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Conserved domains on  [gi|488311691|ref|WP_002381076|]
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MULTISPECIES: YdbC family protein [Enterococcus]

Protein Classification

YdbC family protein( domain architecture ID 10008558)

YdbC family protein similar to Lactococcus lactis Single-stranded DNA (ssDNA) binding protein YdbC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4443 COG4443
Uncharacterized conserved protein [Function unknown];
4-70 2.07e-36

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443543  Cd Length: 70  Bit Score: 116.53  E-value: 2.07e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488311691  4 EFSYEILEEVAVLSENARGWRKELNLISWNGRPPKFDLREWAPDHEKMGKGITLTNEEFAELSKTIK 70
Cdd:COG4443   3 EIKYEIVEEIGVLSESSKGWTKELNLVSWNGREPKYDIRDWSPDHTKMGKGITLTKEELKELKDILN 69
 
Name Accession Description Interval E-value
COG4443 COG4443
Uncharacterized conserved protein [Function unknown];
4-70 2.07e-36

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443543  Cd Length: 70  Bit Score: 116.53  E-value: 2.07e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488311691  4 EFSYEILEEVAVLSENARGWRKELNLISWNGRPPKFDLREWAPDHEKMGKGITLTNEEFAELSKTIK 70
Cdd:COG4443   3 EIKYEIVEEIGVLSESSKGWTKELNLVSWNGREPKYDIRDWSPDHTKMGKGITLTKEELKELKDILN 69
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 22-65 6.09e-10

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: 49.01  E-value: 6.09e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488311691  22 GWRKELNLISWNGRPpKFDLREWAPDHEKM---GKGITLTNEEFAEL 65
Cdd:pfam02229  4 SKKRRVTVREFKGKT-LVDIREYYEKDGELkpgKKGISLTLEQWKAL 49
 
Name Accession Description Interval E-value
COG4443 COG4443
Uncharacterized conserved protein [Function unknown];
4-70 2.07e-36

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443543  Cd Length: 70  Bit Score: 116.53  E-value: 2.07e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488311691  4 EFSYEILEEVAVLSENARGWRKELNLISWNGRPPKFDLREWAPDHEKMGKGITLTNEEFAELSKTIK 70
Cdd:COG4443   3 EIKYEIVEEIGVLSESSKGWTKELNLVSWNGREPKYDIRDWSPDHTKMGKGITLTKEELKELKDILN 69
PC4 pfam02229
Transcriptional Coactivator p15 (PC4); p15 has a bipartite structure composed of an ...
 22-65 6.09e-10

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: 49.01  E-value: 6.09e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488311691  22 GWRKELNLISWNGRPpKFDLREWAPDHEKM---GKGITLTNEEFAEL 65
Cdd:pfam02229  4 SKKRRVTVREFKGKT-LVDIREYYEKDGELkpgKKGISLTLEQWKAL 49
 
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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