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Conserved domains on  [gi|1972245634|ref|NP_001379738|]
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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 ...
 9-138 1.09e-52

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: 162.78  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634   9 LEKRDKTLVDATEALAGKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVVF---VSFDRSESDLKMYMSEHGDWYHI 85
Cdd:cd02964     1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEivfVSRDRSEESFNEYFSEMPPWLAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972245634  86 PYGNDAIKELSTK-YGVSGIPALIIVKPDGTEVTKDGRNDVQNgkDPKATVAKW 138
Cdd:cd02964    81 PFEDEELRELLEKqFKVEGIPTLVVLKPDGDVVTTNARDEVEE--DPGACAFPW 132
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 9-138 1.09e-52

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: 162.78  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634   9 LEKRDKTLVDATEALAGKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVVF---VSFDRSESDLKMYMSEHGDWYHI 85
Cdd:cd02964     1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEivfVSRDRSEESFNEYFSEMPPWLAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972245634  86 PYGNDAIKELSTK-YGVSGIPALIIVKPDGTEVTKDGRNDVQNgkDPKATVAKW 138
Cdd:cd02964    81 PFEDEELRELLEKqFKVEGIPTLVVLKPDGDVVTTNARDEVEE--DPGACAFPW 132
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 25-115 3.33e-23

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: 86.59  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  25 GKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVV--FVSFDRSESDLKMYMSE-HGDWYHIPYGNDAIKELSTKYGV 101
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEivFVSLDRDLEEFKDYLKKmPKDWLSVPFDDDERNELKRKYGV 80

                          90
                  ....*....|....
gi 1972245634 102 SGIPALIIVKPDGT 115
Cdd:pfam13905  81 NAIPTLVLLDPNGE 94
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 21-119 1.01e-14

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 66.25  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  21 EALAGKAVGFYFSAHWCPPCRGFTPILKDFYeEVEDEFEVVFVSFDRSESDLKMYMSEHGDWYhiPYGNDAIKELSTKYG 100
Cdd:COG0526    24 ADLKGKPVLVNFWATWCPPCRAEMPVLKELA-EEYGGVVFVGVDVDENPEAVKAFLKELGLPY--PVLLDPDGELAKAYG 100

                          90
                  ....*....|....*....
gi 1972245634 101 VSGIPALIIVKPDGTEVTK 119
Cdd:COG0526   101 VRGIPTTVLIDKDGKIVAR 119
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 32-138 3.94e-06

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: 42.66  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  32 FSAHWCPPCRGFTPILKDFYEevedefevvfvsfdrsesdlkmymSEHGDWYHIPYGNDAIKELSTKYGVSGIPALIIVK 111
Cdd:TIGR01068  21 FWAPWCGPCKMIAPILEELAK------------------------EYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76

                          90       100
                  ....*....|....*....|....*..
gi 1972245634 112 pDGTEVtkdgrnDVQNGKDPKATVAKW 138
Cdd:TIGR01068  77 -NGKEV------DRSVGALPKAALKQL 96
PRK10996 PRK10996
thioredoxin 2; Provisional
 32-138 6.25e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 40.05  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  32 FSAHWCPPCRGFTPILKDfyeevedefevvfvsfdrsesdlkMYMSEHGDWYHIPYGNDAIKELSTKYGVSGIPALIIVK 111
Cdd:PRK10996   59 FWAPWCGPCRNFAPIFED------------------------VAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                          90       100
                  ....*....|....*....|....*..
gi 1972245634 112 pDGTEVtkdgrnDVQNGKDPKATVAKW 138
Cdd:PRK10996  115 -NGQVV------DMLNGAVPKAPFDSW 134
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 9-138 1.09e-52

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: 162.78  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634   9 LEKRDKTLVDATEALAGKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVVF---VSFDRSESDLKMYMSEHGDWYHI 85
Cdd:cd02964     1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEivfVSRDRSEESFNEYFSEMPPWLAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972245634  86 PYGNDAIKELSTK-YGVSGIPALIIVKPDGTEVTKDGRNDVQNgkDPKATVAKW 138
Cdd:cd02964    81 PFEDEELRELLEKqFKVEGIPTLVVLKPDGDVVTTNARDEVEE--DPGACAFPW 132
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 21-122 6.86e-34

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: 115.08  E-value: 6.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  21 EALAGKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVVF---VSFDRSESDLKMYMSEHgDWYHIPYGNDAIKE-LS 96
Cdd:cd03009    14 SSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEivfISWDRDEESFNDYFSKM-PWLAVPFSDRERRSrLN 92

                          90       100
                  ....*....|....*....|....*.
gi 1972245634  97 TKYGVSGIPALIIVKPDGTEVTKDGR 122
Cdd:cd03009    93 RTFKIEGIPTLIILDADGEVVTTDAR 118
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 25-115 3.33e-23

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: 86.59  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  25 GKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVV--FVSFDRSESDLKMYMSE-HGDWYHIPYGNDAIKELSTKYGV 101
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEivFVSLDRDLEEFKDYLKKmPKDWLSVPFDDDERNELKRKYGV 80

                          90
                  ....*....|....
gi 1972245634 102 SGIPALIIVKPDGT 115
Cdd:pfam13905  81 NAIPTLVLLDPNGE 94
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 21-119 1.01e-14

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 66.25  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  21 EALAGKAVGFYFSAHWCPPCRGFTPILKDFYeEVEDEFEVVFVSFDRSESDLKMYMSEHGDWYhiPYGNDAIKELSTKYG 100
Cdd:COG0526    24 ADLKGKPVLVNFWATWCPPCRAEMPVLKELA-EEYGGVVFVGVDVDENPEAVKAFLKELGLPY--PVLLDPDGELAKAYG 100

                          90
                  ....*....|....*....
gi 1972245634 101 VSGIPALIIVKPDGTEVTK 119
Cdd:COG0526   101 VRGIPTTVLIDKDGKIVAR 119
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 20-114 1.78e-13

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: 62.32  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  20 TEALAGKAVGFYFSAHWCPPCRGFTPILKDFyeevedefevvfvSFD--------RSESDLKM--YMSEHGdwYHIPYGN 89
Cdd:cd03011    15 LESLSGKPVLVYFWATWCPVCRFTSPTVNQL-------------AADypvvsvalRSGDDGAVarFMQKKG--YGFPVIN 79

                          90       100
                  ....*....|....*....|....*
gi 1972245634  90 DAIKELSTKYGVSGIPALIIVKPDG 114
Cdd:cd03011    80 DPDGVISARWGVSVTPAIVIVDPGG 104
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 21-126 8.22e-12

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: 58.68  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  21 EALAGKAVGFYFSAHWCPPCRGFTPILKDF--------YEEVEDEFEVVFVSFDRSESDLKMYMSEH-GDWYHIPYGNDA 91
Cdd:cd03008    21 ARLENRVLLLFFGAVVSPQCQLFAPKLKDFfvrltdefYVDRSAQLALVYVSMDQSEQQQESFLKDMpKKWLFLPFEDEF 100

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972245634  92 IKELSTKYGVSGIPALIIVKPDGTEVTKDGRNDVQ 126
Cdd:cd03008   101 RRELEAQFSVEELPTVVVLKPDGDVLAANAVDEIL 135
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 20-119 3.01e-10

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: 53.78  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  20 TEALAGKAVGFYFSAHWCPPCRGFTPILKDFYeevedeFEVVFVSF--------DRSESDLKMYMSEHGdwYHIPYGNDA 91
Cdd:cd02966    14 LSDLKGKVVLVNFWASWCPPCRAEMPELEALA------KEYKDDGVevvgvnvdDDDPAAVKAFLKKYG--ITFPVLLDP 85

                          90       100
                  ....*....|....*....|....*...
gi 1972245634  92 IKELSTKYGVSGIPALIIVKPDGTEVTK 119
Cdd:cd02966    86 DGELAKAYGVRGLPTTFLIDRDGRIRAR 113
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 24-138 1.04e-09

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: 52.13  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  24 AGKAVGFYFSAHWCPPCRGFTPILKDFyeevedefevvfvsfdrsesdlkmyMSEHGDWYHIPYGN-DAIKELSTKYGVS 102
Cdd:COG3118    17 SDKPVLVDFWAPWCGPCKMLAPVLEEL-------------------------AAEYGGKVKFVKVDvDENPELAAQFGVR 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1972245634 103 GIPALIIVKpDGTEVtkdgrnDVQNGKDPKATVAKW 138
Cdd:COG3118    72 SIPTLLLFK-DGQPV------DRFVGALPKEQLREF 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 20-138 1.12e-08

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: 49.09  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  20 TEALAGKAVGFYFSAHWCPPCRGFTPILKDFyeevedefevvfvsfdrsesdlkmyMSEHGD--WYHIpygN-DAIKELS 96
Cdd:cd02947     5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEEL-------------------------AEEYPKvkFVKV---DvDENPELA 56

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1972245634  97 TKYGVSGIPALIIVKpDGTEVtkdgrnDVQNGKDPKATVAKW 138
Cdd:cd02947    57 EEYGVRSIPTFLFFK-NGKEV------DRVVGADPKEELEEF 91
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
15-115 3.01e-08

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 49.09  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  15 TLVDAT------EALAGKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVVFV-SFDRSESdLKMYMSEHGdwYHIPY 87
Cdd:COG1225     5 TLPDLDgktvslSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGvSSDSDEA-HKKFAEKYG--LPFPL 81

                          90       100
                  ....*....|....*....|....*...
gi 1972245634  88 GNDAIKELSTKYGVSGIPALIIVKPDGT 115
Cdd:COG1225    82 LSDPDGEVAKAYGVRGTPTTFLIDPDGK 109
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 32-138 3.94e-06

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: 42.66  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  32 FSAHWCPPCRGFTPILKDFYEevedefevvfvsfdrsesdlkmymSEHGDWYHIPYGNDAIKELSTKYGVSGIPALIIVK 111
Cdd:TIGR01068  21 FWAPWCGPCKMIAPILEELAK------------------------EYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76

                          90       100
                  ....*....|....*....|....*..
gi 1972245634 112 pDGTEVtkdgrnDVQNGKDPKATVAKW 138
Cdd:TIGR01068  77 -NGKEV------DRSVGALPKAALKQL 96
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 16-115 5.82e-06

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: 43.61  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  16 LVDATEALAGKAVGFYFSAHWCPPCRGFTPILKDFYEEVEDEFEVVFVsfDRSESDLKMyMSEHGDWYHIpYGNDAIKEL 95
Cdd:TIGR00385  54 FYTADVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQGLPIVGVDYK--DDRQNAIKF-LKELGNPYQL-SLFDPDGML 129

                          90       100
                  ....*....|....*....|
gi 1972245634  96 STKYGVSGIPALIIVKPDGT 115
Cdd:TIGR00385 130 GLDLGVYGAPETFLVDGNGV 149
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 3-119 5.58e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 40.27  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634   3 LLAGVKLEKRDKTLVDATEALA-----GKAVGFYFSAHWCPPCRgftpILKDFYeevedefevvfvsFDRSEsdLKMYMS 77
Cdd:COG2143    13 LLAAAAAAQEISFLLDLEEDLAlakaeGKPILLFFESDWCPYCK----KLHKEV-------------FSDPE--VAAYLK 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972245634  78 EHGDWYHI-PYGNDAI----------KELSTKYGVSGIPALIIVKPDGTEVTK 119
Cdd:COG2143    74 ENFVVVQLdAEGDKEVtdfdgetlteKELARKYGVRGTPTLVFFDAEGKEIAR 126
PRK10996 PRK10996
thioredoxin 2; Provisional
 32-138 6.25e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 40.05  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  32 FSAHWCPPCRGFTPILKDfyeevedefevvfvsfdrsesdlkMYMSEHGDWYHIPYGNDAIKELSTKYGVSGIPALIIVK 111
Cdd:PRK10996   59 FWAPWCGPCRNFAPIFED------------------------VAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                          90       100
                  ....*....|....*....|....*..
gi 1972245634 112 pDGTEVtkdgrnDVQNGKDPKATVAKW 138
Cdd:PRK10996  115 -NGQVV------DMLNGAVPKAPFDSW 134
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 21-116 3.36e-04

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 39.02  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  21 EALA-GKAVGFYFSAHWCPPCRgftpilkdfyeevedefevvfvSFDR---SESDLKMYMSEH-----GDWYHipyGNDA 91
Cdd:COG4232   315 EARAeGKPVFVDFTADWCVTCK----------------------ENERtvfSDPEVQAALADDvvllkADVTD---NDPE 369

                          90       100
                  ....*....|....*....|....*
gi 1972245634  92 IKELSTKYGVSGIPALIIVKPDGTE 116
Cdd:COG4232   370 ITALLKRFGRFGVPTYVFYDPDGEE 394
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
23-119 1.64e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 36.52  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  23 LAGKAVGFYFSAHWCPPCRGFTPILKDFYEE-VEDEFEVVFVSFDRSESDLKMYMSEHGDWYHIPYgnDAIKELSTKYGV 101
Cdd:PRK03147   59 LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKyKEKGVEIIAVNVDETELAVKNFVNRYGLTFPVAI--DKGRQVIDAYGV 136

                          90
                  ....*....|....*...
gi 1972245634 102 SGIPALIIVKPDGtEVTK 119
Cdd:PRK03147  137 GPLPTTFLIDKDG-KVVK 153
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 21-114 3.38e-03

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 34.89  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  21 EALA-GKAVGFYFSAHWCPPCrgftpilKDFYEEvedefevvfvSFDRSE--SDLKM---YMseHGDWYHipyGNDAIKE 94
Cdd:cd02953     6 QALAqGKPVFVDFTADWCVTC-------KVNEKV----------VFSDPEvqAALKKdvvLL--RADWTK---NDPEITA 63

                          90       100
                  ....*....|....*....|
gi 1972245634  95 LSTKYGVSGIPALIIVKPDG 114
Cdd:cd02953    64 LLKRFGVFGPPTYLFYGPGG 83
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 13-50 3.45e-03

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 34.94  E-value: 3.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1972245634  13 DKTLVDATealAGKAVGFYfsAHWCPPCRGFTPILKDF 50
Cdd:cd02992    12 NSALLGSP---SAWLVEFY--ASWCGHCRAFAPTWKKL 44
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 22-115 8.76e-03

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: 34.12  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972245634  22 ALAGKAVGFYF-SAHWCPPCRGFTPILKDFYEEVEDEFEVVFV-SFDRSESdLKMYMSEHGDWYhiPYGNDAIKELSTKY 99
Cdd:pfam00578  22 DYRGKWVVLFFyPADWTPVCTTELPALADLYEEFKKLGVEVLGvSVDSPES-HKAFAEKYGLPF--PLLSDPDGEVARAY 98

                          90       100
                  ....*....|....*....|..
gi 1972245634 100 GV------SGIPALIIVKPDGT 115
Cdd:pfam00578  99 GVlneeegGALRATFVIDPDGK 120
 
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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