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Conserved domains on  [gi|109083569|ref|XP_001102891|]
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thioredoxin-related transmembrane protein 1 [Macaca mulatta]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10122268)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 29-129 1.55e-72

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: 217.63  E-value: 1.55e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKD 108
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|.
gi 109083569 109 GEFRRYQGPRTKKDFINFISD 129
Cdd:cd02994   81 GVFRRYQGPRDKEDLISFIEE 101
 
Name Accession Description Interval E-value
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 29-129 1.55e-72

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: 217.63  E-value: 1.55e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKD 108
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|.
gi 109083569 109 GEFRRYQGPRTKKDFINFISD 129
Cdd:cd02994   81 GVFRRYQGPRDKEDLISFIEE 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 30-129 1.67e-21

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: 86.52  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   30 NVRVITDENWRELL---EGDWMIEFYAPWCPACQNLQPEWESFAewgEDLEVNV--AKVDVTEQPGLSGRFIITALPTIY 104
Cdd:pfam00085   1 VVVVLTDANFDEVVqksSKPVLVDFYAPWCGPCKMLAPEYEELA---QEYKGNVvfAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*.
gi 109083569  105 HCKDG-EFRRYQGPRTKKDFINFISD 129
Cdd:pfam00085  78 FFKNGqPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 30-127 3.95e-18

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 77.55  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  30 NVRVITDENWRE-LLEGD--WMIEFYAPWCPACQNLQPEWESFA-EWGEDleVNVAKVDVTEQPGLSGRFIITALPTIYH 105
Cdd:COG3118    1 AVVELTDENFEEeVLESDkpVLVDFWAPWCGPCKMLAPVLEELAaEYGGK--VKFVKVDVDENPELAAQFGVRSIPTLLL 78

                         90       100
                 ....*....|....*....|...
gi 109083569 106 CKDGEFR-RYQGPRTKKDFINFI 127
Cdd:COG3118   79 FKDGQPVdRFVGALPKEQLREFL 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 29-130 6.81e-18

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: 82.80  E-value: 6.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   29 SNVRVITDENWRELLEGD--WMIEFYAPWCPACQNLQPEWESFAEW--GEDLEVNVAKVDVTEQPGLSGRFIITALPTIY 104
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHefVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100
                  ....*....|....*....|....*...
gi 109083569  105 HCKDGEFRR--YQGPRTKKDFINFISDK 130
Cdd:TIGR01130  81 IFRNGEDSVsdYNGPRDADGIVKYMKKQ 108
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 29-203 6.42e-16

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 74.66  E-value: 6.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLE-------GDWMIEFYAPWCPACQNLQPEWESFAEWGEDlEVNVAKVDVTEQPGLSGRFIITALP 101
Cdd:PTZ00443  30 NALVLLNDKNFEKLTQastgattGPWFVKFYAPWCSHCRKMAPAWERLAKALKG-QVNVADLDATRALNLAKRFAIKGYP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569 102 TIYHCKDGEFRRYQ-GPRTKKDFINFISDKEWKSI-EPVsswfgPGSVLMSSMSALFQLSMWIRACHNYfieDLGLPvwG 179
Cdd:PTZ00443 109 TLLLFDKGKMYQYEgGDRSTEKLAAFALGDFKKALgAPV-----PAPLSFFALTIDFFVSGTNEALRIY---DAAFA--G 178

                        170       180
                 ....*....|....*....|....
gi 109083569 180 SYTVFALATLFsGLLLGLCMIFVA 203
Cdd:PTZ00443 179 FFTISSFAFLF-GILMGLMIALFA 201
 
Name Accession Description Interval E-value
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 29-129 1.55e-72

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: 217.63  E-value: 1.55e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKD 108
Cdd:cd02994    1 SNVVELTDSNWTLVLEGEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|.
gi 109083569 109 GEFRRYQGPRTKKDFINFISD 129
Cdd:cd02994   81 GVFRRYQGPRDKEDLISFIEE 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 33-127 4.44e-33

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: 116.56  E-value: 4.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  33 VITDENWRELL--EGDWMIEFYAPWCPACQNLQPEWESFAEW-GEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDG 109
Cdd:cd02961    2 ELTDDNFDELVkdSKDVLVEFYAPWCGHCKALAPEYEKLAKElKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNG 81

                         90       100
                 ....*....|....*....|
gi 109083569 110 --EFRRYQGPRTKKDFINFI 127
Cdd:cd02961   82 skEPVKYEGPRTLESLVEFI 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 30-129 1.67e-21

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: 86.52  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   30 NVRVITDENWRELL---EGDWMIEFYAPWCPACQNLQPEWESFAewgEDLEVNV--AKVDVTEQPGLSGRFIITALPTIY 104
Cdd:pfam00085   1 VVVVLTDANFDEVVqksSKPVLVDFYAPWCGPCKMLAPEYEELA---QEYKGNVvfAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*.
gi 109083569  105 HCKDG-EFRRYQGPRTKKDFINFISD 129
Cdd:pfam00085  78 FFKNGqPVDDYVGARPKDALAAFLKA 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 30-126 7.98e-19

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: 79.25  E-value: 7.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  30 NVRVITDENW-RELLEGD--WMIEFYAPWCPACQNLQPEWESFAewgEDLE--VNVAKVDVTEQPGLSGRFIITALPTIY 104
Cdd:cd03001    1 DVVELTDSNFdKKVLNSDdvWLVEFYAPWCGHCKNLAPEWKKAA---KALKgiVKVGAVDADVHQSLAQQYGVRGFPTIK 77

                         90       100
                 ....*....|....*....|....
gi 109083569 105 HCKDGEFR--RYQGPRTKKDFINF 126
Cdd:cd03001   78 VFGAGKNSpqDYQGGRTAKAIVSA 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 30-127 3.95e-18

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 77.55  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  30 NVRVITDENWRE-LLEGD--WMIEFYAPWCPACQNLQPEWESFA-EWGEDleVNVAKVDVTEQPGLSGRFIITALPTIYH 105
Cdd:COG3118    1 AVVELTDENFEEeVLESDkpVLVDFWAPWCGPCKMLAPVLEELAaEYGGK--VKFVKVDVDENPELAAQFGVRSIPTLLL 78

                         90       100
                 ....*....|....*....|...
gi 109083569 106 CKDGEFR-RYQGPRTKKDFINFI 127
Cdd:COG3118   79 FKDGQPVdRFVGALPKEQLREFL 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 29-130 6.81e-18

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: 82.80  E-value: 6.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   29 SNVRVITDENWRELLEGD--WMIEFYAPWCPACQNLQPEWESFAEW--GEDLEVNVAKVDVTEQPGLSGRFIITALPTIY 104
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHefVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100
                  ....*....|....*....|....*...
gi 109083569  105 HCKDGEFRR--YQGPRTKKDFINFISDK 130
Cdd:TIGR01130  81 IFRNGEDSVsdYNGPRDADGIVKYMKKQ 108
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 34-127 2.22e-17

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: 75.43  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  34 ITDENWRELLEGD--WMIEFYAPWCPACQNLQPEWESFAE-WGEDLEVNVAKVDVT--EQPGLSGRFIITALPTIYHCKD 108
Cdd:cd02997    5 LTDEDFRKFLKKEkhVLVMFYAPWCGHCKKMKPEFTKAATeLKEDGKGVLAAVDCTkpEHDALKEEYNVKGFPTFKYFEN 84

                         90       100
                 ....*....|....*....|
gi 109083569 109 GEFRR-YQGPRTKKDFINFI 127
Cdd:cd02997   85 GKFVEkYEGERTAEDIIEFM 104
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 30-127 2.55e-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: 72.70  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  30 NVRVITDENW-RELLEGDWMIEFYAPWCPACQNLQPEWESFA--EWGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHC 106
Cdd:cd03005    1 GVLELTEDNFdHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAkkFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 109083569 107 KDGE-FRRYQGPRTKKDFINFI 127
Cdd:cd03005   81 KDGEkVDKYKGTRDLDSLKEFV 102
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 44-126 2.99e-16

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: 72.49  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  44 EGDWMIEFYAPWCPACQNLQPEWesfAEWGEDLE-----VNVAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPR 118
Cdd:cd03000   15 EDIWLVDFYAPWCGHCKKLEPVW---NEVGAELKssgspVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYNYRGPR 91


                 ....*...
gi 109083569 119 TKKDFINF 126
Cdd:cd03000   92 TKDDIVEF 99
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 31-127 3.53e-16

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: 72.20  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  31 VRVITDENWREL-LEG--DWMIEFYAPWCPACQNLQPEWESFAEWGEDLE-VNVAKVDVT--EQPGLsgrFIITALPTIY 104
Cdd:cd02995    2 VKVVVGKNFDEVvLDSdkDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDnVVIAKMDATanDVPSE---FVVDGFPTIL 78

                         90       100
                 ....*....|....*....|....*.
gi 109083569 105 HCKDGEFRR---YQGPRTKKDFINFI 127
Cdd:cd02995   79 FFPAGDKSNpikYEGDRTLEDLIKFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 31-128 4.56e-16

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 77.41  E-value: 4.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   31 VRVITDENWRELL---EGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNV--AKVDVTEQ--PGlsgrFIITALPTI 103
Cdd:TIGR01130 348 VKVLVGKNFDEIVldeTKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVviAKMDATANdvPP----FEVEGFPTI 423

                          90       100
                  ....*....|....*....|....*...
gi 109083569  104 YHCKDGEFR---RYQGPRTKKDFINFIS 128
Cdd:TIGR01130 424 KFVPAGKKSepvPYDGDRTLEDFSKFIA 451
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 29-203 6.42e-16

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 74.66  E-value: 6.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLE-------GDWMIEFYAPWCPACQNLQPEWESFAEWGEDlEVNVAKVDVTEQPGLSGRFIITALP 101
Cdd:PTZ00443  30 NALVLLNDKNFEKLTQastgattGPWFVKFYAPWCSHCRKMAPAWERLAKALKG-QVNVADLDATRALNLAKRFAIKGYP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569 102 TIYHCKDGEFRRYQ-GPRTKKDFINFISDKEWKSI-EPVsswfgPGSVLMSSMSALFQLSMWIRACHNYfieDLGLPvwG 179
Cdd:PTZ00443 109 TLLLFDKGKMYQYEgGDRSTEKLAAFALGDFKKALgAPV-----PAPLSFFALTIDFFVSGTNEALRIY---DAAFA--G 178

                        170       180
                 ....*....|....*....|....
gi 109083569 180 SYTVFALATLFsGLLLGLCMIFVA 203
Cdd:PTZ00443 179 FFTISSFAFLF-GILMGLMIALFA 201
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 37-127 9.39e-16

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: 71.05  E-value: 9.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  37 ENWRELLEGDW--MIEFYAPWCPACQNLQPEWESFAEwgEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDG-EFRR 113
Cdd:cd02947    1 EEFEELIKSAKpvVVDFWAPWCGPCKAIAPVLEELAE--EYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGkEVDR 78

                         90
                 ....*....|....
gi 109083569 114 YQGPRTKKDFINFI 127
Cdd:cd02947   79 VVGADPKEELEEFL 92
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 31-129 3.99e-15

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 74.79  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  31 VRVITDENWRELL-EGDW-MIEFYAPWCPACQNLQPEWESFAEWGEDL--EVNVAKVDVTEQPGLSGRFIITALPTIYHC 106
Cdd:PTZ00102  34 VTVLTDSTFDKFItENEIvLVKFYAPWCGHCKRLAPEYKKAAKMLKEKksEIVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100
                 ....*....|....*....|...
gi 109083569 107 KDGEFRRYQGPRTKKDFINFISD 129
Cdd:PTZ00102 114 NKGNPVNYSGGRTADGIVSWIKK 136
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 30-127 4.76e-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: 69.20  E-value: 4.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  30 NVRVITDENWRELLEGD---WMIEFYAPWCPACQNLQPEWESFAE-WGEDLEVNVAKVDVTE-QPGLSGRFIITALPTI- 103
Cdd:cd02998    1 NVVELTDSNFDKVVGDDkkdVLVEFYAPWCGHCKNLAPEYEKLAAvFANEDDVVIAKVDADEaNKDLAKKYGVSGFPTLk 80

                         90       100
                 ....*....|....*....|....*
gi 109083569 104 -YHCKDGEFRRYQGPRTKKDFINFI 127
Cdd:cd02998   81 fFPKGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 29-116 6.45e-15

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: 68.86  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLE---GDWMIEFYAPWCPACQNLQPEWESFAEWGEDLeVNVAKVDVTEQPGLSGRFIITALPTI-- 103
Cdd:cd03004    1 PSVITLTPEDFPELVLnrkEPWLVDFYAPWCGPCQALLPELRKAARALKGK-VKVGSVDCQKYESLCQQANIRAYPTIrl 79

                         90
                 ....*....|...
gi 109083569 104 YHCKDGEFRRYQG 116
Cdd:cd03004   80 YPGNASKYHSYNG 92
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 34-129 7.28e-15

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: 68.86  E-value: 7.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   34 ITDENWRE-LLEGDWM--IEFYAPWCPACQNLQPEWESFAEWGEDlEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDG- 109
Cdd:TIGR01068   1 LTDANFDEtIASSDKPvlVDFWAPWCGPCKMIAPILEELAKEYEG-KVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGk 79

                          90       100
                  ....*....|....*....|
gi 109083569  110 EFRRYQGPRTKKDFINFISD 129
Cdd:TIGR01068  80 EVDRSVGALPKAALKQLINK 99
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 48-128 3.08e-12

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: 61.99  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  48 MIEFYAPWCPACQNLQPEWESFAEwGEDLEVNVAKVDVTEQPG--LSGRFIITALPTI-------YHCKDGEfRRYQGPR 118
Cdd:cd03002   22 LVEFYAPWCGHCKNLKPEYAKAAK-ELDGLVQVAAVDCDEDKNkpLCGKYGVQGFPTLkvfrppkKASKHAV-EDYNGER 99

                         90
                 ....*....|
gi 109083569 119 TKKDFINFIS 128
Cdd:cd03002  100 SAKAIVDFVL 109
PRK10996 PRK10996
thioredoxin 2; Provisional
 35-110 3.11e-10

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 57.00  E-value: 3.11e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109083569  35 TDENWRELLEGDW--MIEFYAPWCPACQNLQPEWESFAEWGEDlEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGE 110
Cdd:PRK10996  41 TGETLDKLLQDDLpvVIDFWAPWCGPCRNFAPIFEDVAAERSG-KVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQ 117
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 46-128 9.53e-10

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 58.61  E-value: 9.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  46 DWMIEFYAPWCPACQNLQPEWESFAE-WGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGEFR--RYQGPRTKKD 122
Cdd:PTZ00102 377 DVLLEIYAPWCGHCKNLEPVYNELGEkYKDNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTpiPYEGERTVEG 456


                 ....*.
gi 109083569 123 FINFIS 128
Cdd:PTZ00102 457 FKEFVN 462
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 48-114 1.03e-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: 51.16  E-value: 1.03e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  48 MIEFYAPWCPACQNLQPEWESFAEwgEDLEVNVAKVDVTEQPGL---SGRFIITALPTIYHCKDGEFRRY 114
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELAL--LNKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVKY 68
PTZ00051 PTZ00051
thioredoxin; Provisional
 33-110 5.20e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 49.87  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  33 VITDENWRELLEGDWMI--EFYAPWCPACQNLQPEWESFAEwgEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGE 110
Cdd:PTZ00051   5 VTSQAEFESTLSQNELVivDFYAEWCGPCKRIAPFYEECSK--EYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 47-126 2.32e-07

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 47.91  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  47 WMIEFYAPWCPACQNLQPEWESFAEWGEDLeVNVAKVDVTEQPGLSGRFIITALPTIYHCKDG-EFRRYQGPRTKKDFIN 125
Cdd:cd03003   21 WFVNFYSPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGmNPEKYYGDRSKESLVK 99


                 .
gi 109083569 126 F 126
Cdd:cd03003  100 F 100
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 29-127 2.77e-07

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: 48.16  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLEGDWM--IEFYAPWCPACQNLQPEWESFA-----EWGEDLEVNVAKVDVTEQPGLSGRFIITALP 101
Cdd:cd02996    1 SEIVSLTSGNIDDILQSAELvlVNFYADWCRFSQMLHPIFEEAAakikeEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                         90       100
                 ....*....|....*....|....*...
gi 109083569 102 TIYHCKDGEF--RRYQGPRTKKDFINFI 127
Cdd:cd02996   81 TLKLFRNGMMmkREYRGQRSVEALAEFV 108
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 29-83 2.80e-07

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: 48.22  E-value: 2.80e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  29 SNVRVITDENWRELLEGD-----WMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAKV 83
Cdd:cd02993    1 EAVVTLSRAEIEALAKGErrnqsTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVKVAKF 60
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 47-103 1.12e-06

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: 46.49  E-value: 1.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109083569  47 WMIEFYAPWCPACQNLQPEWESFAewgEDLE-----VNVAKVDVTEQP--GLSGRFIITALPTI 103
Cdd:cd02992   22 WLVEFYASWCGHCRAFAPTWKKLA---RDLRkwrpvVRVAAVDCADEEnvALCRDFGVTGYPTL 82
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 49-109 1.61e-06

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: 45.34  E-value: 1.61e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109083569  49 IEFYAPWCPACQNLQPEWESFAEwGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDG 109
Cdd:cd02956   17 VDFWAPRSPPSKELLPLLERLAE-EYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAG 76
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 35-109 3.43e-06

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: 44.57  E-value: 3.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109083569  35 TDENWRELLEGDW----MIEFYAPWCPACQNLQPEWESFAEwGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDG 109
Cdd:cd02984    1 SEEEFEELLKSDAskllVLHFWAPWAEPCKQMNQVFEELAK-EAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNG 78
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 51-127 3.92e-06

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: 44.66  E-value: 3.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109083569  51 FYAPWCPACQNLQPEWESFAEWGEDLEvnVAKVDVTEQ-PGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKDFINFI 127
Cdd:cd02999   25 FYASWCPFSASFRPHFNALSSMFPQIR--HLAIEESSIkPSLLSRYGVVGFPTILLFNSTPRVRYNGTRTLDSLAAFY 100
trxA PRK09381
thioredoxin TrxA;
44-110 4.45e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 44.67  E-value: 4.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109083569  44 EGDWMIEFYAPWCPACQNLQPEWESFAEWGEDlEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGE 110
Cdd:PRK09381  21 DGAILVDFWAEWCGPCKMIAPILDEIADEYQG-KLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGE 86
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 47-130 4.81e-05

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 41.59  E-value: 4.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  47 WMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRY-QGPRTKKDFIN 125
Cdd:cd02963   27 YLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSVPAIVGIINGQVTFYhDSSFTKQHVVD 106


                 ....*
gi 109083569 126 FISDK 130
Cdd:cd02963  107 FVRKL 111
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 47-127 3.71e-04

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: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569   47 WMIEFYAPWCPACQNLQPEWESFAE--WGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKD-- 122
Cdd:TIGR00424 374 WLVVLYAPWCPFCQAMEASYLELAEklAGSGVKVAKFRADGDQKEFAKQELQLGSFPTILFFPKHSSRPIKYPSEKRDvd 453


                  ....*....
gi 109083569  123 ----FINFI 127
Cdd:TIGR00424 454 slmsFVNLL 462
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 47-127 5.68e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 39.29  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  47 WMIEFYAPWCPACQNLQPEWESFAEwgEDLEVNVAKVDVTEQPGLSGRFI----------------------ITALPTIY 104
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAE--EYGGVVFVGVDVDENPEAVKAFLkelglpypvlldpdgelakaygVRGIPTTV 108

                         90       100
                 ....*....|....*....|....*
gi 109083569 105 H-CKDGEFR-RYQGPRTKKDFINFI 127
Cdd:COG0526  109 LiDKDGKIVaRHVGPLSPEELEEAL 133
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 48-85 1.08e-03

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: 38.47  E-value: 1.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 109083569  48 MIEFYAPWCPACQNLQPEWESFAEWGEDlEVNVAKVDV 85
Cdd:cd02950   24 LVEFYADWCTVCQEMAPDVAKLKQKYGD-QVNFVMLNV 60
PLN02309 PLN02309
5'-adenylylsulfate reductase
 44-82 3.04e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 38.62  E-value: 3.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 109083569  44 EGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAK 82
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAK 403
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 30-129 4.24e-03

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 36.98  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083569  30 NVRVITDENWRELLEGD----WMIEFYAPWCPACQNLQPeweSFAEWGEDLEVN---VAKVDVTEQPGLSGRFIITA--- 99
Cdd:cd02962   29 HIKYFTPKTLEEELERDkrvtWLVEFFTTWSPECVNFAP---VFAELSLKYNNNnlkFGKIDIGRFPNVAEKFRVSTspl 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 109083569 100 ---LPTIYHCKDGE--FRR--YQGPRTKKDFINFISD 129
Cdd:cd02962  106 skqLPTIILFQGGKevARRpyYNDSKGRAVPFTFSKE 142
 
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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