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Conserved domains on  [gi|18396691|ref|NP_566214|]
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APR-like 5 [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 ...
 55-156 5.70e-50

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: 160.60  E-value: 5.70e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  55 PPIEVDGdSLDRLMASQHGNaYMSVLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAVEHSQALPSVFSRYGIHSLPSILM 134
Cdd:cd02999   1 PPEEVLN-IALDLMAFNRED-YTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILL 78

                        90       100
                ....*....|....*....|..
gi 18396691 135 VNQTLNARYHGRKDLISLIEFY 156
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 ...
 55-156 5.70e-50

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: 160.60  E-value: 5.70e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  55 PPIEVDGdSLDRLMASQHGNaYMSVLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAVEHSQALPSVFSRYGIHSLPSILM 134
Cdd:cd02999   1 PPEEVLN-IALDLMAFNRED-YTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILL 78

                        90       100
                ....*....|....*....|..
gi 18396691 135 VNQTLNARYHGRKDLISLIEFY 156
Cdd:cd02999  79 FNSTPRVRYNGTRTLDSLAAFY 100
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 56-154 5.34e-06

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: 44.43  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  56 PIEVDGDSLDRLMASQHGNaymsVL--FYASWCPFSRAVRPKFDMLSSMF-PQIQH--LAVEHSQALPsvfSRYGIHSLP 130
Cdd:COG3118   2 VVELTDENFEEEVLESDKP----VLvdFWAPWCGPCKMLAPVLEELAAEYgGKVKFvkVDVDENPELA---AQFGVRSIP 74

                        90       100
                ....*....|....*....|....*...
gi 18396691 131 S-ILMVNQTLNARYHG---RKDLISLIE 154
Cdd:COG3118  75 TlLLFKDGQPVDRFVGalpKEQLREFLD 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 74-172 7.59e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 43.97  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691   74 NAYMSVLFYASWCPFSRAVRPKFD----MLSSMFPQIqHLAVEHSQALPSVFSRYGIHSLPSILMVNQTLNARYHGRKDL 149
Cdd:PTZ00102  49 NEIVLVKFYAPWCGHCKRLAPEYKkaakMLKEKKSEI-VLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTA 127

                         90       100
                 ....*....|....*....|...
gi 18396691  150 ISLIEFYEEATGlqPVQYVAEGE 172
Cdd:PTZ00102 128 DGIVSWIKKLTG--PAVTEVESA 148
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 79-133 1.52e-03

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: 37.27  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18396691    79 VLFYASWCPFSRAVRPKFDMLSS-MFPQIQH--LAVEHSQALPsvfSRYGIHSLPSIL 133
Cdd:TIGR01068  19 VDFWAPWCGPCKMIAPILEELAKeYEGKVKFvkLNVDENPDIA---AKYGIRSIPTLL 73
 
Name Accession Description Interval E-value
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 55-156 5.70e-50

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: 160.60  E-value: 5.70e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  55 PPIEVDGdSLDRLMASQHGNaYMSVLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAVEHSQALPSVFSRYGIHSLPSILM 134
Cdd:cd02999   1 PPEEVLN-IALDLMAFNRED-YTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILL 78

                        90       100
                ....*....|....*....|..
gi 18396691 135 VNQTLNARYHGRKDLISLIEFY 156
Cdd:cd02999  79 FNSTPRVRYNGTRTLDSLAAFY 100
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 57-155 1.66e-14

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: 68.02  E-value: 1.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  57 IEVDGDSLDRLMASqhgNAYMSVLFYASWCPFSRAVRPKFDMLSSMF---PQIQHLAVEHSQAlPSVFSRYGIHSLPSIL 133
Cdd:cd02961   1 VELTDDNFDELVKD---SKDVLVEFYAPWCGHCKALAPEYEKLAKELkgdGKVVVAKVDCTAN-NDLCSEYGVRGYPTIK 76

                        90       100
                ....*....|....*....|....
gi 18396691 134 MVNQTLNA--RYHGRKDLISLIEF 155
Cdd:cd02961  77 LFPNGSKEpvKYEGPRTLESLVEF 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 79-154 9.44e-10

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: 54.49  E-value: 9.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  79 VLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAVEhSQALPSVFSRYGIHSLPS-ILMVNQTLNARYHG---RKDLISLIE 154
Cdd:cd02947  15 VDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVD-VDENPELAEEYGVRSIPTfLFFKNGKEVDRVVGadpKEELEEFLE 93
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 79-144 1.22e-07

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: 48.08  E-value: 1.22e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18396691  79 VLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAVEHSQ--ALPSVFSRYGIHSLPSILMVNQTLNARYH 144
Cdd:cd01659   2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEdpALEKELKRYGVGGVPTLVVFGPGIGVKYG 69
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 56-154 5.34e-06

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: 44.43  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  56 PIEVDGDSLDRLMASQHGNaymsVL--FYASWCPFSRAVRPKFDMLSSMF-PQIQH--LAVEHSQALPsvfSRYGIHSLP 130
Cdd:COG3118   2 VVELTDENFEEEVLESDKP----VLvdFWAPWCGPCKMLAPVLEELAAEYgGKVKFvkVDVDENPELA---AQFGVRSIP 74

                        90       100
                ....*....|....*....|....*...
gi 18396691 131 S-ILMVNQTLNARYHG---RKDLISLIE 154
Cdd:COG3118  75 TlLLFKDGQPVDRFVGalpKEQLREFLD 102
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 57-158 5.21e-05

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: 41.60  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  57 IEVDGDSLDRLMASQhgnaYMsVLFYASWCPFSRAVRPKFDMLS--SMFPQIQHLAVEHSQAlPSVFSRYGIHSLPSILM 134
Cdd:cd02994   4 VELTDSNWTLVLEGE----WM-IEFYAPWCPACQQLQPEWEEFAdwSDDLGINVAKVDVTQE-PGLSGRFFVTALPTIYH 77

                        90       100
                ....*....|....*....|....
gi 18396691 135 VNQTLNARYHGRKDLISLIEFYEE 158
Cdd:cd02994  78 AKDGVFRRYQGPRDKEDLISFIEE 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 74-172 7.59e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 43.97  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691   74 NAYMSVLFYASWCPFSRAVRPKFD----MLSSMFPQIqHLAVEHSQALPSVFSRYGIHSLPSILMVNQTLNARYHGRKDL 149
Cdd:PTZ00102  49 NEIVLVKFYAPWCGHCKRLAPEYKkaakMLKEKKSEI-VLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTA 127

                         90       100
                 ....*....|....*....|...
gi 18396691  150 ISLIEFYEEATGlqPVQYVAEGE 172
Cdd:PTZ00102 128 DGIVSWIKKLTG--PAVTEVESA 148
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 79-161 1.90e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.83  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  79 VLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAV--------------EHSQALPSVF-------SRYGIHSLPSILMVNQ 137
Cdd:COG0526  33 VNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVdvdenpeavkaflkELGLPYPVLLdpdgelaKAYGVRGIPTTVLIDK 112

                        90       100
                ....*....|....*....|....*.
gi 18396691 138 --TLNARYHGRKDLISLIEFYEEATG 161
Cdd:COG0526 113 dgKIVARHVGPLSPEELEEALEKLLA 138
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 57-155 4.59e-04

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: 38.91  E-value: 4.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  57 IEVDGDSLDRLMASqhgNAYMSVLFYASWCPFSRAVRPKFDMLSSMFPQiqhlavEHSQALPSVF------------SRY 124
Cdd:cd02996   4 VSLTSGNIDDILQS---AELVLVNFYADWCRFSQMLHPIFEEAAAKIKE------EFPDAGKVVWgkvdcdkesdiaDRY 74

                        90       100       110
                ....*....|....*....|....*....|...
gi 18396691 125 GIHSLPSI-LMVN-QTLNARYHGRKDLISLIEF 155
Cdd:cd02996  75 RINKYPTLkLFRNgMMMKREYRGQRSVEALAEF 107
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 79-137 5.53e-04

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: 38.41  E-value: 5.53e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  79 VLFYASWCPFSRAVRPKFDMLSS-MFPQIQHLAVEhSQALPSVFSRYGIHSLPSILMVNQ 137
Cdd:cd02984  19 LHFWAPWAEPCKQMNQVFEELAKeAFPSVLFLSIE-AEELPEISEKFEITAVPTFVFFRN 77
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 55-132 9.61e-04

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: 38.02  E-value: 9.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396691  55 PPIEVDGDSLDRLMASQhgNAYMSVLFYASWCPFSRAVRPKFDMLSSMF---PQIQHLAV-----EHSQAlpsVFSRYGI 126
Cdd:cd02992   2 PVIVLDAASFNSALLGS--PSAWLVEFYASWCGHCRAFAPTWKKLARDLrkwRPVVRVAAvdcadEENVA---LCRDFGV 76


                ....*.
gi 18396691 127 HSLPSI 132
Cdd:cd02992  77 TGYPTL 82
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 79-133 1.52e-03

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: 37.27  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18396691    79 VLFYASWCPFSRAVRPKFDMLSS-MFPQIQH--LAVEHSQALPsvfSRYGIHSLPSIL 133
Cdd:TIGR01068  19 VDFWAPWCGPCKMIAPILEELAKeYEGKVKFvkLNVDENPDIA---AKYGIRSIPTLL 73
PTZ00051 PTZ00051
thioredoxin; Provisional
 73-131 2.51e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 36.78  E-value: 2.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396691   73 GNAYMSVLFYASWCPFSRAVRPKFDMLSSMFPQIQHLAVEHSQaLPSVFSRYGIHSLPS 131
Cdd:PTZ00051  17 QNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDE-LSEVAEKENITSMPT 74
 
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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