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Conserved domains on  [gi|1938385734|ref|YP_009966061|]
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transcriptional regulator [Escherichia phage H8]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PC4 super family cl21701
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 21-64 6.49e-05

Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. The DNA-binding activity of the carboxy-terminal is disguised by the amino-terminal p15 domain. Activity is controlled by protein kinases that target the regulatory domain.


The actual alignment was detected with superfamily member pfam02229:

Pssm-ID: 473935  Cd Length: 52  Bit Score: 37.45  E-value: 6.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1938385734  21 WEKeGEQVRLTVSEFRGNLYMGIRYWLLDiNDEWFPTKSGFSFP 64
Cdd:pfam02229   1 WEL-SKKRRVTVREFKGKTLVDIREYYEK-DGELKPGKKGISLT 42
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 41-97 3.10e-03

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member cd06451:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 356  Bit Score: 35.34  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938385734  41 MGIRYWLLDINDEWFPTKSGFSFPYTleTTSQLFYAFTQILSE--SEVLHEVQKRAEEL 97
Cdd:cd06451   211 TKPKGFYFDLLLLLKYWGEGYSYPHT--PPVNLLYALREALDLilEEGLENRWARHRRL 267
 
Name Accession Description Interval E-value
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 21-64 6.49e-05

Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. The DNA-binding activity of the carboxy-terminal is disguised by the amino-terminal p15 domain. Activity is controlled by protein kinases that target the regulatory domain.


Pssm-ID: 460501  Cd Length: 52  Bit Score: 37.45  E-value: 6.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1938385734  21 WEKeGEQVRLTVSEFRGNLYMGIRYWLLDiNDEWFPTKSGFSFP 64
Cdd:pfam02229   1 WEL-SKKRRVTVREFKGKTLVDIREYYEK-DGELKPGKKGISLT 42
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 41-97 3.10e-03

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 35.34  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938385734  41 MGIRYWLLDINDEWFPTKSGFSFPYTleTTSQLFYAFTQILSE--SEVLHEVQKRAEEL 97
Cdd:cd06451   211 TKPKGFYFDLLLLLKYWGEGYSYPHT--PPVNLLYALREALDLilEEGLENRWARHRRL 267
 
Name Accession Description Interval E-value
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 21-64 6.49e-05

Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. The DNA-binding activity of the carboxy-terminal is disguised by the amino-terminal p15 domain. Activity is controlled by protein kinases that target the regulatory domain.


Pssm-ID: 460501  Cd Length: 52  Bit Score: 37.45  E-value: 6.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1938385734  21 WEKeGEQVRLTVSEFRGNLYMGIRYWLLDiNDEWFPTKSGFSFP 64
Cdd:pfam02229   1 WEL-SKKRRVTVREFKGKTLVDIREYYEK-DGELKPGKKGISLT 42
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 41-97 3.10e-03

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 35.34  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938385734  41 MGIRYWLLDINDEWFPTKSGFSFPYTleTTSQLFYAFTQILSE--SEVLHEVQKRAEEL 97
Cdd:cd06451   211 TKPKGFYFDLLLLLKYWGEGYSYPHT--PPVNLLYALREALDLilEEGLENRWARHRRL 267
 
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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