Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274    51 NYDASHHEGDVVSGLGWLIRNSQGTVLECGMGKFQGRMTPEEAECSALIWAIQATSAFGYTKVIFEGDNSNVNRLINTKS 130
Cdd:pfam13456   1 NFDGAFKCDSGLAGAGVVIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGLQLAWKLGIRHLIVEGDSATVVQLINGRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18404274   131 -DNPRLKHYLDTIKSWIPSFTSTEFIFTHREQNQCADTLVKKA 172
Cdd:pfam13456  81 pKQSKLANLLDEIRKLLKRFESVSFEHIPREQNRVADTLAKMA 123

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274    51 NYDASHHEGDVVSGLGWLIRNSQGTVLECGMGKFQGRMTPEEAECSALIWAIQATSAFGYTKVIFEGDNSNVNRLINTKS 130
Cdd:pfam13456   1 NFDGAFKCDSGLAGAGVVIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGLQLAWKLGIRHLIVEGDSATVVQLINGRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18404274   131 -DNPRLKHYLDTIKSWIPSFTSTEFIFTHREQNQCADTLVKKA 172
Cdd:pfam13456  81 pKQSKLANLLDEIRKLLKRFESVSFEHIPREQNRVADTLAKMA 123

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 18404274 222 ELNSQTPHVMVMFTARWCGPCRDMIPILNKMDSEYKNeFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGAD 301
Cdd:cd02947   5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGAD 83

                        90
                ....*....|
gi 18404274 302 PK-KLRELVK 310
Cdd:cd02947  84 PKeELEEFLE 93

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274   230 VMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGADPK-KLREL 308
Cdd:TIGR01068  17 VLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKaALKQL 96

                  ....*
gi 18404274   309 VKKYI 313
Cdd:TIGR01068  97 INKNL 101

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 18404274   222 ELNSQTPHVMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGAD 301
Cdd:pfam00085  13 VVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGAR 92

                          90
                  ....*....|.
gi 18404274   302 PK-KLRELVKK 311
Cdd:pfam00085  93 PKdALAAFLKA 103

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274    51 NYDASHHEGDVVSGLGWLIRNSQGTVLECGMGKFQGRMTPEEAECSALIWAIQATSAFGYTKVIFEGDNSNVNRLINTKS 130
Cdd:pfam13456   1 NFDGAFKCDSGLAGAGVVIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGLQLAWKLGIRHLIVEGDSATVVQLINGRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18404274   131 -DNPRLKHYLDTIKSWIPSFTSTEFIFTHREQNQCADTLVKKA 172
Cdd:pfam13456  81 pKQSKLANLLDEIRKLLKRFESVSFEHIPREQNRVADTLAKMA 123

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 18404274 222 ELNSQTPHVMVMFTARWCGPCRDMIPILNKMDSEYKNeFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGAD 301
Cdd:cd02947   5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGAD 83

                        90
                ....*....|
gi 18404274 302 PK-KLRELVK 310
Cdd:cd02947  84 PKeELEEFLE 93

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274   230 VMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGADPK-KLREL 308
Cdd:TIGR01068  17 VLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKaALKQL 96

                  ....*
gi 18404274   309 VKKYI 313
Cdd:TIGR01068  97 INKNL 101

thioredoxin; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274  225 SQTPHVMVMFTARWCGPCRDMIPILNKMDSEYKNeFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGADPKK 304
Cdd:PTZ00051  16 SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTK-MVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGANDEA 94

                 ....
gi 18404274  305 LREL 308
Cdd:PTZ00051  95 LKQL 98

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274  223 LNSQTPhVMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGADP 302
Cdd:PRK10996  49 LQDDLP-VVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGAVP 127

                 .
gi 18404274  303 K 303
Cdd:PRK10996 128 K 128

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18404274 222 ELNSQTPHVMVMFTARWCGPCRDMIPILNKMDSEYKNE--FKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQM 294
Cdd:cd02961  10 ELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDgkVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGSKE 84

thioredoxin TrxA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274  231 MVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGADPK-KLRELV 309
Cdd:PRK09381  25 LVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKgQLKEFL 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 18404274 220 ITELNSQTPHVmVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFD--TEIrfTERFDISYLPTTLVFKGGEQMAKV 297
Cdd:cd02984   8 LLKSDASKLLV-LHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEelPEI--SEKFEITAVPTFVFFRNGTIVDRV 84

                        90
                ....*....|...
gi 18404274 298 TGADPKKLRELVK 310
Cdd:cd02984  85 SGADPKELAKKVE 97

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18404274 237 RWCGPCRDMIPILNKMDSEYKNE-FKFYTVNFDTeIRFTERFDISYLPTTLVFKGGEQMAKVTGADPKKLRELV 309
Cdd:cd02948  27 EWCGPCKAVVSLFKKIKNELGDDlLHFATAEADT-IDTLKRYRGKCEPTFLFYKNGELVAVIRGANAPLLNKTI 99

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274 229 HVMVMFTARWCGPCRdmipilnKMDSE----------YKNEFKFYTVNFD-------------TEIRFTERFDISYLPTT 285
Cdd:COG2143  42 PILLFFESDWCPYCK-------KLHKEvfsdpevaayLKENFVVVQLDAEgdkevtdfdgetlTEKELARKYGVRGTPTL 114

                        90       100
                ....*....|....*....|....*....
gi 18404274 286 LVF-KGGEQMAKVTGADPKKLRELVKKYI 313
Cdd:COG2143 115 VFFdAEGKEIARIPGYLKPETFLALLKYV 143

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274 220 ITELNSQT---------PHVMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIR---FTERFDISYLPTTLV 287
Cdd:cd02998   2 VVELTDSNfdkvvgddkKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEAnkdLAKKYGVSGFPTLKF 81

                ....*.
gi 18404274 288 FKGGEQ 293
Cdd:cd02998  82 FPKGST 87

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 18404274 220 ITELNSQT---------PHVMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIR--FTERFDISYLPTTLVF 288
Cdd:cd03002   2 VYELTPKNfdkvvhntnYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNkpLCGKYGVQGFPTLKVF 81

                        90       100
                ....*....|....*....|....*
gi 18404274 289 KGGEQMAKVTGAD---PKKLRELVK 310
Cdd:cd03002  82 RPPKKASKHAVEDyngERSAKAIVD 106

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 18404274 231 MVMFTARWCGPCRDMIPILNKMDSEYKNeFKFYTVNFDT---EIRFTERFDISYLPTTLVFKGGEQ 293
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEdpaLEKELKRYGVGGVPTLVVFGPGIG 65

ribonuclease H; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274   63 SGLGWLIRNSQGTV-LECGMGKfqgrMTPEEAECSALIWAIQATSAFGYTKVIFEGDNSNVNRLI-----NTKSDNPRLK 136
Cdd:PRK13907  17 SGAGVFIKGVQPAVqLSLPLGT----MSNHEAEYHALLAALKYCTEHNYNIVSFRTDSQLVERAVekeyaKNKMFAPLLE 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18404274  137 HYLDTIKS-------WIPSftstefifthrEQNQCADTLVKKAI 173
Cdd:PRK13907  93 EALQYIKSfdlffikWIPS-----------SQNKVADELARKAI 125

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404274 232 VMFTARWCGPCRDMIPILNKMDSEYKNE---FKFYTVNFDTEIRFTERFDISYLPTTLVFKGGEQMAKVTGA 300
Cdd:cd03005  21 VKFFAPWCGHCKRLAPTWEQLAKKFNNEnpsVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92

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
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404274 231 MVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFDTEIRFTERFDISYLPTTLVFKGGE 292
Cdd:cd03004  23 LVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPGNA 84

disulphide isomerase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18404274  230 VMVMFTARWCGPCRDMIPILNKMDSEYKNEFKFYTVNFD---TEIRFtERFDISYLPTTLVFKGGE 292
Cdd:PTZ00102 378 VLLEIYAPWCGHCKNLEPVYNELGEKYKDNDSIIVAKMNgtaNETPL-EEFSWSAFPTILFVKAGE 442

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404274 232 VMFTARWCGPCRDMIPILNKmdseyKN-EFKFYTVNFDTEIR--FTERFDISYLPTtlVFKGGEQMakvTGADPKKLREL 308
Cdd:COG0695   3 TLYTTPGCPYCARAKRLLDE-----KGiPYEEIDVDEDPEAReeLRERSGRRTVPV--IFIGGEHL---GGFDEGELDAL 72

                ..
gi 18404274 309 VK 310
Cdd:COG0695  73 LA 74

thioredoxin-like protein

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18404274  233 MFTARWCGPCRDMIPILNKMDseykneFKFYTVNFDTEIRFTERFDISYLPTTLvfkGGEQMAKVTGAdPKKLRELVKK 311
Cdd:PHA02125   4 LFGAEWCANCKMVKPMLANVE------YTYVDVDTDEGVELTAKHHIRSLPTLV---NTSTLDRFTGV-PRNVAELKEK 72

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
                  ....*....|....*....|....*....|
gi 18404274   230 VMVMFTARWCGPCRDMIPILNKMDSEYKNE 259
Cdd:TIGR01130 367 VLVEFYAPWCGHCKNLAPIYEELAEKYKDA 396