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Conserved domains on  [gi|17537617|ref|NP_496604|]
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GST N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11555146)

glutathione S-transferase (GST) family protein may catalyze 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

CATH:  3.40.30.10|1.20.1050.10
PubMed:  11695986|9074797|15822171|15607001
SCOP:  4000472|4000976

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 15-89 2.31e-38

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: 129.28  E-value: 2.31e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617  15 HVYLVQFPRAGCIPSPSPYAFKVETFLRVADIPYTNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFH 89
Cdd:cd03080   1 MITLYQFPRAFGVPSLSPFCLKVETFLRMAGIPYENKFGGLAKRSPKGKLPFIELNGEKIADSELIIDHLEEKYG 75
GST_C_6 pfam17171
Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.
 181-245 7.07e-22

Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.


:

Pssm-ID: 465369  Cd Length: 64  Bit Score: 86.05  E-value: 7.07e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617   181 AKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIRAYIDEKvPNVMEYVIRI 245
Cdd:pfam17171   1 AKKDLRALSERLGDKPFFFGDKPTSLDALVFGHLALILYTPLPSPALRIHLKEY-PNLVAYCERI 64
 
Name Accession Description Interval E-value
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 15-89 2.31e-38

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: 129.28  E-value: 2.31e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617  15 HVYLVQFPRAGCIPSPSPYAFKVETFLRVADIPYTNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFH 89
Cdd:cd03080   1 MITLYQFPRAFGVPSLSPFCLKVETFLRMAGIPYENKFGGLAKRSPKGKLPFIELNGEKIADSELIIDHLEEKYG 75
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 32-123 9.76e-28

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


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 102.27  E-value: 9.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617    32 PYAFKVETFLRVADIPYTNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFHKSDlEDLSASDKAIARAFFALL 111
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVEPSSNPSASPKGKLPFIELNGDLIADSEFIIEFLKEKGVDLD-AGLSPEQKADARALKALV 79

                          90
                  ....*....|..
gi 17537617   112 EHHLCWVSLYSR 123
Cdd:pfam17172  80 EEHLYWALLYER 91
GST_C_6 pfam17171
Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.
 181-245 7.07e-22

Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.


Pssm-ID: 465369  Cd Length: 64  Bit Score: 86.05  E-value: 7.07e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617   181 AKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIRAYIDEKvPNVMEYVIRI 245
Cdd:pfam17171   1 AKKDLRALSERLGDKPFFFGDKPTSLDALVFGHLALILYTPLPSPALRIHLKEY-PNLVAYCERI 64
GST_C_Metaxin cd03193
C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase ...
 176-246 1.48e-21

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: 86.14  E-value: 1.48e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537617 176 EVLDQAKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIRAYiDEKVPNVMEYVIRIK 246
Cdd:cd03193  19 EIYELALEDLEALSTLLGDKKFLFGDKPTSVDATVFAHLASILYPPEDSPLLRVL-VASSPNLVEYCERIR 88
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
30-247 2.66e-09

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 55.67  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617  30 PSPYAFKVETFLRVADIPY----------TNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFHKSDLedLSAS 99
Cdd:COG0625   9 PSPNSRRVRIALEEKGLPYelvpvdlakgEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPPL--LPAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617 100 DKAIARAffallehhLCWVSLysrgqdfgwlaTDTGFGRLLTGIkgfafknfivksfTKKVRGRAAAQGmgtfsREEVLD 179
Cdd:COG0625  87 PAARARV--------RQWLAW-----------ADGDLHPALRNL-------------LERLAPEKDPAA-----IARARA 129

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537617 180 QAKKDLDAISTQLGDKPYLFGSSIkTI-DVTAFAHLAeliYTPQFSPEIRAYidekvPNVMEYVIRIKE 247
Cdd:COG0625 130 ELARLLAVLEARLAGGPYLAGDRF-SIaDIALAPVLR---RLDRLGLDLADY-----PNLAAWLARLAA 189
 
Name Accession Description Interval E-value
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 15-89 2.31e-38

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: 129.28  E-value: 2.31e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617  15 HVYLVQFPRAGCIPSPSPYAFKVETFLRVADIPYTNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFH 89
Cdd:cd03080   1 MITLYQFPRAFGVPSLSPFCLKVETFLRMAGIPYENKFGGLAKRSPKGKLPFIELNGEKIADSELIIDHLEEKYG 75
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 32-123 9.76e-28

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


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 102.27  E-value: 9.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617    32 PYAFKVETFLRVADIPYTNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFHKSDlEDLSASDKAIARAFFALL 111
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVEPSSNPSASPKGKLPFIELNGDLIADSEFIIEFLKEKGVDLD-AGLSPEQKADARALKALV 79

                          90
                  ....*....|..
gi 17537617   112 EHHLCWVSLYSR 123
Cdd:pfam17172  80 EEHLYWALLYER 91
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
 16-87 6.51e-24

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: 91.52  E-value: 6.51e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537617  16 VYLVQFPRAGCIPSPSPYAFKVETFLRVADIPYTNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEH 87
Cdd:cd03054   1 LELYQWGRAFGLPSLSPECLKVETYLRMAGIPYEVVFSSNPWRSPTGKLPFLELNGEKIADSEKIIEYLKKK 72
GST_C_6 pfam17171
Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.
 181-245 7.07e-22

Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.


Pssm-ID: 465369  Cd Length: 64  Bit Score: 86.05  E-value: 7.07e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617   181 AKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIRAYIDEKvPNVMEYVIRI 245
Cdd:pfam17171   1 AKKDLRALSERLGDKPFFFGDKPTSLDALVFGHLALILYTPLPSPALRIHLKEY-PNLVAYCERI 64
GST_C_Metaxin cd03193
C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase ...
 176-246 1.48e-21

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: 86.14  E-value: 1.48e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537617 176 EVLDQAKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIRAYiDEKVPNVMEYVIRIK 246
Cdd:cd03193  19 EIYELALEDLEALSTLLGDKKFLFGDKPTSVDATVFAHLASILYPPEDSPLLRVL-VASSPNLVEYCERIR 88
GST_C_Metaxin1_3 cd03212
C-terminal, alpha helical domain of Metaxin 1, Metaxin 3, and similar proteins; Glutathione ...
 175-249 6.89e-10

C-terminal, alpha helical domain of Metaxin 1, Metaxin 3, and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily, Metaxin 1-like proteins; composed of metaxins 1 and 3, and similar proteins. Mammalian metaxin (or metaxin 1) is a component of the preprotein import complex of the mitochondrial outer membrane. Metaxin extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. Like the murine gene, the human metaxin gene is located downstream to the glucocerebrosidase (GBA) pseudogene and is convergently transcribed. Inherited deficiency of GBA results in Gaucher disease, which presents many diverse clinical phenotypes. Alterations in the metaxin gene, in addition to GBA mutations, may be associated with Gaucher disease. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals.


Pssm-ID: 198321 [Multi-domain]  Cd Length: 137  Bit Score: 56.10  E-value: 6.89e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617 175 EEVLDQAKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIRAYIdEKVPNVMEYVIRIKEKY 249
Cdd:cd03212  63 KELYKDAKECLNLLSERLGEKKFFFGDRPTSLDALVFGYLAPLLKAPLPNNKLQNHL-KGCPNLVQFVDRILQNY 136
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
30-247 2.66e-09

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 55.67  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617  30 PSPYAFKVETFLRVADIPY----------TNINNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHFHKSDLedLSAS 99
Cdd:COG0625   9 PSPNSRRVRIALEEKGLPYelvpvdlakgEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPPL--LPAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617 100 DKAIARAffallehhLCWVSLysrgqdfgwlaTDTGFGRLLTGIkgfafknfivksfTKKVRGRAAAQGmgtfsREEVLD 179
Cdd:COG0625  87 PAARARV--------RQWLAW-----------ADGDLHPALRNL-------------LERLAPEKDPAA-----IARARA 129

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537617 180 QAKKDLDAISTQLGDKPYLFGSSIkTI-DVTAFAHLAeliYTPQFSPEIRAYidekvPNVMEYVIRIKE 247
Cdd:COG0625 130 ELARLLAVLEARLAGGPYLAGDRF-SIaDIALAPVLR---RLDRLGLDLADY-----PNLAAWLARLAA 189
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 31-82 1.60e-08

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: 50.26  E-value: 1.60e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617  31 SPYAFKVETFLRVADIPYTNIN--------NEFKKMSARGQIPFIELNGRQHADSTIIID 82
Cdd:cd00570   9 SPRSLRVRLALEEKGLPYELVPvdlgegeqEEFLALNPLGKVPVLEDGGLVLTESLAILE 68
GST_C_Metaxin2 cd03211
C-terminal, alpha helical domain of Metaxin 2; Glutathione S-transferase (GST) C-terminal ...
 173-245 3.52e-08

C-terminal, alpha helical domain of Metaxin 2; Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a yeast two-hybrid system using metaxin 1 as the bait. Metaxin 2 shares sequence similarity with metaxin 1 but does not contain a C-terminal mitochondrial outer membrane signal-anchor domain. It associates with mitochondrial membranes through its interaction with metaxin 1, which is a component of the mitochondrial preprotein import complex of the outer membrane. The biological function of metaxin 2 is unknown. It is likely that it also plays a role in protein translocation into the mitochondria. However, this has not been experimentally validated. In a recent proteomics study, it has been shown that metaxin 2 is overexpressed in response to lipopolysaccharide-induced liver injury.


Pssm-ID: 198320  Cd Length: 126  Bit Score: 50.73  E-value: 3.52e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17537617 173 SREEVLDQAKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPEIrAYIDEKVPNVMEYVIRI 245
Cdd:cd03211  54 SLDQVFDEVEKCCQALSEKLGTNQYFFGDQPTELDALVFGHLFTILTTPLPNDEL-AAIVKKYPNLVEFCRRI 125
Tom37 pfam10568
Outer mitochondrial membrane transport complex protein; The TOM37 protein is one of the outer ...
 36-122 1.94e-06

Outer mitochondrial membrane transport complex protein; The TOM37 protein is one of the outer membrane proteins that make up the TOM complex for guiding cytosolic mitochondrial beta-barrel proteins from the cytosol across the outer mitochondrial membrane into the intra-membrane space. In conjunction with TOM70 it guides peptides without an MTS into TOM40, the protein that forms the passage through the outer membrane. It has homology with Metaxin-1, also part of the outer mitochondrial membrane beta-barrel protein transport complex.


Pssm-ID: 463150  Cd Length: 126  Bit Score: 46.08  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617    36 KVETFLR--VADIPYT--NINNEFkkMSARGQIPFIELNGRQHADSTI-IIDNLTEHFHKSDL-EDLSASDKAIARAFFA 109
Cdd:pfam10568   3 AAIAYLKllALPAPFEvvPSNNPD--LSPTGELPALIDGDGTWVSGFDsIVEYLRSKGGGYDLdADLSAKQKADSLAYIS 80

                          90
                  ....*....|...
gi 17537617   110 LLEHHLCWVSLYS 122
Cdd:pfam10568  81 LLESKLYPLLLYS 93
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 30-81 2.08e-05

GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. 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: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 41.79  E-value: 2.08e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537617  30 PSPYAFKVETFLRVADIPYTNI----------NNEFKKMSARGQIPFIELNGRQHADSTIII 81
Cdd:cd03056   8 LSGNCYKVRLLLALLGIPYEWVevdilkgetrTPEFLALNPNGEVPVLELDGRVLAESNAIL 69
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 174-244 5.84e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 40.38  E-value: 5.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537617   174 REEVLDQAKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFSPeirayIDEKVPNVMEYVIR 244
Cdd:pfam13410   2 LERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLD-----LREGYPRLRAWLER 67
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 150-232 1.32e-04

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: 40.17  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537617 150 NFIVKSFTKKVRGRAAAQGMGTFSREEVLDQAKKDLDAISTQLGDKPYLFGSSIKTIDVTAFAHLAELIYTPQFS----- 224
Cdd:cd00299  10 ATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYdllde 89


                ....*....
gi 17537617 225 -PEIRAYID 232
Cdd:cd00299  90 yPRLKAWYD 98
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
31-88 1.38e-04

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 39.52  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537617    31 SPYAFKVETFLRVADIPYTNI-------NNEFKKMSARGQIPFIELNGRQHADSTIIIDNLTEHF 88
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVpippgdhPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELY 71
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-82 2.12e-03

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 36.07  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537617    31 SPYAFKVETFLRVADIPYT---------NINNEFKKMSARGQIPFIEL-NGRQHADSTIIID 82
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEielvdldpkDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILE 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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