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Conserved domains on  [gi|1775885014|gb|KAE8646081|]
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hypothetical protein Csa_016840 [Cucumis sativus]

Protein Classification

glutaredoxin( domain architecture ID 10020367)

glutaredoxin is a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 3-100 1.84e-40

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


:

Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 129.11  E-value: 1.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014   3 VNRLAAENEVLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDMEKALVRLqGCNtPPVPAVFIAGDLVGSTNEL 82
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRL-GCS-PAVPAVFVGGKLVGGLENV 78

                          90
                  ....*....|....*...
gi 1775885014  83 MSLHLSGDLNRMLKPYKA 100
Cdd:TIGR02189  79 MALHISGSLVPMLKQAGA 96
 
Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 3-100 1.84e-40

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 129.11  E-value: 1.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014   3 VNRLAAENEVLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDMEKALVRLqGCNtPPVPAVFIAGDLVGSTNEL 82
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRL-GCS-PAVPAVFVGGKLVGGLENV 78

                          90
                  ....*....|....*...
gi 1775885014  83 MSLHLSGDLNRMLKPYKA 100
Cdd:TIGR02189  79 MALHISGSLVPMLKQAGA 96
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 12-91 2.96e-27

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 95.30  E-value: 2.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDMEKALVRLQGCNTppVPAVFIAGDLVGSTNELMSLHLSGDL 91
Cdd:cd03419     2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRT--VPNVFIGGKFIGGCDDLMALHKSGKL 79
Glutaredoxin pfam00462
Glutaredoxin;
12-76 7.57e-11

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 52.89  E-value: 7.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDmekALVRLQGCNTppVPAVFIAGDLV 76
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIRE---ELKELSGWPT--VPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
11-96 1.02e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 42.49  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  11 EVLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDmekALVRLQGCNTppVPAVFIAGDLVGSTNElmslhlsGD 90
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEARE---ELRERSGRRT--VPVIFIGGEHLGGFDE-------GE 68


                  ....*.
gi 1775885014  91 LNRMLK 96
Cdd:COG0695    69 LDALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 12-96 7.17e-06

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 40.57  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDmekALVRLQGCNTppVPAVFIAGDLVGSTNELMSLHLSGDL 91
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKRE---EMIKRSGRTT--VPQIFIDAQHIGGCDDLYALDARGGL 78


                  ....*
gi 1775885014  92 NRMLK 96
Cdd:PRK10638   79 DPLLK 83
 
Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 3-100 1.84e-40

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 129.11  E-value: 1.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014   3 VNRLAAENEVLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDMEKALVRLqGCNtPPVPAVFIAGDLVGSTNEL 82
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRL-GCS-PAVPAVFVGGKLVGGLENV 78

                          90
                  ....*....|....*...
gi 1775885014  83 MSLHLSGDLNRMLKPYKA 100
Cdd:TIGR02189  79 MALHISGSLVPMLKQAGA 96
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 12-91 2.96e-27

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 95.30  E-value: 2.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDMEKALVRLQGCNTppVPAVFIAGDLVGSTNELMSLHLSGDL 91
Cdd:cd03419     2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRT--VPNVFIGGKFIGGCDDLMALHKSGKL 79
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 12-86 5.44e-11

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 53.62  E-value: 5.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSpmVYELDQDPEGrDMEKALVRLQGCNTppVPAVFIAGDLVGSTNELMSLH 86
Cdd:cd02066     2 VVVFSKSTCPYCKRAKRLLESLGIE--FEEIDILEDG-ELREELKELSGWPT--VPQIFINGEFIGGYDDLKALH 71
Glutaredoxin pfam00462
Glutaredoxin;
12-76 7.57e-11

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 52.89  E-value: 7.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDmekALVRLQGCNTppVPAVFIAGDLV 76
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIRE---ELKELSGWPT--VPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
11-96 1.02e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 42.49  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  11 EVLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDmekALVRLQGCNTppVPAVFIAGDLVGSTNElmslhlsGD 90
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEARE---ELRERSGRRT--VPVIFIGGEHLGGFDE-------GE 68


                  ....*.
gi 1775885014  91 LNRMLK 96
Cdd:COG0695    69 LDALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 12-96 7.17e-06

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 40.57  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  12 VLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRDmekALVRLQGCNTppVPAVFIAGDLVGSTNELMSLHLSGDL 91
Cdd:PRK10638    4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKRE---EMIKRSGRTT--VPQIFIDAQHIGGCDDLYALDARGGL 78


                  ....*
gi 1775885014  92 NRMLK 96
Cdd:PRK10638   79 DPLLK 83
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 11-89 9.74e-06

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 40.26  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775885014  11 EVLIISKSSCCLCYAVSVLLRDLGVSPMVYELDQDPEGRD--MEKAlvrlQGCNTppVPAVFIAGDLVGSTNELMSLHLS 88
Cdd:cd03418     1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREemINRS----GGRRT--VPQIFIGDVHIGGCDDLYALERK 74


                  .
gi 1775885014  89 G 89
Cdd:cd03418    75 G 75
 
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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