PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  36 GKLIELDEDNWHLMLQGEWMIEFFAPWCPACKNLAPTWERFARVAKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKD 115
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|.
gi 665403188 116 GEFRQYRGARDGDALLYFVKK 136
Cdd:cd02994   81 GVFRRYQGPRDKEDLISFIEE 101

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  36 GKLIELDEDNWHLMLQGEWMIEFFAPWCPACKNLAPTWERFARVAKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKD 115
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|.
gi 665403188 116 GEFRQYRGARDGDALLYFVKK 136
Cdd:cd02994   81 GVFRRYQGPRDKEDLISFIEE 101

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 665403188  37 KLIELDEDNWH---LMLQGEWMIEFFAPWCPACKNLAPTWERFARVAKDvQVQVAKIDVTTSPSLSGRFFVTALPTIYHV 113
Cdd:COG3118    1 AVVELTDENFEeevLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*
gi 665403188 114 KDGE--FRQyRGARDGDALLYFVKK 136
Cdd:COG3118   80 KDGQpvDRF-VGALPKEQLREFLDK 103

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 665403188   40 ELDEDNWHLMLQGE--WMIEFFAPWCPACKNLAPTWERFARV--AKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKD 115
Cdd:TIGR01130   5 VLTKDNFDDFIKSHefVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90       100
                  ....*....|....*....|....
gi 665403188  116 GEFR--QYRGARDGDALLYFVKKQ 137
Cdd:TIGR01130  85 GEDSvsDYNGPRDADGIVKYMKKQ 108

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  36 GKLIELDEDNWHLMLQGEWMIEFFAPWCPACKNLAPTWERFARVAKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKD 115
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|.
gi 665403188 116 GEFRQYRGARDGDALLYFVKK 136
Cdd:cd02994   81 GVFRRYQGPRDKEDLISFIEE 101

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  39 IELDEDNWH-LMLQGE--WMIEFFAPWCPACKNLAPTWERFARVAKDVqVQVAKIDVTTSPSLSGRFFVTALPTIYHVKD 115
Cdd:cd03001    3 VELTDSNFDkKVLNSDdvWLVEFYAPWCGHCKNLAPEWKKAAKALKGI-VKVGAVDADVHQSLAQQYGVRGFPTIKVFGA 81

                         90       100
                 ....*....|....*....|.
gi 665403188 116 GEFR--QYRGARDGDALLYFV 134
Cdd:cd03001   82 GKNSpqDYQGGRTAKAIVSAA 102

Thioredoxin domain-containing protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  38 LIELDEDNWHLMLQ-------GEWMIEFFAPWCPACKNLAPTWERFARVAKDvQVQVAKIDVTTSPSLSGRFFVTALPTI 110
Cdd:PTZ00443  32 LVLLNDKNFEKLTQastgattGPWFVKFYAPWCSHCRKMAPAWERLAKALKG-QVNVADLDATRALNLAKRFAIKGYPTL 110

                         90
                 ....*....|...
gi 665403188 111 YHVKDGEFRQYRG 123
Cdd:PTZ00443 111 LLFDKGKMYQYEG 123

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188   41 LDEDNWHLmlqgewmIEFFAPWCPACKNLAPTWERFARvAKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKDG-EFR 119
Cdd:pfam00085  15 QKSSKPVL-------VDFYAPWCGPCKMLAPEYEELAQ-EYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGqPVD 86

                          90
                  ....*....|....*..
gi 665403188  120 QYRGARDGDALLYFVKK 136
Cdd:pfam00085  87 DYVGARPKDALAAFLKA 103

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 665403188   40 ELDEDNWHLMLQGE--WMIEFFAPWCPACKNLAPTWERFARV--AKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKD 115
Cdd:TIGR01130   5 VLTKDNFDDFIKSHefVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90       100
                  ....*....|....*....|....
gi 665403188  116 GEFR--QYRGARDGDALLYFVKKQ 137
Cdd:TIGR01130  85 GEDSvsDYNGPRDADGIVKYMKKQ 108

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  55 MIEFFAPWCPACKNLAPTWERFARVAKDVQ-VQVAKIDVTTS--PSLsgrFFVTALPTIYHVKDGEFRQ---YRGARDGD 128
Cdd:cd02995   22 LVEFYAPWCGHCKALAPIYEELAEKLKGDDnVVIAKMDATANdvPSE---FVVDGFPTILFFPAGDKSNpikYEGDRTLE 98

                 ....*.
gi 665403188 129 ALLYFV 134
Cdd:cd02995   99 DLIKFI 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 665403188  55 MIEFFAPWCPACKNLAPTWERFArvAKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKDG-EFRQYRGARDGDALLYF 133
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELA--EEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGkEVDRVVGADPKEELEEF 91

                 ..
gi 665403188 134 VK 135
Cdd:cd02947   92 LE 93

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 665403188   55 MIEFFAPWCPACKNLAPTWERFARVAKDVQ--VQVAKIDVTTS--PSlsgrFFVTALPTIYHVKDGEFRQ---YRGARDG 127
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAEsdVVIAKMDATANdvPP----FEVEGFPTIKFVPAGKKSEpvpYDGDRTL 443

                  ....*....
gi 665403188  128 DALLYFVKK 136
Cdd:TIGR01130 444 EDFSKFIAK 452

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  36 GKLIELDEDNWHLMLQGEW--MIEFFAPWCPACKNLAPTWERFARVAKDvQVQVAKIDVTTSPSLSGRFFVTALPTIYHV 113
Cdd:PRK10996  35 GEVINATGETLDKLLQDDLpvVIDFWAPWCGPCRNFAPIFEDVAAERSG-KVRFVKVNTEAERELSARFRIRSIPTIMIF 113

                 ....
gi 665403188 114 KDGE 117
Cdd:PRK10996 114 KNGQ 117

disulphide isomerase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  55 MIEFFAPWCPACKNLAPTWERFARVAKDV-QVQVAKIDVTTSPSLSGRFFVTALPTIYHVKDGEFR--QYRGARDGDALL 131
Cdd:PTZ00102 379 LLEIYAPWCGHCKNLEPVYNELGEKYKDNdSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTpiPYEGERTVEGFK 458

                 ....*
gi 665403188 132 YFVKK 136
Cdd:PTZ00102 459 EFVNK 463

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  55 MIEFFAPWCPACKNLAPTWERFARvAKDVQVQVAKIDVTTSPS--LSGRFFVTALPTI-------YHVKDGEfRQYRGAR 125
Cdd:cd03002   22 LVEFYAPWCGHCKNLKPEYAKAAK-ELDGLVQVAAVDCDEDKNkpLCGKYGVQGFPTLkvfrppkKASKHAV-EDYNGER 99

                         90
                 ....*....|
gi 665403188 126 DGDALLYFVK 135
Cdd:cd03002  100 SAKAIVDFVL 109

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  37 KLIELDEDNWHLMLQGE--WMIEFFAPWCPACKNLAPTWERFARVAKDVqVQVAKIDVTTSPSLSGRFFVTALPTIYHVK 114
Cdd:cd03003    2 EIVTLDRGDFDAAVNSGeiWFVNFYSPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                         90       100
                 ....*....|....*....|
gi 665403188 115 DG-EFRQYRGARDGDALLYF 133
Cdd:cd03003   81 SGmNPEKYYGDRSKESLVKF 100

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665403188  55 MIEFFAPWCPACKNLAPTWERFARVAKDVQVQVAKIDVTTSPSLSGRFF-VTALPTIYHVKDGEFRQY 121
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYgVGGVPTLVVFGPGIGVKY 68

thioredoxin TrxA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  37 KLIELDEDNWH---LMLQGEWMIEFFAPWCPACKNLAPTWERFARVAKDvQVQVAKIDVTTSPSLSGRFFVTALPTIYHV 113
Cdd:PRK09381   4 KIIHLTDDSFDtdvLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQG-KLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82

                 ....
gi 665403188 114 KDGE 117
Cdd:PRK09381  83 KNGE 86

thioredoxin; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665403188  55 MIEFFAPWCPACKNLAPTWERFARvaKDVQVQVAKIDVTTSPSLSGRFFVTALPTIYHVKDGE 117
Cdd:PTZ00051  22 IVDFYAEWCGPCKRIAPFYEECSK--EYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665403188  54 WMIEFFAPWCPACKNLAPTWERFARVAKDVQVQVAKIDVTTSPSLSGRFFVTA------LPTIYHVKDG 116
Cdd:cd02962   50 WLVEFFTTWSPECVNFAPVFAELSLKYNNNNLKFGKIDIGRFPNVAEKFRVSTsplskqLPTIILFQGG 118

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403188  54 WMIEFFAPWCPACKNLAPTWERFARVAKDVQVQVAKI--DVTTSPSLSGRFFVTALPTIYHVKDG--EFRQYRG-ARDGD 128
Cdd:cd02993   24 TLVVLYAPWCPFCQAMEASYEELAEKLAGSNVKVAKFnaDGEQREFAKEELQLKSFPTILFFPKNsrQPIKYPSeQRDVD 103

                 ....*.
gi 665403188 129 ALLYFV 134
Cdd:cd02993  104 SLLMFV 109