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Conserved domains on  [gi|18017602|ref|NP_542126|]
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SH3 domain-binding glutamic acid-rich-like protein 3 [Mus musculus]

Protein Classification

GRX_SH3BGR domain-containing protein( domain architecture ID 11154530)

GRX_SH3BGR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
2-93 2.37e-49

SH3-binding, glutamic acid-rich protein;


:

Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 151.08  E-value: 2.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18017602    2 SGLRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAGNPKATPPQIVNGNHYCGDYELFVEAV 81
Cdd:pfam04908  1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMRENPPNGAPLPPQIFNEDQYCGDYDAFFEAV 80

                         90
                 ....*....|..
gi 18017602   82 EQDTLQEFLKLA 93
Cdd:pfam04908 81 EANTLYEFLGLA 92
 
Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
2-93 2.37e-49

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 151.08  E-value: 2.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18017602    2 SGLRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAGNPKATPPQIVNGNHYCGDYELFVEAV 81
Cdd:pfam04908  1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMRENPPNGAPLPPQIFNEDQYCGDYDAFFEAV 80

                         90
                 ....*....|..
gi 18017602   82 EQDTLQEFLKLA 93
Cdd:pfam04908 81 EANTLYEFLGLA 92
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 4-92 3.78e-47

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: 145.49  E-value: 3.78e-47
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18017602  4 LRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAGN--PKATPPQIVNGNHYCGDYELFVEAV 81
Cdd:cd03030  2 IKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNenGKPLPPQIFNGDEYCGDYEAFFEAK 81

                       90
               ....*....|.
gi 18017602 82 EQDTLQEFLKL 92
Cdd:cd03030 82 ENNTLEEFLKL 92
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
26-72 3.24e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 43.65  E-value: 3.24e-07
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*...
gi 18017602 26 RILDGKRIQYQLVDISQDNALRDEMRTLAGNPKAtpPQI-VNGNHYCG 72
Cdd:COG0695 18 RLLDEKGIPYEEIDVDEDPEAREELRERSGRRTV--PVIfIGGEHLGG 63
 
Name Accession Description Interval E-value
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
2-93 2.37e-49

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 151.08  E-value: 2.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18017602    2 SGLRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAGNPKATPPQIVNGNHYCGDYELFVEAV 81
Cdd:pfam04908  1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMRENPPNGAPLPPQIFNEDQYCGDYDAFFEAV 80

                         90
                 ....*....|..
gi 18017602   82 EQDTLQEFLKLA 93
Cdd:pfam04908 81 EANTLYEFLGLA 92
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 4-92 3.78e-47

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: 145.49  E-value: 3.78e-47
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18017602  4 LRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAGN--PKATPPQIVNGNHYCGDYELFVEAV 81
Cdd:cd03030  2 IKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNenGKPLPPQIFNGDEYCGDYEAFFEAK 81

                       90
               ....*....|.
gi 18017602 82 EQDTLQEFLKL 92
Cdd:cd03030 82 ENNTLEEFLKL 92
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 6-82 1.38e-18

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: 72.50  E-value: 1.38e-18
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18017602  6 VYSTSVtgsreiKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAGNPkaTPPQIVNGNHYCGDYELFVEAVE 82
Cdd:cd02066  4 VFSKST------CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWP--TVPQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
24-69 3.49e-09

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 48.27  E-value: 3.49e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 18017602   24 VTRILDGKRIQYQLVDISQDNALRDEMRTLAGNPkaTPPQI-VNGNH 69
Cdd:pfam00462 15 AKRLLKSLGVDFEEIDVDEDPEIREELKELSGWP--TVPQVfIDGEH 59
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
26-72 3.24e-07

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 43.65  E-value: 3.24e-07
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*...
gi 18017602 26 RILDGKRIQYQLVDISQDNALRDEMRTLAGNPKAtpPQI-VNGNHYCG 72
Cdd:COG0695 18 RLLDEKGIPYEEIDVDEDPEAREELRERSGRRTV--PVIfIGGEHLGG 63
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 6-91 9.22e-07

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: 43.76  E-value: 9.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18017602   6 VYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRTLAG--NPKATPPQIVNGNHYCGDYELFVEAVEQ 83
Cdd:cd03031   4 LYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGaeLKAVSLPRVFVDGRYLGGAEEVLRLNES 83


                ....*...
gi 18017602  84 DTLQEFLK 91
Cdd:cd03031  84 GELRKLLK 91
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 26-69 4.84e-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: 40.65  E-value: 4.84e-06
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*
gi 18017602 26 RILDGKRIQYQLVDISQDNALRDEMRTLAGNpKATPPQI-VNGNH 69
Cdd:cd03418 18 ALLDKKGVDYEEIDVDGDPALREEMINRSGG-RRTVPQIfIGDVH 61
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 26-72 9.95e-03

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 31.81  E-value: 9.95e-03
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
gi 18017602 26 RILDGKRIQYQLVDISQDNALRDEMRTLAGNpKATPPQIVNGNHYCG 72
Cdd:cd02976 18 RFLDERGIPFEEVDVDEDPEALEELKKLNGY-RSVPVVVIGDEHLSG 63
 
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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