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Conserved domains on  [gi|18418521|ref|NP_568360|]
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APR-like 7 [Arabidopsis thaliana]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10122309)

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_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 51-152 4.39e-43

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: 142.88  E-value: 4.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  51 PPIEVDGDLLDkLMDANHGNaYISILFYTSRCPFSRAVRPKFDVLSSMFPHITHLIVEQSQALPSVFSRYGIHSLPSILM 130
Cdd:cd02999   1 PPEEVLNIALD-LMAFNRED-YTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILL 78

                        90       100
                ....*....|....*....|..
gi 18418521 131 VNQTMKMRYHGPKDLASLIQFY 152
Cdd:cd02999  79 FNSTPRVRYNGTRTLDSLAAFY 100
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 51-152 4.39e-43

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: 142.88  E-value: 4.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  51 PPIEVDGDLLDkLMDANHGNaYISILFYTSRCPFSRAVRPKFDVLSSMFPHITHLIVEQSQALPSVFSRYGIHSLPSILM 130
Cdd:cd02999   1 PPEEVLNIALD-LMAFNRED-YTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILL 78

                        90       100
                ....*....|....*....|..
gi 18418521 131 VNQTMKMRYHGPKDLASLIQFY 152
Cdd:cd02999  79 FNSTPRVRYNGTRTLDSLAAFY 100
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 75-151 6.98e-04

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: 38.26  E-value: 6.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  75 ILFYTSRCPFSRAVRPKFDVLSSMF-PHITHLIV--EQSQALPSvfsRYGIHSLPS-ILMVNQTMKMRYHGPKDLASLIQ 150
Cdd:COG3118  23 VDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVdvDENPELAA---QFGVRSIPTlLLFKDGQPVDRFVGALPKEQLRE 99


                .
gi 18418521 151 F 151
Cdd:COG3118 100 F 100
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 51-152 4.39e-43

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: 142.88  E-value: 4.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  51 PPIEVDGDLLDkLMDANHGNaYISILFYTSRCPFSRAVRPKFDVLSSMFPHITHLIVEQSQALPSVFSRYGIHSLPSILM 130
Cdd:cd02999   1 PPEEVLNIALD-LMAFNRED-YTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILL 78

                        90       100
                ....*....|....*....|..
gi 18418521 131 VNQTMKMRYHGPKDLASLIQFY 152
Cdd:cd02999  79 FNSTPRVRYNGTRTLDSLAAFY 100
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 53-151 2.73e-10

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: 56.46  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  53 IEVDGDLLDKLMdanHGNAYISILFYTSRCPFSRAVRPKFDVLSSMFPHITHLIVEQ--SQALPSVFSRYGIHSLPSILM 130
Cdd:cd02961   1 VELTDDNFDELV---KDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKvdCTANNDLCSEYGVRGYPTIKL 77

                        90       100
                ....*....|....*....|...
gi 18418521 131 VNQTMKM--RYHGPKDLASLIQF 151
Cdd:cd02961  78 FPNGSKEpvKYEGPRTLESLVEF 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 75-153 4.42e-07

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: 47.17  E-value: 4.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  75 ILFYTSRCPFSRAVRPKFDVLSSMFPHITHLIVEqSQALPSVFSRYGIHSLPS-ILMVNQTMKMRYHGPKDLASLIQFYK 153
Cdd:cd02947  15 VDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVD-VDENPELAEEYGVRSIPTfLFFKNGKEVDRVVGADPKEELEEFLE 93
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 75-140 2.92e-06

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: 44.23  E-value: 2.92e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18418521  75 ILFYTSRCPFSRAVRPKFDVLSSMFPHITHLIV--EQSQALPSVFSRYGIHSLPSILMVNQTMKMRYH 140
Cdd:cd01659   2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVdvDEDPALEKELKRYGVGGVPTLVVFGPGIGVKYG 69
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 75-151 6.98e-04

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: 38.26  E-value: 6.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  75 ILFYTSRCPFSRAVRPKFDVLSSMF-PHITHLIV--EQSQALPSvfsRYGIHSLPS-ILMVNQTMKMRYHGPKDLASLIQ 150
Cdd:COG3118  23 VDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVdvDENPELAA---QFGVRSIPTlLLFKDGQPVDRFVGALPKEQLRE 99


                .
gi 18418521 151 F 151
Cdd:COG3118 100 F 100
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 75-154 8.37e-03

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: 35.05  E-value: 8.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418521  75 ILFYTSRCPFSRAVRPKFDVLSsmfphithlivEQSQAL------------PSVFSRYGIHSLPSILMVNQTMKMRYHGP 142
Cdd:cd02994  21 IEFYAPWCPACQQLQPEWEEFA-----------DWSDDLginvakvdvtqePGLSGRFFVTALPTIYHAKDGVFRRYQGP 89

                        90
                ....*....|..
gi 18418521 143 KDLASLIQFYKE 154
Cdd:cd02994  90 RDKEDLISFIEE 101
 
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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