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Conserved domains on  [gi|1149767564|ref|XP_020148549|]
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uncharacterized protein LOC109733742 [Aegilops tauschii subsp. strangulata]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10122597)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 135-212 7.92e-46

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


:

Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 150.19  E-value: 7.92e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149767564 135 PIEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKGSPtFRPKVLEMGGKRQFPYMVDPNTGVAMYESDDIINYLAKTY 212
Cdd:cd03041     1 PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSP-KRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 254-330 1.79e-41

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


:

Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 139.02  E-value: 1.79e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149767564 254 PIEIWAYEGSPFCKIARETLVELELPHLLHSCARGSPKRQDFFKKYGLFQAPYIEDPNTGVKMFESADIVEYLRATY 330
Cdd:cd03041     1 PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSPKRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
 
Name Accession Description Interval E-value
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 135-212 7.92e-46

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 150.19  E-value: 7.92e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149767564 135 PIEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKGSPtFRPKVLEMGGKRQFPYMVDPNTGVAMYESDDIINYLAKTY 212
Cdd:cd03041     1 PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSP-KRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 254-330 1.79e-41

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 139.02  E-value: 1.79e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149767564 254 PIEIWAYEGSPFCKIARETLVELELPHLLHSCARGSPKRQDFFKKYGLFQAPYIEDPNTGVKMFESADIVEYLRATY 330
Cdd:cd03041     1 PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSPKRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
139-214 1.34e-14

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 67.64  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149767564 139 YEFEGCPFCRKVREMVSVLDLDVLYYPCPKGSPtfRPKVLEMGGKRQFPYMVDPntGVAMYESDDIINYLAKTYGD 214
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDH--PPELLAKNPLGKVPVLEDD--GGILCESLAIIDYLEELYPG 73
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
260-331 2.02e-10

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 56.08  E-value: 2.02e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149767564 260 YEGSPFCKIARETLVELELPHLLHSCARGSpKRQDFFKKYGLFQAPYIEDPntGVKMFESADIVEYLRATYA 331
Cdd:pfam13417   4 FPGSPYARRVRIALNEKGLPYEFVPIPPGD-HPPELLAKNPLGKVPVLEDD--GGILCESLAIIDYLEELYP 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
135-209 4.05e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 46.73  E-value: 4.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149767564 135 PIEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKgSPTFRPKVLEMGGKRQFPYMVDPNTGVAMYESDDIINYLA 209
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDE-DPEAREELRERSGRRTVPVIFIGGEHLGGFDEGELDALLA 74
PRK10387 PRK10387
glutaredoxin 2; Provisional
 138-213 3.25e-05

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 44.10  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149767564 138 IYEFEGCPFCRKVR----------EMVSVLDLDVlyypcpkGSPTfrpkvlEMGGKRQFPYMVDPNtGVAMYESDDIINY 207
Cdd:PRK10387    3 LYIYDHCPFCVKARmifglknipvELIVLANDDE-------ATPI------RMIGQKQVPILQKDD-GSYMPESLDIVHY 68


                  ....*.
gi 1149767564 208 LAKTYG 213
Cdd:PRK10387   69 IDELDG 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
255-326 2.64e-03

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 38.34  E-value: 2.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149767564 255 IEIWAYEGSPFCKIARETLVELELPHLLH--SCARGSPKRQDFFKKYGLFQAPYIEDpnTGVKMFESADIVEYL 326
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVpvDLAKGEQKSPEFLALNPLGKVPVLVD--DGLVLTESLAILEYL 73
 
Name Accession Description Interval E-value
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 135-212 7.92e-46

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 150.19  E-value: 7.92e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149767564 135 PIEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKGSPtFRPKVLEMGGKRQFPYMVDPNTGVAMYESDDIINYLAKTY 212
Cdd:cd03041     1 PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSP-KRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 254-330 1.79e-41

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 139.02  E-value: 1.79e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149767564 254 PIEIWAYEGSPFCKIARETLVELELPHLLHSCARGSPKRQDFFKKYGLFQAPYIEDPNTGVKMFESADIVEYLRATY 330
Cdd:cd03041     1 PLELYEFEGSPFCRLVREVLTELELDVILYPCPKGSPKRDKFLEKGGKVQVPYLVDPNTGVQMFESADIVKYLFKTY 77
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
139-214 1.34e-14

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 67.64  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149767564 139 YEFEGCPFCRKVREMVSVLDLDVLYYPCPKGSPtfRPKVLEMGGKRQFPYMVDPntGVAMYESDDIINYLAKTYGD 214
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDH--PPELLAKNPLGKVPVLEDD--GGILCESLAIIDYLEELYPG 73
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
260-331 2.02e-10

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 56.08  E-value: 2.02e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149767564 260 YEGSPFCKIARETLVELELPHLLHSCARGSpKRQDFFKKYGLFQAPYIEDPntGVKMFESADIVEYLRATYA 331
Cdd:pfam13417   4 FPGSPYARRVRIALNEKGLPYEFVPIPPGD-HPPELLAKNPLGKVPVLEDD--GGILCESLAIIDYLEELYP 72
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 255-326 1.42e-09

Glutathione S-transferase (GST) family, N-terminal 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 subfamily, a member of the DsbA family). 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 53.73  E-value: 1.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149767564 255 IEIWAYEGSPFCKIARETLVELELPHLLHSCARGSPKRQDFFKKYGLFQAPYIEDPntGVKMFESADIVEYL 326
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDG--GLVLTESLAILEYL 70
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 144-211 3.07e-08

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 49.94  E-value: 3.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149767564 144 CPFCRKVREMVSVLDLDVLYYPCPKGSPTFRPKVLEMGGKRQFPYMVDPNtGVAMYESDDIINYLAKT 211
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLDPKDKPPELLALNPLGTVPVLVLPD-GTVLTDSLVILEYLEEL 68
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 136-209 1.37e-07

Glutathione S-transferase (GST) family, N-terminal 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 subfamily, a member of the DsbA family). 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 47.95  E-value: 1.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149767564 136 IEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKGSPtFRPKVLEMGGKRQFPYMVDPntGVAMYESDDIINYLA 209
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEG-EQEEFLALNPLGKVPVLEDG--GLVLTESLAILEYLA 71
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
135-209 4.05e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 46.73  E-value: 4.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149767564 135 PIEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKgSPTFRPKVLEMGGKRQFPYMVDPNTGVAMYESDDIINYLA 209
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDE-DPEAREELRERSGRRTVPVIFIGGEHLGGFDEGELDALLA 74
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 138-210 1.13e-05

GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 239335 [Multi-domain]  Cd Length: 71  Bit Score: 42.77  E-value: 1.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149767564 138 IYEFEGCPFCRKVREMVSVLDLD----VLYYPCPKGSptfrpkvLEMGGKRQFPYMVDpNTGVAMYESDDIINYLAK 210
Cdd:cd03037     3 LYIYEHCPFCVKARMIAGLKNIPveqiILQNDDEATP-------IRMIGAKQVPILEK-DDGSFMAESLDIVAFIDE 71
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
136-216 3.19e-05

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 44.12  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149767564 136 IEIYEFEGCPFCRKVREMVSVLDLD--VLYYPCPKGSpTFRPKVLEMGGKRQFPYMVDpnTGVAMYESDDIINYLAKTYG 213
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPyeLVPVDLAKGE-QKSPEFLALNPLGKVPVLVD--DGLVLTESLAILEYLAERYP 78


                  ...
gi 1149767564 214 DGS 216
Cdd:COG0625    79 EPP 81
PRK10387 PRK10387
glutaredoxin 2; Provisional
 138-213 3.25e-05

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 44.10  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149767564 138 IYEFEGCPFCRKVR----------EMVSVLDLDVlyypcpkGSPTfrpkvlEMGGKRQFPYMVDPNtGVAMYESDDIINY 207
Cdd:PRK10387    3 LYIYDHCPFCVKARmifglknipvELIVLANDDE-------ATPI------RMIGQKQVPILQKDD-GSYMPESLDIVHY 68


                  ....*.
gi 1149767564 208 LAKTYG 213
Cdd:PRK10387   69 IDELDG 74
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
 135-210 1.75e-04

GST_N 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.


Pssm-ID: 239338  Cd Length: 77  Bit Score: 39.70  E-value: 1.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149767564 135 PIEIYEFEGCPFCRKVRemvSVLDLDVLYYPCPKGSPTFRpKVLEMGGKRQFP-YMVD-PNTGVAMYESDDIINYLAK 210
Cdd:cd03040     1 KITLYQYKTCPFCCKVR---AFLDYHGIPYEVVEVNPVSR-KEIKWSSYKKVPiLRVEsGGDGQQLVDSSVIISTLKT 74
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 263-326 2.33e-04

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 38.77  E-value: 2.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149767564 263 SPFCKIARETLVELELPHLLH-SCARGSPKRQDFFKKYGLFQAPYIEDPNTGVkMFESADIVEYL 326
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIElVDLDPKDKPPELLALNPLGTVPVLVLPDGTV-LTDSLVILEYL 65
Glutaredoxin pfam00462
Glutaredoxin;
136-187 1.98e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 35.94  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1149767564 136 IEIYEFEGCPFCRKVREMVSVLDLDVLYYPCPKgSPTFRPKVLEMGGKRQFP 187
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDE-DPEIREELKELSGWPTVP 51
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
255-326 2.64e-03

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 38.34  E-value: 2.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149767564 255 IEIWAYEGSPFCKIARETLVELELPHLLH--SCARGSPKRQDFFKKYGLFQAPYIEDpnTGVKMFESADIVEYL 326
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVpvDLAKGEQKSPEFLALNPLGKVPVLVD--DGLVLTESLAILEYL 73
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
254-327 5.09e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.17  E-value: 5.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149767564 254 PIEIWAYEGSPFCKIARETLVELELPHLLHSCARGSPKRQDFFKKYGLFQAPYIEDPNTGVKMFESADIVEYLR 327
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFDEGELDALLA 74
 
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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