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Conserved domains on  [gi|1046221699|ref|WP_065613593|]
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thermonuclease family protein [Xanthomonas euvesicatoria]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
7-163 5.41e-50

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


:

Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 160.61  E-value: 5.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699   7 LKLLKCWVLSVLVLIALPVSAAELVGRAT-VTDGDTITVAH----QRIRLWGIDAPESAQQCnahdGSAWPCGRRAAAAL 81
Cdd:COG1525     1 MRKLLLALLLALAALAAAAAAATLTAGVVrVIDGDTLRVRDdgkgERVRLAGIDAPELGQPC----GPEQPCGEEARQAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  82 DGYLLDKTVHCQP-KDTDRYGRTVAECFVQGQSVNAWMVRSGWAVAYRQYA-----TAFEVDERLAQQQRRNLWQGAFQM 155
Cdd:COG1525    77 RALLAGKTVTLEPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSpdkyaDRYLAAEAEARAARRGLWSDAFPV 156

                  ....*...
gi 1046221699 156 PADYRRDK 163
Cdd:COG1525   157 PPEWRRRK 164
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
7-163 5.41e-50

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 160.61  E-value: 5.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699   7 LKLLKCWVLSVLVLIALPVSAAELVGRAT-VTDGDTITVAH----QRIRLWGIDAPESAQQCnahdGSAWPCGRRAAAAL 81
Cdd:COG1525     1 MRKLLLALLLALAALAAAAAAATLTAGVVrVIDGDTLRVRDdgkgERVRLAGIDAPELGQPC----GPEQPCGEEARQAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  82 DGYLLDKTVHCQP-KDTDRYGRTVAECFVQGQSVNAWMVRSGWAVAYRQYA-----TAFEVDERLAQQQRRNLWQGAFQM 155
Cdd:COG1525    77 RALLAGKTVTLEPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSpdkyaDRYLAAEAEARAARRGLWSDAFPV 156

                  ....*...
gi 1046221699 156 PADYRRDK 163
Cdd:COG1525   157 PPEWRRRK 164
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
36-149 2.83e-27

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 101.20  E-value: 2.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  36 VTDGDTITVAHQ-----RIRLWGIDAPESAQQCNAHDGSAWPCGRRAAAALDGYLLDKTVHCQPKDTDRYGRTVAECFVQ 110
Cdd:cd00175     2 VIDGDTIRVRLPpgpliTVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLN 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046221699 111 G-QSVNAWMVRSGWAVAYRQYATAFEVDERL------AQQQRRNLW 149
Cdd:cd00175    82 GgENIAEELVKEGLARVYRYYPDDSEYYDELleaeeaAKKARKGLW 127
SNc smart00318
Staphylococcal nuclease homologues;
36-149 4.91e-26

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 98.10  E-value: 4.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699   36 VTDGDTITVAHQ-----RIRLWGIDAPESAQQCNAHDGSAWPCGRRAAAALDGYLLDKTVHCQPKDTDRYGRTVAECFVQ 110
Cdd:smart00318  10 VIDGDTIRVRLPkgpliTIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLN 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1046221699  111 GQS-VNAWMVRSGWAVAYRQY------ATAFEVDERLAQQQRRNLW 149
Cdd:smart00318  90 GGNnIAEELVKEGLAKVYRYAdkdeyvYDELLEAEEAAKKARKGLW 135
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
48-149 6.07e-21

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 83.91  E-value: 6.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  48 RIRLWGIDAPESAQQCNAhdgsAWPCGRRAAAALDGYLLDKTVHCQPKDTDRYGRTVAECFVQGQSVNAWMVRSGWAVAY 127
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTP----VQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVY 76
                          90       100
                  ....*....|....*....|....*...
gi 1046221699 128 RQYATAFEVD------ERLAQQQRRNLW 149
Cdd:pfam00565  77 KAYPPNFKHYdellaaEEEAKKKKKGLW 104
PRK06518 PRK06518
hypothetical protein; Provisional
32-163 2.53e-19

hypothetical protein; Provisional


Pssm-ID: 235818  Cd Length: 177  Bit Score: 81.82  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  32 GRATVTDGDT---ITVA-----HQRIRLWGIDAPESAQQCNAhDGSAWPCGRRAAAALDGYLLDKTVHCQPKdTDRYGRT 103
Cdd:PRK06518   26 GRAQVTSGVTfklIADGwrkeiTRDIRLYGVDTCAPRQKARL-GDQEWPCGAVATAWLVTKTLNKWLSCRQA-RMENGVH 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046221699 104 VAECFVQGQSVNAWMVRSGWAVAY---------RQYATAfevdERLAQQQRRNLWQGAFQMPADYRRDK 163
Cdd:PRK06518  104 YAQCFVDGVDIAALGLAEGMAVLSkddhedpgpAQYASL----EEKARKAYRGLWSSTFQMPWDWRRDH 168
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
7-163 5.41e-50

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 160.61  E-value: 5.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699   7 LKLLKCWVLSVLVLIALPVSAAELVGRAT-VTDGDTITVAH----QRIRLWGIDAPESAQQCnahdGSAWPCGRRAAAAL 81
Cdd:COG1525     1 MRKLLLALLLALAALAAAAAAATLTAGVVrVIDGDTLRVRDdgkgERVRLAGIDAPELGQPC----GPEQPCGEEARQAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  82 DGYLLDKTVHCQP-KDTDRYGRTVAECFVQGQSVNAWMVRSGWAVAYRQYA-----TAFEVDERLAQQQRRNLWQGAFQM 155
Cdd:COG1525    77 RALLAGKTVTLEPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSpdkyaDRYLAAEAEARAARRGLWSDAFPV 156

                  ....*...
gi 1046221699 156 PADYRRDK 163
Cdd:COG1525   157 PPEWRRRK 164
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
36-149 2.83e-27

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 101.20  E-value: 2.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  36 VTDGDTITVAHQ-----RIRLWGIDAPESAQQCNAHDGSAWPCGRRAAAALDGYLLDKTVHCQPKDTDRYGRTVAECFVQ 110
Cdd:cd00175     2 VIDGDTIRVRLPpgpliTVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLN 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046221699 111 G-QSVNAWMVRSGWAVAYRQYATAFEVDERL------AQQQRRNLW 149
Cdd:cd00175    82 GgENIAEELVKEGLARVYRYYPDDSEYYDELleaeeaAKKARKGLW 127
SNc smart00318
Staphylococcal nuclease homologues;
36-149 4.91e-26

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 98.10  E-value: 4.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699   36 VTDGDTITVAHQ-----RIRLWGIDAPESAQQCNAHDGSAWPCGRRAAAALDGYLLDKTVHCQPKDTDRYGRTVAECFVQ 110
Cdd:smart00318  10 VIDGDTIRVRLPkgpliTIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLN 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1046221699  111 GQS-VNAWMVRSGWAVAYRQY------ATAFEVDERLAQQQRRNLW 149
Cdd:smart00318  90 GGNnIAEELVKEGLAKVYRYAdkdeyvYDELLEAEEAAKKARKGLW 135
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
48-149 6.07e-21

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 83.91  E-value: 6.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  48 RIRLWGIDAPESAQQCNAhdgsAWPCGRRAAAALDGYLLDKTVHCQPKDTDRYGRTVAECFVQGQSVNAWMVRSGWAVAY 127
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTP----VQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVY 76
                          90       100
                  ....*....|....*....|....*...
gi 1046221699 128 RQYATAFEVD------ERLAQQQRRNLW 149
Cdd:pfam00565  77 KAYPPNFKHYdellaaEEEAKKKKKGLW 104
PRK06518 PRK06518
hypothetical protein; Provisional
32-163 2.53e-19

hypothetical protein; Provisional


Pssm-ID: 235818  Cd Length: 177  Bit Score: 81.82  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046221699  32 GRATVTDGDT---ITVA-----HQRIRLWGIDAPESAQQCNAhDGSAWPCGRRAAAALDGYLLDKTVHCQPKdTDRYGRT 103
Cdd:PRK06518   26 GRAQVTSGVTfklIADGwrkeiTRDIRLYGVDTCAPRQKARL-GDQEWPCGAVATAWLVTKTLNKWLSCRQA-RMENGVH 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046221699 104 VAECFVQGQSVNAWMVRSGWAVAY---------RQYATAfevdERLAQQQRRNLWQGAFQMPADYRRDK 163
Cdd:PRK06518  104 YAQCFVDGVDIAALGLAEGMAVLSkddhedpgpAQYASL----EEKARKAYRGLWSSTFQMPWDWRRDH 168
 
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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