TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    9 EAFQEALAAAgdKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVGE 88
Cdd:cd02947   1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                        90
                ....*....|....
gi 6755911   89 FSGAN-KEKLEASI 101
Cdd:cd02947  79 VVGADpKEELEEFL 92

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    7 SKEAFQEALAAAgDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSN-VVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQK 85
Cdd:COG3118   6 TDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                        90       100
                ....*....|....*....|
gi 6755911   86 VGEFSGA-NKEKLEASITEY 104
Cdd:COG3118  85 VDRFVGAlPKEQLREFLDKV 104

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    9 EAFQEALAAAgdKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVGE 88
Cdd:cd02947   1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                        90
                ....*....|....
gi 6755911   89 FSGAN-KEKLEASI 101
Cdd:cd02947  79 VVGADpKEELEEFL 92

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    7 SKEAFQEALAAAgDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSN-VVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQK 85
Cdd:COG3118   6 TDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                        90       100
                ....*....|....*....|
gi 6755911   86 VGEFSGA-NKEKLEASITEY 104
Cdd:COG3118  85 VDRFVGAlPKEQLREFLDKV 104

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    7 SKEAFQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLC-DKYSNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQK 85
Cdd:cd02984   1 SEEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAkEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                        90
                ....*....|....*.
gi 6755911   86 VGEFSGANKEKLEASI 101
Cdd:cd02984  81 VDRVSGADPKELAKKV 96

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911   14 ALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVDD----------------------CQDVAADCEV 71
Cdd:COG0526  22 SLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDEnpeavkaflkelglpypvlldpDGELAKAYGV 101

                        90       100       110
                ....*....|....*....|....*....|....*
gi 6755911   72 KCMPTFQFY-KKGQKVGEFSGA-NKEKLEASITEY 104
Cdd:COG0526 102 RGIPTTVLIdKDGKIVARHVGPlSPEELEEALEKL 136

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755911    20 DKLVVVDFSATWCGPCKMIKPFFHSLCDKYS-NVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVGEFSGA 92
Cdd:PRK10996  52 DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSgKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGA 125

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911   11 FQEALAaaGDKLVVVDFSATWCGPCKMIKPFFHSLCDKY---SNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKG-QKV 86
Cdd:cd02961   8 FDELVK--DSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGsKEP 85

                        90
                ....*....|....*....
gi 6755911   87 GEFSGANKEKleaSITEYA 105
Cdd:cd02961  86 VKYEGPRTLE---SLVEFI 101

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911   11 FQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYS-NVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVGEF 89
Cdd:cd02956   3 FQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQgQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGF 82

                ....*.
gi 6755911   90 SGANKE 95
Cdd:cd02956  83 QGAQPE 88

disulphide isomerase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755911    20 DKLVVVDFSATWCGPCKMIKPFFHSLC----DKYSNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVgEFSGA 92
Cdd:PTZ00102  49 NEIVLVKFYAPWCGHCKRLAPEYKKAAkmlkEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPV-NYSGG 124

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755911   21 KLVVVDFSATWCGPCKMIKPFFHSLCDKYSN---VVFLEVDVDDC-QDVAADCEVKCMPTFQFYKKGQKVGE-FSGA 92
Cdd:cd02998  19 KDVLVEFYAPWCGHCKNLAPEYEKLAAVFANeddVVIAKVDADEAnKDLAKKYGVSGFPTLKFFPKGSTEPVkYEGG 95

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911      7 SKEAFQEALAaaGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYS----NVVFLEVDVDDCQDVAADCEVKCMPTFQFYKK 82
Cdd:TIGR01130   7 TKDNFDDFIK--SHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgpPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90
                  ....*....|.
gi 6755911     83 G-QKVGEFSGA 92
Cdd:TIGR01130  85 GeDSVSDYNGP 95

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    8 KEAFQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYS---NVVFLEVDVDDCQDVAADCEVKCMPTFQFY-KKG 83
Cdd:cd02950   8 ASSTPPEVALSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGdqvNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLdREG 87

                        90       100
                ....*....|....*....|
gi 6755911   84 QKVGEFSGA-NKEKLEASIT 102
Cdd:cd02950  88 NEEGQSIGLqPKQVLAQNLD 107

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911     20 DKLVVVDFSATWCGPCKMIKPFFHSLCDKY----SNVVFLEVDVDDcQDVAADcEVKCMPTFQFYKKGQK 85
Cdd:TIGR01130 364 TKDVLVEFYAPWCGHCKNLAPIYEELAEKYkdaeSDVVIAKMDATA-NDVPPF-EVEGFPTIKFVPAGKK 431

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911   11 FQEALAAA--GDKLVVVDFSATWCGPCKMIK--PFFHSLCDKY--SNVVFLEVDVDD-------------CQDVAADCEV 71
Cdd:COG2143  29 LEEDLALAkaEGKPILLFFESDWCPYCKKLHkeVFSDPEVAAYlkENFVVVQLDAEGdkevtdfdgetltEKELARKYGV 108

                        90       100
                ....*....|....*....|....
gi 6755911   72 KCMPTFQFY-KKGQKVGEFSGANK 94
Cdd:COG2143 109 RGTPTLVFFdAEGKEIARIPGYLK 132

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    9 EAFQEALAAAgdKLVVVDFSATWCGPCKMIKPF-FHS-----LCDKysNVVFLEVDV--DDCQDVA--ADCEVKCMPTFQ 78
Cdd:cd02953   2 AALAQALAQG--KPVFVDFTADWCVTCKVNEKVvFSDpevqaALKK--DVVLLRADWtkNDPEITAllKRFGVFGPPTYL 77

                ....*.
gi 6755911   79 FYKKGQ 84
Cdd:cd02953  78 FYGPGG 83

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911    9 EAFQEaLAAAGDKLVVVDFSATWCGPCKMIKPFFhslcDKYSNVVFLEVDVD--DCQDVAADCE---VKCMPTFQFYKKG 83
Cdd:cd03004   9 EDFPE-LVLNRKEPWLVDFYAPWCGPCQALLPEL----RKAARALKGKVKVGsvDCQKYESLCQqanIRAYPTIRLYPGN 83

                ..
gi 6755911   84 QK 85
Cdd:cd03004  84 AS 85

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755911   20 DKLVVVDFSATWCGPCKMIKPFFHSLCD---KYSNVVFLEVDVD-DCQD-VAADCEVKCMPTFQFYKKGQKVGEFSGank 94
Cdd:cd02997  17 EKHVLVMFYAPWCGHCKKMKPEFTKAATelkEDGKGVLAAVDCTkPEHDaLKEEYNVKGFPTFKYFENGKFVEKYEG--- 93

                        90
                ....*....|
gi 6755911   95 EKLEASITEY 104
Cdd:cd02997  94 ERTAEDIIEF 103

thiol:disulfide interchange protein precursor; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755911     3 KLIESKEAFQEALAAA--GDKLVVVDFSATWCGPCKMI-KPFFH--SLCDKYSNVVFLEVDV--DDCQDVA 66
Cdd:PRK00293 455 QRIKTVAELDQALAEAkgKGKPVMLDLYADWCVACKEFeKYTFSdpQVQQALADTVLLQADVtaNNAEDVA 525

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 6755911   12 QEALAAAGDKLVVVDFSATWCGPCKMIKP----FFHSLCDKYSN--VVFLEVD 58
Cdd:cd02964   9 VVPVSALEGKTVGLYFSASWCPPCRAFTPklveFYEKLKEEGKNfeIVFVSRD 61

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755911      9 EAFQEALAAagDKLVVVDFSATWCGPCKMIKPFFHS----LCDKYSNVVFLEVDVDD 61
Cdd:pfam13899   8 EALAAAAER--GKPVLVDFGADWCFTCQVLERDFLSheevKAALAKNFVLLRLDWTS 62

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755911   20 DKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFL-EVDVDDCQDVAADCEVKCMPTFQFYKKGQK 85
Cdd:cd03001  18 DDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVgAVDADVHQSLAQQYGVRGFPTIKVFGAGKN 84