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Conserved domains on  [gi|239735607|ref|NP_660326|]
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nucleoredoxin-like protein 2 isoform 2 [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 10-104 1.26e-37

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02964:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 132  Bit Score: 124.26  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239735607  10 LVTCKGATVEAEAALQNKVVALYFAAARCAPSRDFTPLLCDFYTALVAEArrpAPFEVVFVSADGSSQEMLDFMRELHgA 89
Cdd:cd02964    1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEG---KNFEIVFVSRDRSEESFNEYFSEMP-P 76

                         90
                 ....*....|....*
gi 239735607  90 WLALPFHDPYRQRSL 104
Cdd:cd02964   77 WLAVPFEDEELRELL 91
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 10-104 1.26e-37

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: 124.26  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239735607  10 LVTCKGATVEAEAALQNKVVALYFAAARCAPSRDFTPLLCDFYTALVAEArrpAPFEVVFVSADGSSQEMLDFMRELHgA 89
Cdd:cd02964    1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEG---KNFEIVFVSRDRSEESFNEYFSEMP-P 76

                         90
                 ....*....|....*
gi 239735607  90 WLALPFHDPYRQRSL 104
Cdd:cd02964   77 WLAVPFEDEELRELL 91
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 26-101 5.93e-22

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: 83.13  E-value: 5.93e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239735607   26 NKVVALYFAAARCAPSRDFTPLLCDFYTALvaeaRRPAPFEVVFVSADGSSQEMLDFMRELHGAWLALPFHDPYRQ 101
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKL----KKKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERN 72
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 22-93 6.69e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.06  E-value: 6.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239735607  22 AALQNKVVALYFAAARCAPSRDFTPLLCDFYtalvaeaRRPAPFEVVFVSADGSSQEMLDFMRELHGAWLAL 93
Cdd:COG0526   24 ADLKGKPVLVNFWATWCPPCRAEMPVLKELA-------EEYGGVVFVGVDVDENPEAVKAFLKELGLPYPVL 88
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 10-104 1.26e-37

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: 124.26  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239735607  10 LVTCKGATVEAEAALQNKVVALYFAAARCAPSRDFTPLLCDFYTALVAEArrpAPFEVVFVSADGSSQEMLDFMRELHgA 89
Cdd:cd02964    1 LFLLDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEG---KNFEIVFVSRDRSEESFNEYFSEMP-P 76

                         90
                 ....*....|....*
gi 239735607  90 WLALPFHDPYRQRSL 104
Cdd:cd02964   77 WLAVPFEDEELRELL 91
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 26-101 5.93e-22

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: 83.13  E-value: 5.93e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239735607   26 NKVVALYFAAARCAPSRDFTPLLCDFYTALvaeaRRPAPFEVVFVSADGSSQEMLDFMRELHGAWLALPFHDPYRQ 101
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKL----KKKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERN 72
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 15-105 8.00e-19

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: 76.17  E-value: 8.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239735607  15 GATVEAEAaLQNKVVALYFAAARCAPSRDFTPLLCDFYTALvaeARRPAPFEVVFVSADGSSQEMLDFMRELhgAWLALP 94
Cdd:cd03009    8 GGKVPVSS-LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKL---KESGKNFEIVFISWDRDEESFNDYFSKM--PWLAVP 81

                         90
                 ....*....|.
gi 239735607  95 FHDPYRQRSLA 105
Cdd:cd03009   82 FSDRERRSRLN 92
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 19-110 1.22e-16

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: 71.00  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239735607  19 EAEAALQNKVVALYFAAARCAPSRDFTPLLCDFYTALVAEA--RRPAPFEVVFVSADGSSQEMLDFMRELHGAWLALPFH 96
Cdd:cd03008   18 EIVARLENRVLLLFFGAVVSPQCQLFAPKLKDFFVRLTDEFyvDRSAQLALVYVSMDQSEQQQESFLKDMPKKWLFLPFE 97

                         90
                 ....*....|....*....
gi 239735607  97 DPYR-----QRSLALLPRL 110
Cdd:cd03008   98 DEFRreleaQFSVEELPTV 116
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 22-93 6.69e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.06  E-value: 6.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239735607  22 AALQNKVVALYFAAARCAPSRDFTPLLCDFYtalvaeaRRPAPFEVVFVSADGSSQEMLDFMRELHGAWLAL 93
Cdd:COG0526   24 ADLKGKPVLVNFWATWCPPCRAEMPVLKELA-------EEYGGVVFVGVDVDENPEAVKAFLKELGLPYPVL 88
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 22-87 1.76e-03

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: 35.67  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239735607  22 AALQNKVVALYFAAARCAPSRDFTPLLCDFYtalvaEARRPAPFEVVFVSADGSS-QEMLDFMRELH 87
Cdd:cd02966   15 SDLKGKVVLVNFWASWCPPCRAEMPELEALA-----KEYKDDGVEVVGVNVDDDDpAAVKAFLKKYG 76
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
22-95 5.02e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 34.84  E-value: 5.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239735607  22 AALQNKVVALYFAAARCAPSRDFTPLLCDFYTALvaearRPAPFEVVFVSADgSSQEMLDFMRELHgawlaLPF 95
Cdd:COG1225   17 SDLRGKPVVLYFYATWCPGCTAELPELRDLYEEF-----KDKGVEVLGVSSD-SDEAHKKFAEKYG-----LPF 79
 
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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