C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  83 KPQNPKDLMQYNYWMHYAEGSLMPYLVMTLVMSNVPKHVPFLIKPIANKICDGVKGGFINPRLKEHAAFLEDYLSQHEYF 162
Cdd:cd03189    1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFRPISRKIADKPLQAFINPELKRHLDFLEDHLAKHPYF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497802588 163 AGD-FSFADIQMSFPVVAMQERVKANN--PQMVAYAKRIQQRP 202
Cdd:cd03189   81 AGDeLTAADIMMSFPLEAALARGPLLEqyPNIAAYLERIEARP 123

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  14 RILWALEELGLEYQVKFYKRLPTFAAPPELKQIHPLGKAPVLTDGDLVIAESAVILEYLQttydteNKFKPQNPkDLM-- 91
Cdd:PLN02395  15 RALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYA------EKYRSQGP-DLLgk 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  92 ------QYNYWMHYAEGSLMPYLVmtlvmsNVPKHVPFlikpiANKICDGVKGGFINPRLKEHAAFLEDY---LSQHEYF 162
Cdd:PLN02395  88 tieergQVEQWLDVEATSYHPPLL------NLTLHILF-----ASKMGFPADEKVIKESEEKLAKVLDVYearLSKSKYL 156

                        170
                 ....*....|
gi 497802588 163 AGDF-SFADI 171
Cdd:PLN02395 157 AGDFvSLADL 166

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  83 KPQNPKDLMQYNYWMHYAEGSLMPYLVMTLVMSNVPKHVPFLIKPIANKICDGVKGGFINPRLKEHAAFLEDYLSQHEYF 162
Cdd:cd03189    1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFRPISRKIADKPLQAFINPELKRHLDFLEDHLAKHPYF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497802588 163 AGD-FSFADIQMSFPVVAMQERVKANN--PQMVAYAKRIQQRP 202
Cdd:cd03189   81 AGDeLTAADIMMSFPLEAALARGPLLEqyPNIAAYLERIEARP 123

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 497802588    1 MITLHHLEQSRSLRILWALEELGLEYQVKFYKRLPTFAAPPELKQIHPLGKAPVLTDGDLVIAESAVILEYL 72
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYI 74

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497802588   12 SLRILWALEELGLEYQVKFYKRLPtFAAPPELKQIHPLGKAPVL-TDGDLVIAESAVILEYLQTT 75
Cdd:pfam13409   5 SHRVRLALEEKGLPYEIELVDLDP-KDKPPELLALNPLGTVPVLvLPDGTVLTDSLVILEYLEEL 68

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497802588   2 ITLHHLEQS-RSLRILWALEELGLEYQVKFYKRLPTFAAPPELKQIHPLGKAPVLTDGDLVIAESAVILEYL 72
Cdd:cd03056    1 MKLYGFPLSgNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497802588   2 ITLHHLEQSRSLRILWALEELGLEYQVKFYKRLPTFAAPPELKQIHPLGKAPVL-TDGDLVIAESAVILEYL 72
Cdd:cd03057    1 MKLYYSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALvLDDGEVLTESAAILQYL 72

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing 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 N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588   1 MITLHHLEQSRSLRILWALEELGLEYQVKFYKRLPTFAAPPELKQIHPLGKAPVLTD---GDLVIAESAVILEYLQTTYD 77
Cdd:cd03048    1 MITLYTHGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLAEKYD 80

                 .
gi 497802588  78 T 78
Cdd:cd03048   81 K 81

GST_N family, unknown subfamily 3; 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497802588  10 SRSLRIlwALEELGLEYQVKFYKRLPTFAaPPELKQIHPLGKAPVL-TDGDLVIAESAVILEYL 72
Cdd:cd03049   12 VRKVRV--AAHETGLGDDVELVLVNPWSD-DESLLAVNPLGKIPALvLDDGEALFDSRVICEYL 72

GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from aryl or alkyl sulfate esters.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 497802588  41 PELKQIHPLGKAPVLTDGDLVIAESAVILEYLQTTY 76
Cdd:cd03050   41 PEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76

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 497802588 126 KPIANKICDGVKGGFINpRLKEHAAFLEDYLSQHEYFAGD-FSFADIQMsFPVVAMQERVK---ANNPQMVAYAKRIQQR 201
Cdd:cd03188   29 RWADDALAEEVKAAARE-RLERRLAYLDAQLAGGPYLLGDqFSVADAYL-FVVLRWARAVGldlSDWPHLAAYLARVAAR 106

                 ....*.
gi 497802588 202 PAFQIA 207
Cdd:cd03188  107 PAVQAA 112

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  14 RILWALEELGLEYQVKFYKRLPTFAAPPELKQIHPLGKAPVLTDGDLVIAESAVILEYLQttydteNKFKPQNPkDLM-- 91
Cdd:PLN02395  15 RALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYA------EKYRSQGP-DLLgk 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  92 ------QYNYWMHYAEGSLMPYLVmtlvmsNVPKHVPFlikpiANKICDGVKGGFINPRLKEHAAFLEDY---LSQHEYF 162
Cdd:PLN02395  88 tieergQVEQWLDVEATSYHPPLL------NLTLHILF-----ASKMGFPADEKVIKESEEKLAKVLDVYearLSKSKYL 156

                        170
                 ....*....|
gi 497802588 163 AGDF-SFADI 171
Cdd:PLN02395 157 AGDFvSLADL 166

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  14 RILWALEELGLEYQVkFYKRLPTF-AAPPELKQIHPLGKAPVLTDGDLVIAESAVILEYLQTTY-DTENKFKPQNPKDLM 91
Cdd:PLN02473  16 RVLLCFLEKGIEFEV-IHVDLDKLeQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKYaDQGTDLLGKTLEHRA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497802588  92 QYNYWMHyAEGSLMPYLVMTLVMSnvpkhvpFLIKPIANKICDGVKGGFINPRLKEHAAFLEDYLSQHEYFAGD-FSFAD 170
Cdd:PLN02473  95 IVDQWVE-VENNYFYAVALPLVIN-------LVFKPRLGEPCDVALVEELKVKFDKVLDVYENRLATNRYLGGDeFTLAD 166

                 .
gi 497802588 171 I 171
Cdd:PLN02473 167 L 167

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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 active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497802588 152 LEDYLSQHEYFAGD-FSFADIQmSFP----VVAMQERVKANNPQMVAYAKRIQQRPAFQ 205
Cdd:cd03178   52 LDKRLSDRPYLAGEeYSIADIA-LYPwthyADLGGFADLSEYPNVKRWLERIAARPAVQ 109

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497802588  17 WALEELGLEYQVKFYkrlpTFAAPPE--LKQIHPLGKAPVLTDGDLVIAESAVILEYL 72
Cdd:cd03039   17 LLLADAGVEYEDVRI----TYEEWPEldLKPTLPFGQLPVLEIDGKKLTQSNAILRYL 70

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497802588 143 PRLKEHAA----FLEDYLSQHEYFAGD-FSFADIQ----MSFPVVAMQeRVKANNPQMVAYAKRIQQRPAF 204
Cdd:cd03182   47 ERNKKRVIdflpVLDKRLAESPYVAGDrFSIADITafvaLDFAKNLKL-PVPEELTALRRWYERMAARPSA 116

GST_N family, Class Delta and Epsilon 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. 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. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497802588   2 ITLHHLEQSRSLR-ILWALEELGLEYQVKFYkrlpTFAAP----PELKQIHPLGKAPVLTDGDLVIAESAVILEYLQ 73
Cdd:cd03045    1 IDLYYLPGSPPCRaVLLTAKALGLELNLKEV----NLMKGehlkPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLV 73