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Conserved domains on  [gi|817720408|ref|WP_046673718|]
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MULTISPECIES: co-chaperone YbbN [Sphingobacterium]

Protein Classification

thioredoxin family protein( domain architecture ID 11459707)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-71 2.02e-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: 51.74  E-value: 2.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817720408  12 CAPCAQVSAYLDQKGIQYET------VNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:COG3118   30 CGPCKMLAPVLEELAAEYGGkvkfvkVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE 95
 
Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-71 2.02e-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: 51.74  E-value: 2.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817720408  12 CAPCAQVSAYLDQKGIQYET------VNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:COG3118   30 CGPCKMLAPVLEELAAEYGGkvkfvkVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE 95
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 4-71 3.70e-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: 51.02  E-value: 3.70e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817720408  4 IIKFEKNDCAPCAQVSAYLDQ-----KGIQYETVNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:cd02947  14 VVDFWAPWCGPCKAIAPVLEElaeeyPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPKE 86
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 4-71 5.76e-10

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: 50.75  E-value: 5.76e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817720408    4 IIKFEKNDCAPCAQVSAYLDQKGIQYET------VNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:TIGR01068  18 LVDFWAPWCGPCKMIAPILEELAKEYEGkvkfvkLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKA 91
PRK10996 PRK10996
thioredoxin 2; Provisional
 12-57 1.32e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 40.05  E-value: 1.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 817720408  12 CAPC-------AQVSAylDQKG-IQYETVNPFDEPDLAARFKIRTVPTVIVLEN 57
Cdd:PRK10996  64 CGPCrnfapifEDVAA--ERSGkVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
7-75 1.46e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 34.32  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817720408    7 FEKNDCAPCAQ----------VSAYLDQKG-IQYETVNPFDEP-----------DLAARFKIRTVPTVIVLENEEIQHRI 64
Cdd:pfam13098  11 FTDPDCPYCKKlkkelledpdVTVYLGPNFvFIAVNIWCAKEVakaftdilenkELGRKYGVRGTPTIVFFDGKGELLRL 90

                          90
                  ....*....|..
gi 817720408   65 IGF-KPEELAAI 75
Cdd:pfam13098  91 PGYvPAEEFLAL 102
 
Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-71 2.02e-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: 51.74  E-value: 2.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817720408  12 CAPCAQVSAYLDQKGIQYET------VNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:COG3118   30 CGPCKMLAPVLEELAAEYGGkvkfvkVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE 95
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 4-71 3.70e-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: 51.02  E-value: 3.70e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817720408  4 IIKFEKNDCAPCAQVSAYLDQ-----KGIQYETVNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:cd02947  14 VVDFWAPWCGPCKAIAPVLEElaeeyPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPKE 86
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
7-74 4.06e-10

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 50.20  E-value: 4.06e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817720408  7 FEKNDCAPCAQVSAYLDQKGIQYETVN----PFDEPDLAARFKIRTVPTVIVleNEEIqhrIIGFKPEELAA 74
Cdd:COG0695   5 YTTPGCPYCARAKRLLDEKGIPYEEIDvdedPEAREELRERSGRRTVPVIFI--GGEH---LGGFDEGELDA 71
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 4-71 5.76e-10

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: 50.75  E-value: 5.76e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817720408    4 IIKFEKNDCAPCAQVSAYLDQKGIQYET------VNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:TIGR01068  18 LVDFWAPWCGPCKMIAPILEELAKEYEGkvkfvkLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKA 91
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 3-76 3.37e-09

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 47.99  E-value: 3.37e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817720408  3 RIIKFEKNDCAPCAQVSAYLDQKGIQYETVNPFDEPDLAARFK----IRTVPtVIVLENEeiqhRIIGFKPEELAAIA 76
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKklngYRSVP-VVVIGDE----HLSGFRPDKLRALL 73
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 10-72 6.65e-08

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 44.68  E-value: 6.65e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817720408  10 NDCAPCAQVSAYLDQKGIQYETV----NPFDEPDLAARFKIRTVPTVIVleNEEIqhrIIGFKPEEL 72
Cdd:TIGR02196  8 PWCPPCVKAKEYLTSKGVAFEEIdvekDAAAREELLKVYGQRGVPVIVI--GHKI---VVGFDPEKL 69
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 12-74 1.20e-05

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: 39.56  E-value: 1.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817720408 12 CAPCAQVSAYLDQ------KGIQYETVNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEELAA 74
Cdd:cd02984  26 AEPCKQMNQVFEElakeafPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSGADPKELAK 94
PRK10996 PRK10996
thioredoxin 2; Provisional
 12-57 1.32e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 40.05  E-value: 1.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 817720408  12 CAPC-------AQVSAylDQKG-IQYETVNPFDEPDLAARFKIRTVPTVIVLEN 57
Cdd:PRK10996  64 CGPCrnfapifEDVAA--ERSGkVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115
PRK10329 PRK10329
glutaredoxin-like protein NrdH;
3-53 2.40e-04

glutaredoxin-like protein NrdH;


Pssm-ID: 182381  Cd Length: 81  Bit Score: 36.04  E-value: 2.40e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 817720408  3 RIIKFEKNDCAPCAQVSAYLDQKGIQYETVNPFDEPDLAARFK---IRTVPTVI 53
Cdd:PRK10329  2 RITIYTRNDCVQCHATKRAMESRGFDFEMINVDRVPEAAETLRaqgFRQLPVVI 55
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 38-72 2.57e-04

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


Pssm-ID: 239287  Cd Length: 113  Bit Score: 36.40  E-value: 2.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817720408  38 PDLAARFKIRTVPTVIVLENEEIQHRIIGFkpEEL 72
Cdd:cd02989   65 PFLVEKLNIKVLPTVILFKNGKTVDRIVGF--EEL 97
trxA PRK09381
thioredoxin TrxA;
4-66 3.94e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 35.81  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817720408   4 IIKFEKNDCAPCAQVSAYLDQKGIQYE------TVNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIG 66
Cdd:PRK09381  25 LVDFWAEWCGPCKMIAPILDEIADEYQgkltvaKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVG 93
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
7-75 1.46e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 34.32  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817720408    7 FEKNDCAPCAQ----------VSAYLDQKG-IQYETVNPFDEP-----------DLAARFKIRTVPTVIVLENEEIQHRI 64
Cdd:pfam13098  11 FTDPDCPYCKKlkkelledpdVTVYLGPNFvFIAVNIWCAKEVakaftdilenkELGRKYGVRGTPTIVFFDGKGELLRL 90

                          90
                  ....*....|..
gi 817720408   65 IGF-KPEELAAI 75
Cdd:pfam13098  91 PGYvPAEEFLAL 102
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 4-67 2.21e-03

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


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 33.68  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817720408   4 IIKFEKNDCAPCAQVSAYLDQKGIQYETVN----PFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGF 67
Cdd:cd02957   28 VVHFYEPGFPRCKILDSHLEELAAKYPETKfvkiNAEKAFLVNYLDIKVLPTLLVYKNGELIDNIVGF 95
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 12-71 4.09e-03

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 33.01  E-value: 4.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817720408 12 CAPCAQVSAYLDQKGIQYE------TVNPFDEPDLAARFKIRTVPTVIVLENEEIQHRIIGFKPEE 71
Cdd:cd02956  24 SPPSKELLPLLERLAEEYQgqfvlaKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEE 89
 
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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