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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361   1 MLKLHGFAVSNYYNMVKLALLEKGLPFEEV---LFFGGPAPEA-LAKSPRGKVPTLEtEHGFV-SETGVILDYIEQTQPG 75
Cdd:COG0625     1 MMKLYGSPPSPNSRRVRIALEEKGLPYELVpvdLAKGEQKSPEfLALNPLGKVPVLV-DDGLVlTESLAILEYLAERYPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361  76 KPLLPADAFGQAKVRELLREIELYIELPARTCYgeAFFGTAVEPLIKERARVDLLAGFATLkcNGRF--QPYVAGEQMTI 153
Cdd:COG0625    80 PPLLPADPAARARVRQWLAWADGDLHPALRNLL--ERLAPEKDPAAIARARAELARLLAVL--EARLagGPYLAGDRFSI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2238044361 154 ADLMFCFSVDLACVVGkkvlnvDFLADFPQAAALLEKLRGNPHMARIVADKDAAMP 209
Cdd:COG0625   156 ADIALAPVLRRLDRLG------LDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361   1 MLKLHGFAVSNYYNMVKLALLEKGLPFEEV---LFFGGPAPEA-LAKSPRGKVPTLEtEHGFV-SETGVILDYIEQTQPG 75
Cdd:COG0625     1 MMKLYGSPPSPNSRRVRIALEEKGLPYELVpvdLAKGEQKSPEfLALNPLGKVPVLV-DDGLVlTESLAILEYLAERYPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361  76 KPLLPADAFGQAKVRELLREIELYIELPARTCYgeAFFGTAVEPLIKERARVDLLAGFATLkcNGRF--QPYVAGEQMTI 153
Cdd:COG0625    80 PPLLPADPAARARVRQWLAWADGDLHPALRNLL--ERLAPEKDPAAIARARAELARLLAVL--EARLagGPYLAGDRFSI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2238044361 154 ADLMFCFSVDLACVVGkkvlnvDFLADFPQAAALLEKLRGNPHMARIVADKDAAMP 209
Cdd:COG0625   156 ADIALAPVLRRLDRLG------LDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEVL--FFGGPAPEALAKSPRGKVPTLETEHGFVSETGVILDYIE 70
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPvdLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEVLFFGGPAPEALAK-SPRGKVPTLETEHGFV-SETGVILDYIEQTQPGKPLL 79
Cdd:PRK10357    1 MKLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQyNPLGKVPALVTEEGECwFDSPIIAEYIELLNVAPAML 80

                          90
                  ....*....|...
gi 2238044361  80 PADAFGQAKVREL 92
Cdd:PRK10357   81 PRDPLAALRVRQL 93

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361   1 MLKLHGFAVSNYYNMVKLALLEKGLPFEEV---LFFGGPAPEA-LAKSPRGKVPTLEtEHGFV-SETGVILDYIEQTQPG 75
Cdd:COG0625     1 MMKLYGSPPSPNSRRVRIALEEKGLPYELVpvdLAKGEQKSPEfLALNPLGKVPVLV-DDGLVlTESLAILEYLAERYPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361  76 KPLLPADAFGQAKVRELLREIELYIELPARTCYgeAFFGTAVEPLIKERARVDLLAGFATLkcNGRF--QPYVAGEQMTI 153
Cdd:COG0625    80 PPLLPADPAARARVRQWLAWADGDLHPALRNLL--ERLAPEKDPAAIARARAELARLLAVL--EARLagGPYLAGDRFSI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2238044361 154 ADLMFCFSVDLACVVGkkvlnvDFLADFPQAAALLEKLRGNPHMARIVADKDAAMP 209
Cdd:COG0625   156 ADIALAPVLRRLDRLG------LDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEVL--FFGGPAPEALAKSPRGKVPTLETEHGFVSETGVILDYIE 70
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPvdLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361  16 VKLALLEKGLPFEEV---LFFGGP--APEALAKSPRGKVPTLETEHGFVSETGVILDYIEQTQPGKPLLPADAFGQAKVR 90
Cdd:TIGR01262  14 VRIALALKGIDYEYVpvnLLRDGEqrSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPPLLPADPIKRARVR 93

                  ..
gi 2238044361  91 EL 92
Cdd:TIGR01262  94 AL 95

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial 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. 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 class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEVL--FFGGP--APEALAKSPRGKVPTLETEHGFVSETGVILDYI 69
Cdd:cd03053     2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPvdLTKGEhkSPEHLARNPFGQIPALEDGDLKLFESRAITRYL 73

putative glutathione S-transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEVLFFGGPAPEALAK-SPRGKVPTLETEHGFV-SETGVILDYIEQTQPGKPLL 79
Cdd:PRK10357    1 MKLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQyNPLGKVPALVTEEGECwFDSPIIAEYIELLNVAPAML 80

                          90
                  ....*....|...
gi 2238044361  80 PADAFGQAKVREL 92
Cdd:PRK10357   81 PRDPLAALRVRQL 93

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEVL----FFGGPAPEALAKSPRGKVPTLETEHGFVSETGVILDYIEQ 71
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPldfgAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKG--LPFEEVLFFGGP--APEALAKSPRGKVPTLETEHG-FVSETGVILDYIE 70
Cdd:cd03051     1 MKLYDSPTAPNPRRVRIFLAEKGidVPLVTVDLAAGEqrSPEFLAKNPAGTVPVLELDDGtVITESVAICRYLE 74

GST_N family, Class Beta 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238044361  19 ALLEKGLPFE--EVLFFGGPAPEA--LAKSPRGKVPTLETEHGFV-SETGVILDYIEQTQP 74
Cdd:cd03057    17 ALEELGLPFElvRVDLRTKTQKGAdyLAINPKGQVPALVLDDGEVlTESAAILQYLADLHP 77

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238044361   2 LKLHGFAVSNYYnMVKLALLEKGLPFE-EVLFFGGPA---PEALAKSPRGKVPTLEtEHGFV-SETGVILDYI 69
Cdd:cd03046     1 ITLYHLPRSRSF-RILWLLEELGLPYElVLYDRGPGEqapPEYLAINPLGKVPVLV-DGDLVlTESAAIILYL 71

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2238044361  13 YNM--------VKLALLEKGLPFEEVLFFGGPAPE-ALAKSPRGKVPTLETEHG-FVSETGVILDYIE 70
Cdd:cd03055    22 YSMrfcpyaqrARLVLAAKNIPHEVININLKDKPDwFLEKNPQGKVPALEIDEGkVVYESLIICEYLD 89

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361  82 DAFGQAKVRELLREIELYIELPArtcyGEAF------FGTAVEPLIKE-----RARVdlLAGFATLKCNGRFQPYVAGEQ 150
Cdd:cd03182     1 TPLEKALIEMWQRRAELQGLAPV----FQAFrhatpgLKPDREVQVPEwgernKKRV--IDFLPVLDKRLAESPYVAGDR 74

                          90       100
                  ....*....|....*....|..
gi 2238044361 151 MTIADLMFCFSVDLACVVGKKV 172
Cdd:cd03182    75 FSIADITAFVALDFAKNLKLPV 96

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2238044361  24 GLPFEEVlfFGGPApealAKSPRGKVPTLETEHGFVSETGVILDYIEQT 72
Cdd:cd03054    30 GIPYEVV--FSSNP----WRSPTGKLPFLELNGEKIADSEKIIEYLKKK 72

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta 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 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238044361 108 YGEAFFGTAVEPLIKERARVDLLAGFATLKCNGRFQPYVAGEQMTIADLMfcfsvdLACVVG-KKVLNVDfLADFPQAAA 186
Cdd:cd03188    26 YPARWADDALAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAY------LFVVLRwARAVGLD-LSDWPHLAA 98

                  ....*....
gi 2238044361 187 LLEKLRGNP 195
Cdd:cd03188    99 YLARVAARP 107

GST_N family, Class Zeta 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 Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238044361   2 LKLHGFAVSNYYNMVKLALLEKGLPFEEV---LFFGGP-APEALAKSPRGKVPTLETEHGFVSETGVILDYIE 70
Cdd:cd03042     1 MILYSYFRSSASYRVRIALNLKGLDYEYVpvnLLKGEQlSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73