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Conserved domains on  [gi|1188073944|ref|XP_020774754|]
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SH3 domain-binding glutamic acid-rich-like protein 2 [Boleophthalmus pectinirostris]

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 ...
 2-97 1.05e-51

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: 157.43  E-value: 1.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188073944   2 VVKVYVASSTGSVAIKKHQQDVVGFLEANRINFQEVDITMLEKERLWMYNNIPKdrqpEKGRPVPPQIFNEDRYCGDYED 81
Cdd:cd03030     1 VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPN----ENGKPLPPQIFNGDEYCGDYEA 76

                          90
                  ....*....|....*.
gi 1188073944  82 FFQSKENNTVFVFLGL 97
Cdd:cd03030    77 FFEAKENNTLEEFLKL 92
 
Name Accession Description Interval E-value
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 2-97 1.05e-51

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: 157.43  E-value: 1.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188073944   2 VVKVYVASSTGSVAIKKHQQDVVGFLEANRINFQEVDITMLEKERLWMYNNIPKdrqpEKGRPVPPQIFNEDRYCGDYED 81
Cdd:cd03030     1 VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPN----ENGKPLPPQIFNGDEYCGDYEA 76

                          90
                  ....*....|....*.
gi 1188073944  82 FFQSKENNTVFVFLGL 97
Cdd:cd03030    77 FFEAKENNTLEEFLKL 92
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
1-98 1.64e-47

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 146.84  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188073944   1 MVVKVYVASSTGSVAIKKHQQDVVGFLEANRINFQEVDITMLEKERLWMYNNipkdrqPEKGRPVPPQIFNEDRYCGDYE 80
Cdd:pfam04908   1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMREN------PPNGAPLPPQIFNEDQYCGDYD 74

                          90
                  ....*....|....*...
gi 1188073944  81 DFFQSKENNTVFVFLGLK 98
Cdd:pfam04908  75 AFFEAVEANTLYEFLGLA 92
 
Name Accession Description Interval E-value
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 2-97 1.05e-51

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: 157.43  E-value: 1.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188073944   2 VVKVYVASSTGSVAIKKHQQDVVGFLEANRINFQEVDITMLEKERLWMYNNIPKdrqpEKGRPVPPQIFNEDRYCGDYED 81
Cdd:cd03030     1 VIKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPN----ENGKPLPPQIFNGDEYCGDYEA 76

                          90
                  ....*....|....*.
gi 1188073944  82 FFQSKENNTVFVFLGL 97
Cdd:cd03030    77 FFEAKENNTLEEFLKL 92
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
1-98 1.64e-47

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 146.84  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188073944   1 MVVKVYVASSTGSVAIKKHQQDVVGFLEANRINFQEVDITMLEKERLWMYNNipkdrqPEKGRPVPPQIFNEDRYCGDYE 80
Cdd:pfam04908   1 MVLKVYVASSSGSPEIKKKQQRVLMILDANKIPFDEVDITKDEEQRRWMREN------PPNGAPLPPQIFNEDQYCGDYD 74

                          90
                  ....*....|....*...
gi 1188073944  81 DFFQSKENNTVFVFLGLK 98
Cdd:pfam04908  75 AFFEAVEANTLYEFLGLA 92
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 2-87 9.45e-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: 73.27  E-value: 9.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188073944   2 VVKVYVASStgsvaiKKHQQDVVGFLEANRINFQEVDITMLEKERLWMYNNIpkdrqpekGRPVPPQIFNEDRYCGDYED 81
Cdd:cd02066     1 KVVVFSKST------CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELS--------GWPTVPQIFINGEFIGGYDD 66


                  ....*.
gi 1188073944  82 FFQSKE 87
Cdd:cd02066    67 LKALHE 72
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 26-81 8.19e-04

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: 35.26  E-value: 8.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1188073944  26 FLEANRINFQEVDITMLEKERLWMYNNipkdrqpEKGRPVPPQIFNEDRYCGDYED 81
Cdd:cd03418    19 LLDKKGVDYEEIDVDGDPALREEMINR-------SGGRRTVPQIFIGDVHIGGCDD 67
CIDE_N_FSP27 cd06538
CIDE_N domain of FSP27 proteins. The CIDE-N (cell death-inducing DFF45-like effector, ...
 69-96 6.00e-03

CIDE_N domain of FSP27 proteins. The CIDE-N (cell death-inducing DFF45-like effector, N-terminal) domain is found in the FSP27/CIDE-C protein, which has been identified as a n adipocyte lipid droplet protein that negatively regulates lipolysis and promotes triglyceride accumulation. The CIDE protein family includes 3 members: CIDE-A, CIDE-B, and FSP27(CIDE-C). Based on sequence similarity with DFF40 and DFF45, CIDE proteins were initially characterized as mitochondrial activators of apoptosis. The CIDE-N domain of FSP27 is sufficient to increase apoptosis in vitro when overexpressed.


Pssm-ID: 119371  Cd Length: 79  Bit Score: 33.25  E-value: 6.00e-03
                          10        20
                  ....*....|....*....|....*...
gi 1188073944  69 IFNEDRYCGDYEDFFQSKENNTVFVFLG 96
Cdd:cd06538    43 VLDEDGTGVDTEEFFQALADNTVFMVLG 70
 
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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