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 225579139 420 EEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGE 499
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 225579139 500 FSGAL-VEKLEKSIA 513
Cdd:cd02947   79 VVGADpKEELEEFLE 93

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 225579139 420 EEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGE 499
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 225579139 500 FSGAL-VEKLEKSIA 513
Cdd:cd02947   79 VVGADpKEELEEFLE 93

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 225579139  415 VIKDKEEFEEVLKDAgEKLVAVDFSAPWCGPCRKMRPHFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN 493
Cdd:pfam00085   3 VVLTDANFDEVVQKS-SKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 225579139  494 EEKVGEFSGAL-VEKLEKSIAE 514
Cdd:pfam00085  82 GQPVDDYVGARpKDALAAFLKA 103

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 225579139  417 KDKEEFEEVLKDaGEKLVAVDFSAPWCGPCRKMRPHFHSLSLK-HEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE 495
Cdd:TIGR01068   1 LTDANFDETIAS-SDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79

                  ....*....
gi 225579139  496 KVGEFSGAL 504
Cdd:TIGR01068  80 EVDRSVGAL 88

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 225579139 420 EEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGE 499
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 225579139 500 FSGAL-VEKLEKSIA 513
Cdd:cd02947   79 VVGADpKEELEEFLE 93

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 225579139  415 VIKDKEEFEEVLKDAgEKLVAVDFSAPWCGPCRKMRPHFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN 493
Cdd:pfam00085   3 VVLTDANFDEVVQKS-SKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 225579139  494 EEKVGEFSGAL-VEKLEKSIAE 514
Cdd:pfam00085  82 GQPVDDYVGARpKDALAAFLKA 103

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 418 DKEEFEEVLKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEV---DTEDCEQLVQDCEVFHLPTFQFYKNE 494
Cdd:cd02985    2 SVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDG 81

                 ....*...
gi 225579139 495 EKVGEFSG 502
Cdd:cd02985   82 EKIHEEEG 89

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 225579139  417 KDKEEFEEVLKDaGEKLVAVDFSAPWCGPCRKMRPHFHSLSLK-HEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE 495
Cdd:TIGR01068   1 LTDANFDETIAS-SDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79

                  ....*....
gi 225579139  496 KVGEFSGAL 504
Cdd:TIGR01068  80 EVDRSVGAL 88

thioredoxin 2; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 420 EEFEEVLKDagEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVI-FLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVG 498
Cdd:PRK10996  43 ETLDKLLQD--DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVrFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120

                 ....*.
gi 225579139 499 EFSGAL 504
Cdd:PRK10996 121 MLNGAV 126

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 225579139 436 VDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDC---EQLVQDCEVFHLPTFQFYKNEEKV 497
Cdd:cd01659    2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDpalEKELKRYGVGGVPTLVVFGPGIGV 66

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579139 432 KLVAVDFSAPWCGPCRKMRPHFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGEFSG 502
Cdd:cd02949   14 RLILVLYTSPTCGPCRTLKPILNKVIDEFdGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85

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 225579139 436 VDFSAPWCGPCRKMRPHFHSLSLKHE----DVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGEFSGA 503
Cdd:cd03005   21 VKFFAPWCGHCKRLAPTWEQLAKKFNnenpSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92

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 225579139 418 DKEEFEEVLKDAGeKLVAVDFSAPWCGPCRKMRPHFHSLS---LKHEDVIFLEVDTEDCEQLVqdCEVFHL---PTFQFY 491
Cdd:cd02998    6 TDSNFDKVVGDDK-KDVLVEFYAPWCGHCKNLAPEYEKLAavfANEDDVVIAKVDADEANKDL--AKKYGVsgfPTLKFF 82

                         90
                 ....*....|...
gi 225579139 492 -KNEEKVGEFSGA 503
Cdd:cd02998   83 pKGSTEPVKYEGG 95

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 411 GMVRVIKDKEEFEEVLKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEqLVQDCEVFHLPTFQF 490
Cdd:cd02957    4 GEVREISSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAF-LVNYLDIKVLPTLLV 82

                         90
                 ....*....|..
gi 225579139 491 YKNEEKVGEFSG 502
Cdd:cd02957   83 YKNGELIDNIVG 94

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 422 FEEVLKDAGE--KLVAVDFSAPWCGPCRKM-RPHFHSLSLKH---EDVIFLEVD-------------TEDCEQLVQDCEV 482
Cdd:COG2143   29 LEEDLALAKAegKPILLFFESDWCPYCKKLhKEVFSDPEVAAylkENFVVVQLDaegdkevtdfdgeTLTEKELARKYGV 108

                         90       100
                 ....*....|....*....|...
gi 225579139 483 FHLPTFQFY-KNEEKVGEFSGAL 504
Cdd:COG2143  109 RGTPTLVFFdAEGKEIARIPGYL 131

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 225579139  419 KEEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHS----LSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN- 493
Cdd:TIGR01130   8 KDNFDDFIKSH--EFVLVEFYAPWCGHCKSLAPEYEKaadeLKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNg 85

                          90
                  ....*....|
gi 225579139  494 EEKVGEFSGA 503
Cdd:TIGR01130  86 EDSVSDYNGP 95

104 kDa microneme/rhoptry antigen; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139  57 KHEGSPKS-----------STKNTQLKQEDISKTSSYSKQTNSSNIPKSLAITTYPKQGSTLKPAANGTHDREAEKPKSS 125
Cdd:PTZ00449 506 KHDEPPEGpeasglppkapGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDP 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 126 edliqskkgdifKPSEDSIQSKKGDMPKSSEDPIQSKKDDTAKSLedtiqskngDMPKSSEDPIQSKKDDTARSLEDSIQ 205
Cdd:PTZ00449 586 ------------KHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELL---------DIPKSPKRPESPKSPKRPPPPQRPSS 644

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 206 SKKGDMPKSSDTIQSKESETPKFlqdTIQSKGGKINKQVKDSMKSKESKIRKPLKDSIQSkenkIPKSSQDSAQPKEGKI 285
Cdd:PTZ00449 645 PERPEGPKIIKSPKPPKSPKPPF---DPKFKEKFYDDYLDAAAKSKETKTTVVLDESFES----ILKETLPETPGTPFTT 717

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 286 HKPLKDSLPSKE-------GDISKPSEDTIqakEEITVSPEDTIQAKEEITMSPEDTIQAKEeitVSPEDtIQAKeeiTV 358
Cdd:PTZ00449 718 PRPLPPKLPRDEefpfepiGDPDAEQPDDI---EFFTPPEEERTFFHETPADTPLPDILAEE---FKEED-IHAE---TG 787

                 ....*..
gi 225579139 359 SPEDTMQ 365
Cdd:PTZ00449 788 EPDEAMK 794

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225579139 426 LKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLS--LKHEDVIFLEVDTED 472
Cdd:cd02966   14 LSDLKGKVVLVNFWASWCPPCRAEMPELEALAkeYKDDGVEVVGVNVDD 62

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
                 ....*....|....*....|....*....|....*....|
gi 225579139 418 DKEEFEEVLKDAGeKLVAVDFSAPWCGPCRKMRPHFHSLS 457
Cdd:cd03002    6 TPKNFDKVVHNTN-YTTLVEFYAPWCGHCKNLKPEYAKAA 44

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 225579139  404 EIETLEEGMVRVIKDKEeFEEVLKDAGeKLVAVDFSAPWCGPCRKMRPHFHSLSLKH----EDVIFLEVDTEDCEqlVQD 479
Cdd:TIGR01130 339 PIPEDDEGPVKVLVGKN-FDEIVLDET-KDVLVEFYAPWCGHCKNLAPIYEELAEKYkdaeSDVVIAKMDATAND--VPP 414

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 225579139  480 CEVFHLPTFQFYKNEEK---VGEFSGALVEKLEKSIAE 514
Cdd:TIGR01130 415 FEVEGFPTIKFVPAGKKsepVPYDGDRTLEDFSKFIAK 452

thioredoxin TrxA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579139 424 EVLKDAGekLVAVDFSAPWCGPCRKMRPHFHSLSLKHE-DVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE----KVG 498
Cdd:PRK09381  16 DVLKADG--AILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEvaatKVG 93

                         90
                 ....*....|....*.
gi 225579139 499 EFS-GALVEKLEKSIA 513
Cdd:PRK09381  94 ALSkGQLKEFLDANLA 109