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Conserved domains on  [gi|300794258|ref|NP_001178864|]
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glutaredoxin domain-containing cysteine-rich protein 1 [Rattus norvegicus]

Protein Classification

glutaredoxin family protein( domain architecture ID 10122541)

glutaredoxin (GRX) family protein belonging to the thioredoxin superfamily, may function as a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 138-285 4.53e-74

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: 223.27  E-value: 4.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIYTTCLRVVRTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSM 217
Cdd:cd03031    1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300794258 218 NESGELQDLLTKIERVQHPHECPSCGGFGFLPCSVCHGSKMSVFRNCFtDAFKALKCTACNENGLQRC 285
Cdd:cd03031   81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-AAGGFLRCPECNENGLVRC 147
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 138-285 4.53e-74

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: 223.27  E-value: 4.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIYTTCLRVVRTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSM 217
Cdd:cd03031    1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300794258 218 NESGELQDLLTKIERVQHPHECPSCGGFGFLPCSVCHGSKMSVFRNCFtDAFKALKCTACNENGLQRC 285
Cdd:cd03031   81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-AAGGFLRCPECNENGLVRC 147
Glutaredoxin pfam00462
Glutaredoxin;
139-207 1.01e-07

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 47.88  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794258  139 VVIYTTclrvvrTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELdercRRVSEAPSLPVVFIDGHY 207
Cdd:pfam00462   1 VVLYTK------PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREEL----KELSGWPTVPQVFIDGEH 59
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
138-227 5.28e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 46.34  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIYTT--ClrvvrttfERCELVRKIFQNHRVKFEEKNIALNGDYGKELdercRRVSEAPSLPVVFIDGHYLGGAekil 215
Cdd:COG0695    1 KVTLYTTpgC--------PYCARAKRLLDEKGIPYEEIDVDEDPEAREEL----RERSGRRTVPVIFIGGEHLGGF---- 64

                         90
                 ....*....|..
gi 300794258 216 smnESGELQDLL 227
Cdd:COG0695   65 ---DEGELDALL 73
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 139-229 1.76e-05

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: 42.83  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258  139 VVIYTT---CLrvvrttferCELVRKIFQNHRVKFEEKNIAlNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKIL 215
Cdd:TIGR02189  10 VVIFSRsscCM---------CHVVKRLLLTLGVNPAVHEID-KEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVM 79

                          90
                  ....*....|....
gi 300794258  216 SMNESGELQDLLTK 229
Cdd:TIGR02189  80 ALHISGSLVPMLKQ 93
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
169-227 3.01e-03

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 36.80  E-value: 3.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300794258 169 KFEEKNIALNGDYGKELDercrRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDLL 227
Cdd:PRK10824  46 RFAYVDILQNPDIRAELP----KYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLI 100
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 138-285 4.53e-74

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: 223.27  E-value: 4.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIYTTCLRVVRTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSM 217
Cdd:cd03031    1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300794258 218 NESGELQDLLTKIERVQHPHECPSCGGFGFLPCSVCHGSKMSVFRNCFtDAFKALKCTACNENGLQRC 285
Cdd:cd03031   81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-AAGGFLRCPECNENGLVRC 147
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 138-219 2.19e-16

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: 72.11  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIYTTclrvvrTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELdercRRVSEAPSLPVVFIDGHYLGGAEKILSM 217
Cdd:cd02066    1 KVVVFSK------STCPYCKRAKRLLESLGIEFEEIDILEDGELREEL----KELSGWPTVPQIFINGEFIGGYDDLKAL 70


                 ..
gi 300794258 218 NE 219
Cdd:cd02066   71 HE 72
Glutaredoxin pfam00462
Glutaredoxin;
139-207 1.01e-07

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 47.88  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794258  139 VVIYTTclrvvrTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELdercRRVSEAPSLPVVFIDGHY 207
Cdd:pfam00462   1 VVLYTK------PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREEL----KELSGWPTVPQVFIDGEH 59
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
138-227 5.28e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 46.34  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIYTT--ClrvvrttfERCELVRKIFQNHRVKFEEKNIALNGDYGKELdercRRVSEAPSLPVVFIDGHYLGGAekil 215
Cdd:COG0695    1 KVTLYTTpgC--------PYCARAKRLLDEKGIPYEEIDVDEDPEAREEL----RERSGRRTVPVIFIGGEHLGGF---- 64

                         90
                 ....*....|..
gi 300794258 216 smnESGELQDLL 227
Cdd:COG0695   65 ---DEGELDALL 73
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 138-226 1.29e-06

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: 45.61  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 138 RVVIY--TTClrvvrttfERCELVRKIFQNHRVKFEEKNIALNGDyGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKIL 215
Cdd:cd03419    1 PVVVFskSYC--------PYCKRAKSLLKELGVKPAVVELDQHED-GSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLM 71

                         90
                 ....*....|.
gi 300794258 216 SMNESGELQDL 226
Cdd:cd03419   72 ALHKSGKLVKL 82
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 162-224 1.88e-06

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 45.18  E-value: 1.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300794258 162 IFQNHRVKFEEKNIALNgdygKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQ 224
Cdd:cd03028   32 ILNQLGVDFGTFDILED----EEVRQGLKEYSNWPTFPQLYVNGELVGGCDIVKEMHESGELQ 90
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 139-229 1.76e-05

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: 42.83  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258  139 VVIYTT---CLrvvrttferCELVRKIFQNHRVKFEEKNIAlNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKIL 215
Cdd:TIGR02189  10 VVIFSRsscCM---------CHVVKRLLLTLGVNPAVHEID-KEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVM 79

                          90
                  ....*....|....
gi 300794258  216 SMNESGELQDLLTK 229
Cdd:TIGR02189  80 ALHISGSLVPMLKQ 93
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 167-227 1.86e-04

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.


Pssm-ID: 239328 [Multi-domain]  Cd Length: 92  Bit Score: 39.56  E-value: 1.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300794258 167 RVKFEEKNIALNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDLL 227
Cdd:cd03030   30 KIEFEEVDISMNEENRQWMRENVPNENGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 156-214 2.58e-04

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: 38.65  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 156 CELVRKIFQNHRVKFEEknIAL-NGDYGKELdercRRVSEAPSLPVVFIDGHYLGGAEKI 214
Cdd:cd03029   14 CARAKAALQENGISYEE--IPLgKDITGRSL----RAVTGAMTVPQVFIDGELIGGSDDL 67
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
169-227 3.01e-03

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 36.80  E-value: 3.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300794258 169 KFEEKNIALNGDYGKELDercrRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDLL 227
Cdd:PRK10824  46 RFAYVDILQNPDIRAELP----KYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLI 100
PRK10638 PRK10638
glutaredoxin 3; Provisional
 139-227 5.52e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 35.18  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794258 139 VVIYTtclrvvRTTFERCELVRKIFQNHRVKFEEknIALNGDYGKElDERCRRvSEAPSLPVVFIDGHYLGGAEKILSMN 218
Cdd:PRK10638   4 VEIYT------KATCPFCHRAKALLNSKGVSFQE--IPIDGDAAKR-EEMIKR-SGRTTVPQIFIDAQHIGGCDDLYALD 73


                 ....*....
gi 300794258 219 ESGELQDLL 227
Cdd:PRK10638  74 ARGGLDPLL 82
 
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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