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Conserved domains on  [gi|1370515142|ref|XP_024303456|]
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prostaglandin E synthase 2 isoform X1 [Homo sapiens]

Protein Classification

GST_C_mPGES2 domain-containing protein( domain architecture ID 10123627)

GST_C_mPGES2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_mPGES2 cd03197
C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione ...
 33-179 5.56e-86

C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione S-transferase (GST) C-terminal domain family, microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH, or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature, and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated and a C-terminal soluble domain with a GST-like structure. The C-terminal GST-like domain contains two structural domains, an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST active site is located in a cleft between the two structural domains.


:

Pssm-ID: 198306  Cd Length: 149  Bit Score: 249.45  E-value: 5.56e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515142  33 GKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNV 112
Cdd:cd03197     1 AQLADPEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRLKKKRNIKDDV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515142 113 REDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAI 179
Cdd:cd03197    81 RESLYDALNDWVKALGKKRKFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWYERMKEAV 147
 
Name Accession Description Interval E-value
GST_C_mPGES2 cd03197
C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione ...
 33-179 5.56e-86

C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione S-transferase (GST) C-terminal domain family, microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH, or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature, and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated and a C-terminal soluble domain with a GST-like structure. The C-terminal GST-like domain contains two structural domains, an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST active site is located in a cleft between the two structural domains.


Pssm-ID: 198306  Cd Length: 149  Bit Score: 249.45  E-value: 5.56e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515142  33 GKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNV 112
Cdd:cd03197     1 AQLADPEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRLKKKRNIKDDV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515142 113 REDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAI 179
Cdd:cd03197    81 RESLYDALNDWVKALGKKRKFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWYERMKEAV 147
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
105-176 1.90e-03

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 37.57  E-value: 1.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515142 105 RHRLQDNVREDLYEAADKWVAAVGK-------DRPFMGGQKPNLADLAVYGVLRVMEGLDafDDLMQHTHIQPWYLRVE 176
Cdd:COG0625   112 LERLAPEKDPAAIARARAELARLLAvlearlaGGPYLAGDRFSIADIALAPVLRRLDRLG--LDLADYPNLAAWLARLA 188
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 90-177 2.09e-03

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 36.11  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515142  90 MGAAAMYLISKRLKSRHRLQDNVREDLYEAADKwVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ 169
Cdd:pfam00043   5 RMQIALLPYVPPEEKKEPEVDEALEKVARVLSA-LEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACLREKFPNLK 83


                  ....*...
gi 1370515142 170 PWYLRVER 177
Cdd:pfam00043  84 AWFERVAA 91
 
Name Accession Description Interval E-value
GST_C_mPGES2 cd03197
C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione ...
 33-179 5.56e-86

C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione S-transferase (GST) C-terminal domain family, microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH, or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature, and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated and a C-terminal soluble domain with a GST-like structure. The C-terminal GST-like domain contains two structural domains, an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST active site is located in a cleft between the two structural domains.


Pssm-ID: 198306  Cd Length: 149  Bit Score: 249.45  E-value: 5.56e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515142  33 GKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNV 112
Cdd:cd03197     1 AQLADPEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRLKKKRNIKDDV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515142 113 REDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAI 179
Cdd:cd03197    81 RESLYDALNDWVKALGKKRKFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWYERMKEAV 147
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 93-175 4.95e-05

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 40.56  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515142  93 AAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKdRPFMGGQKPNLADLAVYGVLRVMEGLD-AFDDLMQHTHIQPW 171
Cdd:cd00299    18 RLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAG-RPYLAGDQFSLADVALAPVLARLEALGpYYDLLDEYPRLKAW 96


                  ....
gi 1370515142 172 YLRV 175
Cdd:cd00299    97 YDRL 100
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
105-176 1.90e-03

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 37.57  E-value: 1.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515142 105 RHRLQDNVREDLYEAADKWVAAVGK-------DRPFMGGQKPNLADLAVYGVLRVMEGLDafDDLMQHTHIQPWYLRVE 176
Cdd:COG0625   112 LERLAPEKDPAAIARARAELARLLAvlearlaGGPYLAGDRFSIADIALAPVLRRLDRLG--LDLADYPNLAAWLARLA 188
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 90-177 2.09e-03

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 36.11  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515142  90 MGAAAMYLISKRLKSRHRLQDNVREDLYEAADKwVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ 169
Cdd:pfam00043   5 RMQIALLPYVPPEEKKEPEVDEALEKVARVLSA-LEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACLREKFPNLK 83


                  ....*...
gi 1370515142 170 PWYLRVER 177
Cdd:pfam00043  84 AWFERVAA 91
 
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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