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Conserved domains on  [gi|24639512|ref|NP_726866|]
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uncharacterized protein Dmel_CG12206, isoform C [Drosophila melanogaster]

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 ...
 434-579 4.93e-64

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: 206.70  E-value: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639512 434 KVVLYTTSMGIIRDTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETI--RVPQLFVEGQLIGDANIVERL 511
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKavSLPRVFVDGRYLGGAEEVLRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639512 512 NESGELRQLLRPYKSIATAYTCQTCGGYRMLPCPACNGSKKSMHRNHFtAEFVALKCMNCDEVGLIKC 579
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 ...
 434-579 4.93e-64

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: 206.70  E-value: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639512 434 KVVLYTTSMGIIRDTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETI--RVPQLFVEGQLIGDANIVERL 511
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKavSLPRVFVDGRYLGGAEEVLRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639512 512 NESGELRQLLRPYKSIATAYTCQTCGGYRMLPCPACNGSKKSMHRNHFtAEFVALKCMNCDEVGLIKC 579
Cdd:cd03031  81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-AAGGFLRCPECNENGLVRC 147
Glutaredoxin pfam00462
Glutaredoxin;
435-502 1.19e-12

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 62.91  E-value: 1.19e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639512   435 VVLYTTSmgiirdTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETirVPQLFVEGQLI 502
Cdd:pfam00462   1 VVLYTKP------TCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPT--VPQVFIDGEHI 60
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
453-521 1.32e-08

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 52.81  E-value: 1.32e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639512 453 ANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETIrvPQLFVEGQLIGDANIVERLNESGELRQLL 521
Cdd:COG0278  34 ARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTI--PQLYVKGEFIGGCDIIREMYESGELQKLL 100
PRK10638 PRK10638
glutaredoxin 3; Provisional
 452-522 2.25e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 37.49  E-value: 2.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639512  452 CANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETirVPQLFVEGQLIGDANIVERLNESGELRQLLR 522
Cdd:PRK10638  15 CHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTT--VPQIFIDAQHIGGCDDLYALDARGGLDPLLK 83
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 434-579 4.93e-64

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: 206.70  E-value: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639512 434 KVVLYTTSMGIIRDTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETI--RVPQLFVEGQLIGDANIVERL 511
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKavSLPRVFVDGRYLGGAEEVLRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639512 512 NESGELRQLLRPYKSIATAYTCQTCGGYRMLPCPACNGSKKSMHRNHFtAEFVALKCMNCDEVGLIKC 579
Cdd:cd03031  81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENAT-AAGGFLRCPECNENGLVRC 147
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 434-513 5.53e-19

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: 81.36  E-value: 5.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639512 434 KVVLYTTSmgiirdTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETirVPQLFVEGQLIGDANIVERLNE 513
Cdd:cd02066   1 KVVVFSKS------TCPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPT--VPQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
435-502 1.19e-12

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 62.91  E-value: 1.19e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639512   435 VVLYTTSmgiirdTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETirVPQLFVEGQLI 502
Cdd:pfam00462   1 VVLYTKP------TCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPT--VPQVFIDGEHI 60
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
453-521 1.32e-08

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 52.81  E-value: 1.32e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639512 453 ANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETIrvPQLFVEGQLIGDANIVERLNESGELRQLL 521
Cdd:COG0278  34 ARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTI--PQLYVKGEFIGGCDIIREMYESGELQKLL 100
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
434-522 2.33e-08

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 50.97  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639512 434 KVVLYTTsmgiirDTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETirVPQLFVEGQLIGDAniverlnE 513
Cdd:COG0695   1 KVTLYTT------PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRT--VPVIFIGGEHLGGF-------D 65


                ....*....
gi 24639512 514 SGELRQLLR 522
Cdd:COG0695  66 EGELDALLA 74
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 451-518 5.68e-07

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: 47.49  E-value: 5.68e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24639512 451 KC---ANVKKILRTLLIKFEERDIFMSveyqQEMRERMQD----ETIrvPQLFVEGQLIGDANIVERLNESGELR 518
Cdd:cd03028  22 RCgfsRKVVQILNQLGVDFGTFDILED----EEVRQGLKEysnwPTF--PQLYVNGELVGGCDIVKEMHESGELQ 90
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
438-522 1.68e-05

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 43.61  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639512   438 YTTSMGIIRDTYAKCANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETIRVPQLFVEGQLIGDANIVERLNESGEL 517
Cdd:pfam04908   6 YVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMRENPPNGAPLPPQIFNEDQYCGDYDAFFEAVEANTL 85


                  ....*
gi 24639512   518 RQLLR 522
Cdd:pfam04908  86 YEFLG 90
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 452-520 4.65e-05

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: 42.14  E-value: 4.65e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639512 452 CANVKKILRTLLIKF--EERDIFmsvEYQQEMRERMQDETIR--VPQLFVEGQLIGDANIVERLNESGELRQL 520
Cdd:cd03419  13 CKRAKSLLKELGVKPavVELDQH---EDGSEIQDYLQELTGQrtVPNVFIGGKFIGGCDDLMALHKSGKLVKL 82
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 455-523 8.97e-05

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: 41.49  E-value: 8.97e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639512 455 VKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETIRV--PQLFVEGQLIGDANIVERLNESGELRQLLRP 523
Cdd:cd03030  22 VLGFLEAKKIEFEEVDISMNEENRQWMRENVPNENGKPlpPQIFNGDEYCGDYEAFFEAKENNTLEEFLKL 92
PRK10638 PRK10638
glutaredoxin 3; Provisional
 452-522 2.25e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 37.49  E-value: 2.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639512  452 CANVKKILRTLLIKFEERDIFMSVEYQQEMRERMQDETirVPQLFVEGQLIGDANIVERLNESGELRQLLR 522
Cdd:PRK10638  15 CHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTT--VPQIFIDAQHIGGCDDLYALDARGGLDPLLK 83
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
493-535 2.65e-03

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 37.96  E-value: 2.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 24639512  493 PQLFVEGQLIGDANIVERLNESGELRQLLrpyKSIATAYTCQT 535
Cdd:PRK10824  72 PQLWVDGELVGGCDIVIEMYQRGELQQLI---KETAAKYKSEE 111
 
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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