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Conserved domains on  [gi|122937474|ref|NP_001073985|]
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glutaredoxin domain-containing cysteine-rich protein 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 ...
 197-243 2.05e-08

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 cd03031:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 147  Bit Score: 51.85  E-value: 2.05e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 122937474 197 CFHCRGSGSATCSLCHGSKFSMLANRFKEsYRALRCPACNENGLQPC 243
Cdd:cd03031  102 CEGCGGARFVPCSECNGSCKVFAENATAA-GGFLRCPECNENGLVRC 147
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 197-243 2.05e-08

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 51.85  E-value: 2.05e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 122937474 197 CFHCRGSGSATCSLCHGSKFSMLANRFKEsYRALRCPACNENGLQPC 243
Cdd:cd03031  102 CEGCGGARFVPCSECNGSCKVFAENATAA-GGFLRCPECNENGLVRC 147
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 184-242 1.86e-03

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 37.10  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122937474 184 NRYTQEGDIPedsCFHCRGSGSATCSLC--HGSKFSMLANRFKESYR--------ALRCPACNENGLQP 242
Cdd:PLN03165  34 NAAKRENTQP---CFPCSGTGAQVCRFCvgSGNVTVELGGGEKEVSKcincdgagSLTCTTCQGSGIQP 99
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 197-243 2.05e-08

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 51.85  E-value: 2.05e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 122937474 197 CFHCRGSGSATCSLCHGSKFSMLANRFKEsYRALRCPACNENGLQPC 243
Cdd:cd03031  102 CEGCGGARFVPCSECNGSCKVFAENATAA-GGFLRCPECNENGLVRC 147
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 184-242 1.86e-03

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 37.10  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122937474 184 NRYTQEGDIPedsCFHCRGSGSATCSLC--HGSKFSMLANRFKESYR--------ALRCPACNENGLQP 242
Cdd:PLN03165  34 NAAKRENTQP---CFPCSGTGAQVCRFCvgSGNVTVELGGGEKEVSKcincdgagSLTCTTCQGSGIQP 99
 
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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