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Conserved domains on  [gi|672091817|gb|KFF87842|]
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hypothetical protein JL05_07015 [Serratia nematodiphila DZ0503SBS1]

Protein Classification

barstar family protein( domain architecture ID 10006576)

barstar family protein similar to Bacillus amyloliquefaciens Barstar, an intracellular inhibitor of the extracellular ribonuclease barnase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BarS COG2732
Barstar, RNAse (barnase) inhibitor [Transcription];
3-89 5.79e-25

Barstar, RNAse (barnase) inhibitor [Transcription];


:

Pssm-ID: 442038  Cd Length: 90  Bit Score: 89.21  E-value: 5.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091817  3 KVEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLPVEIEFTHLNARSKRR---FGAIILLFEEAEEEL 79
Cdd:COG2732   1 TVVIDGSEIRDEEDFYRQLARALDFPDYFGRNLDALWDCLTGGVELPVELVWKNAEASRRRLgedFEALIEVLEEAEEEL 80

                        90
                ....*....|
gi 672091817 80 EGSLRFNIRE 89
Cdd:COG2732  81 EGDLRFNLRD 90
 
Name Accession Description Interval E-value
BarS COG2732
Barstar, RNAse (barnase) inhibitor [Transcription];
3-89 5.79e-25

Barstar, RNAse (barnase) inhibitor [Transcription];


Pssm-ID: 442038  Cd Length: 90  Bit Score: 89.21  E-value: 5.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091817  3 KVEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLPVEIEFTHLNARSKRR---FGAIILLFEEAEEEL 79
Cdd:COG2732   1 TVVIDGSEIRDEEDFYRQLARALDFPDYFGRNLDALWDCLTGGVELPVELVWKNAEASRRRLgedFEALIEVLEEAEEEL 80

                        90
                ....*....|
gi 672091817 80 EGSLRFNIRE 89
Cdd:COG2732  81 EGDLRFNLRD 90
Barstar cd05142
Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus ...
 3-87 3.19e-23

Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase.


Pssm-ID: 240165  Cd Length: 87  Bit Score: 85.07  E-value: 3.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091817  3 KVEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLPVEIEFTHLNARSKR-RFGAI-ILLFEEAEEELE 80
Cdd:cd05142   1 KVVIDGEEIRSIEDLHQILKKELALPEYYGENLDALWDCLTGWVELPLTIEWKNFEQSKQRlGNYAEsLLQVFAEAEEEG 80


                ....*..
gi 672091817 81 GSLRFNI 87
Cdd:cd05142  81 GDLKFNV 87
Barstar pfam01337
Barstar (barnase inhibitor);
5-59 6.26e-07

Barstar (barnase inhibitor);


Pssm-ID: 460165  Cd Length: 82  Bit Score: 43.32  E-value: 6.26e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672091817   5 EFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLP-VEIEFTHLNA 59
Cdd:pfam01337  1 TIDGAGVRDKADLLDAIARALGFPDYFGRNLDALYDCLTDLSWAPgYVLVWEGADA 56
 
Name Accession Description Interval E-value
BarS COG2732
Barstar, RNAse (barnase) inhibitor [Transcription];
3-89 5.79e-25

Barstar, RNAse (barnase) inhibitor [Transcription];


Pssm-ID: 442038  Cd Length: 90  Bit Score: 89.21  E-value: 5.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091817  3 KVEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLPVEIEFTHLNARSKRR---FGAIILLFEEAEEEL 79
Cdd:COG2732   1 TVVIDGSEIRDEEDFYRQLARALDFPDYFGRNLDALWDCLTGGVELPVELVWKNAEASRRRLgedFEALIEVLEEAEEEL 80

                        90
                ....*....|
gi 672091817 80 EGSLRFNIRE 89
Cdd:COG2732  81 EGDLRFNLRD 90
Barstar cd05142
Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus ...
 3-87 3.19e-23

Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase.


Pssm-ID: 240165  Cd Length: 87  Bit Score: 85.07  E-value: 3.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091817  3 KVEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLPVEIEFTHLNARSKR-RFGAI-ILLFEEAEEELE 80
Cdd:cd05142   1 KVVIDGEEIRSIEDLHQILKKELALPEYYGENLDALWDCLTGWVELPLTIEWKNFEQSKQRlGNYAEsLLQVFAEAEEEG 80


                ....*..
gi 672091817 81 GSLRFNI 87
Cdd:cd05142  81 GDLKFNV 87
Barstar_like cd00489
Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus ...
 4-65 2.29e-08

Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it, thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase.


Pssm-ID: 238273  Cd Length: 85  Bit Score: 46.95  E-value: 2.29e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672091817  4 VEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLPVEIEFTHLNArSKRRF 65
Cdd:cd00489   1 VVIDGEDIADWEDFHARLKKKLGFPDYYGHNLDALWDCLTGLVEEPLVLRWRNLEH-LKRLT 61
Barstar pfam01337
Barstar (barnase inhibitor);
5-59 6.26e-07

Barstar (barnase inhibitor);


Pssm-ID: 460165  Cd Length: 82  Bit Score: 43.32  E-value: 6.26e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672091817   5 EFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVTGDIGLP-VEIEFTHLNA 59
Cdd:pfam01337  1 TIDGAGVRDKADLLDAIARALGFPDYFGRNLDALYDCLTDLSWAPgYVLVWEGADA 56
Barstar_evA4336-like cd05141
Barstar_evA4336-like contains uncharacterized sequences similar to the uncharacterized, ...
 4-43 4.02e-04

Barstar_evA4336-like contains uncharacterized sequences similar to the uncharacterized, predicted RNAase inhibitor evA4336 found in Azoarcus sp. EvN1. This is a subfamily of the Barstar family of RNAase inhibitors. Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. Barstar also binds and inhibits a ribonuclease called RNase Sa (produced by Streptomyces aureofaciens) which belongs to the same enzyme family as does barnase.


Pssm-ID: 240164  Cd Length: 81  Bit Score: 35.73  E-value: 4.02e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 672091817  4 VEFDFEQIQDVPTFYRDFAHKFALDEGFGANLDALWDVVT 43
Cdd:cd05141   1 IVLDLSGIADKAALLDALAAALDFPSWFGHNWDALADCLT 40
 
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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