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Conserved domains on  [gi|977381787|ref|NP_001306026|]
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metaxin-2 isoform 3 [Homo sapiens]

Protein Classification

metaxin-2( domain architecture ID 10122961)

metaxin-2 associates with mitochondrial membranes through its interaction with metaxin 1 and plays a role in protein translocation into the mitochondrion

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Metaxin2 cd03211
C-terminal, alpha helical domain of Metaxin 2; Glutathione S-transferase (GST) C-terminal ...
 125-227 1.02e-62

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: 192.10  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787 125 AELYLQWCDEATVGE-----------------------WEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFF 181
Cdd:cd03211    1 AELYISWCDEETYNEvtkprygsvypwplnhilayrkqREVLRKLKALGWSDKSLDQVFDEVEKCCQALSEKLGTNQYFF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 977381787 182 NKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIE 227
Cdd:cd03211   81 GDQPTELDALVFGHLFTILTTPLPNDELAAIVKKYPNLVEFCRRIE 126
GST_N_Metaxin2 cd03079
GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a ...
 22-95 3.96e-45

GST_N 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: 239377  Cd Length: 74  Bit Score: 145.65  E-value: 3.96e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 977381787  22 ATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAK 95
Cdd:cd03079    1 AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQFVEAK 74
 
Name Accession Description Interval E-value
GST_C_Metaxin2 cd03211
C-terminal, alpha helical domain of Metaxin 2; Glutathione S-transferase (GST) C-terminal ...
 125-227 1.02e-62

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: 192.10  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787 125 AELYLQWCDEATVGE-----------------------WEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFF 181
Cdd:cd03211    1 AELYISWCDEETYNEvtkprygsvypwplnhilayrkqREVLRKLKALGWSDKSLDQVFDEVEKCCQALSEKLGTNQYFF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 977381787 182 NKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIE 227
Cdd:cd03211   81 GDQPTELDALVFGHLFTILTTPLPNDELAAIVKKYPNLVEFCRRIE 126
GST_N_Metaxin2 cd03079
GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a ...
 22-95 3.96e-45

GST_N 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: 239377  Cd Length: 74  Bit Score: 145.65  E-value: 3.96e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 977381787  22 ATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAK 95
Cdd:cd03079    1 AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQFVEAK 74
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 39-136 3.78e-33

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


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 115.37  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787   39 AASLAVQAFLQMCNLPIKVVCRANaEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLEEVQKAEMKAYMELV 118
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVEPSSN-PSASPKGKLPFIELNGDLIADSEFIIEFLKEKGVDLDAGLSPEQKADARALKALV 79

                          90
                  ....*....|....*...
gi 977381787  119 NNMLLTAELYLQWCDEAT 136
Cdd:pfam17172  80 EEHLYWALLYERWLDPEN 97
GST_C_6 pfam17171
Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.
 163-226 8.83e-27

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


Pssm-ID: 465369  Cd Length: 64  Bit Score: 97.99  E-value: 8.83e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 977381787  163 VDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRI 226
Cdd:pfam17171   1 AKKDLRALSERLGDKPFFFGDKPTSLDALVFGHLALILYTPLPSPALRIHLKEYPNLVAYCERI 64
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
41-229 1.56e-06

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 47.20  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787  41 SLAVQAFLQMCNLPIKVV-------CRANAEY--MSPSGKVPFIHVGNQVVSELGPIVQFV--KAKGHSL--SDGLEEVQ 107
Cdd:COG0625   13 SRRVRIALEEKGLPYELVpvdlakgEQKSPEFlaLNPLGKVPVLVDDGLVLTESLAILEYLaeRYPEPPLlpADPAARAR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787 108 kaemkaymelvnnmlltaelYLQWCDEAtVGEWE----VKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFFNK 183
Cdd:COG0625   93 --------------------VRQWLAWA-DGDLHpalrNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 977381787 184 QPTELDALVFGHLYTIlttqltnDELSEKVKNYSNLLAFCRRIEQH 229
Cdd:COG0625  152 RFSIADIALAPVLRRL-------DRLGLDLADYPNLAAWLARLAAR 190
 
Name Accession Description Interval E-value
GST_C_Metaxin2 cd03211
C-terminal, alpha helical domain of Metaxin 2; Glutathione S-transferase (GST) C-terminal ...
 125-227 1.02e-62

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: 192.10  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787 125 AELYLQWCDEATVGE-----------------------WEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFF 181
Cdd:cd03211    1 AELYISWCDEETYNEvtkprygsvypwplnhilayrkqREVLRKLKALGWSDKSLDQVFDEVEKCCQALSEKLGTNQYFF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 977381787 182 NKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIE 227
Cdd:cd03211   81 GDQPTELDALVFGHLFTILTTPLPNDELAAIVKKYPNLVEFCRRIE 126
GST_N_Metaxin2 cd03079
GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a ...
 22-95 3.96e-45

GST_N 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: 239377  Cd Length: 74  Bit Score: 145.65  E-value: 3.96e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 977381787  22 ATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAK 95
Cdd:cd03079    1 AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQFVEAK 74
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 39-136 3.78e-33

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


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 115.37  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787   39 AASLAVQAFLQMCNLPIKVVCRANaEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLEEVQKAEMKAYMELV 118
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVEPSSN-PSASPKGKLPFIELNGDLIADSEFIIEFLKEKGVDLDAGLSPEQKADARALKALV 79

                          90
                  ....*....|....*...
gi 977381787  119 NNMLLTAELYLQWCDEAT 136
Cdd:pfam17172  80 EEHLYWALLYERWLDPEN 97
GST_C_6 pfam17171
Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.
 163-226 8.83e-27

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


Pssm-ID: 465369  Cd Length: 64  Bit Score: 97.99  E-value: 8.83e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 977381787  163 VDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRI 226
Cdd:pfam17171   1 AKKDLRALSERLGDKPFFFGDKPTSLDALVFGHLALILYTPLPSPALRIHLKEYPNLVAYCERI 64
GST_C_Metaxin cd03193
C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase ...
 156-226 1.91e-23

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: 90.38  E-value: 1.91e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 977381787 156 LDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRI 226
Cdd:cd03193   17 RREIYELALEDLEALSTLLGDKKFLFGDKPTSVDATVFAHLASILYPPEDSPLLRVLVASSPNLVEYCERI 87
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
 22-95 5.98e-23

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: 88.44  E-value: 5.98e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 977381787  22 ATLYQqLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEyMSPSGKVPFIHVGNQVVSELGPIVQFVKAK 95
Cdd:cd03054    1 LELYQ-WGRAFGLPSLSPECLKVETYLRMAGIPYEVVFSSNPW-RSPTGKLPFLELNGEKIADSEKIIEYLKKK 72
Tom37 pfam10568
Outer mitochondrial membrane transport complex protein; The TOM37 protein is one of the outer ...
 41-135 9.97e-23

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: 89.61  E-value: 9.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787   41 SLAVQAFLQMCNLP--IKVVCRANAEyMSPSGKVPFIHVGN-QVVSELGPIVQFVKAK--GHSLSDGLEEVQKAEMKAYM 115
Cdd:pfam10568   1 CLAAIAYLKLLALPapFEVVPSNNPD-LSPTGELPALIDGDgTWVSGFDSIVEYLRSKggGYDLDADLSAKQKADSLAYI 79

                          90       100
                  ....*....|....*....|
gi 977381787  116 ELVNNMLLTAELYLQWCDEA 135
Cdd:pfam10568  80 SLLESKLYPLLLYSLWVDEE 99
GST_C_Metaxin1_3 cd03212
C-terminal, alpha helical domain of Metaxin 1, Metaxin 3, and similar proteins; Glutathione ...
 157-231 3.29e-20

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: 83.07  E-value: 3.29e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 977381787 157 DQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIEQHYF 231
Cdd:cd03212   63 KELYKDAKECLNLLSERLGEKKFFFGDRPTSLDALVFGYLAPLLKAPLPNNKLQNHLKGCPNLVQFVDRILQNYF 137
GST_N_Metaxin1_like cd03078
GST_N family, Metaxin subfamily, Metaxin 1-like proteins; composed of metaxins 1 and 3, and ...
 36-96 1.18e-10

GST_N family, Metaxin subfamily, Metaxin 1-like proteins; composed of metaxins 1 and 3, and similar proteins including Tom37 from fungi. Mammalian metaxin (or metaxin 1) and the fungal protein Tom37 are components of preprotein import complexes 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: 239376  Cd Length: 73  Bit Score: 56.12  E-value: 1.18e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 977381787  36 SDNAASLAVQAFLQMCNLPIKVVcRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKG 96
Cdd:cd03078   14 SVDPECLAVLAYLKFAGAPLKVV-PSNNPWRSPTGKLPALLTSGTKISGPEKIIEYLRKQG 73
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
41-229 1.56e-06

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 47.20  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787  41 SLAVQAFLQMCNLPIKVV-------CRANAEY--MSPSGKVPFIHVGNQVVSELGPIVQFV--KAKGHSL--SDGLEEVQ 107
Cdd:COG0625   13 SRRVRIALEEKGLPYELVpvdlakgEQKSPEFlaLNPLGKVPVLVDDGLVLTESLAILEYLaeRYPEPPLlpADPAARAR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787 108 kaemkaymelvnnmlltaelYLQWCDEAtVGEWE----VKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFFNK 183
Cdd:COG0625   93 --------------------VRQWLAWA-DGDLHpalrNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 977381787 184 QPTELDALVFGHLYTIlttqltnDELSEKVKNYSNLLAFCRRIEQH 229
Cdd:COG0625  152 RFSIADIALAPVLRRL-------DRLGLDLADYPNLAAWLARLAAR 190
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 41-92 3.73e-05

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: 40.63  E-value: 3.73e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 977381787  41 SLAVQAFLQMCNLPIKVVCRANAEY-------MSPSGKVPFIHVGNQVVSELGPIVQFV 92
Cdd:cd00570   12 SLRVRLALEEKGLPYELVPVDLGEGeqeeflaLNPLGKVPVLEDGGLVLTESLAILEYL 70
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 125-226 5.56e-05

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


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 40.95  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787 125 AELYLQWCDEATVGE--WEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTT 202
Cdd:cd00299    1 VRALEDWADATLAPPlvRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                         90       100
                 ....*....|....*....|....
gi 977381787 203 qltnDELSEKVKNYSNLLAFCRRI 226
Cdd:cd00299   81 ----GPYYDLLDEYPRLKAWYDRL 100
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 156-225 3.06e-03

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 35.37  E-value: 3.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 977381787  156 LDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEkvknYSNLLAFCRR 225
Cdd:pfam13410   2 LERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDLREG----YPRLRAWLER 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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