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Conserved domains on  [gi|1137221430|gb|OMO87381|]
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hypothetical protein CCACVL1_09090 [Corchorus capsularis]

Protein Classification

prostaglandin E synthase 2( domain architecture ID 10122593)

prostaglandin E synthase 2, a glutathione S-transferase (GST) family protein, is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2

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 ...
 174-315 1.15e-81

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: 244.05  E-value: 1.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 174 DEEKKWCQWVDNHLVHVLSPNIYRSASEALESFDYITTHGNFSFTERLVAKYAGATAMYFVSKKLKKRHNIT-DERAALY 252
Cdd:cd03197     6 PEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRLKKKRNIKdDVRESLY 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137221430 253 EAAETWVDALKGRH-YLGGSKPNLADLAVFGVLRPIRYLKSGKDMVEHTRIGEWYTRMENAVGE 315
Cdd:cd03197    86 DALNDWVKALGKKRkFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWYERMKEAVGS 149
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
 93-164 3.87e-42

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: 140.62  E-value: 3.87e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKEIKWSDYKKVPILKVD----GEQMVDSSDIIDKLFQRI 164
Cdd:cd03040     1 KITLYQYKTCPFCCKVRAFLDYHGIPYEVVEVNPVSRKEIKWSSYKKVPILRVEsggdGQQLVDSSVIISTLKTYL 76
 
Name Accession Description Interval E-value
GST_C_mPGES2 cd03197
C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione ...
 174-315 1.15e-81

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: 244.05  E-value: 1.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 174 DEEKKWCQWVDNHLVHVLSPNIYRSASEALESFDYITTHGNFSFTERLVAKYAGATAMYFVSKKLKKRHNIT-DERAALY 252
Cdd:cd03197     6 PEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRLKKKRNIKdDVRESLY 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137221430 253 EAAETWVDALKGRH-YLGGSKPNLADLAVFGVLRPIRYLKSGKDMVEHTRIGEWYTRMENAVGE 315
Cdd:cd03197    86 DALNDWVKALGKKRkFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWYERMKEAVGS 149
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
 93-164 3.87e-42

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: 140.62  E-value: 3.87e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKEIKWSDYKKVPILKVD----GEQMVDSSDIIDKLFQRI 164
Cdd:cd03040     1 KITLYQYKTCPFCCKVRAFLDYHGIPYEVVEVNPVSRKEIKWSSYKKVPILRVEsggdGQQLVDSSVIISTLKTYL 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
96-310 1.05e-16

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 77.24  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIVEVNpISKKEIKWSDYK------KVPILKVDGEQMVDSSDIIDKLFQRINPDGT 169
Cdd:COG0625     4 LYGSPPSPNSRRVRIALEEKGLPYELVPVD-LAKGEQKSPEFLalnplgKVPVLVDDGLVLTESLAILEYLAERYPEPPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 170 IPDGDEEK----KWCQWVDNHLVHVLSPNIYRSASEAlesfdyitthgnfsfTERLVAKYagatamyfvskklkkrhnit 245
Cdd:COG0625    83 LPADPAARarvrQWLAWADGDLHPALRNLLERLAPEK---------------DPAAIARA-------------------- 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1137221430 246 deRAALYEAAETWVDALKGRHYLGGSKPNLADLAVFGVLRPIRYLksGKDMVEHTRIGEWYTRME 310
Cdd:COG0625   128 --RAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRL--GLDLADYPNLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
96-163 7.16e-15

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 68.41  E-value: 7.16e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKE--IKWSDYKKVPILKVDGEQMVDSSDIIDKLFQR 163
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPelLAKNPLGKVPVLEDDGGILCESLAIIDYLEEL 70
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
93-160 3.20e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 60.98  E-value: 3.20e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKE-IKWSDYKKVPILKVDGEQMV--DSSDIIDKL 160
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVdeDPEAREElRERSGRRTVPVIFIGGEHLGgfDEGELDALL 73
PRK10387 PRK10387
glutaredoxin 2; Provisional
 96-193 1.28e-07

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 51.42  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIV------EVNPISKkeikwSDYKKVPIL-KVDGEQMVDSSDI---IDKLFQriN 165
Cdd:PRK10387    3 LYIYDHCPFCVKARMIFGLKNIPVELIvlanddEATPIRM-----IGQKQVPILqKDDGSYMPESLDIvhyIDELDG--K 75

                          90       100
                  ....*....|....*....|....*...
gi 1137221430 166 PDGTIPDGDEEKKWCQWVDNHLVHVLSP 193
Cdd:PRK10387   76 PLLTGKRSPAIEEWLRKVFGYLNKLLYP 103
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 94-160 2.29e-06

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 44.68  E-value: 2.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKEI-KWSDYKKVPILKVDGEQMVD-SSDIIDKL 160
Cdd:TIGR02196   2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVekDAAAREELlKVYGQRGVPVIVIGHKIVVGfDPEKLDQL 72
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 248-308 7.67e-06

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 43.08  E-value: 7.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137221430 248 RAALYEAAETWVDALKGRHYLGGSKPNLADLAVFGVLRPIRYLKSGKD-MVEHTRIGEWYTR 308
Cdd:pfam13410   6 REQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDlREGYPRLRAWLER 67
 
Name Accession Description Interval E-value
GST_C_mPGES2 cd03197
C-terminal, alpha helical domain of microsomal Prostaglandin E synthase Type 2; Glutathione ...
 174-315 1.15e-81

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: 244.05  E-value: 1.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 174 DEEKKWCQWVDNHLVHVLSPNIYRSASEALESFDYITTHGNFSFTERLVAKYAGATAMYFVSKKLKKRHNIT-DERAALY 252
Cdd:cd03197     6 PEEKKWRKWVDDVLVHLLSPNIYRTFSEALQAFDYITTVGNFGPWERIVAKYVGAAAMYLISKRLKKKRNIKdDVRESLY 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137221430 253 EAAETWVDALKGRH-YLGGSKPNLADLAVFGVLRPIRYLKSGKDMVEHTRIGEWYTRMENAVGE 315
Cdd:cd03197    86 DALNDWVKALGKKRkFHGGSKPNLADLAVYGVLRSIEGLDAFKDVLANTKIGPWYERMKEAVGS 149
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
 93-164 3.87e-42

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: 140.62  E-value: 3.87e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKEIKWSDYKKVPILKVD----GEQMVDSSDIIDKLFQRI 164
Cdd:cd03040     1 KITLYQYKTCPFCCKVRAFLDYHGIPYEVVEVNPVSRKEIKWSSYKKVPILRVEsggdGQQLVDSSVIISTLKTYL 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
96-310 1.05e-16

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 77.24  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIVEVNpISKKEIKWSDYK------KVPILKVDGEQMVDSSDIIDKLFQRINPDGT 169
Cdd:COG0625     4 LYGSPPSPNSRRVRIALEEKGLPYELVPVD-LAKGEQKSPEFLalnplgKVPVLVDDGLVLTESLAILEYLAERYPEPPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 170 IPDGDEEK----KWCQWVDNHLVHVLSPNIYRSASEAlesfdyitthgnfsfTERLVAKYagatamyfvskklkkrhnit 245
Cdd:COG0625    83 LPADPAARarvrQWLAWADGDLHPALRNLLERLAPEK---------------DPAAIARA-------------------- 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1137221430 246 deRAALYEAAETWVDALKGRHYLGGSKPNLADLAVFGVLRPIRYLksGKDMVEHTRIGEWYTRME 310
Cdd:COG0625   128 --RAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRL--GLDLADYPNLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
96-163 7.16e-15

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 68.41  E-value: 7.16e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKE--IKWSDYKKVPILKVDGEQMVDSSDIIDKLFQR 163
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPelLAKNPLGKVPVLEDDGGILCESLAIIDYLEEL 70
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 94-160 9.62e-13

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: 62.59  E-value: 9.62e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKE---IKWSDYKKVPILKVDGEQMVDSSDIIDKL 160
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQeefLALNPLGKVPVLEDGGLVLTESLAILEYL 70
Glutaredoxin pfam00462
Glutaredoxin;
94-148 1.68e-12

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 61.37  E-value: 1.68e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKEIKW-SDYKKVPILKVDGE 148
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVdeDPEIREELKElSGWPTVPQVFIDGE 58
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
93-160 3.20e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 60.98  E-value: 3.20e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKE-IKWSDYKKVPILKVDGEQMV--DSSDIIDKL 160
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVdeDPEAREElRERSGRRTVPVIFIGGEHLGgfDEGELDALL 73
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 96-157 2.04e-09

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: 53.17  E-value: 2.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPY-KIVEVNPISKKEIKWSDYKKVPIL-KVDGEQMVDSSDII 157
Cdd:cd03037     3 LYIYEHCPFCVKARMIAGLKNIPVeQIILQNDDEATPIRMIGAKQVPILeKDDGSFMAESLDIV 66
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
96-285 2.93e-08

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 53.31  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIV------EVNPISK--KeikwsdyKKVPIL-KVDGEQMVDSSDI---IDKLFQR 163
Cdd:COG2999     3 LYIYDHCPFCVRARMIFGLKNIPVELIvllnddEETPIRMigK-------KMVPILeKDDGSYMPESLDIvhyIDELDGK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 164 inPDGTIPDGDEEKKWCQWVDNHLVHVLSPniyRSASEALESFDyitthgnfsfTERLVAkyagatamYFVSKKLKKRHN 243
Cdd:COG2999    76 --PILTGPVRPEIAAWLKKVSSYVNRLLYP---RWAKAPLPEFA----------TPSARA--------YFINKKEASIGD 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1137221430 244 ITD---ERAALYEAAETWVDAL----KGRHYLGGsKPNLADLAVFGVLR 285
Cdd:COG2999   133 FEEllaNTPELIAELNQDLEELepliKSPSAVNG-ELSLDDIILFPLLR 180
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 101-160 8.10e-08

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 48.78  E-value: 8.10e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1137221430 101 ACPFCNKVKAFLDYNNIPYKIVEV--NPISKKE--IKWSDYKKVPILKV-DGEQMVDSSDIIDKL 160
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVdlDPKDKPPelLALNPLGTVPVLVLpDGTVLTDSLVILEYL 65
PRK10387 PRK10387
glutaredoxin 2; Provisional
 96-193 1.28e-07

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 51.42  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYKIV------EVNPISKkeikwSDYKKVPIL-KVDGEQMVDSSDI---IDKLFQriN 165
Cdd:PRK10387    3 LYIYDHCPFCVKARMIFGLKNIPVELIvlanddEATPIRM-----IGQKQVPILqKDDGSYMPESLDIvhyIDELDG--K 75

                          90       100
                  ....*....|....*....|....*...
gi 1137221430 166 PDGTIPDGDEEKKWCQWVDNHLVHVLSP 193
Cdd:PRK10387   76 PLLTGKRSPAIEEWLRKVFGYLNKLLYP 103
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
 94-160 1.66e-07

GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities.


Pssm-ID: 239352 [Multi-domain]  Cd Length: 72  Bit Score: 47.99  E-value: 1.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137221430  94 VVLYQY-------EACPFCNKVKAFLDYNNIPYKIVEVNPISKkeikwSDYKKVPILKVDGEQMVDSSDIIDKL 160
Cdd:cd03054     1 LELYQWgrafglpSLSPECLKVETYLRMAGIPYEVVFSSNPWR-----SPTGKLPFLELNGEKIADSEKIIEYL 69
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 216-309 1.71e-07

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: 48.65  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430 216 SFTERLVAKYAGATAMYFVSKKLKKRHNITDERAALYEAAETWVDALKGRHYLGGSKPNLADLAVFGVLRPIRYLKSGKD 295
Cdd:cd00299     6 DWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYD 85

                          90
                  ....*....|....*
gi 1137221430 296 MVE-HTRIGEWYTRM 309
Cdd:cd00299    86 LLDeYPRLKAWYDRL 100
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 93-160 3.02e-07

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 47.22  E-value: 3.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKEIK-WSDYKKVPILKVDGEQMVDSSDI-IDKL 160
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVdeDPEALEELKkLNGYRSVPVVVIGDEHLSGFRPDkLRAL 72
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 94-164 8.45e-07

GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.


Pssm-ID: 239378 [Multi-domain]  Cd Length: 75  Bit Score: 46.08  E-value: 8.45e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1137221430  94 VVLYQYEAC-------PFCNKVKAFLDYNNIPYKIVEVNPISKkeikwSDYKKVPILKVDGEQMVDSSDIIDKLFQRI 164
Cdd:cd03080     2 ITLYQFPRAfgvpslsPFCLKVETFLRMAGIPYENKFGGLAKR-----SPKGKLPFIELNGEKIADSELIIDHLEEKY 74
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 96-162 1.91e-06

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: 45.03  E-value: 1.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPYkivEVNPISK------KEIKWSDYKKVPILkVD---GEQMVDSSDIIDKLFQ 162
Cdd:cd03041     4 LYEFEGSPFCRLVREVLTELELDV---ILYPCPKgspkrdKFLEKGGKVQVPYL-VDpntGVQMFESADIVKYLFK 75
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 94-160 2.29e-06

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 44.68  E-value: 2.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKEI-KWSDYKKVPILKVDGEQMVD-SSDIIDKL 160
Cdd:TIGR02196   2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVekDAAAREELlKVYGQRGVPVIVIGHKIVVGfDPEKLDQL 72
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 102-172 3.74e-06

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 47.68  E-value: 3.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137221430 102 CPFCNKVKAFLDYNNIPYKIVEVNPISKKE--IKWSDYKKVPILKVDgEQMVDSSDIIDKLFQRINPD---GTIPD 172
Cdd:PLN02817   73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEwfLKISPEGKVPVVKLD-EKWVADSDVITQALEEKYPDpplATPPE 147
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 82-157 4.45e-06

GST_N family, Class Omega subfamily; 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. 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. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 44.27  E-value: 4.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1137221430  82 EPPRSekflPKEVVLYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKEIKWSDYK--KVPILKVDGEQMVDSSDII 157
Cdd:cd03055    11 EPPPV----PGIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPqgKVPALEIDEGKVVYESLII 84
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 96-162 5.60e-06

Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase, and may have more to do with resistance to redox stress. [Energy metabolism, Electron transport]


Pssm-ID: 274018 [Multi-domain]  Cd Length: 209  Bit Score: 46.30  E-value: 5.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137221430  96 LYQYEACPFCNKVKAFLDYNNIPY-KIVEVNPISKKEIKWSDYKKVPIL-KVDGEQMVDSSDI---IDKLFQ 162
Cdd:TIGR02182   2 LYIYDHCPFCVRARMIFGLKNIPVeKHVLLNDDEETPIRMIGAKQVPILqKDDGRAMPESLDIvayFDKLDG 73
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 248-308 7.67e-06

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 43.08  E-value: 7.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137221430 248 RAALYEAAETWVDALKGRHYLGGSKPNLADLAVFGVLRPIRYLKSGKD-MVEHTRIGEWYTR 308
Cdd:pfam13410   6 REQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDlREGYPRLRAWLER 67
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 93-167 1.78e-05

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 43.39  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  93 EVVLYQYEACPFCNKVKAFLDYNNIPYK--IVEVNPISKKEIKwsdykkvPILKVDgEQMVDssDII---DKLFQRINPD 167
Cdd:cd03032     1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEerNLFKQPLTKEELK-------EILSLT-ENGVE--DIIstrSKAFKNLNID 70
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 103-160 3.49e-05

Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 41.79  E-value: 3.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1137221430 103 PFCNKVKAFLDYNNIPYKIVEVNPISKkeikwSDYKKVPILKVDGEQMVDSSDIIDKL 160
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVEPSSNPSA-----SPKGKLPFIELNGDLIADSEFIIEFL 53
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 246-311 4.06e-05

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: 41.50  E-value: 4.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137221430 246 DERAALYEAAETWvdaLKGRHYLGGSKPNLADLAVFGVLRPIRYLKSGKDMVEHTRIGEWYTRMEN 311
Cdd:pfam00043  29 EKVARVLSALEEV---LKGQTYLVGDKLTLADIALAPALLWLYELDPACLREKFPNLKAWFERVAA 91
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
 94-144 1.18e-04

Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine.


Pssm-ID: 239334  Cd Length: 111  Bit Score: 40.69  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYK---IVEVNPiSKKEIK-WSDYKKVPILK 144
Cdd:cd03036     1 LKFYEYPKCSTCRKAKKWLDEHGVDYTaidIVEEPP-SKEELKkWLEKSGLPLKK 54
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 102-162 7.97e-04

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 37.45  E-value: 7.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137221430 102 CPFCNKVKAFLDYNNIPYKIVEV--NPISKKEIK-WSDYKKVPILKVDGEqMVDSSDIIDKLFQ 162
Cdd:cd02066    10 CPYCKRAKRLLESLGIEFEEIDIleDGELREELKeLSGWPTVPQIFINGE-FIGGYDDLKALHE 72
spxA PRK01655
transcriptional regulator Spx; Reviewed
 94-167 9.30e-04

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 38.90  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYkiVEVN----PISKKEIKwsdykkvPILKV--DGeqmvdSSDII---DKLFQRI 164
Cdd:PRK01655    2 VTLFTSPSCTSCRKAKAWLEEHDIPF--TERNifssPLTIDEIK-------QILRMteDG-----TDEIIstrSKVFQKL 67


                  ...
gi 1137221430 165 NPD 167
Cdd:PRK01655   68 NVD 70
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
 94-133 1.38e-03

Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase.


Pssm-ID: 239275  Cd Length: 105  Bit Score: 37.47  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYKIVEV--NPISKKEIK 133
Cdd:cd02977     1 ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYlkEPPTKEELK 42
GST_C_Metaxin cd03193
C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase ...
 232-295 2.54e-03

C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities. Other members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.


Pssm-ID: 198302 [Multi-domain]  Cd Length: 88  Bit Score: 36.45  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1137221430 232 YFVSKKLKKRHNITDERAALYEAAETWVDA----LKGRHYLGGSKPNLADLAVFGVLRPIRYLKSGKD 295
Cdd:cd03193     1 ARALSRMVETHLYWALRREIYELALEDLEAlstlLGDKKFLFGDKPTSVDATVFAHLASILYPPEDSP 68
GST_C_GluRS_N cd10306
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ...
 250-312 2.94e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198339 [Multi-domain]  Cd Length: 87  Bit Score: 36.18  E-value: 2.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137221430 250 ALYEAAETWVDALKGRHYLGGSKPNLADLAVFGVLRP----IRYLKSGKdmveHTRIGEWYTRMENA 312
Cdd:cd10306    25 ALSQALEELDSHLTLRTFIVGYSLSLADIAVWGALRGngvaGSLIKNKV----YVNLSRWFSFLESL 87
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 94-157 4.40e-03

GST_N family, Class Tau subfamily; 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. 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 35.33  E-value: 4.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137221430  94 VVLYQYEACPFCNKVKAFLDYNNIPYKIVEVNPISKKEIKWSD---YKKVPILKVDGEQMVDSSDII 157
Cdd:cd03058     1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASnpvHKKIPVLLHNGKPICESLIIV 67
 
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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