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Conserved domains on  [gi|158958335|sp|Q6ZRP7|]
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RecName: Full=Sulfhydryl oxidase 2; AltName: Full=Neuroblastoma-derived sulfhydryl oxidase; AltName: Full=Quiescin Q6-like protein 1; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
 318-421 2.74e-59

Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine dinucleotide (FAD) binding domain found in Quiescin sulfhydryl oxidases (QSOX) (EC:1.8.3.2). QSOX is a multi-domain disulfide catalyst that is localized primarily to the Golgi apparatus and secreted fluids and has attracted attention due to its over-production in tumors. Structural studies indicate that the closure of the Trx1 domain over the FAD-binding site may enhance the active-site chemistry for disulfide formation.


:

Pssm-ID: 465728  Cd Length: 104  Bit Score: 194.78  E-value: 2.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  318 DKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDL 397
Cdd:pfam18371   1 DRSKVYMADLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPETKISYSALLDA 80

                          90       100
                  ....*....|....*....|....
gi 158958335  398 VNNKMRISGIFLTNHIKWVGCQGS 421
Cdd:pfam18371  81 LDNKKEAPGAVLPEEVRWVGCQGS 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 61-174 2.20e-57

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: 189.79  E-value: 2.20e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  61 DAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYP 140
Cdd:cd02992    1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 158958335 141 TFRYFKAFTKEFTTGENFKGPDRELRTVRQTMID 174
Cdd:cd02992   81 TLRYFPPFSKEATDGLKQEGPERDVNELREALIL 114
QSOX_Trx1 super family cl39497
QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an ...
 185-292 6.20e-28

QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an oxidoreductase present in Homo sapiens capable of both generating and transferring disulfide modules within a single polypeptide. The domain is thioredoxin-like, hence referred to as Trx1 domain. Trx1 domain has a di-cysteine motif (Cys-X-X-Cys) which is related to the redox-active domains of protein disulfide isomerase. The Trx1 domain is responsible for intramolecular disulfide transfer through the di-cysteine motif.


The actual alignment was detected with superfamily member pfam18108:

Pssm-ID: 465653  Cd Length: 108  Bit Score: 108.44  E-value: 6.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  185 PPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIY 264
Cdd:pfam18108   1 PPACPPLQPAHSSEIDEFFQTNNVEYLALIFEANDSYVGREVILDLAQHDNVAVRRVLNTEAMLVKKLGVTVFPSCYLLY 80

                          90       100
                  ....*....|....*....|....*...
gi 158958335  265 PNGSHGLINVVKPLRAFFSSYLKSLPDV 292
Cdd:pfam18108  81 RNGSAIRLPVGGETRFFYRLALQRLPGL 108
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
 430-531 9.91e-27

Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial proteins. Erv1p of Saccharomyces cerevisiae mitochondria is required for the maturation of Fe/S proteins in the cytosol. The ALR (augmenter of liver regeneration) represents a mammalian orthologue of yeast Erv1p. Both Erv1p and full-length ALR are located in the mitochondrial intermembrane an d it thought to operate downstream of the mitochondrial ABC transporter.


:

Pssm-ID: 461423  Cd Length: 93  Bit Score: 104.24  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  430 CSLWKLFHTLTVEASTHPDAlvgtgfedDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHN 509
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEKPTE--------EQQKDMKAFLDLFSHFYPCGECAEHFQKYLAKNPPQVSSRDALSLWLCEAHN 72

                          90       100
                  ....*....|....*....|..
gi 158958335  510 MVNGRLAGHLSEDPRFpKLQWP 531
Cdd:pfam04777  73 EVNERLGKPEFDCSKV-KERWP 93
 
Name Accession Description Interval E-value
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
 318-421 2.74e-59

Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine dinucleotide (FAD) binding domain found in Quiescin sulfhydryl oxidases (QSOX) (EC:1.8.3.2). QSOX is a multi-domain disulfide catalyst that is localized primarily to the Golgi apparatus and secreted fluids and has attracted attention due to its over-production in tumors. Structural studies indicate that the closure of the Trx1 domain over the FAD-binding site may enhance the active-site chemistry for disulfide formation.


Pssm-ID: 465728  Cd Length: 104  Bit Score: 194.78  E-value: 2.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  318 DKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDL 397
Cdd:pfam18371   1 DRSKVYMADLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPETKISYSALLDA 80

                          90       100
                  ....*....|....*....|....
gi 158958335  398 VNNKMRISGIFLTNHIKWVGCQGS 421
Cdd:pfam18371  81 LDNKKEAPGAVLPEEVRWVGCQGS 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 61-174 2.20e-57

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: 189.79  E-value: 2.20e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  61 DAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYP 140
Cdd:cd02992    1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 158958335 141 TFRYFKAFTKEFTTGENFKGPDRELRTVRQTMID 174
Cdd:cd02992   81 TLRYFPPFSKEATDGLKQEGPERDVNELREALIL 114
QSOX_Trx1 pfam18108
QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an ...
 185-292 6.20e-28

QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an oxidoreductase present in Homo sapiens capable of both generating and transferring disulfide modules within a single polypeptide. The domain is thioredoxin-like, hence referred to as Trx1 domain. Trx1 domain has a di-cysteine motif (Cys-X-X-Cys) which is related to the redox-active domains of protein disulfide isomerase. The Trx1 domain is responsible for intramolecular disulfide transfer through the di-cysteine motif.


Pssm-ID: 465653  Cd Length: 108  Bit Score: 108.44  E-value: 6.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  185 PPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIY 264
Cdd:pfam18108   1 PPACPPLQPAHSSEIDEFFQTNNVEYLALIFEANDSYVGREVILDLAQHDNVAVRRVLNTEAMLVKKLGVTVFPSCYLLY 80

                          90       100
                  ....*....|....*....|....*...
gi 158958335  265 PNGSHGLINVVKPLRAFFSSYLKSLPDV 292
Cdd:pfam18108  81 RNGSAIRLPVGGETRFFYRLALQRLPGL 108
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
 430-531 9.91e-27

Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial proteins. Erv1p of Saccharomyces cerevisiae mitochondria is required for the maturation of Fe/S proteins in the cytosol. The ALR (augmenter of liver regeneration) represents a mammalian orthologue of yeast Erv1p. Both Erv1p and full-length ALR are located in the mitochondrial intermembrane an d it thought to operate downstream of the mitochondrial ABC transporter.


Pssm-ID: 461423  Cd Length: 93  Bit Score: 104.24  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  430 CSLWKLFHTLTVEASTHPDAlvgtgfedDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHN 509
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEKPTE--------EQQKDMKAFLDLFSHFYPCGECAEHFQKYLAKNPPQVSSRDALSLWLCEAHN 72

                          90       100
                  ....*....|....*....|..
gi 158958335  510 MVNGRLAGHLSEDPRFpKLQWP 531
Cdd:pfam04777  73 EVNERLGKPEFDCSKV-KERWP 93
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 63-146 3.63e-11

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: 60.32  E-value: 3.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335   63 VWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDwasAIRVAALDCMEekNQAVCHDYDIHFYPTF 142
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDE--NPDLASKYGVRGYPTL 76


                  ....
gi 158958335  143 RYFK 146
Cdd:pfam00085  77 IFFK 80
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 83-146 4.24e-09

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: 59.30  E-value: 4.24e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335   83 LVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKnqAVCHDYDIHFYPTFRYFK 146
Cdd:TIGR01130  22 LVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEK--DLAQKYGVSGYPTLKIFR 83
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 60-155 2.34e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 57.07  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  60 EDAVWVLDSGSVRGATANSSAAwLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAvcHDYDIHFY 139
Cdd:PTZ00102  31 SEHVTVLTDSTFDKFITENEIV-LVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELA--QEFGVRGY 107

                         90
                 ....*....|....*.
gi 158958335 140 PTFRYFKAFTKEFTTG 155
Cdd:PTZ00102 108 PTIKFFNKGNPVNYSG 123
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 83-146 6.29e-06

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: 45.20  E-value: 6.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335  83 LVQFYSSWCGHCIGYAPTWRALAgdvRDWASAIRVAALDCmeEKNQAVCHDYDIHFYPTFRYFK 146
Cdd:COG3118   22 LVDFWAPWCGPCKMLAPVLEELA---AEYGGKVKFVKVDV--DENPELAAQFGVRSIPTLLLFK 80
ERV1 COG5054
Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins ...
 431-515 5.14e-05

Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227387  Cd Length: 181  Bit Score: 44.48  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335 431 SLWKLFHTLtveASTHPDALVGTGFEDdpqavlqtMRRYVHTF---FGCKECGEHFEEMAKESMDSVKTPDQAILWLWKK 507
Cdd:COG5054   85 SSWTLLHTV---AANYPARPTPQQRDD--------LRSFLFLFsitYPCGECSKHFQKLLDVYPPQVSSREAATTWACEV 153


                 ....*...
gi 158958335 508 HNMVNGRL 515
Cdd:COG5054  154 HNKVNEKL 161
 
Name Accession Description Interval E-value
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
 318-421 2.74e-59

Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine dinucleotide (FAD) binding domain found in Quiescin sulfhydryl oxidases (QSOX) (EC:1.8.3.2). QSOX is a multi-domain disulfide catalyst that is localized primarily to the Golgi apparatus and secreted fluids and has attracted attention due to its over-production in tumors. Structural studies indicate that the closure of the Trx1 domain over the FAD-binding site may enhance the active-site chemistry for disulfide formation.


Pssm-ID: 465728  Cd Length: 104  Bit Score: 194.78  E-value: 2.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  318 DKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDL 397
Cdd:pfam18371   1 DRSKVYMADLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPETKISYSALLDA 80

                          90       100
                  ....*....|....*....|....
gi 158958335  398 VNNKMRISGIFLTNHIKWVGCQGS 421
Cdd:pfam18371  81 LDNKKEAPGAVLPEEVRWVGCQGS 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 61-174 2.20e-57

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: 189.79  E-value: 2.20e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  61 DAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYP 140
Cdd:cd02992    1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 158958335 141 TFRYFKAFTKEFTTGENFKGPDRELRTVRQTMID 174
Cdd:cd02992   81 TLRYFPPFSKEATDGLKQEGPERDVNELREALIL 114
QSOX_Trx1 pfam18108
QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an ...
 185-292 6.20e-28

QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an oxidoreductase present in Homo sapiens capable of both generating and transferring disulfide modules within a single polypeptide. The domain is thioredoxin-like, hence referred to as Trx1 domain. Trx1 domain has a di-cysteine motif (Cys-X-X-Cys) which is related to the redox-active domains of protein disulfide isomerase. The Trx1 domain is responsible for intramolecular disulfide transfer through the di-cysteine motif.


Pssm-ID: 465653  Cd Length: 108  Bit Score: 108.44  E-value: 6.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  185 PPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIY 264
Cdd:pfam18108   1 PPACPPLQPAHSSEIDEFFQTNNVEYLALIFEANDSYVGREVILDLAQHDNVAVRRVLNTEAMLVKKLGVTVFPSCYLLY 80

                          90       100
                  ....*....|....*....|....*...
gi 158958335  265 PNGSHGLINVVKPLRAFFSSYLKSLPDV 292
Cdd:pfam18108  81 RNGSAIRLPVGGETRFFYRLALQRLPGL 108
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
 430-531 9.91e-27

Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial proteins. Erv1p of Saccharomyces cerevisiae mitochondria is required for the maturation of Fe/S proteins in the cytosol. The ALR (augmenter of liver regeneration) represents a mammalian orthologue of yeast Erv1p. Both Erv1p and full-length ALR are located in the mitochondrial intermembrane an d it thought to operate downstream of the mitochondrial ABC transporter.


Pssm-ID: 461423  Cd Length: 93  Bit Score: 104.24  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  430 CSLWKLFHTLTVEASTHPDAlvgtgfedDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHN 509
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEKPTE--------EQQKDMKAFLDLFSHFYPCGECAEHFQKYLAKNPPQVSSRDALSLWLCEAHN 72

                          90       100
                  ....*....|....*....|..
gi 158958335  510 MVNGRLAGHLSEDPRFpKLQWP 531
Cdd:pfam04777  73 EVNERLGKPEFDCSKV-KERWP 93
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 77-176 2.74e-22

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: 91.90  E-value: 2.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  77 NSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRdWASAIRVAALDCmeEKNQAVCHDYDIHFYPTFRYFKAFTKEFttgE 156
Cdd:cd02961   13 KDSKDVLVEFYAPWCGHCKALAPEYEKLAKELK-GDGKVVVAKVDC--TANNDLCSEYGVRGYPTIKLFPNGSKEP---V 86

                         90       100
                 ....*....|....*....|
gi 158958335 157 NFKGPdrelRTVrQTMIDFL 176
Cdd:cd02961   87 KYEGP----RTL-ESLVEFI 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 66-172 2.93e-18

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: 80.87  E-value: 2.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  66 LDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRdwaSAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYF 145
Cdd:cd03002    5 LTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELD---GLVQVAAVDCDEDKNKPLCGKYGVQGFPTLKVF 81

                         90       100
                 ....*....|....*....|....*...
gi 158958335 146 KAFTKEFT-TGENFKGPdRELRTVRQTM 172
Cdd:cd03002   82 RPPKKASKhAVEDYNGE-RSAKAIVDFV 108
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 62-152 1.24e-13

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: 67.32  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  62 AVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAgdvRDWASAIRVAALDCmeEKNQAVCHDYDIHFYPT 141
Cdd:cd03004    2 SVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAA---RALKGKVKVGSVDC--QKYESLCQQANIRAYPT 76

                         90
                 ....*....|.
gi 158958335 142 FRYFKAFTKEF 152
Cdd:cd03004   77 IRLYPGNASKY 87
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 77-147 2.54e-13

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: 66.54  E-value: 2.54e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158958335  77 NSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDwasAIRVAALDCmeEKNQAVCHDYDIHFYPTFRYFKA 147
Cdd:cd03001   16 NSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKG---IVKVGAVDA--DVHQSLAQQYGVRGFPTIKVFGA 81
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 78-176 5.50e-13

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: 65.38  E-value: 5.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  78 SSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNqaVCHDYDIHFYPTFRYFKAFTKefttGEN 157
Cdd:cd03005   15 AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRE--LCSEFQVRGYPTLLLFKDGEK----VDK 88

                         90
                 ....*....|....*....
gi 158958335 158 FKGPdRELrtvrQTMIDFL 176
Cdd:cd03005   89 YKGT-RDL----DSLKEFV 102
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 77-165 3.13e-12

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: 63.42  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  77 NSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDwASAIRVAALDCmEEKNQAVCHDYDIHFYPTFRYFKAFTKEfttGE 156
Cdd:cd02998   16 DDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAN-EDDVVIAKVDA-DEANKDLAKKYGVSGFPTLKFFPKGSTE---PV 90


                 ....*....
gi 158958335 157 NFKGpDREL 165
Cdd:cd02998   91 KYEG-GRDL 98
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 66-161 1.08e-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: 61.77  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  66 LDSGSVRGATaNSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRdwaSAIRVAALDCMEekNQAVCHDYDIHFYPTFRYF 145
Cdd:cd03003    6 LDRGDFDAAV-NSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMD---GVIRIGAVNCGD--DRMLCRSQGVNSYPSLYVF 79

                         90
                 ....*....|....*..
gi 158958335 146 KA-FTKEFTTGENFKGP 161
Cdd:cd03003   80 PSgMNPEKYYGDRSKES 96
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 82-175 2.50e-11

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: 60.93  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  82 WLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMeeKNQAVCHDYDIHFYPTFRYFK---AFtkefttgeNF 158
Cdd:cd03000   18 WLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDAT--AYSSIASEFGVRGYPTIKLLKgdlAY--------NY 87

                         90
                 ....*....|....*..
gi 158958335 159 KGPdrelRTvRQTMIDF 175
Cdd:cd03000   88 RGP----RT-KDDIVEF 99
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 63-146 3.63e-11

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: 60.32  E-value: 3.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335   63 VWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDwasAIRVAALDCMEekNQAVCHDYDIHFYPTF 142
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDE--NPDLASKYGVRGYPTL 76


                  ....
gi 158958335  143 RYFK 146
Cdd:pfam00085  77 IFFK 80
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 83-146 1.61e-09

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: 55.79  E-value: 1.61e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335  83 LVQFYSSWCGHCIGYAPTWRALAGDVRDwASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFK 146
Cdd:cd02997   21 LVMFYAPWCGHCKKMKPEFTKAATELKE-DGKGVLAAVDCTKPEHDALKEEYNVKGFPTFKYFE 83
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 83-146 4.24e-09

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: 59.30  E-value: 4.24e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335   83 LVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKnqAVCHDYDIHFYPTFRYFK 146
Cdd:TIGR01130  22 LVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEK--DLAQKYGVSGYPTLKIFR 83
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 60-155 2.34e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 57.07  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  60 EDAVWVLDSGSVRGATANSSAAwLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAvcHDYDIHFY 139
Cdd:PTZ00102  31 SEHVTVLTDSTFDKFITENEIV-LVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELA--QEFGVRGY 107

                         90
                 ....*....|....*.
gi 158958335 140 PTFRYFKAFTKEFTTG 155
Cdd:PTZ00102 108 PTIKFFNKGNPVNYSG 123
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 83-187 5.78e-08

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: 55.84  E-value: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335   83 LVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEekNQAvcHDYDIHFYPTFRYFKAFTKefTTGENFKGpD 162
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATA--NDV--PPFEVEGFPTIKFVPAGKK--SEPVPYDG-D 440

                          90       100
                  ....*....|....*....|....*.
gi 158958335  163 RELrtvrQTMIDFLQNH-TEGSRPPA 187
Cdd:TIGR01130 441 RTL----EDFSKFIAKHaTFPLEGKA 462
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 72-145 3.32e-07

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 51.93  E-value: 3.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335  72 RGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRdwaSAIRVAALDCMEEKNqaVCHDYDIHFYPTFRYF 145
Cdd:PTZ00443  45 QASTGATTGPWFVKFYAPWCSHCRKMAPAWERLAKALK---GQVNVADLDATRALN--LAKRFAIKGYPTLLLF 113
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 83-151 2.08e-06

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: 46.78  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158958335  83 LVQFYSSWCGHCIGYAPTWRALAGDVRDwASAIRVAALDCmeEKNQaVCHDYDIHFYPTFRYFKAFTKE 151
Cdd:cd02995   22 LVEFYAPWCGHCKALAPIYEELAEKLKG-DDNVVIAKMDA--TAND-VPSEFVVDGFPTILFFPAGDKS 86
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 83-146 2.25e-06

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: 46.40  E-value: 2.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335  83 LVQFYSSWCGHCIGYAPTWRALAGDvrdwASAIRVAALDCmeEKNQAVCHDYDIHFYPTFRYFK 146
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEE----YPKVKFVKVDV--DENPELAEEYGVRSIPTFLFFK 71
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 83-146 6.29e-06

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: 45.20  E-value: 6.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158958335  83 LVQFYSSWCGHCIGYAPTWRALAgdvRDWASAIRVAALDCmeEKNQAVCHDYDIHFYPTFRYFK 146
Cdd:COG3118   22 LVDFWAPWCGPCKMLAPVLEELA---AEYGGKVKFVKVDV--DENPELAAQFGVRSIPTLLLFK 80
ERV1 COG5054
Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins ...
 431-515 5.14e-05

Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227387  Cd Length: 181  Bit Score: 44.48  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335 431 SLWKLFHTLtveASTHPDALVGTGFEDdpqavlqtMRRYVHTF---FGCKECGEHFEEMAKESMDSVKTPDQAILWLWKK 507
Cdd:COG5054   85 SSWTLLHTV---AANYPARPTPQQRDD--------LRSFLFLFsitYPCGECSKHFQKLLDVYPPQVSSREAATTWACEV 153


                 ....*...
gi 158958335 508 HNMVNGRL 515
Cdd:COG5054  154 HNKVNEKL 161
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 82-125 1.32e-03

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: 38.51  E-value: 1.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 158958335  82 WLVQFYSSWCGHCIGYAPTWRALAgdvrDWASA--IRVAALDCMEE 125
Cdd:cd02994   19 WMIEFYAPWCPACQQLQPEWEEFA----DWSDDlgINVAKVDVTQE 60
PTZ00051 PTZ00051
thioredoxin; Provisional
 83-146 1.53e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 38.32  E-value: 1.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158958335  83 LVQFYSSWCGHCIGYAPTWRALAgdvRDWASAIRVAA-LDCMEEknqaVCHDYDIHFYPTFRYFK 146
Cdd:PTZ00051  22 IVDFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVdVDELSE----VAEKENITSMPTFKVFK 79
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 82-129 6.45e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 37.75  E-value: 6.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 158958335  82 WLVQFYSSWCGHCIGYAPTWRALAGDVRDwasaIRVAALDCMEEKNQA 129
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAEEYGG----VVFVGVDVDENPEAV 74
PRK10996 PRK10996
thioredoxin 2; Provisional
 66-146 7.48e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 37.36  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158958335  66 LDSGSVRGATANSSAAWL-------VQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAAldcmeEKNQAVCHDYDIHF 138
Cdd:PRK10996  32 LFDGEVINATGETLDKLLqddlpvvIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNT-----EAERELSARFRIRS 106


                 ....*...
gi 158958335 139 YPTFRYFK 146
Cdd:PRK10996 107 IPTIMIFK 114
 
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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