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Conserved domains on  [gi|17567813|ref|NP_508654|]
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Sulfhydryl oxidase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 48-161 6.85e-53

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: 176.69  E-value: 6.85e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  48 DPILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADDKNMPLCREHSVSSYP 127
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 17567813 128 SLRYFKYNSHNKDDGMKYSGDKYDINKLAHDIAG 161
Cdd:cd02992  81 TLRYFPPFSKEATDGLKQEGPERDVNELREALIL 114
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
 419-515 1.62e-18

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: 80.74  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   419 CGLWTLAHTITVEAYK----QEKHNtafkpvidvLEPFRAFIFHFLSCSECAQNFTKEAEKNQLHlVTRPEDVYAWLWRV 494
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEkpteEQQKD---------MKAFLDLFSHFYPCGECAEHFQKYLAKNPPQ-VSSRDALSLWLCEA 70

                          90       100
                  ....*....|....*....|.
gi 17567813   495 HNFVNKRLSGSLTDDPSFKKQ 515
Cdd:pfam04777  71 HNEVNERLGKPEFDCSKVKER 91
FAD_SOX super family cl39711
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
 317-410 2.04e-12

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.


The actual alignment was detected with superfamily member pfam18371:

Pssm-ID: 465728  Cd Length: 104  Bit Score: 63.82  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   317 DLKSAMSYMLYKEIPRREEIRDEPMAVLKQWMHTLKKYAPGTTPMRRLFFRLDEWIQLQSV--VTANEWITKVDEIQQAL 394
Cdd:pfam18371   9 DLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPEtkISYSALLDALDNKKEAP 88

                          90
                  ....*....|....*.
gi 17567813   395 GNPLPKEITWMACAGS 410
Cdd:pfam18371  89 GAVLPEEVRWVGCQGS 104
 
Name Accession Description Interval E-value
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 48-161 6.85e-53

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: 176.69  E-value: 6.85e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  48 DPILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADDKNMPLCREHSVSSYP 127
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 17567813 128 SLRYFKYNSHNKDDGMKYSGDKYDINKLAHDIAG 161
Cdd:cd02992  81 TLRYFPPFSKEATDGLKQEGPERDVNELREALIL 114
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
 419-515 1.62e-18

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: 80.74  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   419 CGLWTLAHTITVEAYK----QEKHNtafkpvidvLEPFRAFIFHFLSCSECAQNFTKEAEKNQLHlVTRPEDVYAWLWRV 494
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEkpteEQQKD---------MKAFLDLFSHFYPCGECAEHFQKYLAKNPPQ-VSSRDALSLWLCEA 70

                          90       100
                  ....*....|....*....|.
gi 17567813   495 HNFVNKRLSGSLTDDPSFKKQ 515
Cdd:pfam04777  71 HNEVNERLGKPEFDCSKVKER 91
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 49-147 4.61e-13

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: 65.33  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813    49 PILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEkwaplVQVTVVNCADDKNMPLCREHSVSSYPS 128
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK-----GNVVFAKVDVDENPDLASKYGVRGYPT 75

                          90
                  ....*....|....*....
gi 17567813   129 LRYFKynshNKDDGMKYSG 147
Cdd:pfam00085  76 LIFFK----NGQPVDDYVG 90
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
 317-410 2.04e-12

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: 63.82  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   317 DLKSAMSYMLYKEIPRREEIRDEPMAVLKQWMHTLKKYAPGTTPMRRLFFRLDEWIQLQSV--VTANEWITKVDEIQQAL 394
Cdd:pfam18371   9 DLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPEtkISYSALLDALDNKKEAP 88

                          90
                  ....*....|....*.
gi 17567813   395 GNPLPKEITWMACAGS 410
Cdd:pfam18371  89 GAVLPEEVRWVGCQGS 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 50-147 2.13e-12

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: 69.70  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813    50 ILELDVDTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADdkNMPLCREHSVSSYPSL 129
Cdd:TIGR01130   3 VLVLTKDNFDDFI-KSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATE--EKDLAQKYGVSGYPTL 79

                          90
                  ....*....|....*...
gi 17567813   130 RYFKYNSHNKDDgmkYSG 147
Cdd:TIGR01130  80 KIFRNGEDSVSD---YNG 94
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 50-133 1.74e-11

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: 60.99  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  50 ILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVvncadDKNMPLCREHSVSSYPSL 129
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDV-----DENPELAAQFGVRSIPTL 76


                ....
gi 17567813 130 RYFK 133
Cdd:COG3118  77 LLFK 80
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 22-208 6.63e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 64.77  E-value: 6.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   22 FMLFILVVILAFSAGGSSGESLYDKDDpILELDVDTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPL 101
Cdd:PTZ00102   7 LSSLFLLLILLAFAVFGSAEEHFISEH-VTVLTDSTFDKFI-TENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  102 VQVTVVNCadDKNMPLCREHSVSSYPSLRYFkynshNKDDGMKYSGDKydinklahdiaglaqadaQKQNPESW------ 175
Cdd:PTZ00102  85 IVLASVDA--TEEMELAQEFGVRGYPTIKFF-----NKGNPVNYSGGR------------------TADGIVSWikkltg 139

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17567813  176 PTFLPLSDTTTLEEVFKSIGTTSYLAIVVQDSP 208
Cdd:PTZ00102 140 PAVTEVESASEIKLIAKKIFVAFYGEYTSKDSE 172
ERV1 COG5054
Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins ...
 422-508 5.07e-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: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813 422 WTLAHTItVEAYKQEkhntafkPVIDVLEPFRAFIF---HFLSCSECAQNFTKEAEKNQLHLVTRpEDVYAWLWRVHNFV 498
Cdd:COG5054  87 WTLLHTV-AANYPAR-------PTPQQRDDLRSFLFlfsITYPCGECSKHFQKLLDVYPPQVSSR-EAATTWACEVHNKV 157

                        90
                ....*....|
gi 17567813 499 NKRLSGSLTD 508
Cdd:COG5054 158 NEKLGKPKFD 167
 
Name Accession Description Interval E-value
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 48-161 6.85e-53

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: 176.69  E-value: 6.85e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  48 DPILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADDKNMPLCREHSVSSYP 127
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEENVALCRDFGVTGYP 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 17567813 128 SLRYFKYNSHNKDDGMKYSGDKYDINKLAHDIAG 161
Cdd:cd02992  81 TLRYFPPFSKEATDGLKQEGPERDVNELREALIL 114
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 51-149 3.92e-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: 91.13  E-value: 3.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  51 LELDVDTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLeKWAPLVQVTVVNCadDKNMPLCREHSVSSYPSLR 130
Cdd:cd02961   1 VELTDDNFDELV-KDSKDVLVEFYAPWCGHCKALAPEYEKLAKEL-KGDGKVVVAKVDC--TANNDLCSEYGVRGYPTIK 76

                        90
                ....*....|....*....
gi 17567813 131 YFKYNSHNkddGMKYSGDK 149
Cdd:cd02961  77 LFPNGSKE---PVKYEGPR 92
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 49-149 9.31e-20

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: 84.72  E-value: 9.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  49 PILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEkwaPLVQVTVVNCADDKNMPLCREHSVSSYPS 128
Cdd:cd03002   1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELD---GLVQVAAVDCDEDKNKPLCGKYGVQGFPT 77

                        90       100
                ....*....|....*....|..
gi 17567813 129 LRYFK-YNSHNKDDGMKYSGDK 149
Cdd:cd03002  78 LKVFRpPKKASKHAVEDYNGER 99
Evr1_Alr pfam04777
Erv1 / Alr family; Biogenesis of Fe/S clusters involves a number of essential mitochondrial ...
 419-515 1.62e-18

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: 80.74  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   419 CGLWTLAHTITVEAYK----QEKHNtafkpvidvLEPFRAFIFHFLSCSECAQNFTKEAEKNQLHlVTRPEDVYAWLWRV 494
Cdd:pfam04777   1 RSTWTLLHTLAAYYPEkpteEQQKD---------MKAFLDLFSHFYPCGECAEHFQKYLAKNPPQ-VSSRDALSLWLCEA 70

                          90       100
                  ....*....|....*....|.
gi 17567813   495 HNFVNKRLSGSLTDDPSFKKQ 515
Cdd:pfam04777  71 HNEVNERLGKPEFDCSKVKER 91
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 51-147 6.58e-16

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: 73.47  E-value: 6.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  51 LELDVDTFSAAIygSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADDknMPLCREHSVSSYPSLR 130
Cdd:cd03005   3 LELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQH--RELCSEFQVRGYPTLL 78

                        90
                ....*....|....*..
gi 17567813 131 YFKynshNKDDGMKYSG 147
Cdd:cd03005  79 LFK----DGEKVDKYKG 91
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 50-149 6.84e-16

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: 73.71  E-value: 6.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  50 ILELDVDTFSAAIYGSKkAHFIEFYSSWCGACIGYAPTFKKFAKQLEKwapLVQVTVVNCADDKnmPLCREHSVSSYPSL 129
Cdd:cd03003   3 IVTLDRGDFDAAVNSGE-IWFVNFYSPRCSHCHDLAPTWREFAKEMDG---VIRIGAVNCGDDR--MLCRSQGVNSYPSL 76

                        90       100
                ....*....|....*....|
gi 17567813 130 RYFKYNShnkdDGMKYSGDK 149
Cdd:cd03003  77 YVFPSGM----NPEKYYGDR 92
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 50-149 1.26e-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: 73.05  E-value: 1.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  50 ILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKwAPLVQVTVVNCaDDKNMPLCREHSVSSYPSL 129
Cdd:cd02998   2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAN-EDDVVIAKVDA-DEANKDLAKKYGVSGFPTL 79

                        90       100
                ....*....|....*....|
gi 17567813 130 RYFKYNShnkDDGMKYSGDK 149
Cdd:cd02998  80 KFFPKGS---TEPVKYEGGR 96
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 50-148 5.29e-14

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: 68.09  E-value: 5.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  50 ILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLekwAPLVQVTVVNCadDKNMPLCREHSVSSYPSL 129
Cdd:cd03004   3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARAL---KGKVKVGSVDC--QKYESLCQQANIRAYPTI 77

                        90
                ....*....|....*....
gi 17567813 130 RYFKYNSHNkddGMKYSGD 148
Cdd:cd03004  78 RLYPGNASK---YHSYNGW 93
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 49-147 4.61e-13

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: 65.33  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813    49 PILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEkwaplVQVTVVNCADDKNMPLCREHSVSSYPS 128
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK-----GNVVFAKVDVDENPDLASKYGVRGYPT 75

                          90
                  ....*....|....*....
gi 17567813   129 LRYFKynshNKDDGMKYSG 147
Cdd:pfam00085  76 LIFFK----NGQPVDDYVG 90
FAD_SOX pfam18371
Flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase; This is a flavin adenine ...
 317-410 2.04e-12

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: 63.82  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   317 DLKSAMSYMLYKEIPRREEIRDEPMAVLKQWMHTLKKYAPGTTPMRRLFFRLDEWIQLQSV--VTANEWITKVDEIQQAL 394
Cdd:pfam18371   9 DLESALHYSLRVELAKHSVLEGEELKALKDYVTVLAKYFPGRPSVKNLLQSLDSWLQSQPEtkISYSALLDALDNKKEAP 88

                          90
                  ....*....|....*.
gi 17567813   395 GNPLPKEITWMACAGS 410
Cdd:pfam18371  89 GAVLPEEVRWVGCQGS 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 50-147 2.13e-12

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: 69.70  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813    50 ILELDVDTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADdkNMPLCREHSVSSYPSL 129
Cdd:TIGR01130   3 VLVLTKDNFDDFI-KSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATE--EKDLAQKYGVSGYPTL 79

                          90
                  ....*....|....*...
gi 17567813   130 RYFKYNSHNKDDgmkYSG 147
Cdd:TIGR01130  80 KIFRNGEDSVSD---YNG 94
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 50-133 1.74e-11

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: 60.99  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  50 ILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVvncadDKNMPLCREHSVSSYPSL 129
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDV-----DENPELAAQFGVRSIPTL 76


                ....
gi 17567813 130 RYFK 133
Cdd:COG3118  77 LLFK 80
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 22-208 6.63e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 64.77  E-value: 6.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   22 FMLFILVVILAFSAGGSSGESLYDKDDpILELDVDTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPL 101
Cdd:PTZ00102   7 LSSLFLLLILLAFAVFGSAEEHFISEH-VTVLTDSTFDKFI-TENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  102 VQVTVVNCadDKNMPLCREHSVSSYPSLRYFkynshNKDDGMKYSGDKydinklahdiaglaqadaQKQNPESW------ 175
Cdd:PTZ00102  85 IVLASVDA--TEEMELAQEFGVRGYPTIKFF-----NKGNPVNYSGGR------------------TADGIVSWikkltg 139

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17567813  176 PTFLPLSDTTTLEEVFKSIGTTSYLAIVVQDSP 208
Cdd:PTZ00102 140 PAVTEVESASEIKLIAKKIFVAFYGEYTSKDSE 172
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 49-147 4.69e-09

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: 54.21  E-value: 4.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  49 PILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKwapLVQVTVVNCadDKNMPLCREHSVSSYPS 128
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKG---IVKVGAVDA--DVHQSLAQQYGVRGFPT 75

                        90
                ....*....|....*....
gi 17567813 129 LRYFKynsHNKDDGMKYSG 147
Cdd:cd03001  76 IKVFG---AGKNSPQDYQG 91
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 56-133 2.01e-08

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: 51.79  E-value: 2.01e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17567813  56 DTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKwaplVQVTVVNcaDDKNMPLCREHSVSSYPSLRYFK 133
Cdd:cd02947   1 EEFEELI-KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVD--VDENPELAEEYGVRSIPTFLFFK 71
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 56-148 7.57e-08

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: 50.63  E-value: 7.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  56 DTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADDknMPlcREHSVSSYPSLRYFKyn 135
Cdd:cd02995   8 KNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATAND--VP--SEFVVDGFPTILFFP-- 81

                        90
                ....*....|...
gi 17567813 136 SHNKDDGMKYSGD 148
Cdd:cd02995  82 AGDKSNPIKYEGD 94
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 50-134 1.13e-07

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: 50.01  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  50 ILELDVDTFSAAIygSKKAH-FIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVqVTVVNCADDKNMPLCREHSVSSYPS 128
Cdd:cd02997   2 VVHLTDEDFRKFL--KKEKHvLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGV-LAAVDCTKPEHDALKEEYNVKGFPT 78


                ....*.
gi 17567813 129 LRYFKY 134
Cdd:cd02997  79 FKYFEN 84
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 66-137 6.71e-06

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 45.44  E-value: 6.71e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17567813  66 KKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAplVQVTVVNCADDKNmpLCREHSVSSYPSL------RYFKYNSH 137
Cdd:cd02963  24 KKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLG--VGIATVNAGHERR--LARKLGAHSVPAIvgiingQVTFYHDS 97
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 45-149 6.84e-06

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: 48.90  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813    45 DKDDPILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNcADDKNMPlcrEHSVS 124
Cdd:TIGR01130 343 DDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMD-ATANDVP---PFEVE 418

                          90       100
                  ....*....|....*....|....*
gi 17567813   125 SYPSLRYFKYNShnKDDGMKYSGDK 149
Cdd:TIGR01130 419 GFPTIKFVPAGK--KSEPVPYDGDR 441
ERV1 COG5054
Mitochondrial sulfhydryl oxidase involved in the biogenesis of cytosolic Fe/S proteins ...
 422-508 5.07e-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: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813 422 WTLAHTItVEAYKQEkhntafkPVIDVLEPFRAFIF---HFLSCSECAQNFTKEAEKNQLHLVTRpEDVYAWLWRVHNFV 498
Cdd:COG5054  87 WTLLHTV-AANYPAR-------PTPQQRDDLRSFLFlfsITYPCGECSKHFQKLLDVYPPQVSSR-EAATTWACEVHNKV 157

                        90
                ....*....|
gi 17567813 499 NKRLSGSLTD 508
Cdd:COG5054 158 NEKLGKPKFD 167
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 45-149 6.70e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 45.90  E-value: 6.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   45 DKDDPILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCADDKNMplcREHSVS 124
Cdd:PTZ00102 354 EQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDSIIVAKMNGTANETPL---EEFSWS 430

                         90       100
                 ....*....|....*....|....*
gi 17567813  125 SYPSLRYFKYNSHnkdDGMKYSGDK 149
Cdd:PTZ00102 431 AFPTILFVKAGER---TPIPYEGER 452
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 70-156 1.07e-04

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 43.85  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   70 FIEFYSSWCGACIGYAPTFKKFAKQLEKwaplvqvtVVNCAD---DKNMPLCREHSVSSYPSLRYFkynshNKDDGMKYS 146
Cdd:PTZ00443  56 FVKFYAPWCSHCRKMAPAWERLAKALKG--------QVNVADldaTRALNLAKRFAIKGYPTLLLF-----DKGKMYQYE 122

                         90
                 ....*....|
gi 17567813  147 GDKYDINKLA 156
Cdd:PTZ00443 123 GGDRSTEKLA 132
PRK10996 PRK10996
thioredoxin 2; Provisional
 37-94 3.51e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 3.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17567813   37 GSSGESLYDKDdpILELDVDTFSAAIyGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQ 94
Cdd:PRK10996  26 GRCGHDLFDGE--VINATGETLDKLL-QDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE 80
PTZ00051 PTZ00051
thioredoxin; Provisional
 71-133 3.53e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 40.24  E-value: 3.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17567813   71 IEFYSSWCGACIGYAPTFKKFAKQLEKWApLVQVTVVNCADdknmpLCREHSVSSYPSLRYFK 133
Cdd:PTZ00051  23 VDFYAEWCGPCKRIAPFYEECSKEYTKMV-FVKVDVDELSE-----VAEKENITSMPTFKVFK 79
trxA PRK09381
thioredoxin TrxA;
48-133 3.53e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 40.43  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813   48 DPILELDVDTFSAAIYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKwaplvQVTVVNCADDKNMPLCREHSVSSYP 127
Cdd:PRK09381   3 DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQG-----KLTVAKLNIDQNPGTAPKYGIRGIP 77


                 ....*.
gi 17567813  128 SLRYFK 133
Cdd:PRK09381  78 TLLLFK 83
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 65-113 5.33e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.44  E-value: 5.33e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17567813  65 SKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKwaplVQVTVVNCADDK 113
Cdd:COG0526  27 KGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG----VVFVGVDVDENP 71
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 70-132 5.57e-04

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 40.40  E-value: 5.57e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17567813  70 FIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNcadDKNMPLCREHSVSSYPSLRYF 132
Cdd:cd02950  24 LVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDN---PKWLPEIDRYRVDGIPHFVFL 83
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 62-134 1.50e-03

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


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 38.53  E-value: 1.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17567813  62 IYGSKKAHFIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTV---VNCadDKNMPLCREHSVSSYPSLRYFKY 134
Cdd:cd02996  14 ILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVwgkVDC--DKESDIADRYRINKYPTLKLFRN 87
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 70-160 3.16e-03

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: 37.43  E-value: 3.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567813  70 FIEFYSSWCGACIGYAPTFKKFAKQLEKWAPLVQVTVVNCAddKNMPLCREHSVSSYPSLRYFKynshnKDDGMKYSGD- 148
Cdd:cd03000  19 LVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDAT--AYSSIASEFGVRGYPTIKLLK-----GDLAYNYRGPr 91

                        90
                ....*....|...
gi 17567813 149 -KYDINKLAHDIA 160
Cdd:cd03000  92 tKDDIVEFANRVA 104
 
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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