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Conserved domains on  [gi|471218818|ref|XP_004023944|]
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hypothetical protein IMG5_202410 [Ichthyophthirius multifiliis]

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 ...
 21-148 2.77e-45

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: 144.68  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  21 LGKNGLLDVTPLKtNKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKVLEIILIPFDITEEEFKTYYKQM-PWLAIPL 99
Cdd:cd02964    4 LDGEGVVPVSALE-GKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEMpPWLAVPF 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 471218818 100 GDERIKKF-TSYFKIKAIPKLIILKPNGEAAATNGRMDVIQEGEDAFNKW 148
Cdd:cd02964   83 EDEELRELlEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDPGACAFPW 132
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 21-148 2.77e-45

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: 144.68  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  21 LGKNGLLDVTPLKtNKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKVLEIILIPFDITEEEFKTYYKQM-PWLAIPL 99
Cdd:cd02964    4 LDGEGVVPVSALE-GKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEMpPWLAVPF 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 471218818 100 GDERIKKF-TSYFKIKAIPKLIILKPNGEAAATNGRMDVIQEGEDAFNKW 148
Cdd:cd02964   83 EDEELRELlEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDPGACAFPW 132
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 35-127 3.33e-30

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: 105.08  E-value: 3.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818   35 NKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKVlEIILIPFDITEEEFKTYYKQMP--WLAIPLGDERIKKFTSYFK 112
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNV-EIVFVSLDRDLEEFKDYLKKMPkdWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*
gi 471218818  113 IKAIPKLIILKPNGE 127
Cdd:pfam13905  80 VNAIPTLVLLDPNGE 94
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-136 3.28e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.00  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  36 KVTCLYFSASYCPPCQAFTPLLIDFYNEinMEDkvLEIILIPFDITEEEFKTYYKQMPwLAIPLGDERIKKFTSYFKIKA 115
Cdd:COG0526   29 KPVLVNFWATWCPPCRAEMPVLKELAEE--YGG--VVFVGVDVDENPEAVKAFLKELG-LPYPVLLDPDGELAKAYGVRG 103

                         90       100
                 ....*....|....*....|..
gi 471218818 116 IPKLIILKPNG-EAAATNGRMD 136
Cdd:COG0526  104 IPTTVLIDKDGkIVARHVGPLS 125
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 21-148 2.77e-45

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: 144.68  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  21 LGKNGLLDVTPLKtNKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKVLEIILIPFDITEEEFKTYYKQM-PWLAIPL 99
Cdd:cd02964    4 LDGEGVVPVSALE-GKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFVSRDRSEESFNEYFSEMpPWLAVPF 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 471218818 100 GDERIKKF-TSYFKIKAIPKLIILKPNGEAAATNGRMDVIQEGEDAFNKW 148
Cdd:cd02964   83 EDEELRELlEKQFKVEGIPTLVVLKPDGDVVTTNARDEVEEDPGACAFPW 132
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 21-145 1.54e-41

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: 135.11  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  21 LGKNGllDVTPLKT--NKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKVLEIILIPFDITEEEFKTYYKQMPWLAIP 98
Cdd:cd03009    4 LRNDG--GKVPVSSleGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKNFEIVFISWDRDEESFNDYFSKMPWLAVP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 471218818  99 LGD-ERIKKFTSYFKIKAIPKLIILKPNGEAAATNGRMDVIQEGEDAF 145
Cdd:cd03009   82 FSDrERRSRLNRTFKIEGIPTLIILDADGEVVTTDARELVLEYGADAF 129
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 35-127 3.33e-30

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: 105.08  E-value: 3.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818   35 NKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKVlEIILIPFDITEEEFKTYYKQMP--WLAIPLGDERIKKFTSYFK 112
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNV-EIVFVSLDRDLEEFKDYLKKMPkdWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*
gi 471218818  113 IKAIPKLIILKPNGE 127
Cdd:pfam13905  80 VNAIPTLVLLDPNGE 94
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 35-149 6.96e-21

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: 82.94  E-value: 6.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  35 NKVTCLYFSASYCPPCQAFTPLLIDFYNEINMEDKV-----LEIILIPFDITEEEFKTYYKQMP--WLAIPLGDERIKKF 107
Cdd:cd03008   25 NRVLLLFFGAVVSPQCQLFAPKLKDFFVRLTDEFYVdrsaqLALVYVSMDQSEQQQESFLKDMPkkWLFLPFEDEFRREL 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 471218818 108 TSYFKIKAIPKLIILKPNGEAAATNGRMDVIQEGEDAFNKWK 149
Cdd:cd03008  105 EAQFSVEELPTVVVLKPDGDVLAANAVDEILRLGPACFRNWQ 146
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-136 3.28e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.00  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  36 KVTCLYFSASYCPPCQAFTPLLIDFYNEinMEDkvLEIILIPFDITEEEFKTYYKQMPwLAIPLGDERIKKFTSYFKIKA 115
Cdd:COG0526   29 KPVLVNFWATWCPPCRAEMPVLKELAEE--YGG--VVFVGVDVDENPEAVKAFLKELG-LPYPVLLDPDGELAKAYGVRG 103

                         90       100
                 ....*....|....*....|..
gi 471218818 116 IPKLIILKPNG-EAAATNGRMD 136
Cdd:COG0526  104 IPTTVLIDKDGkIVARHVGPLS 125
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 36-127 1.36e-07

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: 47.23  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  36 KVTCLYFSASYCPPCQAFTPLLIDFYNEinMEDKVLEIILIPFDI-TEEEFKTYYKQMPwLAIPLGDERIKKFTSYFKIK 114
Cdd:cd02966   20 KVVLVNFWASWCPPCRAEMPELEALAKE--YKDDGVEVVGVNVDDdDPAAVKAFLKKYG-ITFPVLLDPDGELAKAYGVR 96

                         90
                 ....*....|...
gi 471218818 115 AIPKLIILKPNGE 127
Cdd:cd02966   97 GLPTTFLIDRDGR 109
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
36-147 1.21e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 42.54  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  36 KVTCLYFSASYCPPCQAFTPLLIDFYNEInmEDKVLEIILIPFDITEE--EFKTYYKqMPWlaiPLG-DERiKKFTSYFK 112
Cdd:COG1225   22 KPVVLYFYATWCPGCTAELPELRDLYEEF--KDKGVEVLGVSSDSDEAhkKFAEKYG-LPF---PLLsDPD-GEVAKAYG 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 471218818 113 IKAIPKLIILKPNGE-AAATNGRMDVIQEGEDAFNK 147
Cdd:COG1225   95 VRGTPTTFLIDPDGKiRYVWVGPVDPRPHLEEVLEA 130
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 32-131 5.24e-05

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: 40.19  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  32 LKTNKVTCLYFSASYCPPCQAFTPLLIDFYNEinMEDKVLeIILIpfDITEEefktyykqmPWLAiplgderikkftSYF 111
Cdd:COG3118   15 LESDKPVLVDFWAPWCGPCKMLAPVLEELAAE--YGGKVK-FVKV--DVDEN---------PELA------------AQF 68

                         90       100
                 ....*....|....*....|
gi 471218818 112 KIKAIPKLIILKpNGEAAAT 131
Cdd:COG3118   69 GVRSIPTLLLFK-DGQPVDR 87
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 32-127 5.06e-04

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: 37.15  E-value: 5.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471218818  32 LKTNKVTCLYFSASYCPPCQAFTPLLidfyneinmedkvleiilipfditeEEFKTYYKQMPWLAIPLGDERikKFTSYF 111
Cdd:cd02947    7 IKSAKPVVVDFWAPWCGPCKAIAPVL-------------------------EELAEEYPKVKFVKVDVDENP--ELAEEY 59

                         90
                 ....*....|....*.
gi 471218818 112 KIKAIPKLIILKpNGE 127
Cdd:cd02947   60 GVRSIPTFLFFK-NGK 74
 
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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