C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251  86 MKERALIDMYSEGILDLTEMIIQLVICPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLELLL 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58331251 166 YVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPGSQRKPAMDAKQIEEARKVF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251  86 MKERALIDMYSEGILDLTEMIIQLVICPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLELLL 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58331251 166 YVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPGSQRKPAMDAKQIEEARKVF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135

glutathione s-transferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251    1 MSGKPVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPED----LEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIA 76
Cdd:PTZ00057   1 MAEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRFGENGDafieFKNFKKEKDTPFEQVPILEMDNIIFAQSQAIVRYLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   77 TKYDLYGKDMKERALIDMYSEGILDLTEMIIQLVICppdQREAKTALAKDRTKnrYLPAFEKVLKSHGQDYLVGNRLTRV 156
Cdd:PTZ00057  81 KKYKICGESELNEFYADMIFCGVQDIHYKFNNTNLF---KQNETTFLNEELPK--WSGYFENILKKNHCNYFVGDNLTYA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 58331251  157 DIHLLELLLYVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLqpgSQRKPAM 208
Cdd:PTZ00057 156 DLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYI---SNRKESV 204

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   101 DLTEMIIQLVICPPDQREAK-TALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHL-LELLLYVEEFDASLLTPF 178
Cdd:pfam14497   2 DLHHPIASSLYYEDEKKKAKrRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALfQVLDGLLYPKAPDALDKY 81

                          90       100
                  ....*....|....*....|.
gi 58331251   179 PLLKAFKSRISSLPNVKKFLQ 199
Cdd:pfam14497  82 PKLKALHERVAARPNIKAYLA 102

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   23 LAAAGVEFEekliQSPEDLEKLK-KDGNLM----FDQVPMVEIDGMKLAQTRAILNYIATKY-----DLYGKDMKERALI 92
Cdd:PLN02395  20 LIEKGVEFE----TVPVDLMKGEhKQPEYLalqpFGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQV 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58331251   93 DM--------YSEGILDLTEMII--QLVICPPDQR---EAKTALAK-------DRTKNRYL 133
Cdd:PLN02395  96 EQwldveatsYHPPLLNLTLHILfaSKMGFPADEKvikESEEKLAKvldvyeaRLSKSKYL 156

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251  86 MKERALIDMYSEGILDLTEMIIQLVICPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLELLL 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58331251 166 YVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPGSQRKPAMDAKQIEEARKVF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135

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        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58331251   5 PVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPEDLEKLKKdGNLMFDQVPMVEIDGMKLAQTRAILNYIA 76
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPELDLK-PTLPFGQLPVLEIDGKKLTQSNAILRYLA 71

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 58331251     5 PVLHYFNARG--RMECIRWLLAAAGVEFEEKLIQS---PEDLEKLKKDGNLmfDQVPMVEIDGMKLAQTRAILNYIA 76
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagPEKSPELLKLNPL--GKVPALEDGGKKLTESRAILEYIA 75

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   7 LHYFNARGRMECIRWLLAAAGVEFEEKLI------QSPEDLEKLkkdgNLMFdQVPMVEIDGMKLAQTRAILNYIATKYD 80
Cdd:COG0625   4 LYGSPPSPNSRRVRIALEEKGLPYELVPVdlakgeQKSPEFLAL----NPLG-KVPVLVDDGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251  81 ---LYGKDMKERALIDM---YSEGILDltEMIIQLV-ICPPDQREAKTALAKDRTKnRYLPAFEKVLKshGQDYLVGNRL 153
Cdd:COG0625  79 eppLLPADPAARARVRQwlaWADGDLH--PALRNLLeRLAPEKDPAAIARARAELA-RLLAVLEARLA--GGPYLAGDRF 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 58331251 154 TRVDIHLLELLLYVEEFDASlLTPFPLLKAFKSRISSLPNVKKFLQPG 201
Cdd:COG0625 154 SIADIALAPVLRRLDRLGLD-LADYPNLAAWLARLAARPAFQRALAAA 200

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 58331251   5 PVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPEDLEKLKKDGNLmFDQVPMVEIDGMKLAQTRAILNYIA 76
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71

GST_N family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58331251   4 KPVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPEDLEKLKKdgNLMFDQVPMVEIDGMKLAQTRAILNYIATK 78
Cdd:cd03076   1 PYTLTYFPVRGRAEAIRLLLADQGISWEEERVTYEEWQESLKP--KMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   27 GVEFEEKLIqspeDLEKL--KKDGNLM---FDQVPMVEIDGMKLAQTRAILNYIATKY-----DLYGKDMKERALIDMYS 96
Cdd:PLN02473  25 GIEFEVIHV----DLDKLeqKKPEHLLrqpFGQVPAIEDGDLKLFESRAIARYYATKYadqgtDLLGKTLEHRAIVDQWV 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   97 E------GILDLTeMIIQLVICPPDQREAKTALAKD-RTK-NRYLPAFEKVLKSHgqDYLVGNRLTRVDI 158
Cdd:PLN02473 101 EvennyfYAVALP-LVINLVFKPRLGEPCDVALVEElKVKfDKVLDVYENRLATN--RYLGGDEFTLADL 167

GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1), thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251   5 PVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPE-----------DLEKLKKDgnlmFDQVPMVEIDGMKLAQTRAILN 73
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdydrsqwlnEKFKLGLD----FPNLPYYIDGDVKLTQSNAILR 76

                ....*.
gi 58331251  74 YIATKY 79
Cdd:cd03075  77 YIARKH 82

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58331251  19 IRWLLAAAGVEFE-------EKLIQSPEDLEKLKkdgnlmFDQVPMVEIDGMKLAQTRAILNYIA 76
Cdd:cd03056  15 VRLLLALLGIPYEwvevdilKGETRTPEFLALNP------NGEVPVLELDGRVLAESNAILVYLA 73

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
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58331251  23 LAAAGVEFEekLIqsPEDLEKL-KKDGNLM----FDQVPMVEIDGMKLAQTRAILNYIATK 78
Cdd:cd03053  20 LEEKGVDYE--LV--PVDLTKGeHKSPEHLarnpFGQIPALEDGDLKLFESRAITRYLAEK 76

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal 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. 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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331251 120 KTALAKDRTKN---RYLPAFEKVLKSHGQDYLVGNRLTRVDIH----LLELLLYVEEFDASLLTPFPLLKAFKSRISSLP 192
Cdd:cd10293  33 KVPSAIERYTNeirRVLGVLETALAERYRVWLVGDKFTIADLAfvpwNNVVDMIFIDPELDIKKEFPHVYKWLKRMLARP 112

                ....
gi 58331251 193 NVKK 196
Cdd:cd10293 113 AVKK 116