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Conserved domains on  [gi|1063678685|ref|NP_001318945|]
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Thioredoxin superfamily protein [Arabidopsis thaliana]

Protein Classification

thioredoxin family protein( domain architecture ID 10121244)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  11441809|15558583|12074972|30367780

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 94-196 9.59e-20

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: 79.91  E-value: 9.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  94 DELLSVLEKSKetnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDqeapVIFLKHNVvdeyDEQSEVAERLRIKAVPLFH 173
Cdd:cd02947     1 EEFEELIKSAK----PVVVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDV----DENPELAEEYGVRSIPTFL 68

                          90       100
                  ....*....|....*....|....
gi 1063678685 174 FYKNGVLLESFA-TRDKERIDAAI 196
Cdd:cd02947    69 FFKNGKEVDRVVgADPKEELEEFL 92
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 94-196 9.59e-20

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: 79.91  E-value: 9.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  94 DELLSVLEKSKetnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDqeapVIFLKHNVvdeyDEQSEVAERLRIKAVPLFH 173
Cdd:cd02947     1 EEFEELIKSAK----PVVVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDV----DENPELAEEYGVRSIPTFL 68

                          90       100
                  ....*....|....*....|....
gi 1063678685 174 FYKNGVLLESFA-TRDKERIDAAI 196
Cdd:cd02947    69 FFKNGKEVDRVVgADPKEELEEFL 92
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 87-198 5.76e-15

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: 67.64  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  87 VTEFKTDDELLSVLEKSKEtnsLVVVDFYRTACGSCKYIEQGFSKLCKQsgdQEAPVIFLKHNVvdeyDEQSEVAERLRI 166
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSK---PVLVDFYAPWCGPCKMLAPEYEELAQE---YKGNVVFAKVDV----DENPDLASKYGV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063678685 167 KAVPLFHFYKNGVLLESF-ATRDKERIDAAILK 198
Cdd:pfam00085  71 RGYPTLIFFKNGQPVDDYvGARPKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 101-192 9.38e-14

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 64.51  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685 101 EKSKETNSLVVVDFYRTACGSCKYIEQGFSKLCKQsgdqEAPVIFLKHNVvdeyDEQSEVAERLRIKAVPLFHFYKNGVL 180
Cdd:PTZ00051   12 ESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKE----YTKMVFVKVDV----DELSEVAEKENITSMPTFKVFKNGSV 83

                          90
                  ....*....|..
gi 1063678685 181 LESFATRDKERI 192
Cdd:PTZ00051   84 VDTLLGANDEAL 95
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 92-199 1.10e-12

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: 61.76  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  92 TDDELLSVLEKSKEtnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapVIFLKHNVvdeyDEQSEVAERLRIKAVPL 171
Cdd:COG3118     6 TDENFEEEVLESDK---PVLVDFWAPWCGPCKMLAPVLEELAAEYGGK---VKFVKVDV----DENPELAAQFGVRSIPT 75

                          90       100
                  ....*....|....*....|....*....
gi 1063678685 172 FHFYKNGVLLESFA-TRDKERIDAAILKY 199
Cdd:COG3118    76 LLLFKDGQPVDRFVgALPKEQLREFLDKV 104
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 91-199 1.09e-11

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: 58.84  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  91 KTDDELLSVLEKSketNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapVIFLKHNVvdeyDEQSEVAERLRIKAVP 170
Cdd:TIGR01068   1 LTDANFDETIASS---DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGK---VKFVKLNV----DENPDIAAKYGIRSIP 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063678685 171 LFHFYKNGVLLESFA-TRDKERIDAAILKY 199
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVgALPKAALKQLINKN 100
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 94-196 9.59e-20

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: 79.91  E-value: 9.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  94 DELLSVLEKSKetnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDqeapVIFLKHNVvdeyDEQSEVAERLRIKAVPLFH 173
Cdd:cd02947     1 EEFEELIKSAK----PVVVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDV----DENPELAEEYGVRSIPTFL 68

                          90       100
                  ....*....|....*....|....
gi 1063678685 174 FYKNGVLLESFA-TRDKERIDAAI 196
Cdd:cd02947    69 FFKNGKEVDRVVgADPKEELEEFL 92
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 87-198 5.76e-15

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: 67.64  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  87 VTEFKTDDELLSVLEKSKEtnsLVVVDFYRTACGSCKYIEQGFSKLCKQsgdQEAPVIFLKHNVvdeyDEQSEVAERLRI 166
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSK---PVLVDFYAPWCGPCKMLAPEYEELAQE---YKGNVVFAKVDV----DENPDLASKYGV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063678685 167 KAVPLFHFYKNGVLLESF-ATRDKERIDAAILK 198
Cdd:pfam00085  71 RGYPTLIFFKNGQPVDDYvGARPKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 101-192 9.38e-14

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 64.51  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685 101 EKSKETNSLVVVDFYRTACGSCKYIEQGFSKLCKQsgdqEAPVIFLKHNVvdeyDEQSEVAERLRIKAVPLFHFYKNGVL 180
Cdd:PTZ00051   12 ESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKE----YTKMVFVKVDV----DELSEVAEKENITSMPTFKVFKNGSV 83

                          90
                  ....*....|..
gi 1063678685 181 LESFATRDKERI 192
Cdd:PTZ00051   84 VDTLLGANDEAL 95
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 92-199 1.10e-12

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: 61.76  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  92 TDDELLSVLEKSKEtnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapVIFLKHNVvdeyDEQSEVAERLRIKAVPL 171
Cdd:COG3118     6 TDENFEEEVLESDK---PVLVDFWAPWCGPCKMLAPVLEELAAEYGGK---VKFVKVDV----DENPELAAQFGVRSIPT 75

                          90       100
                  ....*....|....*....|....*....
gi 1063678685 172 FHFYKNGVLLESFA-TRDKERIDAAILKY 199
Cdd:COG3118    76 LLLFKDGQPVDRFVgALPKEQLREFLDKV 104
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 91-199 1.09e-11

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: 58.84  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  91 KTDDELLSVLEKSketNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapVIFLKHNVvdeyDEQSEVAERLRIKAVP 170
Cdd:TIGR01068   1 LTDANFDETIASS---DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGK---VKFVKLNV----DENPDIAAKYGIRSIP 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063678685 171 LFHFYKNGVLLESFA-TRDKERIDAAILKY 199
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVgALPKAALKQLINKN 100
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 103-195 1.56e-08

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: 50.35  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685 103 SKETNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapVIFLKHnvvdEYDEQSEVAERLRIKAVPLFHFYKNGVLLe 182
Cdd:cd02984    10 KSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPS---VLFLSI----EAEELPEISEKFEITAVPTFVFFRNGTIV- 81

                          90
                  ....*....|...
gi 1063678685 183 sfatrdkERIDAA 195
Cdd:cd02984    82 -------DRVSGA 87
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 70-200 2.93e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 52.83  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  70 NLVELSDENDDLCPvECVTEFkTDDELlsvlEKSKETNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQEAPVIFLKhn 149
Cdd:PTZ00102   18 AFAVFGSAEEHFIS-EHVTVL-TDSTF----DKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLAS-- 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063678685 150 vVDEyDEQSEVAERLRIKAVPLFHFYKNGVLLESFATRDKERIDAAILKYT 200
Cdd:PTZ00102   90 -VDA-TEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLT 138
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 94-199 2.69e-06

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.


Pssm-ID: 239283  Cd Length: 103  Bit Score: 44.40  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  94 DELLSVLEKSKetNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDqeapVIFLKHNVvDEYDEQSEVAERLRIKAVPLFH 173
Cdd:cd02985     4 EELDEALKKAK--GRLVVLEFALKHSGPSVKIYPTMVKLSRTCND----VVFLLVNG-DENDSTMELCRREKIIEVPHFL 76

                          90       100
                  ....*....|....*....|....*.
gi 1063678685 174 FYKNGVLLESFATRDKERIDAAILKY 199
Cdd:cd02985    77 FYKDGEKIHEEEGIGPDELIGDVLYY 102
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 98-185 1.03e-05

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: 42.64  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  98 SVLEKSKETnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapVIFLKHNVvdeyDEQSEVAERLRIKAVPLFHFYKN 177
Cdd:cd02956     5 QVLQESTQV--PVVVDFWAPRSPPSKELLPLLERLAEEYQGQ---FVLAKVNC----DAQPQIAQQFGVQALPTVYLFAA 75


                  ....*...
gi 1063678685 178 GVLLESFA 185
Cdd:cd02956    76 GQPVDGFQ 83
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 92-184 3.39e-05

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 41.39  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  92 TDDELLSVLEKSKEtNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDqeapVIFLKHNVvdeydEQSEVAERLRIKAVPL 171
Cdd:cd02957    10 SSKEFLEEVTKASK-GTRVVVHFYEPGFPRCKILDSHLEELAAKYPE----TKFVKINA-----EKAFLVNYLDIKVLPT 79

                          90
                  ....*....|...
gi 1063678685 172 FHFYKNGVLLESF 184
Cdd:cd02957    80 LLVYKNGELIDNI 92
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 110-202 1.03e-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: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685 110 VVVDFYRTACGSCKYIEQGFSKLCKQSGD-----------QEAPVIFLKHNVVDE---YDEQSEVAERLRIKAVP-LFHF 174
Cdd:COG0526    31 VLVNFWATWCPPCRAEMPVLKELAEEYGGvvfvgvdvdenPEAVKAFLKELGLPYpvlLDPDGELAKAYGVRGIPtTVLI 110

                          90       100
                  ....*....|....*....|....*....
gi 1063678685 175 YKNGVLLESFATR-DKERIDAAILKYTSS 202
Cdd:COG0526   111 DKDGKIVARHVGPlSPEELEEALEKLLAK 139
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 87-184 3.24e-04

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.


Pssm-ID: 239287  Cd Length: 113  Bit Score: 38.71  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  87 VTEFKTDDELLSVLEKSKetnsLVVVDFYRTACGSCKYIEQGFSKLCKQSGDqeapVIFLKHNVvdeydEQSE-VAERLR 165
Cdd:cd02989     6 YREVSDEKEFFEIVKSSE----RVVCHFYHPEFFRCKIMDKHLEILAKKHLE----TKFIKVNA-----EKAPfLVEKLN 72

                          90
                  ....*....|....*....
gi 1063678685 166 IKAVPLFHFYKNGVLLESF 184
Cdd:cd02989    73 IKVLPTVILFKNGKTVDRI 91
PRK10996 PRK10996
thioredoxin 2; Provisional
 92-178 7.25e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 38.51  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  92 TDDELLSVLEKSKEtnslVVVDFYRTACGSCkyieQGFSKLCKQSGDQEA-PVIFLKhnvVDEYDEQsEVAERLRIKAVP 170
Cdd:PRK10996   41 TGETLDKLLQDDLP----VVIDFWAPWCGPC----RNFAPIFEDVAAERSgKVRFVK---VNTEAER-ELSARFRIRSIP 108


                  ....*...
gi 1063678685 171 LFHFYKNG 178
Cdd:PRK10996  109 TIMIFKNG 116
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 88-182 8.31e-04

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 37.31  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  88 TEFKTDDELlsvlEKSKETNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQeapvifLKHNVVDEYDeQSEVAERLRIK 167
Cdd:cd02948     2 VEINNQEEW----EELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDD------LLHFATAEAD-TIDTLKRYRGK 70

                          90
                  ....*....|....*
gi 1063678685 168 AVPLFHFYKNGVLLE 182
Cdd:cd02948    71 CEPTFLFYKNGELVA 85
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 85-199 1.93e-03

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: 38.50  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  85 ECVTEFKTD--DELLsvlekskETNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQEAPVIFLKhnvVDEYDEQsEVAE 162
Cdd:TIGR01130   1 EDVLVLTKDnfDDFI-------KSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAK---VDATEEK-DLAQ 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063678685 163 RLRIKAVPLFHFYKNGVLLESFAT--RDKEridaAILKY 199
Cdd:TIGR01130  70 KYGVSGYPTLKIFRNGEDSVSDYNgpRDAD----GIVKY 104
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 92-199 4.34e-03

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: 35.37  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685  92 TDDELLSVLEKSKEtnslVVVDFYRTACGSCKYIEQGFSK---LCKQSGdqeaPVIFLKHNVVDeyDEQSEVAERLRIKA 168
Cdd:cd02997     6 TDEDFRKFLKKEKH----VLVMFYAPWCGHCKKMKPEFTKaatELKEDG----KGVLAAVDCTK--PEHDALKEEYNVKG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063678685 169 VPLFHFYKNGVLLESFatrDKERIDAAILKY 199
Cdd:cd02997    76 FPTFKYFENGKFVEKY---EGERTAEDIIEF 103
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
110-195 9.59e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 35.23  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678685 110 VVVDFYRTACGSCKYIEQGFSKLCKQSGDQEAPVIFL------KH-NVVDEY--------DEQSEVAERLRIKAVPlfHF 174
Cdd:COG1225    24 VVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVssdsdeAHkKFAEKYglpfpllsDPDGEVAKAYGVRGTP--TT 101

                          90       100
                  ....*....|....*....|....
gi 1063678685 175 Y---KNGVLLESFATRDKERIDAA 195
Cdd:COG1225   102 FlidPDGKIRYVWVGPVDPRPHLE 125
 
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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