
Cdd:cd00237    1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNG-DNVKIYNEIELYDRVDPNdskhkrtdrsilcclrkgke 79

                         90       100
                 ....*....|....*....|....*..
gi 543583707  63 -------------LNWLSVDFNNWKDW 76
Cdd:cd00237   80 gvawprltkekakPNWLSVDFDNWRDW 106
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 7-79 1.17e-11

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: 56.83  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583707   7 KWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPN------------------------ 62
Cdd:cd06465    4 LWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGGGGKKYEFDLEFYKEIDPEeskykvtgrqiefvlrkkeageyw 83

                         90       100
                 ....*....|....*....|....*.
gi 543583707  63 ---------LNWLSVDFNNWKDwEDD 79
Cdd:cd06465   84 prltkekgkLPWLKVDFDKWVD-EDE 108
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 8-62 2.36e-10

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: 53.06  E-value: 2.36e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 543583707   8 WYDRRDYVFIEFCVED--SKDVNVNFEKSKLTFSCLGGSDNfKHLNEIDLFHCIDPN 62
Cdd:cd06463    1 WYQTLDEVTITIPLKDvtKKDVKVEFTPKSLTVSVKGGGGK-EYLLEGELFGPIDPE 56
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 7-62 5.77e-04

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 36.08  E-value: 5.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583707    7 KWYDRRDYVFIEFCVED----SKDVNVNFEKSKLTFSCLGGSDNFKHlneiDLFHCIDPN 62
Cdd:pfam04969   4 DWYQTLDEVTITIPVKGagikKKDVKVNIKPRSLKVKIKGGYELIDG----ELFHPIDPE 59
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 8-62 1.37e-03

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: 35.26  E-value: 1.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543583707   8 WYDRRDYVFIEFCVE--DSKDVNVNFEKSKLTFSCLGGSDNFKHLN------EIDLFHCIDPN 62
Cdd:cd00298    1 WYQTDDEVVVTVDLPgvKKEDIKVEVEDNVLTISGKREEEEERERSygeferSFELPEDVDPE 63
 
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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