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Conserved domains on  [gi|51873067|ref|NP_001004128|]
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sulfhydryl oxidase 1 isoform b precursor [Homo sapiens]

Protein Classification

sulfhydryl oxidase 1( domain architecture ID 14390978)

sulfhydryl oxidase 1 belongs to the quiescin-sulfhydryl oxidase (QSOX) family, an eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of protein disulfide isomerases (PDI), and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain. 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. 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
QSOX_Trx1 pfam18108
QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an ...
162-269 2.21e-63

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: 203.97  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   162 PPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLF 241
Cdd:pfam18108   1 PPACPPLQPAHSSEIDEFFQTNNVEYLALIFEANDSYVGREVILDLAQHDNVAVRRVLNTEAMLVKKLGVTVFPSCYLLY 80
                          90       100
                  ....*....|....*....|....*...
gi 51873067   242 RNGSVSRVPVLMESRSFYTAYLQRLSGL 269
Cdd:pfam18108  81 RNGSAIRLPVGGETRFFYRLALQRLPGL 108
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
295-396 4.22e-58

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: 189.78  E-value: 4.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   295 DRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTA 374
Cdd:pfam18371   1 DRSKVYMADLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPETKISYSALLDA 80
                          90       100
                  ....*....|....*....|....
gi 51873067   375 LDDRKE--GAVLAKKVNWIGCQGS 396
Cdd:pfam18371  81 LDNKKEapGAVLPEEVRWVGCQGS 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
40-152 2.64e-54

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: 180.16  E-value: 2.64e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  40 DPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFP 119
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 51873067 120 TVRFFKAFTKN---GSGAVFPvaGADVQTLRERLID 152
Cdd:cd02992  81 TLRYFPPFSKEatdGLKQEGP--ERDVNELREALIL 114
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
405-504 2.79e-26

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: 102.70  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   405 CSLWVLFHFLTVQAARQNVDHSQEAAKAkevlpaIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRV 484
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEKPTEEQQKDMKA------FLDLFSHFYPCGECAEHFQKYLAKNPPQVSSRDALSLWLCEAHNEV 74
                          90       100
                  ....*....|....*....|
gi 51873067   485 NARLaGAPSEDPQFPKVQWP 504
Cdd:pfam04777  75 NERL-GKPEFDCSKVKERWP 93
 
Name Accession Description Interval E-value
QSOX_Trx1 pfam18108
QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an ...
162-269 2.21e-63

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: 203.97  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   162 PPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLF 241
Cdd:pfam18108   1 PPACPPLQPAHSSEIDEFFQTNNVEYLALIFEANDSYVGREVILDLAQHDNVAVRRVLNTEAMLVKKLGVTVFPSCYLLY 80
                          90       100
                  ....*....|....*....|....*...
gi 51873067   242 RNGSVSRVPVLMESRSFYTAYLQRLSGL 269
Cdd:pfam18108  81 RNGSAIRLPVGGETRFFYRLALQRLPGL 108
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
295-396 4.22e-58

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: 189.78  E-value: 4.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   295 DRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTA 374
Cdd:pfam18371   1 DRSKVYMADLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPETKISYSALLDA 80
                          90       100
                  ....*....|....*....|....
gi 51873067   375 LDDRKE--GAVLAKKVNWIGCQGS 396
Cdd:pfam18371  81 LDNKKEapGAVLPEEVRWVGCQGS 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
40-152 2.64e-54

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: 180.16  E-value: 2.64e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  40 DPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFP 119
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 51873067 120 TVRFFKAFTKN---GSGAVFPvaGADVQTLRERLID 152
Cdd:cd02992  81 TLRYFPPFSKEatdGLKQEGP--ERDVNELREALIL 114
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
405-504 2.79e-26

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: 102.70  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   405 CSLWVLFHFLTVQAARQNVDHSQEAAKAkevlpaIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRV 484
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEKPTEEQQKDMKA------FLDLFSHFYPCGECAEHFQKYLAKNPPQVSSRDALSLWLCEAHNEV 74
                          90       100
                  ....*....|....*....|
gi 51873067   485 NARLaGAPSEDPQFPKVQWP 504
Cdd:pfam04777  75 NERL-GKPEFDCSKVKERWP 93
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
63-141 6.34e-15

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: 77.41  E-value: 6.34e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51873067    63 VEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETnsAVCRDFNIPGFPTVRFFkaftKNGSGAVFPVAGA 141
Cdd:TIGR01130  23 VEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEK--DLAQKYGVSGYPTLKIF----RNGEDSVSDYNGP 95
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
63-125 4.67e-14

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: 68.41  E-value: 4.67e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067    63 VEFFASWCGHCIAFAPTWKALAEDVKAwrpALYLAALDCAEetNSAVCRDFNIPGFPTVRFFK 125
Cdd:pfam00085  23 VDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDE--NPDLASKYGVRGYPTLIFFK 80
PTZ00102 PTZ00102
disulphide isomerase; Provisional
63-134 1.32e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.08  E-value: 1.32e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067   63 VEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAvcRDFNIPGFPTVRFFKAFTK-NGSGA 134
Cdd:PTZ00102  54 VKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELA--QEFGVRGYPTIKFFNKGNPvNYSGG 124
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
63-150 3.15e-09

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: 54.44  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKawrPALYLAALDCaeETNSAVCRDFNIPGFPTVRFFkaftKNGSgAVFPVAGA- 141
Cdd:COG3118  23 VDFWAPWCGPCKMLAPVLEELAAEYG---GKVKFVKVDV--DENPELAAQFGVRSIPTLLLF----KDGQ-PVDRFVGAl 92

                ....*....
gi 51873067 142 DVQTLRERL 150
Cdd:COG3118  93 PKEQLREFL 101
ERV1 COG5054
Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins ...
406-488 7.50e-04

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: 41.01  E-value: 7.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067 406 SLWVLFHflTVQAARQNVDHSQEAAKAKEVLpairGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVN 485
Cdd:COG5054  85 SSWTLLH--TVAANYPARPTPQQRDDLRSFL----FLFSITYPCGECSKHFQKLLDVYPPQVSSREAATTWACEVHNKVN 158

                ...
gi 51873067 486 ARL 488
Cdd:COG5054 159 EKL 161
 
Name Accession Description Interval E-value
QSOX_Trx1 pfam18108
QSOX Trx-like domain; This domain is found in Quiescin sulfhydryl oxidase (QSOX), an ...
162-269 2.21e-63

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: 203.97  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   162 PPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLF 241
Cdd:pfam18108   1 PPACPPLQPAHSSEIDEFFQTNNVEYLALIFEANDSYVGREVILDLAQHDNVAVRRVLNTEAMLVKKLGVTVFPSCYLLY 80
                          90       100
                  ....*....|....*....|....*...
gi 51873067   242 RNGSVSRVPVLMESRSFYTAYLQRLSGL 269
Cdd:pfam18108  81 RNGSAIRLPVGGETRFFYRLALQRLPGL 108
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
295-396 4.22e-58

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: 189.78  E-value: 4.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   295 DRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTA 374
Cdd:pfam18371   1 DRSKVYMADLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPETKISYSALLDA 80
                          90       100
                  ....*....|....*....|....
gi 51873067   375 LDDRKE--GAVLAKKVNWIGCQGS 396
Cdd:pfam18371  81 LDNKKEapGAVLPEEVRWVGCQGS 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
40-152 2.64e-54

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: 180.16  E-value: 2.64e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  40 DPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFP 119
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 51873067 120 TVRFFKAFTKN---GSGAVFPvaGADVQTLRERLID 152
Cdd:cd02992  81 TLRYFPPFSKEatdGLKQEGP--ERDVNELREALIL 114
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
405-504 2.79e-26

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: 102.70  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   405 CSLWVLFHFLTVQAARQNVDHSQEAAKAkevlpaIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRV 484
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEKPTEEQQKDMKA------FLDLFSHFYPCGECAEHFQKYLAKNPPQVSSRDALSLWLCEAHNEV 74
                          90       100
                  ....*....|....*....|
gi 51873067   485 NARLaGAPSEDPQFPKVQWP 504
Cdd:pfam04777  75 NERL-GKPEFDCSKVKERWP 93
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
54-131 3.93e-24

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: 96.91  E-value: 3.93e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51873067  54 VLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKaWRPALYLAALDCAEetNSAVCRDFNIPGFPTVRFFKAFTKNG 131
Cdd:cd02961  11 LVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELK-GDGKVVVAKVDCTA--NNDLCSEYGVRGYPTIKLFPNGSKEP 85
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
54-126 6.39e-17

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: 76.56  E-value: 6.39e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067  54 VLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAwrpALYLAALDCAEetNSAVCRDFNIPGFPTVRFFKA 126
Cdd:cd03001  14 VLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKG---IVKVGAVDADV--HQSLAQQYGVRGFPTIKVFGA 81
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
41-141 1.89e-16

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: 75.48  E-value: 1.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  41 PLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAedvKAWRPALYLAALDCAEETNSAVCRDFNIPGFPT 120
Cdd:cd03002   1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAA---KELDGLVQVAAVDCDEDKNKPLCGKYGVQGFPT 77
                        90       100
                ....*....|....*....|.
gi 51873067 121 VRFFKAFTKNGSGAVFPVAGA 141
Cdd:cd03002  78 LKVFRPPKKASKHAVEDYNGE 98
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
45-124 1.28e-15

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: 72.67  E-value: 1.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  45 LQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAwRPALYLAALDCaEETNSAVCRDFNIPGFPTVRFF 124
Cdd:cd02998   5 LTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAN-EDDVVIAKVDA-DEANKDLAKKYGVSGFPTLKFF 82
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
63-126 2.85e-15

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: 71.55  E-value: 2.85e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNsaVCRDFNIPGFPTVRFFKA 126
Cdd:cd03005  21 VKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRE--LCSEFQVRGYPTLLLFKD 82
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
63-141 6.34e-15

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: 77.41  E-value: 6.34e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51873067    63 VEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETnsAVCRDFNIPGFPTVRFFkaftKNGSGAVFPVAGA 141
Cdd:TIGR01130  23 VEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEK--DLAQKYGVSGYPTLKIF----RNGEDSVSDYNGP 95
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
63-125 4.67e-14

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: 68.41  E-value: 4.67e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067    63 VEFFASWCGHCIAFAPTWKALAEDVKAwrpALYLAALDCAEetNSAVCRDFNIPGFPTVRFFK 125
Cdd:pfam00085  23 VDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDE--NPDLASKYGVRGYPTLIFFK 80
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
54-131 2.38e-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: 66.16  E-value: 2.38e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51873067  54 VLGSRSAWAVEFFASWCGHCIAFAPTWKALAedvKAWRPALYLAALDCaeETNSAVCRDFNIPGFPTVRFFKAFTKNG 131
Cdd:cd03004  15 VLNRKEPWLVDFYAPWCGPCQALLPELRKAA---RALKGKVKVGSVDC--QKYESLCQQANIRAYPTIRLYPGNASKY 87
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
63-125 4.11e-13

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: 65.80  E-value: 4.11e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKAWRPALyLAALDCAEETNSAVCRDFNIPGFPTVRFFK 125
Cdd:cd02997  22 VMFYAPWCGHCKKMKPEFTKAATELKEDGKGV-LAAVDCTKPEHDALKEEYNVKGFPTFKYFE 83
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
39-130 6.30e-13

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: 71.24  E-value: 6.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067    39 SDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEetNSAvcRDFNIPGF 118
Cdd:TIGR01130 345 EGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATA--NDV--PPFEVEGF 420
                          90
                  ....*....|..
gi 51873067   119 PTVRFFKAFTKN 130
Cdd:TIGR01130 421 PTIKFVPAGKKS 432
PTZ00102 PTZ00102
disulphide isomerase; Provisional
63-134 1.32e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.08  E-value: 1.32e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067   63 VEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAvcRDFNIPGFPTVRFFKAFTK-NGSGA 134
Cdd:PTZ00102  54 VKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELA--QEFGVRGYPTIKFFNKGNPvNYSGG 124
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
63-130 1.78e-11

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: 61.03  E-value: 1.78e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKAwRPALYLAALDCaeeTNSAVCRDFNIPGFPTVRFFKAFTKN 130
Cdd:cd02995  23 VEFYAPWCGHCKALAPIYEELAEKLKG-DDNVVIAKMDA---TANDVPSEFVVDGFPTILFFPAGDKS 86
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
61-131 3.04e-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: 60.16  E-value: 3.04e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51873067  61 WAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAeeTNSAVCRDFNIPGFPTVRFFK---AFTKNG 131
Cdd:cd03000  18 WLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDAT--AYSSIASEFGVRGYPTIKLLKgdlAYNYRG 89
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
63-150 9.27e-10

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: 55.64  E-value: 9.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDvkawRPALYLAALDCaeETNSAVCRDFNIPGFPTVRFFkaftKNGsGAVFPVAGAD 142
Cdd:cd02947  15 VDFWAPWCGPCKAIAPVLEELAEE----YPKVKFVKVDV--DENPELAEEYGVRSIPTFLFF----KNG-KEVDRVVGAD 83

                ....*....
gi 51873067 143 -VQTLRERL 150
Cdd:cd02947  84 pKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
63-150 3.15e-09

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: 54.44  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKawrPALYLAALDCaeETNSAVCRDFNIPGFPTVRFFkaftKNGSgAVFPVAGA- 141
Cdd:COG3118  23 VDFWAPWCGPCKMLAPVLEELAAEYG---GKVKFVKVDV--DENPELAAQFGVRSIPTLLLF----KDGQ-PVDRFVGAl 92

                ....*....
gi 51873067 142 DVQTLRERL 150
Cdd:COG3118  93 PKEQLREFL 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
44-124 8.78e-09

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 56.17  E-value: 8.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   44 LLQADTvrGAVLGSrsaWAVEFFASWCGHCIAFAPTWKALAEDVKAwrpALYLAALDCAEETNsaVCRDFNIPGFPTVRF 123
Cdd:PTZ00443  43 LTQAST--GATTGP---WFVKFYAPWCSHCRKMAPAWERLAKALKG---QVNVADLDATRALN--LAKRFAIKGYPTLLL 112

                 .
gi 51873067  124 F 124
Cdd:PTZ00443 113 F 113
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
53-126 1.40e-07

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: 49.83  E-value: 1.40e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51873067  53 AVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAwrpALYLAALDCAEetNSAVCRDFNIPGFPTVRFFKA 126
Cdd:cd03003  13 AAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDG---VIRIGAVNCGD--DRMLCRSQGVNSYPSLYVFPS 81
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
63-156 5.14e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.30  E-value: 5.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVK--------------AWRPAL------YLAALDcaeeTNSAVCRDFNIPGFPTVr 122
Cdd:COG0526  33 VNFWATWCPPCRAEMPVLKELAEEYGgvvfvgvdvdenpeAVKAFLkelglpYPVLLD----PDGELAKAYGVRGIPTT- 107
                        90       100       110
                ....*....|....*....|....*....|....
gi 51873067 123 FFkaFTKNGSGAVFPVAGADVQTLRERLIDALES 156
Cdd:COG0526 108 VL--IDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PTZ00051 PTZ00051
thioredoxin; Provisional
53-148 1.00e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.18  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   53 AVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDvkawRPALYLAALDCAEEtnSAVCRDFNIPGFPTvrfFKAFtKNGS 132
Cdd:PTZ00051  13 STLSQNELVIVDFYAEWCGPCKRIAPFYEECSKE----YTKMVFVKVDVDEL--SEVAEKENITSMPT---FKVF-KNGS 82
                         90
                 ....*....|....*.
gi 51873067  133 gAVFPVAGADVQTLRE 148
Cdd:PTZ00051  83 -VVDTLLGANDEALKQ 97
trxA PRK09381
thioredoxin TrxA;
39-150 1.57e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 44.28  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   39 SDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDvkaWRPALYLAALDCaeETNSAVCRDFNIPGF 118
Cdd:PRK09381   2 SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADE---YQGKLTVAKLNI--DQNPGTAPKYGIRGI 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 51873067  119 PTVRFFkaftKNGSGAVFPVAGADVQTLRERL 150
Cdd:PRK09381  77 PTLLLF----KNGEVAATKVGALSKGQLKEFL 104
PTZ00102 PTZ00102
disulphide isomerase; Provisional
38-157 1.69e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.44  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067   38 PSD---PLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRpALYLAALDcaEETNSAVCRDFN 114
Cdd:PTZ00102 352 PEEqdgPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDND-SIIVAKMN--GTANETPLEEFS 428
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 51873067  115 IPGFPTVRFFKAftknGSGAVFPVAGAdvQTLrERLIDALESH 157
Cdd:PTZ00102 429 WSAFPTILFVKA----GERTPIPYEGE--RTV-EGFKEFVNKH 464
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
63-125 6.01e-05

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: 42.28  E-value: 6.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51873067    63 VEFFASWCGHCIAFAPTWKALAEDVkawRPALYLAALDCAEETNSAvcRDFNIPGFPTVRFFK 125
Cdd:TIGR01068  19 VDFWAPWCGPCKMIAPILEELAKEY---EGKVKFVKLNVDENPDIA--AKYGIRSIPTLLLFK 76
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
61-85 5.96e-04

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: 39.28  E-value: 5.96e-04
                        10        20
                ....*....|....*....|....*
gi 51873067  61 WAVEFFASWCGHCIAFAPTWKALAE 85
Cdd:cd02994  19 WMIEFYAPWCPACQQLQPEWEEFAD 43
ERV1 COG5054
Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins ...
406-488 7.50e-04

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: 41.01  E-value: 7.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067 406 SLWVLFHflTVQAARQNVDHSQEAAKAKEVLpairGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVN 485
Cdd:COG5054  85 SSWTLLH--TVAANYPARPTPQQRDDLRSFL----FLFSITYPCGECSKHFQKLLDVYPPQVSSREAATTWACEVHNKVN 158

                ...
gi 51873067 486 ARL 488
Cdd:COG5054 159 EKL 161
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
63-120 1.72e-03

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 38.37  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51873067  63 VEFFASWCGHCIAFAPTWKALA--------------------EDVKAW---RPALYLAALDcaeeTNSAVCRDFNIPGFP 119
Cdd:cd02966  24 VNFWASWCPPCRAEMPELEALAkeykddgvevvgvnvddddpAAVKAFlkkYGITFPVLLD----PDGELAKAYGVRGLP 99

                .
gi 51873067 120 T 120
Cdd:cd02966 100 T 100
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
63-129 3.86e-03

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: 36.14  E-value: 3.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKAWRpalyLAALDCAEETNSAVC-RDFNIPGFPTVRFFKAFTK 129
Cdd:cd01659   2 VLFYAPWCPFCQALRPVLAELALLNKGVK----FEAVDVDEDPALEKElKRYGVGGVPTLVVFGPGIG 65
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
30-86 8.00e-03

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 36.79  E-value: 8.00e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 51873067  30 APRSALYSPSDPLTLLQADTVRGAVlgsrsaWAVEFFASWCGHCIAFAPTWKALAED 86
Cdd:cd03010   3 APAFSLPALPGPDKTLTSADLKGKP------YLLNVWASWCAPCREEHPVLMALARQ 53
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
63-126 8.16e-03

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: 36.10  E-value: 8.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51873067  63 VEFFASWCGHCIAFAPTWKALAEDVKAwrpALYLAALDCaeETNSAVCRDFNIPGFPTVRFFKA 126
Cdd:cd02956  17 VDFWAPRSPPSKELLPLLERLAEEYQG---QFVLAKVNC--DAQPQIAQQFGVQALPTVYLFAA 75
 
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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