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Conserved domains on  [gi|41053650|ref|NP_956572|]
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SH3 domain-binding glutamic acid-rich-like protein 3 [Danio rerio]

Protein Classification

SH3 domain-binding glutamic acid-rich-like protein( domain architecture ID 10122531)

SH3 domain-binding glutamic acid-rich-like protein (SH3BGR) belongs to the glutaredoxin (GRX) family but does possess a redox active CXXC motif, similar to human SH3BGRL3 that was identified as a tumor necrosis factor (TNF) alpha inhibitory protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 2-91 1.15e-43

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: 136.63  E-value: 1.15e-43
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053650  2 SIKLYYTTVTASREVKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGN--PTAIPPQIFNEDQYCGNYEMFTEA 79
Cdd:cd03030  1 VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNenGKPLPPQIFNGDEYCGDYEAFFEA 80

                       90
               ....*....|..
gi 41053650 80 VEADTVEQFLKI 91
Cdd:cd03030 81 KENNTLEEFLKL 92
 
Name Accession Description Interval E-value
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 2-91 1.15e-43

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: 136.63  E-value: 1.15e-43
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053650  2 SIKLYYTTVTASREVKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGN--PTAIPPQIFNEDQYCGNYEMFTEA 79
Cdd:cd03030  1 VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNenGKPLPPQIFNGDEYCGDYEAFFEA 80

                       90
               ....*....|..
gi 41053650 80 VEADTVEQFLKI 91
Cdd:cd03030 81 KENNTLEEFLKL 92
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
1-92 1.00e-37

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 121.42  E-value: 1.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053650    1 MSIKLYYTTVTASREVKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTAIPPQIFNEDQYCGNYEMFTEAV 80
Cdd:pfam04908  1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMRENPPNGAPLPPQIFNEDQYCGDYDAFFEAV 80

                         90
                 ....*....|..
gi 41053650   81 EADTVEQFLKIA 92
Cdd:pfam04908 81 EANTLYEFLGLA 92
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
21-74 5.22e-08

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 45.57  E-value: 5.22e-08
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|....
gi 41053650 21 AEVMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTAipPQIFNEDQYCGNYE 74
Cdd:COG0695 14 ARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTV--PVIFIGGEHLGGFD 65
PRK10638 PRK10638
glutaredoxin 3; Provisional
 26-71 7.34e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 32.48  E-value: 7.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 41053650  26 ILESKSIRYELIDISVGGAIRDEMRSKSGNPTAipPQIFNEDQYCG 71
Cdd:PRK10638 21 LLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTV--PQIFIDAQHIG 64
 
Name Accession Description Interval E-value
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 2-91 1.15e-43

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: 136.63  E-value: 1.15e-43
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053650  2 SIKLYYTTVTASREVKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGN--PTAIPPQIFNEDQYCGNYEMFTEA 79
Cdd:cd03030  1 VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNenGKPLPPQIFNGDEYCGDYEAFFEA 80

                       90
               ....*....|..
gi 41053650 80 VEADTVEQFLKI 91
Cdd:cd03030 81 KENNTLEEFLKL 92
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
1-92 1.00e-37

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 121.42  E-value: 1.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053650    1 MSIKLYYTTVTASREVKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTAIPPQIFNEDQYCGNYEMFTEAV 80
Cdd:pfam04908  1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMRENPPNGAPLPPQIFNEDQYCGDYDAFFEAV 80

                         90
                 ....*....|..
gi 41053650   81 EADTVEQFLKIA 92
Cdd:pfam04908 81 EANTLYEFLGLA 92
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 3-81 3.62e-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: 73.66  E-value: 3.62e-19
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053650  3 IKLYYTTVtasrevKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTaiPPQIFNEDQYCGNYEMFTEAVE 81
Cdd:cd02066  2 VVVFSKST------CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPT--VPQIFINGEFIGGYDDLKALHE 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
21-74 5.22e-08

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 45.57  E-value: 5.22e-08
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|....
gi 41053650 21 AEVMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTAipPQIFNEDQYCGNYE 74
Cdd:COG0695 14 ARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTV--PVIFIGGEHLGGFD 65
Glutaredoxin pfam00462
Glutaredoxin;
23-64 9.65e-07

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 42.11  E-value: 9.65e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 41053650   23 VMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTAipPQIF 64
Cdd:pfam00462 15 AKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTV--PQVF 54
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 25-74 4.90e-05

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: 37.95  E-value: 4.90e-05
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
gi 41053650 25 RILESKSIRYELIDISVGGAIRDEMRSKSGNPTAIpPQIFNEDQYCGNYE 74
Cdd:cd03418 18 ALLDKKGVDYEEIDVDGDPALREEMINRSGGRRTV-PQIFIGDVHIGGCD 66
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 2-74 5.32e-04

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: 36.45  E-value: 5.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41053650   2 SIKLYYTTVTASREVKSQQAEVMRILESKSIRYELIDISVGGAIRDEMRSKSGNPTA--IPPQIFNEDQYCGNYE 74
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAELKavSLPRVFVDGRYLGGAE 75
PRK10638 PRK10638
glutaredoxin 3; Provisional
 26-71 7.34e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 32.48  E-value: 7.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 41053650  26 ILESKSIRYELIDISVGGAIRDEMRSKSGNPTAipPQIFNEDQYCG 71
Cdd:PRK10638 21 LLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTV--PQIFIDAQHIG 64
 
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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