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Conserved domains on  [gi|17535459|ref|NP_496200|]
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protein-disulfide reductase [Caenorhabditis elegans]

Protein Classification

thioredoxin family protein( domain architecture ID 10121823)

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; similar to human nucleoredoxin-like protein 2 that may be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|30367780
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 12-144 2.50e-57

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


:

Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 174.72  E-value: 2.50e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  12 NQDSEELDAGEHLKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKHPEFEVVFVSRDREDGDLREYFLEhMGAWTAIP 91
Cdd:cd02964   3 LLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSE-MPPWLAVP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17535459  92 FGTPRIQELLE-QYEVKTIPSMRIVKPNGDVVVQDARTEIQDkgnDPEALWEEW 144
Cdd:cd02964  82 FEDEELRELLEkQFKVEGIPTLVVLKPDGDVVTTNARDEVEE---DPGACAFPW 132
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 12-144 2.50e-57

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 174.72  E-value: 2.50e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  12 NQDSEELDAGEHLKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKHPEFEVVFVSRDREDGDLREYFLEhMGAWTAIP 91
Cdd:cd02964   3 LLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSE-MPPWLAVP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17535459  92 FGTPRIQELLE-QYEVKTIPSMRIVKPNGDVVVQDARTEIQDkgnDPEALWEEW 144
Cdd:cd02964  82 FEDEELRELLEkQFKVEGIPTLVVLKPDGDVVTTNARDEVEE---DPGACAFPW 132
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 26-121 7.52e-32

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 108.93  E-value: 7.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459    26 GKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKHPeFEVVFVSRDREDGDLREYFLEHMGAWTAIPFGTPRIQELLEQYE 105
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKN-VEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*.
gi 17535459   106 VKTIPSMRIVKPNGDV 121
Cdd:pfam13905  80 VNAIPTLVLLDPNGEV 95
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 9-146 7.30e-19

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 77.04  E-value: 7.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   9 KLINQDSEELDAGEhLKGKVVGLYFSASWCPPCRQFTPKLtrffDEIRKKHPEFEVVFVSRDREDGDLREYFLEHMGAWt 88
Cdd:COG0526  12 TLTDLDGKPLSLAD-LKGKPVLVNFWATWCPPCRAEMPVL----KELAEEYGGVVFVGVDVDENPEAVKAFLKELGLPY- 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17535459  89 aiPFGTPRIQELLEQYEVKTIPSMRIVKPNGDVVVQDArteiqdkGNDPEALWEEWLA 146
Cdd:COG0526  86 --PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHV-------GPLSPEELEEALE 134
PTZ00051 PTZ00051
thioredoxin; Provisional
 28-122 3.06e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 46.02  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   28 VVGLYFSASWCPPCRQFTPkltrFFDEIRKKHPefEVVFVSRDREDgdlreyflehmgawtaipfgtprIQELLEQYEVK 107
Cdd:PTZ00051  20 LVIVDFYAEWCGPCKRIAP----FYEECSKEYT--KMVFVKVDVDE-----------------------LSEVAEKENIT 70

                         90
                 ....*....|....*
gi 17535459  108 TIPSMRIVKpNGDVV 122
Cdd:PTZ00051  71 SMPTFKVFK-NGSVV 84
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 18-85 4.47e-03

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 35.52  E-value: 4.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535459    18 LDAGEHLKGKVVGLYFSASWCPPCRQFTPKLTrffdEIRKKhpEFEVVFVS-RDREDGDLReyFLEHMG 85
Cdd:TIGR00385  55 YTADVLTQGKPVLLNVWASWCPPCRAEHPYLN----ELAKQ--GLPIVGVDyKDDRQNAIK--FLKELG 115
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 12-144 2.50e-57

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 174.72  E-value: 2.50e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  12 NQDSEELDAGEHLKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKHPEFEVVFVSRDREDGDLREYFLEhMGAWTAIP 91
Cdd:cd02964   3 LLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSE-MPPWLAVP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17535459  92 FGTPRIQELLE-QYEVKTIPSMRIVKPNGDVVVQDARTEIQDkgnDPEALWEEW 144
Cdd:cd02964  82 FEDEELRELLEkQFKVEGIPTLVVLKPDGDVVTTNARDEVEE---DPGACAFPW 132
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 8-136 1.62e-39

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 129.71  E-value: 1.62e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   8 TKLINQDSEELDAGEhLKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKHPEFEVVFVSRDREDGDLREYFLEhMgAW 87
Cdd:cd03009   1 DFLLRNDGGKVPVSS-LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFNDYFSK-M-PW 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17535459  88 TAIPFGT-PRIQELLEQYEVKTIPSMRIVKPNGDVVVQDARTEIQDKGND 136
Cdd:cd03009  78 LAVPFSDrERRSRLNRTFKIEGIPTLIILDADGEVVTTDARELVLEYGAD 127
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 26-121 7.52e-32

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 108.93  E-value: 7.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459    26 GKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKHPeFEVVFVSRDREDGDLREYFLEHMGAWTAIPFGTPRIQELLEQYE 105
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKN-VEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*.
gi 17535459   106 VKTIPSMRIVKPNGDV 121
Cdd:pfam13905  80 VNAIPTLVLLDPNGEV 95
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 9-146 7.30e-19

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 77.04  E-value: 7.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   9 KLINQDSEELDAGEhLKGKVVGLYFSASWCPPCRQFTPKLtrffDEIRKKHPEFEVVFVSRDREDGDLREYFLEHMGAWt 88
Cdd:COG0526  12 TLTDLDGKPLSLAD-LKGKPVLVNFWATWCPPCRAEMPVL----KELAEEYGGVVFVGVDVDENPEAVKAFLKELGLPY- 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17535459  89 aiPFGTPRIQELLEQYEVKTIPSMRIVKPNGDVVVQDArteiqdkGNDPEALWEEWLA 146
Cdd:COG0526  86 --PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHV-------GPLSPEELEEALE 134
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 12-142 2.19e-17

Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity.


Pssm-ID: 239306  Cd Length: 146  Bit Score: 73.70  E-value: 2.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  12 NQDSEELDA----GEHLKGKVVGLYFSASWCPPCRQFTPKLTRFF----DEIR-KKHPEFEVVFVSRDREDGDLrEYFLE 82
Cdd:cd03008   7 NSDRDELDTereiVARLENRVLLLFFGAVVSPQCQLFAPKLKDFFvrltDEFYvDRSAQLALVYVSMDQSEQQQ-ESFLK 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535459  83 HM-GAWTAIPFGTPRIQELLEQYEVKTIPSMRIVKPNGDVVVQDARTEIQDKGNDPEALWE 142
Cdd:cd03008  86 DMpKKWLFLPFEDEFRRELEAQFSVEELPTVVVLKPDGDVLAANAVDEILRLGPACFRNWQ 146
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 22-124 1.91e-14

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: 64.95  E-value: 1.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  22 EHLKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKhpEFEVVFVS-RDREDGDLREyFLEHMGAwtAIPFGTPRIQEL 100
Cdd:cd02966  15 SDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDD--GVEVVGVNvDDDDPAAVKA-FLKKYGI--TFPVLLDPDGEL 89

                        90       100
                ....*....|....*....|....
gi 17535459 101 LEQYEVKTIPSMRIVKPNGDVVVQ 124
Cdd:cd02966  90 AKAYGVRGLPTTFLIDRDGRIRAR 113
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
24-122 1.61e-12

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 60.65  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  24 LKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKhpEFEVVFVSRDREDgDLREyFLEHMGawtaIPFgtpRI-----Q 98
Cdd:COG1225  19 LRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDK--GVEVLGVSSDSDE-AHKK-FAEKYG----LPF---PLlsdpdG 87

                        90       100
                ....*....|....*....|....
gi 17535459  99 ELLEQYEVKTIPSMRIVKPNGDVV 122
Cdd:COG1225  88 EVAKAYGVRGTPTTFLIDPDGKIR 111
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 16-122 6.94e-11

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: 55.26  E-value: 6.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  16 EELDAgEHLKGKVVGLYFSASWCPPCRQFTPKltrfFDEIRKKHPEFEVVFVSRDREdgdlreyflehmgawtaipfgtp 95
Cdd:cd02947   1 EEFEE-LIKSAKPVVVDFWAPWCGPCKAIAPV----LEELAEEYPKVKFVKVDVDEN----------------------- 52

                        90       100
                ....*....|....*....|....*..
gi 17535459  96 riQELLEQYEVKTIPSMRIVKpNGDVV 122
Cdd:cd02947  53 --PELAEEYGVRSIPTFLFFK-NGKEV 76
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 9-146 3.80e-08

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: 48.28  E-value: 3.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   9 KLINQDSEELDAGEHLKGKVVGLYFSASWCPPCRQFTPKLtrffDEIRKKH-PEFEVVFVSRDREdgdlreyflehmgaw 87
Cdd:COG3118   1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVL----EELAAEYgGKVKFVKVDVDEN--------------- 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17535459  88 taipfgtpriQELLEQYEVKTIPSMRIVKpNGDVVvqdARTEiqdkGNDPEALWEEWLA 146
Cdd:COG3118  62 ----------PELAAQFGVRSIPTLLLFK-DGQPV---DRFV----GALPKEQLREFLD 102
PTZ00051 PTZ00051
thioredoxin; Provisional
 28-122 3.06e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 46.02  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   28 VVGLYFSASWCPPCRQFTPkltrFFDEIRKKHPefEVVFVSRDREDgdlreyflehmgawtaipfgtprIQELLEQYEVK 107
Cdd:PTZ00051  20 LVIVDFYAEWCGPCKRIAP----FYEECSKEYT--KMVFVKVDVDE-----------------------LSEVAEKENIT 70

                         90
                 ....*....|....*
gi 17535459  108 TIPSMRIVKpNGDVV 122
Cdd:PTZ00051  71 SMPTFKVFK-NGSVV 84
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 14-123 3.85e-07

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 46.14  E-value: 3.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  14 DSEELDaGEHLKGKVVGLYFSASWCPPCRQFTPKLTRFFDeirkkhpEFEVVFVS-RDREDGDLREYFLEHMGAWTAI-- 90
Cdd:cd03011   9 DGEQFD-LESLSGKPVLVYFWATWCPVCRFTSPTVNQLAA-------DYPVVSVAlRSGDDGAVARFMQKKGYGFPVInd 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17535459  91 PFGTpriqeLLEQYEVKTIPSMRIVKPNGDVVV 123
Cdd:cd03011  81 PDGV-----ISARWGVSVTPAIVIVDPGGIVFV 108
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
16-129 2.67e-05

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 41.91  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   16 EELDAGEH----LKGKVVGLYFSASWCPPCRQFTPKLTRFFDEIRKKhpEFEVVFVSRDREDGDLREyFLEHMGawTAIP 91
Cdd:PRK03147  47 TDLEGKKIelkdLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEK--GVEIIAVNVDETELAVKN-FVNRYG--LTFP 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 17535459   92 FGTPRIQELLEQYEVKTIPSMRIVKPNGDV--VVQDARTE 129
Cdd:PRK03147 122 VAIDKGRQVIDAYGVGPLPTTFLIDKDGKVvkVITGEMTE 161
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 9-73 5.50e-05

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 40.29  E-value: 5.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17535459     9 KLINQDSEELDAGEhLKGKVVGLYF-SASWCPPCRQFTPKLTRFFDEIRKKhpEFEVVFVSRDRED 73
Cdd:pfam00578   9 ELPDGDGGTVSLSD-YRGKWVVLFFyPADWTPVCTTELPALADLYEEFKKL--GVEVLGVSVDSPE 71
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 1-85 1.09e-04

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 39.48  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   1 MSELLAGTKLINQDSeeldagehLKGKVVGLYFSASWCPPCRQFTPKLTRFfdeirKKHPEFEVVFVS-RDREDGDLRey 79
Cdd:cd03010   8 LPALPGPDKTLTSAD--------LKGKPYLLNVWASWCAPCREEHPVLMAL-----ARQGRVPIYGINyKDNPENALA-- 72


                ....*.
gi 17535459  80 FLEHMG 85
Cdd:cd03010  73 WLARHG 78
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 27-122 3.50e-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: 37.64  E-value: 3.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459  27 KVVGLYFSASWCPPCRQFtpklTRFFDEIRKKHPEfEVVFVSRDREdgdlreyflehmgawtAIPfgtpriqELLEQYEV 106
Cdd:cd02984  15 KLLVLHFWAPWAEPCKQM----NQVFEELAKEAFP-SVLFLSIEAE----------------ELP-------EISEKFEI 66

                        90
                ....*....|....*.
gi 17535459 107 KTIPSMRIVKpNGDVV 122
Cdd:cd02984  67 TAVPTFVFFR-NGTIV 81
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 9-68 1.01e-03

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 37.35  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535459     9 KLINQDSEELDAGEhLKGKVVGLYFSAS-WCPPCRQFTPKLTRFFDEIRKKhpEFEVVFVS 68
Cdd:pfam08534  12 PDAATDGNTVSLSD-FKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEK--GVDVVAVN 69
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
25-121 1.05e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 36.63  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459    25 KGKVVGLYFSASWCPPCRQFTPKLTRfFDEIRKK-HPEFEVVFVSRDREDgdlreyflEHMGAWTaipfGTPRIQELLEQ 103
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKLKKELLE-DPDVTVYlGPNFVFIAVNIWCAK--------EVAKAFT----DILENKELGRK 69

                          90
                  ....*....|....*...
gi 17535459   104 YEVKTIPSMRIVKPNGDV 121
Cdd:pfam13098  70 YGVRGTPTIVFFDGKGEL 87
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 9-106 2.23e-03

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 36.04  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   9 KLINQDSEELDAgEHLKGKVVGLYFSASWCP-PCRQFTPKLTRFFDEIRKKH-PEFEVVFVSRD--REDGD-LREYfLEH 83
Cdd:cd02968   6 TLTDQDGRPVTL-SDLKGKPVLVYFGYTHCPdVCPTTLANLAQALKQLGADGgDDVQVVFISVDpeRDTPEvLKAY-AKA 83

                        90       100
                ....*....|....*....|....
gi 17535459  84 MGA-WTAIPFGTPRIQELLEQYEV 106
Cdd:cd02968  84 FGPgWIGLTGTPEEIEALAKAFGV 107
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 9-106 2.28e-03

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 36.42  E-value: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535459   9 KLINQDSEELDAGEhLKGKVVGLYFSASWCP-PCRQFTPKLTRFFDEIRKKHPE-FEVVFVS----RDREDgDLREYfLE 82
Cdd:COG1999   4 TLTDQDGKPVTLAD-LRGKPVLVFFGYTSCPdVCPTTLANLAQVQEALGEDGGDdVQVLFISvdpeRDTPE-VLKAY-AE 80

                        90       100
                ....*....|....*....|....*..
gi 17535459  83 HMGA--WTAIpFGTP-RIQELLEQYEV 106
Cdd:COG1999  81 AFGAprWIGL-TGDPeEIAALAKAFGV 106
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 18-85 4.47e-03

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 35.52  E-value: 4.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535459    18 LDAGEHLKGKVVGLYFSASWCPPCRQFTPKLTrffdEIRKKhpEFEVVFVS-RDREDGDLReyFLEHMG 85
Cdd:TIGR00385  55 YTADVLTQGKPVLLNVWASWCPPCRAEHPYLN----ELAKQ--GLPIVGVDyKDDRQNAIK--FLKELG 115
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 33-51 5.03e-03

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 34.57  E-value: 5.03e-03
                        10
                ....*....|....*....
gi 17535459  33 FSASWCPPCRQFTPKLTRF 51
Cdd:cd03004  26 FYAPWCGPCQALLPELRKA 44
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 31-78 8.34e-03

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: 33.44  E-value: 8.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17535459  31 LYFSASWCPPCRQFTPKLtrffDEIRKKHPEFEVVFVSRDREDGDLRE 78
Cdd:cd01659   2 VLFYAPWCPFCQALRPVL----AELALLNKGVKFEAVDVDEDPALEKE 45
 
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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