NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|332193618|gb|AEE31739|]
View 

APR-like 4 [Arabidopsis thaliana]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 64-134 7.19e-33

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: 116.30  E-value: 7.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  64 GDERWLQIALDMIHKNKCDYVALLFYASWCPFS-----------------------------STLSKYGVHGFPTLLLLN 114
Cdd:cd02999    1 PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSasfrphfnalssmfpqirhlaieessikpSLLSRYGVVGFPTILLFN 80

                         90       100
                 ....*....|....*....|
gi 332193618 115 STMRARYRGTRMLDSLVAFY 134
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 ...
 64-134 7.19e-33

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: 116.30  E-value: 7.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  64 GDERWLQIALDMIHKNKCDYVALLFYASWCPFS-----------------------------STLSKYGVHGFPTLLLLN 114
Cdd:cd02999    1 PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSasfrphfnalssmfpqirhlaieessikpSLLSRYGVVGFPTILLFN 80

                         90       100
                 ....*....|....*....|
gi 332193618 115 STMRARYRGTRMLDSLVAFY 134
Cdd:cd02999   81 STPRVRYNGTRTLDSLAAFY 100
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 74-139 2.85e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 42.05  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  74 DMIHKNkcDYVALLFYASWCPFSSTLS--------------------------------KYGVHGFPTLLLLNSTMRARY 121
Cdd:PTZ00102  44 KFITEN--EIVLVKFYAPWCGHCKRLApeykkaakmlkekkseivlasvdateemelaqEFGVRGYPTIKFFNKGNPVNY 121

                         90
                 ....*....|....*...
gi 332193618 122 RGTRMLDSLVAFYSDVTG 139
Cdd:PTZ00102 122 SGGRTADGIVSWIKKLTG 139
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 64-134 7.19e-33

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: 116.30  E-value: 7.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  64 GDERWLQIALDMIHKNKCDYVALLFYASWCPFS-----------------------------STLSKYGVHGFPTLLLLN 114
Cdd:cd02999    1 PPEEVLNIALDLMAFNREDYTAVLFYASWCPFSasfrphfnalssmfpqirhlaieessikpSLLSRYGVVGFPTILLFN 80

                         90       100
                 ....*....|....*....|
gi 332193618 115 STMRARYRGTRMLDSLVAFY 134
Cdd:cd02999   81 STPRVRYNGTRTLDSLAAFY 100
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 74-133 6.67e-09

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: 52.23  E-value: 6.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  74 DMIHKNKcdYVALLFYASWCPFSSTL-------------------------------SKYGVHGFPTLLLLNSTMRA--R 120
Cdd:cd02961   10 ELVKDSK--DVLVEFYAPWCGHCKALapeyeklakelkgdgkvvvakvdctanndlcSEYGVRGYPTIKLFPNGSKEpvK 87

                         90
                 ....*....|...
gi 332193618 121 YRGTRMLDSLVAF 133
Cdd:cd02961   88 YEGPRTLESLVEF 100
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 83-133 1.30e-04

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: 40.31  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  83 YVALLFYASWC--------------------------------PFSSTLSKYGVHGFPTLLLL--NSTMRARYRGTRMLD 128
Cdd:cd02998   20 DVLVEFYAPWCghcknlapeyeklaavfaneddvviakvdadeANKDLAKKYGVSGFPTLKFFpkGSTEPVKYEGGRDLE 99


                 ....*
gi 332193618 129 SLVAF 133
Cdd:cd02998  100 DLVKF 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 95-133 1.38e-04

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: 40.13  E-value: 1.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 332193618  95 FSSTLSKYGVHGFPTLLLLNSTMRARYRGTRMLDSLVAF 133
Cdd:cd03000   61 YSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIVEF 99
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 74-139 2.85e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 42.05  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193618  74 DMIHKNkcDYVALLFYASWCPFSSTLS--------------------------------KYGVHGFPTLLLLNSTMRARY 121
Cdd:PTZ00102  44 KFITEN--EIVLVKFYAPWCGHCKRLApeykkaakmlkekkseivlasvdateemelaqEFGVRGYPTIKFFNKGNPVNY 121

                         90
                 ....*....|....*...
gi 332193618 122 RGTRMLDSLVAFYSDVTG 139
Cdd:PTZ00102 122 SGGRTADGIVSWIKKLTG 139
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 68-133 1.82e-03

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: 36.88  E-value: 1.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332193618  68 WLQIALDMIHKNKCDYVALLFyaswCP-FSSTLSKYGVHGFPTLLLLNSTMRA-RYRGTRMLDSLVAF 133
Cdd:cd03005   38 WEQLAKKFNNENPSVKIAKVD----CTqHRELCSEFQVRGYPTLLLFKDGEKVdKYKGTRDLDSLKEF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH