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Conserved domains on  [gi|388452638|ref|NP_001253434|]
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protein disulfide-isomerase TMX3 precursor [Macaca mulatta]

Protein Classification

protein disulfide isomerase family protein( domain architecture ID 12930571)

protein disulfide isomerase (PDI) family protein belongs to the thioredoxin superfamily, and may act as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 27-130 4.78e-71

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


:

Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 219.63  E-value: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  27 FVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK 106
Cdd:cd03000    1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLK 80

                         90       100
                 ....*....|....*....|....
gi 388452638 107 GDLAYNYRGPRTKDDIIEFAHRVS 130
Cdd:cd03000   81 GDLAYNYRGPRTKDDIVEFANRVA 104
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 29-346 4.92e-41

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).


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.14  E-value: 4.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   29 EDLDESFKENrndDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-- 106
Cdd:TIGR01130   9 DNFDDFIKSH---EFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRng 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  107 GDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHR--VFFVYIGGESPLKEKYIDAASELIVYTYFFSAS 184
Cdd:TIGR01130  86 EDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDvvVIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  185 --EEVVPEYVTLKEMPAVLVFKDE--TYFVYD---EYEDGDLSSWINRE--RFQNYLAMDGFLLYELGDTGKLVALAVID 255
Cdd:TIGR01130 166 sdVAAFAKLGAFPDSVVLFKPKDEdeKFSKVDgemDTDVSDLEKFIRAEslPLVGEFTQETAAKYFESGPLVVLYYNVDE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  256 EKNTSVEharLKSIIQEVARDYRDLFHRdFQFGHMDGNDYI-NTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQ 334
Cdd:TIGR01130 246 SLDPFEE---LRNRFLEAAKKFRGKFVN-FAVADEEDFGRElEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEA 321

                         330
                  ....*....|..
gi 388452638  335 FINNILDGTVEA 346
Cdd:TIGR01130 322 FVKDFLDGKLKP 333
 
Name Accession Description Interval E-value
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 27-130 4.78e-71

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 219.63  E-value: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  27 FVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK 106
Cdd:cd03000    1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLK 80

                         90       100
                 ....*....|....*....|....
gi 388452638 107 GDLAYNYRGPRTKDDIIEFAHRVS 130
Cdd:cd03000   81 GDLAYNYRGPRTKDDIVEFANRVA 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 29-346 4.92e-41

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).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.14  E-value: 4.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   29 EDLDESFKENrndDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-- 106
Cdd:TIGR01130   9 DNFDDFIKSH---EFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRng 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  107 GDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHR--VFFVYIGGESPLKEKYIDAASELIVYTYFFSAS 184
Cdd:TIGR01130  86 EDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDvvVIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  185 --EEVVPEYVTLKEMPAVLVFKDE--TYFVYD---EYEDGDLSSWINRE--RFQNYLAMDGFLLYELGDTGKLVALAVID 255
Cdd:TIGR01130 166 sdVAAFAKLGAFPDSVVLFKPKDEdeKFSKVDgemDTDVSDLEKFIRAEslPLVGEFTQETAAKYFESGPLVVLYYNVDE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  256 EKNTSVEharLKSIIQEVARDYRDLFHRdFQFGHMDGNDYI-NTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQ 334
Cdd:TIGR01130 246 SLDPFEE---LRNRFLEAAKKFRGKFVN-FAVADEEDFGRElEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEA 321

                         330
                  ....*....|..
gi 388452638  335 FINNILDGTVEA 346
Cdd:TIGR01130 322 FVKDFLDGKLKP 333
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 32-126 1.39e-33

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 122.01  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   32 DESFKENRNDD-IWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGsPVKVGKMDATSYSSIASEFGVRGYPTIKLL-KGDL 109
Cdd:TIGR01126   3 ASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDP-KIVLAKVDATAEKDLASRFGVSGFPTIKFFpKGSK 81

                          90
                  ....*....|....*..
gi 388452638  110 AYNYRGPRTKDDIIEFA 126
Cdd:TIGR01126  82 PVDYEGGRDLEAIVEFV 98
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 24-345 1.41e-30

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 123.32  E-value: 1.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  24 CKGFVEDLDESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPT 101
Cdd:PTZ00102  30 ISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 102 IKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFV--YIGGESPLKEKYIDAAS---ELIV 176
Cdd:PTZ00102 110 IKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIKLIAKKIFVAFYgeYTSKDSELYKKFEEVADkhrEHAK 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 177 YTYFFSASEEVVpeYVTLKEMPAVLVFKDETYFVYDEY---EDGDLSSWINRERFQNYLAMDGFLLYELGdtgklvalav 253
Cdd:PTZ00102 190 FFVKKHEGKNKI--YVLHKDEEGVELFMGKTKEELEEFvstESFPLFAEINAENYRRYISSGKDLVWFCG---------- 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 254 ideknTSVEHARLKSIIQEVARDYRDLFHrdFQFGHMD--GNDYINTLLMDELtvPTVVVlNTSNQQYFLLDRQIK--NV 329
Cdd:PTZ00102 258 -----TTEDYDKYKSVVRKVARKLREKYA--FVWLDTEqfGSHAKEHLLIEEF--PGLAY-QSPAGRYLLPPAKESfdSV 327

                        330
                 ....*....|....*.
gi 388452638 330 EDMVQFINNILDGTVE 345
Cdd:PTZ00102 328 EALIEFFKDVEAGKVE 343
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 32-125 4.76e-26

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.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 101.54  E-value: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   32 DESFKE--NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKsigSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:pfam00085   7 DANFDEvvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK---GNVVFAKVDVDENPDLASKYGVRGYPTLIFFKnGQ 83

                          90
                  ....*....|....*..
gi 388452638  109 LAYNYRGPRTKDDIIEF 125
Cdd:pfam00085  84 PVDDYVGARPKDALAAF 100
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
160-338 2.19e-24

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 99.36  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  160 ESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEmPAVLVFKDET----YFVYDEYEDGDLSSWINRERFQNYLAMD 235
Cdd:pfam13848   5 DSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKE-PAILLFRKFDeetvHYPGDSINFEDLKKFIQKNCLPLVREFT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  236 GFLLYELGDTGKLVALAVIDEKNtSVEHARLKSIIQEVARDYRDLFHrdFQFGHMDGND-YINTLLMDELTVPTVVVLNT 314
Cdd:pfam13848  84 PENAEELFEEGIPPLLLLFLKKD-DESTEEFKKALEKVAKKFRGKIN--FALVDAKSFGrPLEYFGLSESDLPVIVIVDS 160

                         170       180
                  ....*....|....*....|....
gi 388452638  315 SNQQYFLLDRQIKNVEDMVQFINN 338
Cdd:pfam13848 161 FSHMYKYFPSDEFSPESLKEFIND 184
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 32-125 4.88e-18

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 79.09  E-value: 4.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  32 DESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMksiGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:COG3118    7 DENFEEEvlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY---GGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKdGQ 83

                         90
                 ....*....|....*..
gi 388452638 109 LAYNYRGPRTKDDIIEF 125
Cdd:COG3118   84 PVDRFVGALPKEQLREF 100
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 44-139 1.14e-17

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 81.60  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  44 WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYR-GPRTKDDI 122
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEgGDRSTEKL 131

                         90
                 ....*....|....*...
gi 388452638 123 IEFA-HRVSGALIRPLPS 139
Cdd:PTZ00443 132 AAFAlGDFKKALGAPVPA 149
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 257-340 7.89e-04

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 38.79  E-value: 7.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 257 KNTSVEHARLKSIIQEVARDYRDLFHrdfqFGHMDGNDY---INTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMV 333
Cdd:cd02982   21 NKDDSESEELRERFKEVAKKFKGKLL----FVVVDADDFgrhLEYFGLKEEDLPVIAIINLSDGKKYLMPEEELTAESLE 96


                 ....*..
gi 388452638 334 QFINNIL 340
Cdd:cd02982   97 EFVEDFL 103
 
Name Accession Description Interval E-value
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 27-130 4.78e-71

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 219.63  E-value: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  27 FVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK 106
Cdd:cd03000    1 LVLDLDDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLK 80

                         90       100
                 ....*....|....*....|....
gi 388452638 107 GDLAYNYRGPRTKDDIIEFAHRVS 130
Cdd:cd03000   81 GDLAYNYRGPRTKDDIVEFANRVA 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 29-346 4.92e-41

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).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.14  E-value: 4.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   29 EDLDESFKENrndDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-- 106
Cdd:TIGR01130   9 DNFDDFIKSH---EFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRng 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  107 GDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHR--VFFVYIGGESPLKEKYIDAASELIVYTYFFSAS 184
Cdd:TIGR01130  86 EDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDvvVIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  185 --EEVVPEYVTLKEMPAVLVFKDE--TYFVYD---EYEDGDLSSWINRE--RFQNYLAMDGFLLYELGDTGKLVALAVID 255
Cdd:TIGR01130 166 sdVAAFAKLGAFPDSVVLFKPKDEdeKFSKVDgemDTDVSDLEKFIRAEslPLVGEFTQETAAKYFESGPLVVLYYNVDE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  256 EKNTSVEharLKSIIQEVARDYRDLFHRdFQFGHMDGNDYI-NTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQ 334
Cdd:TIGR01130 246 SLDPFEE---LRNRFLEAAKKFRGKFVN-FAVADEEDFGRElEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEA 321

                         330
                  ....*....|..
gi 388452638  335 FINNILDGTVEA 346
Cdd:TIGR01130 322 FVKDFLDGKLKP 333
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 32-126 7.17e-35

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.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 125.42  E-value: 7.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  32 DESFKE-NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSiGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKG--D 108
Cdd:cd02961    5 DDNFDElVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG-DGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNgsK 83

                         90
                 ....*....|....*...
gi 388452638 109 LAYNYRGPRTKDDIIEFA 126
Cdd:cd02961   84 EPVKYEGPRTLESLVEFI 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 32-126 1.39e-33

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 122.01  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   32 DESFKENRNDD-IWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGsPVKVGKMDATSYSSIASEFGVRGYPTIKLL-KGDL 109
Cdd:TIGR01126   3 ASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDP-KIVLAKVDATAEKDLASRFGVSGFPTIKFFpKGSK 81

                          90
                  ....*....|....*..
gi 388452638  110 AYNYRGPRTKDDIIEFA 126
Cdd:TIGR01126  82 PVDYEGGRDLEAIVEFV 98
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 28-126 1.89e-32

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.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 118.93  E-value: 1.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  28 VEDLDESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLL 105
Cdd:cd03001    3 VELTDSNFDKKvlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI---VKVGAVDADVHQSLAQQYGVRGFPTIKVF 79

                         90       100
                 ....*....|....*....|...
gi 388452638 106 KGDL--AYNYRGPRTKDDIIEFA 126
Cdd:cd03001   80 GAGKnsPQDYQGGRTAKAIVSAA 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 24-345 1.41e-30

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 123.32  E-value: 1.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  24 CKGFVEDLDESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPT 101
Cdd:PTZ00102  30 ISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 102 IKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFV--YIGGESPLKEKYIDAAS---ELIV 176
Cdd:PTZ00102 110 IKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIKLIAKKIFVAFYgeYTSKDSELYKKFEEVADkhrEHAK 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 177 YTYFFSASEEVVpeYVTLKEMPAVLVFKDETYFVYDEY---EDGDLSSWINRERFQNYLAMDGFLLYELGdtgklvalav 253
Cdd:PTZ00102 190 FFVKKHEGKNKI--YVLHKDEEGVELFMGKTKEELEEFvstESFPLFAEINAENYRRYISSGKDLVWFCG---------- 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 254 ideknTSVEHARLKSIIQEVARDYRDLFHrdFQFGHMD--GNDYINTLLMDELtvPTVVVlNTSNQQYFLLDRQIK--NV 329
Cdd:PTZ00102 258 -----TTEDYDKYKSVVRKVARKLREKYA--FVWLDTEqfGSHAKEHLLIEEF--PGLAY-QSPAGRYLLPPAKESfdSV 327

                        330
                 ....*....|....*.
gi 388452638 330 EDMVQFINNILDGTVE 345
Cdd:PTZ00102 328 EALIEFFKDVEAGKVE 343
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 33-125 2.19e-28

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.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 107.76  E-value: 2.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  33 ESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GDLAY 111
Cdd:cd03005    8 DNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKdGEKVD 87

                         90
                 ....*....|....
gi 388452638 112 NYRGPRTKDDIIEF 125
Cdd:cd03005   88 KYKGTRDLDSLKEF 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 32-125 4.76e-26

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.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 101.54  E-value: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   32 DESFKE--NRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKsigSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:pfam00085   7 DANFDEvvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK---GNVVFAKVDVDENPDLASKYGVRGYPTLIFFKnGQ 83

                          90
                  ....*....|....*..
gi 388452638  109 LAYNYRGPRTKDDIIEF 125
Cdd:pfam00085  84 PVDDYVGARPKDALAAF 100
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
160-338 2.19e-24

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 99.36  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  160 ESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEmPAVLVFKDET----YFVYDEYEDGDLSSWINRERFQNYLAMD 235
Cdd:pfam13848   5 DSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKE-PAILLFRKFDeetvHYPGDSINFEDLKKFIQKNCLPLVREFT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  236 GFLLYELGDTGKLVALAVIDEKNtSVEHARLKSIIQEVARDYRDLFHrdFQFGHMDGND-YINTLLMDELTVPTVVVLNT 314
Cdd:pfam13848  84 PENAEELFEEGIPPLLLLFLKKD-DESTEEFKKALEKVAKKFRGKIN--FALVDAKSFGrPLEYFGLSESDLPVIVIVDS 160

                         170       180
                  ....*....|....*....|....
gi 388452638  315 SNQQYFLLDRQIKNVEDMVQFINN 338
Cdd:pfam13848 161 FSHMYKYFPSDEFSPESLKEFIND 184
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 45-125 2.56e-23

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.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 93.78  E-value: 2.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVkVGKMDATSySSIASEFGVRGYPTIKLLKGDLAYN---YRGPRTKDD 121
Cdd:cd02995   22 LVEFYAPWCGHCKALAPIYEELAEKLKGDDNVV-IAKMDATA-NDVPSEFVVDGFPTILFFPAGDKSNpikYEGDRTLED 99


                 ....
gi 388452638 122 IIEF 125
Cdd:cd02995  100 LIKF 103
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 28-125 3.73e-22

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.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 90.77  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  28 VEDL-DESFKENRNDDIW--LVDFYAPWCGHCKKLEPIWNEVGLEMKSiGSPVKVGKMDAT-SYSSIASEFGVRGYPTIK 103
Cdd:cd02998    2 VVELtDSNFDKVVGDDKKdvLVEFYAPWCGHCKNLAPEYEKLAAVFAN-EDDVVIAKVDADeANKDLAKKYGVSGFPTLK 80

                         90       100
                 ....*....|....*....|....
gi 388452638 104 LL-KGDLA-YNYRGPRTKDDIIEF 125
Cdd:cd02998   81 FFpKGSTEpVKYEGGRDLEDLVKF 104
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 32-125 1.94e-21

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 88.91  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  32 DESFKENRNDDI-WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGkMDATS--YSSIASEFGVRGYPTIKLL-KG 107
Cdd:cd02997    7 DEDFRKFLKKEKhVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAA-VDCTKpeHDALKEEYNVKGFPTFKYFeNG 85

                         90
                 ....*....|....*...
gi 388452638 108 DLAYNYRGPRTKDDIIEF 125
Cdd:cd02997   86 KFVEKYEGERTAEDIIEF 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 45-125 3.35e-21

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).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 95.51  E-value: 3.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSsiASEFGVRGYPTIKLLKGDLAYN---YRGPRTKDD 121
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATAND--VPPFEVEGFPTIKFVPAGKKSEpvpYDGDRTLED 445


                  ....
gi 388452638  122 IIEF 125
Cdd:TIGR01130 446 FSKF 449
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 28-126 9.61e-20

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.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 83.88  E-value: 9.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  28 VEDLD-ESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKL 104
Cdd:cd03004    3 VITLTpEDFPELvlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGK---VKVGSVDCQKYESLCQQANIRAYPTIRL 79

                         90       100
                 ....*....|....*....|....*
gi 388452638 105 LKGDLA--YNYRG-PRTKDDIIEFA 126
Cdd:cd03004   80 YPGNASkyHSYNGwHRDADSILEFI 104
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 26-125 1.97e-19

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.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 83.20  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  26 GFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGVRGYPTIKLL 105
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLG--INVAKVDVTQEPGLSGRFFVTALPTIYHA 78

                         90       100
                 ....*....|....*....|
gi 388452638 106 KGDLAYNYRGPRTKDDIIEF 125
Cdd:cd02994   79 KDGVFRRYQGPRDKEDLISF 98
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 32-125 4.88e-18

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 79.09  E-value: 4.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  32 DESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMksiGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:COG3118    7 DENFEEEvlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY---GGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKdGQ 83

                         90
                 ....*....|....*..
gi 388452638 109 LAYNYRGPRTKDDIIEF 125
Cdd:COG3118   84 PVDRFVGALPKEQLREF 100
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 44-139 1.14e-17

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 81.60  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  44 WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYR-GPRTKDDI 122
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEgGDRSTEKL 131

                         90
                 ....*....|....*...
gi 388452638 123 IEFA-HRVSGALIRPLPS 139
Cdd:PTZ00443 132 AAFAlGDFKKALGAPVPA 149
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 32-108 1.91e-16

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]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 74.63  E-value: 1.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 388452638   32 DESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMksiGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGD 108
Cdd:TIGR01068   3 DANFDETiaSSDKPVLVDFWAPWCGPCKMIAPILEELAKEY---EGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 45-126 2.21e-15

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.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 72.01  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  45 LVDFYAPWCGHCKKLEPIWNEVGlemKSIGSPVKVGKM--DATSYSSIASEFGVRGYPTIKLLK------GDLAYNYRGP 116
Cdd:cd03002   22 LVEFYAPWCGHCKNLKPEYAKAA---KELDGLVQVAAVdcDEDKNKPLCGKYGVQGFPTLKVFRppkkasKHAVEDYNGE 98

                         90
                 ....*....|
gi 388452638 117 RTKDDIIEFA 126
Cdd:cd03002   99 RSAKAIVDFV 108
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 22-125 4.87e-15

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 77.10  E-value: 4.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  22 VVCKGFVEDLDESFKenrndDIwLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSpVKVGKMDATSYSSIASEFGVRGYPT 101
Cdd:PTZ00102 362 VVGNTFEEIVFKSDK-----DV-LLEIYAPWCGHCKNLEPVYNELGEKYKDNDS-IIVAKMNGTANETPLEEFSWSAFPT 434

                         90       100
                 ....*....|....*....|....*.
gi 388452638 102 IKLLK--GDLAYNYRGPRTKDDIIEF 125
Cdd:PTZ00102 435 ILFVKagERTPIPYEGERTVEGFKEF 460
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 45-125 3.34e-14

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.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 67.97  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKSigspVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GDLAYNYRGPRTKDDII 123
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDVDENPELAEEYGVRSIPTFLFFKnGKEVDRVVGADPKEELE 89


                 ..
gi 388452638 124 EF 125
Cdd:cd02947   90 EF 91
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 40-125 1.45e-11

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 60.84  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  40 NDDIWLVDFYAPWCGHCKKLEPIWNEvgleMKSIGSPVKVGKMDATS-YSSIASEFGVRGYPTIKLLKGDLAYNYRGPRT 118
Cdd:cd02999   17 REDYTAVLFYASWCPFSASFRPHFNA----LSSMFPQIRHLAIEESSiKPSLLSRYGVVGFPTILLFNSTPRVRYNGTRT 92


                 ....*..
gi 388452638 119 KDDIIEF 125
Cdd:cd02999   93 LDSLAAF 99
trxA PRK09381
thioredoxin TrxA;
32-125 2.09e-11

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 60.46  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  32 DESFKEN--RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKsigSPVKVGKMDATSYSSIASEFGVRGYPTIKLLK-GD 108
Cdd:PRK09381  10 DDSFDTDvlKADGAILVDFWAEWCGPCKMIAPILDEIADEYQ---GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKnGE 86

                         90
                 ....*....|....*..
gi 388452638 109 LAYNYRGPRTKDDIIEF 125
Cdd:PRK09381  87 VAATKVGALSKGQLKEF 103
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 42-126 7.71e-11

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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 58.69  E-value: 7.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  42 DIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIgspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAY-NYRGPRTKD 120
Cdd:cd03003   19 EIWFVNFYSPRCSHCHDLAPTWREFAKEMDGV---IRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPeKYYGDRSKE 95


                 ....*.
gi 388452638 121 DIIEFA 126
Cdd:cd03003   96 SLVKFA 101
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 37-122 1.16e-10

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.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 58.62  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  37 ENRNDDiWLVDFYAPWCGHCKKLEPIWNEVGLEMKsiGSPVKVGKMDATSYSSIAS--EFGVRGYPTIKLLKGDLAYNYR 114
Cdd:cd02993   18 ERRNQS-TLVVLYAPWCPFCQAMEASYEELAEKLA--GSNVKVAKFNADGEQREFAkeELQLKSFPTILFFPKNSRQPIK 94


                 ....*...
gi 388452638 115 GPRTKDDI 122
Cdd:cd02993   95 YPSEQRDV 102
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 44-135 2.07e-10

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 57.66  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  44 WLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIA--SEFGVRGYPTIKLLKGDLAYNYRGPRTKDD 121
Cdd:cd02992   22 WLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVAlcRDFGVTGYPTLRYFPPFSKEATDGLKQEGP 101

                         90
                 ....*....|....
gi 388452638 122 IIEfAHRVSGALIR 135
Cdd:cd02992  102 ERD-VNELREALIL 114
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 39-125 5.08e-09

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 53.55  E-value: 5.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  39 RNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSI---GSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYN--Y 113
Cdd:cd02996   16 QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpdAGKVVWGKVDCDKESDIADRYRINKYPTLKLFRNGMMMKreY 95

                         90
                 ....*....|..
gi 388452638 114 RGPRTKDDIIEF 125
Cdd:cd02996   96 RGQRSVEALAEF 107
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 40-125 2.76e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.38  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  40 NDDIWLVDFYAPWCGHCKKLEPIWNEV-----GLEMKSI---GSPVKVGK------MDATSY----SSIASEFGVRGYPT 101
Cdd:COG0526   27 KGKPVLVNFWATWCPPCRAEMPVLKELaeeygGVVFVGVdvdENPEAVKAflkelgLPYPVLldpdGELAKAYGVRGIPT 106

                         90       100
                 ....*....|....*....|....*.
gi 388452638 102 IKLL--KGDLAYNYRGPRTKDDIIEF 125
Cdd:COG0526  107 TVLIdkDGKIVARHVGPLSPEELEEA 132
PRK10996 PRK10996
thioredoxin 2; Provisional
 18-106 3.56e-08

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 51.99  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  18 LLDMVVCKGFVEDLDESFKenrNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVgkmDATSYSSIASEFGVR 97
Cdd:PRK10996  32 LFDGEVINATGETLDKLLQ---DDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKV---NTEAERELSARFRIR 105


                 ....*....
gi 388452638  98 GYPTIKLLK 106
Cdd:PRK10996 106 SIPTIMIFK 114
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 45-113 1.81e-07

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.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 48.08  E-value: 1.81e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388452638  45 LVDFYAPWCGHCKKLEPIWNEVGLEMKsigsPVKVGKMDATSYSSI---ASEFGVRGYPTIKLLKGDLAYNY 113
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNK----GVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVKY 68
PTZ00051 PTZ00051
thioredoxin; Provisional
 41-106 1.14e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 46.79  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388452638  41 DDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSigspVKVGKMDATSYSSIASEFGVRGYPTIKLLK 106
Cdd:PTZ00051  18 NELVIVDFYAEWCGPCKRIAPFYEECSKEYTK----MVFVKVDVDELSEVAEKENITSMPTFKVFK 79
PLN02309 PLN02309
5'-adenylylsulfate reductase
 37-105 2.81e-06

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 49.40  E-value: 2.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388452638  37 ENRnDDIWLVDFYAPWCGHCKKLEPIWNEvgLEMKSIGSPVKVGKM--DATSYSSIASEFGVRGYPTIKLL 105
Cdd:PLN02309 362 ENR-KEPWLVVLYAPWCPFCQAMEASYEE--LAEKLAGSGVKVAKFraDGDQKEFAKQELQLGSFPTILLF 429
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 37-122 4.92e-06

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 48.86  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   37 ENRNDDiWLVDFYAPWCGHCKKLEPIWNEvgLEMKSIGSPVKVGKM--DATSYSSIASEFGVRGYPTIKLLKGDLAYNYR 114
Cdd:TIGR00424 368 EERKEA-WLVVLYAPWCPFCQAMEASYLE--LAEKLAGSGVKVAKFraDGDQKEFAKQELQLGSFPTILFFPKHSSRPIK 444


                  ....*...
gi 388452638  115 GPRTKDDI 122
Cdd:TIGR00424 445 YPSEKRDV 452
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 27-123 2.03e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 44.51  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  27 FVEDLDESFKENRNddIwLVDFYAPWCGHCKKLEpiwNEVgLEMKSIGSPVK----VGKMDA-------------TSYSS 89
Cdd:COG2143   29 LEEDLALAKAEGKP--I-LLFFESDWCPYCKKLH---KEV-FSDPEVAAYLKenfvVVQLDAegdkevtdfdgetLTEKE 101

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 388452638  90 IASEFGVRGYPTIKLL--KGDLAYNYRGPRTKDDII 123
Cdd:COG2143  102 LARKYGVRGTPTLVFFdaEGKEIARIPGYLKPETFL 137
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 31-129 3.80e-05

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 42.75  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  31 LDESFKEnrnddIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLA 110
Cdd:cd02963   19 VPKSFKK-----PYLIKITSDWCFSCIHIEPVWKEVIQELEPLG--VGIATVNAGHERRLARKLGAHSVPAIVGIINGQV 91

                         90       100
                 ....*....|....*....|
gi 388452638 111 YNYR-GPRTKDDIIEFAHRV 129
Cdd:cd02963   92 TFYHdSSFTKQHVVDFVRKL 111
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 31-107 4.27e-05

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.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 43.52  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  31 LDESFKENrNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGspVKVGKMDATSYSSIASEFGV------RGYPTIKL 104
Cdd:cd02962   38 LEEELERD-KRVTWLVEFFTTWSPECVNFAPVFAELSLKYNNNN--LKFGKIDIGRFPNVAEKFRVstsplsKQLPTIIL 114


                 ...
gi 388452638 105 LKG 107
Cdd:cd02962  115 FQG 117
Calsequestrin pfam01216
Calsequestrin;
68-344 5.34e-05

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 45.01  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638   68 LEMKSIGspvkVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQ---QMFE 144
Cdd:pfam01216  63 LEDKDIG----FGLVDAEKDAALAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGElelQAFE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  145 HMQKRHRVFFVYIGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLK--EMPAVLVFKDETYFVYDE-YEDGDLSS 221
Cdd:pfam01216 139 NIEDEIKLIGFFKSEDSEHYKAFEDAAEEFHPYIKFFATFDKGVAKKLSLKlnEIDFYEAFMDEPIAIPDKpNSEEEIVE 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  222 WINRERFQNYLAMDGFLLYELG----DTGKLVALAvideKNTSVEHARLKSIIQEVARDYRDlfHRDFQFGHMDGND--- 294
Cdd:pfam01216 219 FVEEHQRPTLRKLKPEDMFETWeddlDGIHIVAFA----EEADPDGFEFLEILKAVAQDNTD--NPDLSIIWIDPDDfpl 292

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 388452638  295 ---YINTLLMDELTVPTVVVLNTSNQQYFLL----DRQIKNVEDMVQFINNILDGTV 344
Cdd:pfam01216 293 lvaYWEKTFDIDLFAPQIGVVNVTDADSVWMeiddDDDLPSAEELEDWIEDVLEGEI 349
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 45-107 5.99e-05

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 41.87  E-value: 5.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 388452638  45 LVDFYAPWCGHCKKLEPIWNevGLEMKSIGSPVkVGKMDATSYSSIASEFGVRGYPTIKLLKG 107
Cdd:cd02956   16 VVDFWAPRSPPSKELLPLLE--RLAEEYQGQFV-LAKVNCDAQPQIAQQFGVQALPTVYLFAA 75
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 40-125 5.12e-04

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.


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 39.02  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  40 NDDIWLVDFYAPWCGHCKKLEPIWNEVgleMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKG-DLAYNYRGPRT 118
Cdd:cd02949   12 SDRLILVLYTSPTCGPCRTLKPILNKV---IDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDkELVKEISGVKM 88


                 ....*..
gi 388452638 119 KDDIIEF 125
Cdd:cd02949   89 KSEYREF 95
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 257-340 7.89e-04

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 38.79  E-value: 7.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638 257 KNTSVEHARLKSIIQEVARDYRDLFHrdfqFGHMDGNDY---INTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMV 333
Cdd:cd02982   21 NKDDSESEELRERFKEVAKKFKGKLL----FVVVDADDFgrhLEYFGLKEEDLPVIAIINLSDGKKYLMPEEELTAESLE 96


                 ....*..
gi 388452638 334 QFINNIL 340
Cdd:cd02982   97 EFVEDFL 103
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
45-108 2.96e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.02  E-value: 2.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388452638   45 LVDFYAPWCGHCKKLEPI---WNEVGLEMKSIGSPV----------KVGKMDATSYSSIASEFGVRGYPTIKLLKGD 108
Cdd:pfam13098   8 LVVFTDPDCPYCKKLKKElleDPDVTVYLGPNFVFIavniwcakevAKAFTDILENKELGRKYGVRGTPTIVFFDGK 84
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 45-108 7.82e-03

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 36.51  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388452638  45 LVDFYAPWCGHCKKLEPI-------WNEVGLEMKSiGSPVKVGK-MDATSY---------SSIASEFGVRGYPTIKLLKG 107
Cdd:cd03011   24 LVYFWATWCPVCRFTSPTvnqlaadYPVVSVALRS-GDDGAVARfMQKKGYgfpvindpdGVISARWGVSVTPAIVIVDP 102


                 .
gi 388452638 108 D 108
Cdd:cd03011  103 G 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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