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Conserved domains on  [gi|1002313069|ref|XP_015619921|]
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5'-adenylylsulfate reductase-like 6 [Oryza sativa Japonica Group]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 61-160 2.30e-36

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02999:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 100  Bit Score: 125.55  E-value: 2.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  61 PAEEINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILIAC 140
Cdd:cd02999     1 PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILLFN 80

                          90       100
                  ....*....|....*....|
gi 1002313069 141 GPYAYWPVGSKELDSLVNVY 160
Cdd:cd02999    81 STPRVRYNGTRTLDSLAAFY 100
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 61-160 2.30e-36

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: 125.55  E-value: 2.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  61 PAEEINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILIAC 140
Cdd:cd02999     1 PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILLFN 80

                          90       100
                  ....*....|....*....|
gi 1002313069 141 GPYAYWPVGSKELDSLVNVY 160
Cdd:cd02999    81 STPRVRYNGTRTLDSLAAFY 100
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 64-138 2.19e-09

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 54.06  E-value: 2.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313069  64 EINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMF-PRIKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:COG3118     4 ELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVD-VDENPELAAQFGVRSIPTLLL 78
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 65-138 2.59e-06

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: 45.36  E-value: 2.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313069  65 INGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSS-MFPRIKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKeYEGKVKFVKLN-VDENPDIAAKYGIRSIPTLLL 74
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 83-158 6.96e-06

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: 44.15  E-value: 6.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILIAC-GPYAYWPVGSKELDSLVN 158
Cdd:pfam00085  23 VDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKnGQPVDDYVGARPKDALAA 99
PTZ00051 PTZ00051
thioredoxin; Provisional
 61-135 2.28e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 39.47  E-value: 2.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313069  61 PAEEINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEqTNAMPAVLSRYGVRSFPS 135
Cdd:PTZ00051    1 MVHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVD-VDELSEVAEKENITSMPT 74
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 61-160 2.30e-36

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: 125.55  E-value: 2.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  61 PAEEINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILIAC 140
Cdd:cd02999     1 PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILLFN 80

                          90       100
                  ....*....|....*....|
gi 1002313069 141 GPYAYWPVGSKELDSLVNVY 160
Cdd:cd02999    81 STPRVRYNGTRTLDSLAAFY 100
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 63-158 3.52e-13

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: 64.55  E-value: 3.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  63 EEINGEELVKELSgKEECTAVLFYASWCPFSQRMRPVFDDLSSMF---PRIKHLAVEQTnAMPAVLSRYGVRSFPSILIA 139
Cdd:cd02961     1 VELTDDNFDELVK-DSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgdGKVVVAKVDCT-ANNDLCSEYGVRGYPTIKLF 78

                          90       100
                  ....*....|....*....|...
gi 1002313069 140 CG----PYAYwpVGSKELDSLVN 158
Cdd:cd02961    79 PNgskePVKY--EGPRTLESLVE 99
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 83-138 6.91e-11

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: 57.95  E-value: 6.91e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:cd02947    15 VDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVD-VDENPELAEEYGVRSIPTFLF 69
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 64-138 2.19e-09

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 54.06  E-value: 2.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313069  64 EINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMF-PRIKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:COG3118     4 ELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVD-VDENPELAAQFGVRSIPTLLL 78
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 83-138 8.02e-09

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: 51.55  E-value: 8.02e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAV--EQTNAMPAVLSRYGVRSFPSILI 138
Cdd:cd01659     2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVdvDEDPALEKELKRYGVGGVPTLVV 59
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 83-158 1.59e-07

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: 48.79  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPA---VLSRYGVRSFPSILiacgpyaYWPVGSKE------- 152
Cdd:cd02998    23 VEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEAnkdLAKKYGVSGFPTLK-------FFPKGSTEpvkyegg 95


                  ....*...
gi 1002313069 153 --LDSLVN 158
Cdd:cd02998    96 rdLEDLVK 103
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 65-137 1.52e-06

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: 45.77  E-value: 1.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313069  65 INGEELVKELSgKEECTAVLFYASWCPFSQRMRPVFDDLSSMF---PRIKHLAVEQTNAM-PAVLSRYGVRSFPSIL 137
Cdd:cd02997     5 LTDEDFRKFLK-KEKHVLVMFYAPWCGHCKKMKPEFTKAATELkedGKGVLAAVDCTKPEhDALKEEYNVKGFPTFK 80
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 77-157 2.28e-06

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: 45.52  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  77 KEECTAVLFYASWCPFSQRMRPVFD----DLSSMFPRIKHLAVEQTnAMPAVLSRYGVRSFPSILIACGPYAYWPVGSKE 152
Cdd:cd03000    14 KEDIWLVDFYAPWCGHCKKLEPVWNevgaELKSSGSPVRVGKLDAT-AYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRT 92


                  ....*
gi 1002313069 153 LDSLV 157
Cdd:cd03000    93 KDDIV 97
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 65-138 2.59e-06

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: 45.36  E-value: 2.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313069  65 INGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSS-MFPRIKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKeYEGKVKFVKLN-VDENPDIAAKYGIRSIPTLLL 74
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 61-136 5.19e-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: 44.57  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  61 PAEEINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMF---PRIKHLAV----EQTNAmpAVLSRYGVRSF 133
Cdd:cd02992     2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLrkwRPVVRVAAvdcaDEENV--ALCRDFGVTGY 79


                  ...
gi 1002313069 134 PSI 136
Cdd:cd02992    80 PTL 82
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 83-158 6.96e-06

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: 44.15  E-value: 6.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILIAC-GPYAYWPVGSKELDSLVN 158
Cdd:pfam00085  23 VDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKnGQPVDDYVGARPKDALAA 99
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 54-137 7.04e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 45.07  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  54 RASAERCPA---EEINGEEL-VKELSGKeectAVL--FYASWCPFSQRMRPVFDDLSSMFPRIKHLAV---EQTNAMPAV 124
Cdd:COG0526     2 KAVGKPAPDftlTDLDGKPLsLADLKGK----PVLvnFWATWCPPCRAEMPVLKELAEEYGGVVFVGVdvdENPEAVKAF 77

                          90
                  ....*....|...
gi 1002313069 125 LSRYGVrSFPSIL 137
Cdd:COG0526    78 LKELGL-PYPVLL 89
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 83-175 7.79e-06

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 44.08  E-value: 7.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQ----TNAMPAVlsrYGVRSFPSILiacgpyaYWPVGSKEldslvn 158
Cdd:cd02995    23 VEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKmdatANDVPSE---FVVDGFPTIL-------FFPAGDKS------ 86

                          90
                  ....*....|....*..
gi 1002313069 159 vytavtgqEPIAYLGPR 175
Cdd:cd02995    87 --------NPIKYEGDR 95
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 83-107 5.51e-05

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: 41.61  E-value: 5.51e-05
                          10        20
                  ....*....|....*....|....*
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMF 107
Cdd:cd02996    23 VNFYADWCRFSQMLHPIFEEAAAKI 47
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 68-138 5.58e-05

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: 41.49  E-value: 5.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002313069  68 EELVKELSGKeeCTAVLFYASWCPFSQRMRPVFDDLSS-MFPRIKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:cd02984     6 EELLKSDASK--LLVLHFWAPWAEPCKQMNQVFEELAKeAFPSVLFLSIE-AEELPEISEKFEITAVPTFVF 74
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 83-137 1.13e-04

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: 40.73  E-value: 1.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313069  83 VLFYASWCPFSQRMRPVFDDLSSMF----PRIKHLAVEQTNAMPaVLSRYGVRSFPSIL 137
Cdd:cd03005    21 VKFFAPWCGHCKRLAPTWEQLAKKFnnenPSVKIAKVDCTQHRE-LCSEFQVRGYPTLL 78
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 64-179 1.83e-04

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: 39.96  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  64 EINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILIacgpy 143
Cdd:cd03001     4 ELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKV----- 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002313069 144 ayWPVGSKeldslvnvytavtgqEPIAYLGPRKWSA 179
Cdd:cd03001    79 --FGAGKN---------------SPQDYQGGRTAKA 97
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 68-137 1.94e-04

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: 40.13  E-value: 1.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313069  68 EELVKeLSGKEECTAVLFYASWCPFSQRMRPVFDDLSsmfpriKHLA-----VEQTNA----MPAVLSRYGVRSFPSIL 137
Cdd:cd02993    12 EALAK-GERRNQSTLVVLYAPWCPFCQAMEASYEELA------EKLAgsnvkVAKFNAdgeqREFAKEELQLKSFPTIL 83
PTZ00051 PTZ00051
thioredoxin; Provisional
 61-135 2.28e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 39.47  E-value: 2.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313069  61 PAEEINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEqTNAMPAVLSRYGVRSFPS 135
Cdd:PTZ00051    1 MVHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVD-VDELSEVAEKENITSMPT 74
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 54-136 5.18e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 41.27  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  54 RASAERCPAE--EINGEELVKELSgKEECTAVLFYASWCPFSQRMRPVFDDLSSMF----PRIKHLAVEQTNAMpAVLSR 127
Cdd:PTZ00102   24 SAEEHFISEHvtVLTDSTFDKFIT-ENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLkekkSEIVLASVDATEEM-ELAQE 101


                  ....*....
gi 1002313069 128 YGVRSFPSI 136
Cdd:PTZ00102  102 FGVRGYPTI 110
PLN02309 PLN02309
5'-adenylylsulfate reductase
 67-157 5.23e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 41.31  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  67 GEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMF--PRIK---------HLAVEQTNAMPavlsrygvRSFPS 135
Cdd:PLN02309  354 GIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLagSGVKvakfradgdQKEFAKQELQL--------GSFPT 425

                          90       100
                  ....*....|....*....|....*.
gi 1002313069 136 ILI----ACGPYAYwPVGSKELDSLV 157
Cdd:PLN02309  426 ILLfpknSSRPIKY-PSEKRDVDSLL 450
trxA PRK09381
thioredoxin TrxA;
81-138 2.73e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 36.97  E-value: 2.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313069  81 TAVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILI 138
Cdd:PRK09381   24 ILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 64-158 4.15e-03

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: 36.19  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  64 EINGEELVKELSGKEECTAVLFYASWCPFSQRMRPVFDDLSSMF-PRIKHLAVEQTNAM-PAVLSRYGVRSFPSI-LIAC 140
Cdd:cd03002     4 ELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELdGLVQVAAVDCDEDKnKPLCGKYGVQGFPTLkVFRP 83

                          90       100
                  ....*....|....*....|...
gi 1002313069 141 GPYAYWPV-----GSKELDSLVN 158
Cdd:cd03002    84 PKKASKHAvedynGERSAKAIVD 106
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 64-138 4.46e-03

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 37.68  E-value: 4.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313069  64 EINGEELVKELSGKEECT-AVLFYASWCPFSQRMRPVFDDLSSMFPRIKHLAVEQTNAMPAVLSRYGVRSFPSILI 138
Cdd:PTZ00443   37 DKNFEKLTQASTGATTGPwFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLL 112
PRK10996 PRK10996
thioredoxin 2; Provisional
 51-138 5.97e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 36.59  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313069  51 PSCRASaERCPAEEIN--------GEELV--KELSGKEECTAVL----------FYASWCPFSQRMRPVFDDLSSMFP-R 109
Cdd:PRK10996    6 TSCQAI-NRLPDERIEdaakcgrcGHDLFdgEVINATGETLDKLlqddlpvvidFWAPWCGPCRNFAPIFEDVAAERSgK 84

                          90       100
                  ....*....|....*....|....*....
gi 1002313069 110 IKHLAVEqTNAMPAVLSRYGVRSFPSILI 138
Cdd:PRK10996   85 VRFVKVN-TEAERELSARFRIRSIPTIMI 112
 
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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