Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347  26 YTIDGTVSDSTlNGNTVYLTDMASNTV-LDSAVIADNKFQFTGKADTAFIATL--QSRPYRMHLIVENGNISVEMGESD- 101
Cdd:pfam14289   1 YTIEGTIKGLK-DGTKVYLSYDGGGLVkLDSAVVKNGKFTFKGKVDEPPMAYLliDDKSGALPFFLENGTITIKLDPGDf 79

                          90
                  ....*....|...
gi 2443763347 102 --KFSGTPLNDEM 112
Cdd:pfam14289  80 iaKVKGSPLNDEY 92

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 227 DFTVEQPDGTKVSLSDYvgKGRYVLVDFWASWCGPCRREIPNIKELYDKYHDKGLDVLGVAVWDK-PEDTQKAIEEMQVV 305
Cdd:cd02966     1 DFSLPDLDGKPVSLSDL--KGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDdPAAVKAFLKKYGIT 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2443763347 306 WPQIINAQHIPTDLYGIQVIPHIILFAPDGTIAAR 340
Cdd:cd02966    79 FPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRAR 113

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 221 VGQMFTDFTVEQPDGTKVSLSDYvgKGRYVLVDFWAS-WCGPCRREIPNIKELYDKYHDKGLDVLGVAVwDKPEDTQKAI 299
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDY--RGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSV-DSPESHKAFA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2443763347 300 EEMQVVWPQIINAQHIPTDLYGIQV------IPHIILFAPDGTIAAR 340
Cdd:pfam00578  78 EKYGLPFPLLSDPDGEVARAYGVLNeeeggaLRATFVIDPDGKVRYI 124

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 2443763347 250 VLVDFWASWCGPCRREIPNIKELYDKYHDKgLDVLGVAVWDKPEDTQKaieemqvvwpqiinaqhiptdlYGIQVIPHII 329
Cdd:TIGR01068  17 VLVDFWAPWCGPCKMIAPILEELAKEYEGK-VKFVKLNVDENPDIAAK----------------------YGIRSIPTLL 73

                          90
                  ....*....|.
gi 2443763347 330 LFaPDGTIAAR 340
Cdd:TIGR01068  74 LF-KNGKEVDR 83

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 227 DFTVEQPDGTKVSLSDYvgKGRYVLVDFWASWCGPCRREIPNIKELYDKYHDKGLDVLGVAVwDKPEDTQKAIEEMQVVW 306
Cdd:COG1225     3 DFTLPDLDGKTVSLSDL--RGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS-DSDEAHKKFAEKYGLPF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2443763347 307 PQIINAQHIPTDLYGIQVIPHIILFAPDGTIAARDLREEAMKEKVTEVMTA 357
Cdd:COG1225    80 PLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEA 130

thiol-disulfide oxidoreductase ResA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 217 KKTAVGQMFTDFTVEQPDGTKVSLSDYVGKGryVLVDFWASWCGPCRREIPNIKELYDKYHDKGLDVLGVAVwDKPEDT- 295
Cdd:PRK03147   33 EKVQVGKEAPNFVLTDLEGKKIELKDLKGKG--VFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV-DETELAv 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2443763347 296 QKAIEEMQVVWPQIINAQHIPTDLYGIQVIPHIILFAPDGTIaardlreeamKEKVTEVMT 356
Cdd:PRK03147  110 KNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKV----------VKVITGEMT 160

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 247 GRYVLVDFWASWCGPCRREIPNIKELYDKY-HDKGLDVLGVAVWDKPEDTQKAIEEMQVVWPqiinaqHIPTD------- 318
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkKKKNVEIVFVSLDRDLEEFKDYLKKMPKDWL------SVPFDddernel 74

                          90       100
                  ....*....|....*....|.
gi 2443763347 319 --LYGIQVIPHIILFAPDGTI 337
Cdd:pfam13905  75 krKYGVNAIPTLVLLDPNGEV 95

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 220 AVGQMFTDFTVEQP--DGTKVSLSDYvgKGRYVLVDFWAS-WCGPCRREIPNIKELYDKYHDKGLDVLGVAVWDKPEDTQ 296
Cdd:pfam08534   1 KAGDKAPDFTLPDAatDGNTVSLSDF--KGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2443763347 297 KAIEEMQVVWPQIINAQH---------IPTDLYGIQVIPHIILFAPDGTIAARDL 342
Cdd:pfam08534  79 RFWGKEGLPFPFLSDGNAaftkalglpIEEDASAGLRSPRYAVIDEDGKVVYLFV 133

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 234 DGTKVSLSDYVgKGRYVLVDFWASWCGPCRREIPNIKELYDKYHDKG--LDVLGVAvWDKPEDTQKA-IEEMQvVWPqii 310
Cdd:cd02964     5 DGEGVVPVSAL-EGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGknFEIVFVS-RDRSEESFNEyFSEMP-PWL--- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2443763347 311 naqHIP----------TDLYGIQVIPHIILFAPDGTIAARDLREE 345
Cdd:cd02964    79 ---AVPfedeelrellEKQFKVEGIPTLVVLKPDGDVVTTNARDE 120

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 246 KGRYVLVDFWASWCGPCRREIPNIKELYDKYHDKGLDVLGV-----AVWDKPEDTQKAIEEMQVVWPQIINAQHIPTDLY 320
Cdd:cd03012    22 RGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVhspefAFERDLANVKSAVLRYGITYPVANDNDYATWRAY 101

                          90
                  ....*....|....*..
gi 2443763347 321 GIQVIPHIILFAPDGTI 337
Cdd:cd03012   102 GNQYWPALYLIDPTGNV 118

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 2443763347 250 VLVDFWASWCGPCRREIPNIKELYDKYHDKgLDVLGVAVWDKPEDTQKaieemqvvwpqiinaqhiptdlYGIQVIPHII 329
Cdd:TIGR01068  17 VLVDFWAPWCGPCKMIAPILEELAKEYEGK-VKFVKLNVDENPDIAAK----------------------YGIRSIPTLL 73

                          90
                  ....*....|.
gi 2443763347 330 LFaPDGTIAAR 340
Cdd:TIGR01068  74 LF-KNGKEVDR 83

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443763347 227 DFTVEQPDGTKVSLSDYvgKGRYVLVDFWASWCGpcrrEIPNIK---ELYDKYHDKGLDVLGV 286
Cdd:cd00340     4 DFSVKDIDGEPVSLSKY--KGKVLLIVNVASKCG----FTPQYEgleALYEKYKDRGLVVLGF 60

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 221 VGQMFTDFTVEQPDGTKVSLSDYVGKGRYVLVDFWASWCGPCRREIPNIKELYDKYHDKGLDVLGVAVWDKPedTQKAIE 300
Cdd:cd03018     3 VGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPF--SLRAWA 80

                  ....*.
gi 2443763347 301 EMQVVW 306
Cdd:cd03018    81 EENGLT 86

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2443763347 246 KGRYVLVDFWASWCGPCRREIPNIKELydkyHDKGLDVLGVavwDKPEDTQKAI 299
Cdd:TIGR00385  62 QGKPVLLNVWASWCPPCRAEHPYLNEL----AKQGLPIVGV---DYKDDRQNAI 108

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
                  ....*....|....*....|....*....|
gi 2443763347 250 VLVDFWASWCGPCRREIPNIKELYDKYHDK 279
Cdd:pfam00085  21 VLVDFYAPWCGPCKMLAPEYEELAQEYKGN 50

thioredoxin TrxA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 251 LVDFWASWCGPCRREIPNIKELYDKYHDKgLDVLGVAVWDKPEDTQKaieemqvvwpqiinaqhiptdlYGIQVIPHIIL 330
Cdd:PRK09381   25 LVDFWAEWCGPCKMIAPILDEIADEYQGK-LTVAKLNIDQNPGTAPK----------------------YGIRGIPTLLL 81

                  ....*....
gi 2443763347 331 FApDGTIAA 339
Cdd:PRK09381   82 FK-NGEVAA 89

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 2443763347 251 LVDFWASWCGPCRREIPNIKELydKYHDKGLDVLGVAVWDKPEDTQKAIEEMQVVWPQII 310
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAEL--ALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLV 58

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 227 DFTVEQPDGTKVSLSDYvgKGRYVLVDFWaswcgP------CRREIPNIKELYDKYHDKGLDVLGVAVwDKPEDTQKAIE 300
Cdd:cd02971     4 DFTLPATDGGEVSLSDF--KGKWVVLFFY-----PkdftpvCTTELCAFRDLAEEFAKGGAEVLGVSV-DSPFSHKAWAE 75

                  .
gi 2443763347 301 E 301
Cdd:cd02971    76 K 76

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 2443763347 247 GRYVLVDFWASWCGPCRREIPNIKELYDKYHDKgLDVLGVAVwDKPEdtqkaieemqvvWPQIInaqhiptDLYGIQVIP 326
Cdd:cd02950    20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQ-VNFVMLNV-DNPK------------WLPEI-------DRYRVDGIP 78

                          90       100
                  ....*....|....*....|....*....
gi 2443763347 327 HIILFAPDGTIAAR---DLREEAMKEKVT 352
Cdd:cd02950    79 HFVFLDREGNEEGQsigLQPKQVLAQNLD 107

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443763347 221 VGQMFTDFTVE--QPDG--TKVSLSDYVGKgrYVLVDFW-ASWCGPCRREIPNIKELYDKYHDKGLDVLGVAV 288
Cdd:cd03015     1 VGKKAPDFKATavVPNGefKEISLSDYKGK--WVVLFFYpLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVST 71

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 227 DFTVEQPDGTKVSLSDYVGKGryVLVDFWaswcgP------CRREIPNIKELYDKYHDKGLDVLGVAVwDKPEDTQKAIE 300
Cdd:cd03017     5 DFTLPDQDGETVSLSDLRGKP--VVLYFY-----PkddtpgCTKEACDFRDLYEEFKALGAVVIGVSP-DSVESHAKFAE 76

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 227 DFTVEQPDGTKVSLSDYVGKGRYVLVDFWASWCGPCRREIPNIKELYDKYHDKGLDVLGVAvwdkPEDTQKAIEEMQVVW 306
Cdd:cd02970     4 DFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVG----PESPEKLEAFDKGKF 79

                  ..
gi 2443763347 307 PQ 308
Cdd:cd02970    80 LP 81

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443763347 240 LSDYVGKGRYVLVDFWASWCGPCrreipniKELyDKYhdkgldvlgvaVWDKPEdTQKAIEE----MQVVW----PQIin 311
Cdd:COG4232   313 LAEARAEGKPVFVDFTADWCVTC-------KEN-ERT-----------VFSDPE-VQAALADdvvlLKADVtdndPEI-- 370

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2443763347 312 aqhipTDL---YGIQVIPHIILFAPDGTIAAR 340
Cdd:COG4232   371 -----TALlkrFGRFGVPTYVFYDPDGEELPR 397

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 2443763347 240 LSDYVGKGRYVLVDFWASWCGPCrreipniKELyDKYhdkgldvlgvaVWDKPEdTQKAIEE----MQVVW----PQIin 311
Cdd:cd02953     4 LAQALAQGKPVFVDFTADWCVTC-------KVN-EKV-----------VFSDPE-VQAALKKdvvlLRADWtkndPEI-- 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2443763347 312 aqhipTDL---YGIQVIPHIILFAPDGtiAARDLReeamkekVTEVMTAKK 359
Cdd:cd02953    62 -----TALlkrFGVFGPPTYLFYGPGG--EPEPLR-------LPGFLTADE 98

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
                  ....*....|....*....|....*....|....*....|....
gi 2443763347 245 GKGRYVlVDFWASWCGPCRREIPNIKELYDkyhDKGLDVLGVAV 288
Cdd:cd02948    16 NKGLTV-VDVYQEWCGPCKAVVSLFKKIKN---ELGDDLLHFAT 55

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
                  ....*....|....*....|..
gi 2443763347 251 LVDFWASWCGPCRREIPNIKEL 272
Cdd:cd03004    23 LVDFYAPWCGPCQALLPELRKA 44