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Conserved domains on  [gi|569004722|ref|XP_006526414|]
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glutaredoxin-like protein C5orf63 homolog isoform X1 [Mus musculus]

Protein Classification

glutaredoxin family protein( domain architecture ID 10530477)

glutaredoxin/thioredoxin family protein functions as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein thiol or disulfide bonds using an active site disulfide or dithiol, present in a CXXC motif

CATH:  3.40.30.10
PubMed:  11441809|11012661|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 32-104 2.16e-15

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


:

Pssm-ID: 399055  Cd Length: 80  Bit Score: 65.39  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004722   32 LTLFTKAPCPLCDEAKEVLQPYKDR--FILQEVDITlpENSTWYERYKFDIPVFHLNG------QFLMMHRVNTSKLEKQ 103
Cdd:pfam05768   1 LTLYGKPGCGLCEGAEEVLEPLALElgFELEVIDID--GDPELLAKYGLEIPVLAFVGiskffnLEILSWRLDEEQLAAE 78


                  .
gi 569004722  104 L 104
Cdd:pfam05768  79 L 79
 
Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 32-104 2.16e-15

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 65.39  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004722   32 LTLFTKAPCPLCDEAKEVLQPYKDR--FILQEVDITlpENSTWYERYKFDIPVFHLNG------QFLMMHRVNTSKLEKQ 103
Cdd:pfam05768   1 LTLYGKPGCGLCEGAEEVLEPLALElgFELEVIDID--GDPELLAKYGLEIPVLAFVGiskffnLEILSWRLDEEQLAAE 78


                  .
gi 569004722  104 L 104
Cdd:pfam05768  79 L 79
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
32-65 4.24e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 33.63  E-value: 4.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 569004722  32 LTLFTKAPCPLCDEAKEVLQ----PYkdrfilQEVDIT 65
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDekgiPY------EEIDVD 33
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 33-51 5.70e-03

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 33.26  E-value: 5.70e-03
                         10
                 ....*....|....*....
gi 569004722  33 TLFTKAPCPLCDEAKEVLQ 51
Cdd:cd03029    4 SLFTKPGCPFCARAKAALQ 22
 
Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 32-104 2.16e-15

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 65.39  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004722   32 LTLFTKAPCPLCDEAKEVLQPYKDR--FILQEVDITlpENSTWYERYKFDIPVFHLNG------QFLMMHRVNTSKLEKQ 103
Cdd:pfam05768   1 LTLYGKPGCGLCEGAEEVLEPLALElgFELEVIDID--GDPELLAKYGLEIPVLAFVGiskffnLEILSWRLDEEQLAAE 78


                  .
gi 569004722  104 L 104
Cdd:pfam05768  79 L 79
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
32-65 4.24e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 33.63  E-value: 4.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 569004722  32 LTLFTKAPCPLCDEAKEVLQ----PYkdrfilQEVDIT 65
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDekgiPY------EEIDVD 33
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 33-51 5.70e-03

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 33.26  E-value: 5.70e-03
                         10
                 ....*....|....*....
gi 569004722  33 TLFTKAPCPLCDEAKEVLQ 51
Cdd:cd03029    4 SLFTKPGCPFCARAKAALQ 22
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 20-83 6.35e-03

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 33.10  E-value: 6.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004722   20 RNLSASNRAL--------PVLTLFTKAPCPLC-------DEAKEVLQPYKDRFILQEVDITLPENSTWYERYKFDIPVF 83
Cdd:pfam13899   1 DWLSDLEEALaaaaergkPVLVDFGADWCFTCqvlerdfLSHEEVKAALAKNFVLLRLDWTSRDANITRAFDGQGVPHI 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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