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Conserved domains on  [gi|15222954|ref|NP_177735|]
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chloroplastic drought-induced stress protein of 32 kD [Arabidopsis thaliana]

Protein Classification

TRX_CDSP32 domain-containing protein( domain architecture ID 10122231)

TRX_CDSP32 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 79-181 1.00e-56

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: 178.06  E-value: 1.00e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  79 HSGEEFDVALKNAKSKLVVAEFATSKSDQSNKIYPFMVELSRTCNDVVFLLVMGDESDKTRELCRREKIEKVPHFSFYKS 158
Cdd:cd02985   1 HSVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVNGDENDSTMELCRREKIIEVPHFLFYKD 80

                        90       100
                ....*....|....*....|...
gi 15222954 159 MEKIHEEEGIEPDQLMGDVLYYG 181
Cdd:cd02985  81 GEKIHEEEGIGPDELIGDVLYYG 103
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 194-296 3.25e-54

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: 171.90  E-value: 3.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 194 PDVEKLIDENRTG-GKLIVLDVGLKHCGPCVKVYPTVLKLSRSMsETVVFARMNGDENDSCMEFLKDMNVIEVPTFLFIR 272
Cdd:cd02985   1 HSVEELDEALKKAkGRLVVLEFALKHSGPSVKIYPTMVKLSRTC-NDVVFLLVNGDENDSTMELCRREKIIEVPHFLFYK 79

                        90       100
                ....*....|....*....|....
gi 15222954 273 DGEIRGRYVGSGKGELIGEILRYS 296
Cdd:cd02985  80 DGEKIHEEEGIGPDELIGDVLYYG 103
 
Name Accession Description Interval E-value
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 79-181 1.00e-56

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: 178.06  E-value: 1.00e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  79 HSGEEFDVALKNAKSKLVVAEFATSKSDQSNKIYPFMVELSRTCNDVVFLLVMGDESDKTRELCRREKIEKVPHFSFYKS 158
Cdd:cd02985   1 HSVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVNGDENDSTMELCRREKIIEVPHFLFYKD 80

                        90       100
                ....*....|....*....|...
gi 15222954 159 MEKIHEEEGIEPDQLMGDVLYYG 181
Cdd:cd02985  81 GEKIHEEEGIGPDELIGDVLYYG 103
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 194-296 3.25e-54

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: 171.90  E-value: 3.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 194 PDVEKLIDENRTG-GKLIVLDVGLKHCGPCVKVYPTVLKLSRSMsETVVFARMNGDENDSCMEFLKDMNVIEVPTFLFIR 272
Cdd:cd02985   1 HSVEELDEALKKAkGRLVVLEFALKHSGPSVKIYPTMVKLSRTC-NDVVFLLVNGDENDSTMELCRREKIIEVPHFLFYK 79

                        90       100
                ....*....|....*....|....
gi 15222954 273 DGEIRGRYVGSGKGELIGEILRYS 296
Cdd:cd02985  80 DGEKIHEEEGIGPDELIGDVLYYG 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 206-282 4.12e-10

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: 55.98  E-value: 4.12e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222954 206 GGKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSETVVFARMNGDENdscMEFLKDMNVIEVPTFLFIRDGEIRGRYVG 282
Cdd:COG3118  17 SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDEN---PELAAQFGVRSIPTLLLFKDGQPVDRFVG 90
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 219-289 1.09e-08

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: 51.85  E-value: 1.09e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222954   219 CGPCVKVYPTVLKLSRSMSETVVFARMNGDEN-DSCMEFlkdmNVIEVPTFLFIRDGEIRGRYVGS-GKGELI 289
Cdd:pfam00085  30 CGPCKMLAPEYEELAQEYKGNVVFAKVDVDENpDLASKY----GVRGYPTLIFFKNGQPVDDYVGArPKDALA 98
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 205-282 2.64e-07

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: 48.05  E-value: 2.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222954   205 TGGKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSETVVFARMNGDEN-DSCMEFlkdmNVIEVPTFLFIRDGEIRGRYVG 282
Cdd:TIGR01068  12 SSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENpDIAAKY----GIRSIPTLLLFKNGKEVDRSVG 86
PTZ00051 PTZ00051
thioredoxin; Provisional
 195-288 4.12e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 41.79  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  195 DVEKLIDENrtggKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSEtVVFARMNGDEndsCMEFLKDMNVIEVPTFLFIRDG 274
Cdd:PTZ00051  10 EFESTLSQN----ELVIVDFYAEWCGPCKRIAPFYEECSKEYTK-MVFVKVDVDE---LSEVAEKENITSMPTFKVFKNG 81

                         90
                 ....*....|....
gi 15222954  275 EIRGRYVGSGKGEL 288
Cdd:PTZ00051  82 SVVDTLLGANDEAL 95
PTZ00051 PTZ00051
thioredoxin; Provisional
 75-158 9.43e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 37.93  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954   75 VQKIHSGEEFDVALknAKSKLVVAEFATSKSDQSNKIYPFMVELSRTCNDVVFLLVmgdESDKTRELCRREKIEKVPHFS 154
Cdd:PTZ00051   2 VHIVTSQAEFESTL--SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKV---DVDELSEVAEKENITSMPTFK 76


                 ....
gi 15222954  155 FYKS 158
Cdd:PTZ00051  77 VFKN 80
 
Name Accession Description Interval E-value
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 79-181 1.00e-56

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: 178.06  E-value: 1.00e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  79 HSGEEFDVALKNAKSKLVVAEFATSKSDQSNKIYPFMVELSRTCNDVVFLLVMGDESDKTRELCRREKIEKVPHFSFYKS 158
Cdd:cd02985   1 HSVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVNGDENDSTMELCRREKIIEVPHFLFYKD 80

                        90       100
                ....*....|....*....|...
gi 15222954 159 MEKIHEEEGIEPDQLMGDVLYYG 181
Cdd:cd02985  81 GEKIHEEEGIGPDELIGDVLYYG 103
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 194-296 3.25e-54

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: 171.90  E-value: 3.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 194 PDVEKLIDENRTG-GKLIVLDVGLKHCGPCVKVYPTVLKLSRSMsETVVFARMNGDENDSCMEFLKDMNVIEVPTFLFIR 272
Cdd:cd02985   1 HSVEELDEALKKAkGRLVVLEFALKHSGPSVKIYPTMVKLSRTC-NDVVFLLVNGDENDSTMELCRREKIIEVPHFLFYK 79

                        90       100
                ....*....|....*....|....
gi 15222954 273 DGEIRGRYVGSGKGELIGEILRYS 296
Cdd:cd02985  80 DGEKIHEEEGIGPDELIGDVLYYG 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 195-293 1.94e-14

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: 67.58  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 195 DVEKLIDENrtggKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSEtVVFARMNGDENdscMEFLKDMNVIEVPTFLFIRDG 274
Cdd:cd02947   2 EFEELIKSA----KPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDEN---PELAEEYGVRSIPTFLFFKNG 73

                        90
                ....*....|....*....
gi 15222954 275 EIRGRYVGSGKGELIGEIL 293
Cdd:cd02947  74 KEVDRVVGADPKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 206-282 4.12e-10

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: 55.98  E-value: 4.12e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222954 206 GGKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSETVVFARMNGDENdscMEFLKDMNVIEVPTFLFIRDGEIRGRYVG 282
Cdd:COG3118  17 SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDEN---PELAAQFGVRSIPTLLLFKDGQPVDRFVG 90
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 82-172 4.87e-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: 55.64  E-value: 4.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  82 EEFDVALKNakSKLVVAEFATSKSDQSNKIYPFMVELSRTCNDVVFLLVMGDESdktRELCRREKIEKVPHFSFYKSMEK 161
Cdd:cd02947   1 EEFEELIKS--AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDEN---PELAEEYGVRSIPTFLFFKNGKE 75

                        90
                ....*....|.
gi 15222954 162 IHEEEGIEPDQ 172
Cdd:cd02947  76 VDRVVGADPKE 86
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 219-289 1.09e-08

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: 51.85  E-value: 1.09e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222954   219 CGPCVKVYPTVLKLSRSMSETVVFARMNGDEN-DSCMEFlkdmNVIEVPTFLFIRDGEIRGRYVGS-GKGELI 289
Cdd:pfam00085  30 CGPCKMLAPEYEELAQEYKGNVVFAKVDVDENpDLASKY----GVRGYPTLIFFKNGQPVDDYVGArPKDALA 98
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 207-294 2.22e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.00  E-value: 2.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 207 GKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSEtVVFARMNGDEN-------------------DSCMEFLKDMNVIEVPT 267
Cdd:COG0526  28 GKPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDVDENpeavkaflkelglpypvllDPDGELAKAYGVRGIPT 106

                        90       100
                ....*....|....*....|....*...
gi 15222954 268 FLFI-RDGEIRGRYVGSGKGELIGEILR 294
Cdd:COG0526 107 TVLIdKDGKIVARHVGPLSPEELEEALE 134
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 205-282 2.64e-07

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: 48.05  E-value: 2.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222954   205 TGGKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSETVVFARMNGDEN-DSCMEFlkdmNVIEVPTFLFIRDGEIRGRYVG 282
Cdd:TIGR01068  12 SSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENpDIAAKY----GIRSIPTLLLFKNGKEVDRSVG 86
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 195-295 4.54e-06

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 45.67  E-value: 4.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 195 DVEKLIDENRTGGKLIVLDVGLKHCGPCVKVYPTVLK---LSRSMSETVVFARMNGDEND----------SCMEFLKDMN 261
Cdd:COG2143  28 DLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSdpeVAAYLKENFVVVQLDAEGDKevtdfdgetlTEKELARKYG 107

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15222954 262 VIEVPTFLFI-RDGEIRGRYVGSGKGELIGEILRY 295
Cdd:COG2143 108 VRGTPTLVFFdAEGKEIARIPGYLKPETFLALLKY 142
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 211-277 2.68e-05

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: 41.53  E-value: 2.68e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222954 211 VLDVGLKHCGPCVKVYPtVLKLSRSMSETVVFARMNGDENDSCMEFLKDMNVIEVPTFLFIRDGEIR 277
Cdd:cd01659   1 LVLFYAPWCPFCQALRP-VLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGV 66
PTZ00051 PTZ00051
thioredoxin; Provisional
 195-288 4.12e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 41.79  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  195 DVEKLIDENrtggKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSEtVVFARMNGDEndsCMEFLKDMNVIEVPTFLFIRDG 274
Cdd:PTZ00051  10 EFESTLSQN----ELVIVDFYAEWCGPCKRIAPFYEECSKEYTK-MVFVKVDVDE---LSEVAEKENITSMPTFKVFKNG 81

                         90
                 ....*....|....
gi 15222954  275 EIRGRYVGSGKGEL 288
Cdd:PTZ00051  82 SVVDTLLGANDEAL 95
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 197-283 7.70e-05

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: 41.17  E-value: 7.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 197 EKLIDENRTGGKLIVLDVGLKHCGPCVKVYPTVLKLSRSM-SETVVFARMNGDENDSCMEFLKDMNvievPTFLFIRDGE 275
Cdd:cd02948   7 QEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELgDDLLHFATAEADTIDTLKRYRGKCE----PTFLFYKNGE 82


                ....*...
gi 15222954 276 IRGRYVGS 283
Cdd:cd02948  83 LVAVIRGA 90
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 207-275 1.30e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 43.20  E-value: 1.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222954  207 GKLIVLDVGLKHCGPCVKVYPTVLKLSRSM--SETVVFARMNGDENDSCMEflkDMNVIEVPTFLFIRDGE 275
Cdd:PTZ00102 375 DKDVLLEIYAPWCGHCKNLEPVYNELGEKYkdNDSIIVAKMNGTANETPLE---EFSWSAFPTILFVKAGE 442
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 207-282 2.94e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 39.53  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 207 GKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSET-VVFARMNGDEN--------------------DSCMEFLKDMNVIEV 265
Cdd:cd02966  19 GKVVLVNFWASWCPPCRAEMPELEALAKEYKDDgVEVVGVNVDDDdpaavkaflkkygitfpvllDPDGELAKAYGVRGL 98

                        90
                ....*....|....*...
gi 15222954 266 PTFLFI-RDGEIRGRYVG 282
Cdd:cd02966  99 PTTFLIdRDGRIRARHVG 116
trxA PRK09381
thioredoxin TrxA;
209-288 8.03e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 38.51  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954  209 LIVLDVGLKHCGPCVKVYPTVLKLSRSMSETVVFARMNGDENDSCMeflKDMNVIEVPTFLFIRDGEIRGRYVGS-GKGE 287
Cdd:PRK09381  23 AILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTA---PKYGIRGIPTLLLFKNGEVAATKVGAlSKGQ 99


                 .
gi 15222954  288 L 288
Cdd:PRK09381 100 L 100
PTZ00051 PTZ00051
thioredoxin; Provisional
 75-158 9.43e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 37.93  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954   75 VQKIHSGEEFDVALknAKSKLVVAEFATSKSDQSNKIYPFMVELSRTCNDVVFLLVmgdESDKTRELCRREKIEKVPHFS 154
Cdd:PTZ00051   2 VHIVTSQAEFESTL--SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKV---DVDELSEVAEKENITSMPTFK 76


                 ....
gi 15222954  155 FYKS 158
Cdd:PTZ00051  77 VFKN 80
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 195-288 2.00e-03

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: 36.87  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222954 195 DVEKLIDENRTggKLIVLDVGLKHCGPCVKVYPTVLKLSRSMSETVVFARMNGDENDscmEFLKDMNVIEVPTFLFIRDG 274
Cdd:cd02984   4 EFEELLKSDAS--KLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELP---EISEKFEITAVPTFVFFRNG 78

                        90
                ....*....|....
gi 15222954 275 EIRGRYVGSGKGEL 288
Cdd:cd02984  79 TIVDRVSGADPKEL 92
 
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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