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Conserved domains on  [gi|9790017|ref|NP_062740|]
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prostaglandin E synthase 3 [Mus musculus]

Protein Classification

p23 domain-containing protein( domain architecture ID 10083256)

p23 domain-containing protein

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 ...
 3-109 1.43e-64

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: 192.72  E-value: 1.43e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    3 PASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGsDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGES 82
Cdd:cd00237   1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNG-DNVKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKGKE 79

                        90       100
                ....*....|....*....|....*..
gi 9790017   83 GQSWPRLTKERAKLNWLSVDFNNWKDW 109
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 ...
 3-109 1.43e-64

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: 192.72  E-value: 1.43e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    3 PASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGsDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGES 82
Cdd:cd00237   1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNG-DNVKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKGKE 79

                        90       100
                ....*....|....*....|....*..
gi 9790017   83 GQSWPRLTKERAKLNWLSVDFNNWKDW 109
Cdd:cd00237  80 GVAWPRLTKEKAKPNWLSVDFDNWRDW 106
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 7-79 1.56e-08

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: 48.79  E-value: 1.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9790017      7 KWYDRRDYVFIEFCVED----SKDVNVNFEKSKLTFSCLGGSDNFKHlneiDLFHCIDPNDSKHKRTDRSILCCLRK 79
Cdd:pfam04969   4 DWYQTLDEVTITIPVKGagikKKDVKVNIKPRSLKVKIKGGYELIDG----ELFHPIDPEESSWTIEGKKVEITLKK 76
 
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 ...
 3-109 1.43e-64

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: 192.72  E-value: 1.43e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    3 PASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGsDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGES 82
Cdd:cd00237   1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNG-DNVKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKGKE 79

                        90       100
                ....*....|....*....|....*..
gi 9790017   83 GQSWPRLTKERAKLNWLSVDFNNWKDW 109
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. ...
 7-112 6.59e-33

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: 112.69  E-value: 6.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    7 KWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSW 86
Cdd:cd06465   4 LWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGGGGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAGEYW 83

                        90       100
                ....*....|....*....|....*.
gi 9790017   87 PRLTKERAKLNWLSVDFNNWKDwEDD 112
Cdd:cd06465  84 PRLTKEKGKLPWLKVDFDKWVD-EDE 108
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 8-90 1.57e-22

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: 85.42  E-value: 1.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    8 WYDRRDYVFIEFCVED--SKDVNVNFEKSKLTFSCLGGSDNfKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQS 85
Cdd:cd06463   1 WYQTLDEVTITIPLKDvtKKDVKVEFTPKSLTVSVKGGGGK-EYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79


                ....*
gi 9790017   86 WPRLT 90
Cdd:cd06463  80 WPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 7-79 1.56e-08

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: 48.79  E-value: 1.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9790017      7 KWYDRRDYVFIEFCVED----SKDVNVNFEKSKLTFSCLGGSDNFKHlneiDLFHCIDPNDSKHKRTDRSILCCLRK 79
Cdd:pfam04969   4 DWYQTLDEVTITIPVKGagikKKDVKVNIKPRSLKVKIKGGYELIDG----ELFHPIDPEESSWTIEGKKVEITLKK 76
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 8-79 9.37e-07

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: 44.12  E-value: 9.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    8 WYDRRDYVFIEFCVE--DSKDVNVNFEKSKLTFSCLGGSDNFKHLN------EIDLFHCIDPNDSKHKRTDRSILCCLRK 79
Cdd:cd00298   1 WYQTDDEVVVTVDLPgvKKEDIKVEVEDNVLTISGKREEEEERERSygeferSFELPEDVDPEKSKASLENGVLEITLPK 80
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
 8-90 5.45e-06

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. 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. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 42.19  E-value: 5.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    8 WYDRRDYVFIEFCVE--DSKDVNVNFEKSKLTFSC-LGGSDNFKHlnEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGq 84
Cdd:cd06466   2 WYQTDTSVTVTIYAKnvDKEDVKVEFNEQSLSVSIiLPGGSEYQL--ELDLFGPIDPEQSKVSVLPTKVEITLKKAEPG- 78


                ....*.
gi 9790017   85 SWPRLT 90
Cdd:cd06466  79 SWPSLE 84
p23_NUDC_like cd06467
p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) ...
 7-89 3.87e-05

p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) NUDC is needed for nuclear movement. AnNUDC is localized at the hyphal cortex, and binds NUDF at spindle pole bodies (SPBs) and in the cytoplasm at different stages in the cell cycle. At the SPBs it is part of the dynein molecular motor/NUDF complex that regulates microtubule dynamics. Mammalian(m) NUDC associates both with the dynein complex and also with an anti-inflammatory enzyme, platelet activating factor acetylhydrolase I, PAF-AH(I) complex, through binding mNUDF, the regulatory beta subunit of PAF-AH(I). mNUDC is important for cell proliferation both in normal and tumor tissues. Its expression is elevated in various cell types undergoing mitosis or stimulated to proliferate, with high expression levels observed in leukemic cells and tumors. For a leukemic cell line, human NUDC was shown to activate the thrombopoietin (TPO) receptor (Mpl) by binding to its extracellular domain, and promoting cell proliferation and differentiation. This group also includes the human broadly immunogenic tumor associated antigen, CML66, which is highly expressed in a variety of solid tumors and in leukemias. In normal tissues high expression of CML66 is limited to testis and heart.


Pssm-ID: 107224  Cd Length: 85  Bit Score: 40.22  E-value: 3.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    7 KWYDRRDYVFIEFCVE---DSKDVNVNFEKSKLTFSCLGGSDNFKHlneiDLFHCIDPNDSKHKRTDRSILCC-LRKGES 82
Cdd:cd06467   2 SWTQTLDEVTVTIPLPegtKSKDVKVEITPKHLKVGVKGGEPLLDG----ELYAKVKVDESTWTLEDGKLLEItLEKRNE 77


                ....*..
gi 9790017   83 GQSWPRL 89
Cdd:cd06467  78 GEWWPSL 84
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
 8-90 5.58e-04

p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup.


Pssm-ID: 107239  Cd Length: 84  Bit Score: 36.97  E-value: 5.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790017    8 WYDRRDYVFIEFCVEDSK--DVNVNFEKSKLTFSCLGGSDNFKHLnEIDLFHCIDPNDSKHKRTDRSILCCLRKGEsGQS 85
Cdd:cd06489   2 WYQTESQVVITILIKNVKpeDVSVEFEKRELSATVKLPSGNDYSL-KLHLLHPIVPEQSSYKILSTKIEIKLKKTE-AIR 79


                ....*
gi 9790017   86 WPRLT 90
Cdd:cd06489  80 WSKLE 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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