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Conserved domains on  [gi|159164139]
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Chain A, Protein disulfide-isomerase A4

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 22-123 1.80e-49

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


:

Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 153.60  E-value: 1.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKG 101
Cdd:TIGR01126   1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 159164139  102 QA-VDYDGSRTQEEIVAKVREVS 123
Cdd:TIGR01126  80 SKpVDYEGGRDLEAIVEFVNEKS 102
 
Name Accession Description Interval E-value
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 22-123 1.80e-49

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 153.60  E-value: 1.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKG 101
Cdd:TIGR01126   1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 159164139  102 QA-VDYDGSRTQEEIVAKVREVS 123
Cdd:TIGR01126  80 SKpVDYEGGRDLEAIVEFVNEKS 102
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 21-119 4.60e-42

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: 134.66  E-value: 4.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  21 VLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:cd02961    2 ELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG-DGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 159164139 101 G--QAVDYDGSRTQEEIVAKV 119
Cdd:cd02961   81 GskEPVKYEGPRTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 19-125 2.11e-39

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 137.57  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  19 VWVLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKIL 98
Cdd:PTZ00102  34 VTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100
                 ....*....|....*....|....*..
gi 159164139  99 KKGQAVDYDGSRTQEEIVAKVREVSQP 125
Cdd:PTZ00102 114 NKGNPVNYSGGRTADGIVSWIKKLTGP 140
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 18-121 2.01e-37

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: 123.11  E-value: 2.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   18 GVWVLNDGNFDNFVAD-KDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIK 96
Cdd:pfam00085   1 VVVVLTDANFDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN---VVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*.
gi 159164139   97 ILKKGQAVD-YDGSRTQEEIVAKVRE 121
Cdd:pfam00085  78 FFKNGQPVDdYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 22-122 1.22e-25

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: 93.35  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDT-VLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:COG3118    5 LTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEYGGK---VKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                         90       100
                 ....*....|....*....|...
gi 159164139 101 GQAVD-YDGSRTQEEIVAKVREV 122
Cdd:COG3118   82 GQPVDrFVGALPKEQLREFLDKV 104
 
Name Accession Description Interval E-value
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 22-123 1.80e-49

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 153.60  E-value: 1.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKG 101
Cdd:TIGR01126   1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 159164139  102 QA-VDYDGSRTQEEIVAKVREVS 123
Cdd:TIGR01126  80 SKpVDYEGGRDLEAIVEFVNEKS 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 18-125 3.18e-42

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: 144.82  E-value: 3.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   18 GVWVLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKI 97
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 159164139   98 LKKG--QAVDYDGSRTQEEIVAKVREVSQP 125
Cdd:TIGR01130  82 FRNGedSVSDYNGPRDADGIVKYMKKQSGP 111
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 21-119 4.60e-42

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: 134.66  E-value: 4.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  21 VLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:cd02961    2 ELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG-DGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 159164139 101 G--QAVDYDGSRTQEEIVAKV 119
Cdd:cd02961   81 GskEPVKYEGPRTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 19-125 2.11e-39

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 137.57  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  19 VWVLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKIL 98
Cdd:PTZ00102  34 VTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100
                 ....*....|....*....|....*..
gi 159164139  99 KKGQAVDYDGSRTQEEIVAKVREVSQP 125
Cdd:PTZ00102 114 NKGNPVNYSGGRTADGIVSWIKKLTGP 140
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 18-121 2.01e-37

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: 123.11  E-value: 2.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   18 GVWVLNDGNFDNFVAD-KDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIK 96
Cdd:pfam00085   1 VVVVLTDANFDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN---VVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*.
gi 159164139   97 ILKKGQAVD-YDGSRTQEEIVAKVRE 121
Cdd:pfam00085  78 FFKNGQPVDdYVGARPKDALAAFLKA 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 18-117 5.27e-35

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: 117.00  E-value: 5.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  18 GVWVLNDGNFDNFV-ADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIK 96
Cdd:cd03001    1 DVVELTDSNFDKKVlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI---VKVGAVDADVHQSLAQQYGVRGFPTIK 77

                         90       100
                 ....*....|....*....|...
gi 159164139  97 ILKKGQ--AVDYDGSRTQEEIVA 117
Cdd:cd03001   78 VFGAGKnsPQDYQGGRTAKAIVS 100
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 18-117 7.36e-35

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: 116.58  E-value: 7.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  18 GVWVLNDGNFDNFV-ADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKdNDPPIAVAKIDATSA-SMLASKFDVSGYPTI 95
Cdd:cd02998    1 NVVELTDSNFDKVVgDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFA-NEDDVVIAKVDADEAnKDLAKKYGVSGFPTL 79

                         90       100
                 ....*....|....*....|....
gi 159164139  96 KILKKG--QAVDYDGSRTQEEIVA 117
Cdd:cd02998   80 KFFPKGstEPVKYEGGRDLEDLVK 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 14-121 1.53e-31

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: 116.31  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   14 KEENGVWVLNDGNFDNFVAD--KDtVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASmlASKFDVSG 91
Cdd:TIGR01130 343 DDEGPVKVLVGKNFDEIVLDetKD-VLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATAND--VPPFEVEG 419

                          90       100       110
                  ....*....|....*....|....*....|...
gi 159164139   92 YPTIKILKKG---QAVDYDGSRTQEEIVAKVRE 121
Cdd:TIGR01130 420 FPTIKFVPAGkksEPVPYDGDRTLEDFSKFIAK 452
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 22-117 4.82e-31

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: 107.02  E-value: 4.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSA--SMLASKFDVSGYPTIKILK 99
Cdd:cd02997    5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKE-DGKGVLAAVDCTKPehDALKEEYNVKGFPTFKYFE 83

                         90
                 ....*....|....*....
gi 159164139 100 KGQAV-DYDGSRTQEEIVA 117
Cdd:cd02997   84 NGKFVeKYEGERTAEDIIE 102
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 28-123 1.54e-30

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: 105.61  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  28 DNF--VADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKGQAVD 105
Cdd:cd03000    7 DSFkdVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN 86

                         90
                 ....*....|....*...
gi 159164139 106 YDGSRTQEEIVAKVREVS 123
Cdd:cd03000   87 YRGPRTKDDIVEFANRVA 104
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 26-116 7.15e-30

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: 103.79  E-value: 7.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  26 NFDNFVADKD-TVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDpPIAVAKIDATsASMLASKFDVSGYPTIKILKKG--- 101
Cdd:cd02995    9 NFDEVVLDSDkDVLVEFYAPWCGHCKALAPIYEELAEKLKGDD-NVVIAKMDAT-ANDVPSEFVVDGFPTILFFPAGdks 86

                         90
                 ....*....|....*
gi 159164139 102 QAVDYDGSRTQEEIV 116
Cdd:cd02995   87 NPIKYEGDRTLEDLI 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 22-119 1.21e-25

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: 93.20  E-value: 1.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKD-TVLLEFYAPWCGHCKQFAPEYEKIASTLkdnDPPIAVAKIDATSAS--MLASKFDVSGYPTIKIL 98
Cdd:cd03002    5 LTPKNFDKVVHNTNyTTLVEFYAPWCGHCKNLKPEYAKAAKEL---DGLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKVF 81

                         90       100
                 ....*....|....*....|....*..
gi 159164139  99 KKGQAV------DYDGSRTQEEIVAKV 119
Cdd:cd03002   82 RPPKKAskhaveDYNGERSAKAIVDFV 108
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 22-122 1.22e-25

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: 93.35  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDT-VLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:COG3118    5 LTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEYGGK---VKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                         90       100
                 ....*....|....*....|...
gi 159164139 101 GQAVD-YDGSRTQEEIVAKVREV 122
Cdd:COG3118   82 GQPVDrFVGALPKEQLREFLDKV 104
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 18-115 1.89e-25

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: 92.73  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  18 GVWVLNDGNFDNFVADKDTvLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKI 97
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNH-FVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                         90
                 ....*....|....*....
gi 159164139  98 LKKGQAVD-YDGSRTQEEI 115
Cdd:cd03005   80 FKDGEKVDkYKGTRDLDSL 98
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 26-119 4.17e-22

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: 83.76  E-value: 4.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  26 NFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDndppIAVAKIDATSASMLASKFDVSGYPTIKILKKGQAVD 105
Cdd:cd02947    2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVD 77

                         90
                 ....*....|....*
gi 159164139 106 -YDGSRTQEEIVAKV 119
Cdd:cd02947   78 rVVGADPKEELEEFL 92
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 11-117 8.64e-22

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 86.60  E-value: 8.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  11 LEVKEENGVWVLNDGNFDNFV-----ADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLAS 85
Cdd:PTZ00443  24 LDAEDANALVLLNDKNFEKLTqastgATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAK 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 159164139  86 KFDVSGYPTIKILKKGQAVDYD-GSRTQEEIVA 117
Cdd:PTZ00443 101 RFAIKGYPTLLLFDKGKMYQYEgGDRSTEKLAA 133
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 12-121 2.81e-20

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 85.19  E-value: 2.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  12 EVKEENG-VWVLNDGNFDNFVADKDT-VLLEFYAPWCGHCKQFAPEYEKIASTLKDNDpPIAVAKIDATSASMLASKFDV 89
Cdd:PTZ00102 351 IPEEQDGpVKVVVGNTFEEIVFKSDKdVLLEIYAPWCGHCKNLEPVYNELGEKYKDND-SIIVAKMNGTANETPLEEFSW 429

                         90       100       110
                 ....*....|....*....|....*....|....
gi 159164139  90 SGYPTIKILKKGQ--AVDYDGSRTQEEIVAKVRE 121
Cdd:PTZ00102 430 SAFPTILFVKAGErtPIPYEGERTVEGFKEFVNK 463
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 19-97 8.64e-20

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 78.10  E-value: 8.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  19 VWVLNDGNFDNFVAD-KDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKI 97
Cdd:cd03004    3 VITLTPEDFPELVLNrKEPWLVDFYAPWCGPCQALLPELRKAARALKGK---VKVGSVDCQKYESLCQQANIRAYPTIRL 79
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 22-105 2.72e-19

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: 76.94  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   22 LNDGNFDNFVADKDT-VLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:TIGR01068   1 LTDANFDETIASSDKpVLVDFWAPWCGPCKMIAPILEELAKEYEGK---VKFVKLNVDENPDIAAKYGIRSIPTLLLFKN 77


                  ....*
gi 159164139  101 GQAVD 105
Cdd:TIGR01068  78 GKEVD 82
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 19-96 1.52e-17

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: 72.69  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  19 VWVLNDGNFDNFVADKDT-VLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKID--ATSASMLASKFDVSGYPTI 95
Cdd:cd02992    3 VIVLDAASFNSALLGSPSaWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDcaDEENVALCRDFGVTGYPTL 82


                 .
gi 159164139  96 K 96
Cdd:cd02992   83 R 83
PTZ00051 PTZ00051
thioredoxin; Provisional
 21-105 3.75e-16

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 68.75  E-value: 3.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  21 VLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLkdndPPIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:PTZ00051   5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEY----TKMVFVKVDVDELSEVAEKENITSMPTFKVFKN 80


                 ....*
gi 159164139 101 GQAVD 105
Cdd:PTZ00051  81 GSVVD 85
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 19-121 1.23e-15

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: 67.40  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  19 VWVLNDGNFDNFVadKDTVLLEFYAPWCGHCKQFAPEYEKIAStlKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKIL 98
Cdd:cd02994    3 VVELTDSNWTLVL--EGEWMIEFYAPWCPACQQLQPEWEEFAD--WSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHA 78

                         90       100
                 ....*....|....*....|...
gi 159164139  99 KKGQAVDYDGSRTQEEIVAKVRE 121
Cdd:cd02994   79 KDGVFRRYQGPRDKEDLISFIEE 101
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 22-115 1.59e-15

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: 67.42  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDP---PIAVAKIDATSASMLASKFDVSGYPTIKIL 98
Cdd:cd02996    6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPdagKVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                         90
                 ....*....|....*....
gi 159164139  99 KKGQAV--DYDGSRTQEEI 115
Cdd:cd02996   86 RNGMMMkrEYRGQRSVEAL 104
PRK10996 PRK10996
thioredoxin 2; Provisional
 26-105 2.59e-14

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 65.09  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  26 NFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKILKKGQAVD 105
Cdd:PRK10996  44 TLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGK---VRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 22-117 2.06e-13

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 61.61  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVAdkdtVLleFYAPWCGHCKQFAPEYEKIASTLkdndPPIAVAKIDATSA-SMLASKFDVSGYPTIKILKK 100
Cdd:cd02999   12 LMAFNREDYTA----VL--FYASWCPFSASFRPHFNALSSMF----PQIRHLAIEESSIkPSLLSRYGVVGFPTILLFNS 81

                         90
                 ....*....|....*..
gi 159164139 101 GQAVDYDGSRTQEEIVA 117
Cdd:cd02999   82 TPRVRYNGTRTLDSLAA 98
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 22-116 4.15e-12

PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 58.31  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIAstlKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKG 101
Cdd:cd03003    6 LDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFA---KEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG 82

                         90
                 ....*....|....*.
gi 159164139 102 -QAVDYDGSRTQEEIV 116
Cdd:cd03003   83 mNPEKYYGDRSKESLV 98
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 26-115 1.01e-11

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: 57.28  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  26 NFDNFVADKDT--VLLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKILKKGQA 103
Cdd:cd02956    2 NFQQVLQESTQvpVVVDFWAPRSPPSKELLPLLERLAEEYQGQ---FVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQP 78

                         90
                 ....*....|...
gi 159164139 104 VD-YDGSRTQEEI 115
Cdd:cd02956   79 VDgFQGAQPEEQL 91
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 27-119 3.47e-10

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 53.43  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  27 FDNFV-ADKDTVL-LEFYAPWCGHCKQFAPEYEKIAstlKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKGQAV 104
Cdd:cd02984    5 FEELLkSDASKLLvLHFWAPWAEPCKQMNQVFEELA---KEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIV 81

                         90
                 ....*....|....*.
gi 159164139 105 D-YDGSRTQeEIVAKV 119
Cdd:cd02984   82 DrVSGADPK-ELAKKV 96
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 37-122 8.89e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.46  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  37 VLLEFYAPWCGHCKQFAPEYEKIASTLK---------DNDPPIAVAKIDAT---------SASMLASKFDVSGYPTIKIL 98
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAEEYGgvvfvgvdvDENPEAVKAFLKELglpypvlldPDGELAKAYGVRGIPTTVLI 110

                         90       100
                 ....*....|....*....|....*.
gi 159164139  99 -KKGQAVDYD-GSRTQEEIVAKVREV 122
Cdd:COG0526  111 dKDGKIVARHvGPLSPEELEEALEKL 136
trxA PRK09381
thioredoxin TrxA;
22-102 2.47e-08

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 48.91  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDTV-LLEFYAPWCGHCKQFAPEYEKIASTLKDNdppIAVAKIDATSASMLASKFDVSGYPTIKILKK 100
Cdd:PRK09381   8 LTDDSFDTDVLKADGAiLVDFWAEWCGPCKMIAPILDEIADEYQGK---LTVAKLNIDQNPGTAPKYGIRGIPTLLLFKN 84


                 ..
gi 159164139 101 GQ 102
Cdd:PRK09381  85 GE 86
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 38-107 3.47e-08

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: 47.31  E-value: 3.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159164139  38 LLEFYAPWCGHCKQFAPEYEKiastLKDNDPPIAVAKIDATSASML---ASKFDVSGYPTIKILKKGQAVDYD 107
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAE----LALLNKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVKYG 69
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 32-110 1.03e-06

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 44.37  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  32 ADKDTvLLEFYAPWCGHCKQFAPEYEKIASTLKDNDppIAVAKIDATSASMLASK--FDVSGYPTIKILKKG--QAVDYD 107
Cdd:cd02993   20 RNQST-LVVLYAPWCPFCQAMEASYEELAEKLAGSN--VKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNsrQPIKYP 96


                 ...
gi 159164139 108 GSR 110
Cdd:cd02993   97 SEQ 99
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 22-106 6.76e-06

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 42.67  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  22 LNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIAstlkDNDPPIAVAKIDATSASM------------------- 82
Cdd:cd03011    8 LDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLA----ADYPVVSVALRSGDDGAVarfmqkkgygfpvindpdg 83

                         90       100
                 ....*....|....*....|....*
gi 159164139  83 -LASKFDVSGYPTIKILKKGQAVDY 106
Cdd:cd03011   84 vISARWGVSVTPAIVIVDPGGIVFV 108
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 27-105 2.04e-05

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 41.05  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  27 FDNFVADKDTVLLEFYAPWCGHCKQFAPEY---EKIASTLKDNdppIAVAKIDATSAS----MLASKFDVSGYPTIKILK 99
Cdd:cd02953    4 LAQALAQGKPVFVDFTADWCVTCKVNEKVVfsdPEVQAALKKD---VVLLRADWTKNDpeitALLKRFGVFGPPTYLFYG 80


                 ....*.
gi 159164139 100 KGQAVD 105
Cdd:cd02953   81 PGGEPE 86
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 36-108 2.32e-05

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 41.44  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  36 TVLLEFYAPWCGHCKQFAPE----YEKIAST---------------------LKDNDPPIAVAKIDATSASMLASKFDVS 90
Cdd:cd02964   19 TVGLYFSASWCPPCRAFTPKlvefYEKLKEEgknfeivfvsrdrseesfneyFSEMPPWLAVPFEDEELRELLEKQFKVE 98

                         90
                 ....*....|....*....
gi 159164139  91 GYPTIKILK-KGQAVDYDG 108
Cdd:cd02964   99 GIPTLVVLKpDGDVVTTNA 117
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 12-100 5.12e-05

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


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 41.54  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   12 EVKEENGVWVLNDGNFDNFVA---DKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFD 88
Cdd:TIGR00424 346 DIFDSNNVVSLSRPGIENLLKleeRKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSGVKVAKFRADGDQKEFAKQELQ 425

                          90
                  ....*....|..
gi 159164139   89 VSGYPTIKILKK 100
Cdd:TIGR00424 426 LGSFPTILFFPK 437
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 35-101 7.01e-05

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 39.21  E-value: 7.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   35 DTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDP--PIAVaKIDATSASM-----------------------LASKFDV 89
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNveIVFV-SLDRDLEEFkdylkkmpkdwlsvpfddderneLKRKYGV 80

                          90
                  ....*....|..
gi 159164139   90 SGYPTIKILKKG 101
Cdd:pfam13905  81 NAIPTLVLLDPN 92
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 37-104 8.97e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 39.89  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  37 VLLEFYAPWCGHCKQ-----FAPeyEKIASTLKDNdppIAVAKIDA-------------TSASMLASKFDVSGYPTIKIL 98
Cdd:COG2143   43 ILLFFESDWCPYCKKlhkevFSD--PEVAAYLKEN---FVVVQLDAegdkevtdfdgetLTEKELARKYGVRGTPTLVFF 117


                 ....*..
gi 159164139  99 -KKGQAV 104
Cdd:COG2143  118 dAEGKEI 124
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 36-108 9.09e-05

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 39.58  E-value: 9.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  36 TVLLEFYAPWCGHCKQFAPE----YEKIASTLK---------DND-----------PPIAVAKIDATSASMLASKFDVSG 91
Cdd:cd03009   20 TVGLYFSASWCPPCRAFTPKlvefYEKLKESGKnfeivfiswDRDeesfndyfskmPWLAVPFSDRERRSRLNRTFKIEG 99

                         90
                 ....*....|....*...
gi 159164139  92 YPTIKILK-KGQAVDYDG 108
Cdd:cd03009  100 IPTLIILDaDGEVVTTDA 117
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 38-117 9.41e-05

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: 39.63  E-value: 9.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  38 LLEFYAPWCGHCKQFAPEYEKIASTLKDnDPPIAVAKIDATSASMLASKFDVSGYPTIKILKK-----GQAVdydGSRTQ 112
Cdd:cd02950   24 LVEFYADWCTVCQEMAPDVAKLKQKYGD-QVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDRegneeGQSI---GLQPK 99


                 ....*
gi 159164139 113 EEIVA 117
Cdd:cd02950  100 QVLAQ 104
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 38-122 1.58e-04

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: 38.51  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  38 LLEFYAPWCGHCKQFAPEYEKIASTLKdndpP--IAVAKIDATSASMLASKFDVSGYPTIKILKKGQAVDY-DGSRTQEE 114
Cdd:cd02963   28 LIKITSDWCFSCIHIEPVWKEVIQELE----PlgVGIATVNAGHERRLARKLGAHSVPAIVGIINGQVTFYhDSSFTKQH 103


                 ....*...
gi 159164139 115 IVAKVREV 122
Cdd:cd02963  104 VVDFVRKL 111
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
37-118 2.94e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.79  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139   37 VLLEFYAPWCGHCKQFAPE---YEKIASTLKDNDPPIAV----------AKIDATSASMLASKFDVSGYPTIKIL-KKGQ 102
Cdd:pfam13098   7 VLVVFTDPDCPYCKKLKKElleDPDVTVYLGPNFVFIAVniwcakevakAFTDILENKELGRKYGVRGTPTIVFFdGKGE 86

                          90
                  ....*....|....*.
gi 159164139  103 AVDYDGSRTQEEIVAK 118
Cdd:pfam13098  87 LLRLPGYVPAEEFLAL 102
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 37-73 3.36e-04

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: 37.99  E-value: 3.36e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 159164139  37 VLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPP-IAVA 73
Cdd:cd02966   22 VLVNFWASWCPPCRAEMPELEALAKEYKDDGVEvVGVN 59
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 31-65 4.65e-04

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 37.45  E-value: 4.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 159164139  31 VADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKD 65
Cdd:cd03006   26 RTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSD 60
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
37-67 6.88e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 37.15  E-value: 6.88e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 159164139  37 VLLEFYAPWCGHCKQFAPEYEKIASTLKDND 67
Cdd:COG1225   24 VVLYFYATWCPGCTAELPELRDLYEEFKDKG 54
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 13-76 1.08e-03

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 37.61  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 159164139   13 VKEENGVWVLNDGNFDNFVA---DKDTVLLeFYAPW----CGHCKQFAPEYEKIAS----TLKDNDPPIAVAKID 76
Cdd:pfam04756   7 AKKSNGVIKLNDSNYKRLLSgprDYSVVVL-LTALDprfgCQLCREFQPEFELVAKswfkDHKAGSSKLFFATLD 80
PLN02309 PLN02309
5'-adenylylsulfate reductase
 34-101 1.56e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 37.46  E-value: 1.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159164139  34 KDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNdpPIAVAKI--DATSASMLASKFDVSGYPTIKILKKG 101
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAMEASYEELAEKLAGS--GVKVAKFraDGDQKEFAKQELQLGSFPTILLFPKN 432
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 37-67 2.24e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 36.13  E-value: 2.24e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 159164139  37 VLLEFYAPWCGHCKQFAPEYEKIASTLKDND 67
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDGK 33
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 36-95 4.46e-03

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 35.96  E-value: 4.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159164139  36 TVLLEFYAPWCGHCKQFapeyEKIasTLKDND-----PPIAVAKIDATSAS----MLASKFDVSGYPTI 95
Cdd:PRK00293 476 PVMLDLYADWCVACKEF----EKY--TFSDPQvqqalADTVLLQADVTANNaedvALLKHYNVLGLPTI 538
 
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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