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Conserved domains on  [gi|1240925273|ref|WP_095695293|]
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MULTISPECIES: thermonuclease family protein [Micrococcus]

Protein Classification

thermonuclease family protein( domain architecture ID 11445923)

thermonuclease family protein, may be a thermostable nuclease and catalyze the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond

CATH:  2.40.50.90
SCOP:  4001821

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
37-177 1.05e-10

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


:

Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 58.92  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240925273  37 VAADAARVDIVTVLDGNTVVVNQGGTERTVVLAGVTSagrnPE-GLKVGPNLCMGEESYAWLRDRLPqGATASMTTSDEG 115
Cdd:COG1525    19 AAAATLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDA----PElGQPCGPEQPCGEEARQALRALLA-GKTVTLEPDEGR 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240925273 116 APEGMESAVISIGGGTVNVAMAEAGMGAPTEVAVSERLAEEIAQANQEAVGRGVGLYDIEEP 177
Cdd:COG1525    94 DRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFP 155
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
37-177 1.05e-10

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 58.92  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240925273  37 VAADAARVDIVTVLDGNTVVVNQGGTERTVVLAGVTSagrnPE-GLKVGPNLCMGEESYAWLRDRLPqGATASMTTSDEG 115
Cdd:COG1525    19 AAAATLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDA----PElGQPCGPEQPCGEEARQALRALLA-GKTVTLEPDEGR 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240925273 116 APEGMESAVISIGGGTVNVAMAEAGMGAPTEVAVSERLAEEIAQANQEAVGRGVGLYDIEEP 177
Cdd:COG1525    94 DRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFP 155
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
37-177 1.05e-10

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 58.92  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240925273  37 VAADAARVDIVTVLDGNTVVVNQGGTERTVVLAGVTSagrnPE-GLKVGPNLCMGEESYAWLRDRLPqGATASMTTSDEG 115
Cdd:COG1525    19 AAAATLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDA----PElGQPCGPEQPCGEEARQALRALLA-GKTVTLEPDEGR 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240925273 116 APEGMESAVISIGGGTVNVAMAEAGMGAPTEVAVSERLAEEIAQANQEAVGRGVGLYDIEEP 177
Cdd:COG1525    94 DRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFP 155
 
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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