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Conserved domains on  [gi|492049399|ref|WP_005732586|]
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MULTISPECIES: endonuclease [Pseudomonas]

Protein Classification

HNH endonuclease family protein( domain architecture ID 1640)

HNH endonuclease family protein, similar to Physarum polycephalum intron-encoded endonuclease I-Ppoi which mediates the mobility of intron 3 in the ribosomal DNA

EC:  3.1.-.-
Gene Ontology:  GO:0004519

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HNHc super family cl00083
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
2-224 9.67e-87

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


The actual alignment was detected with superfamily member PRK15137:

Pssm-ID: 469607  Cd Length: 235  Bit Score: 256.71  E-value: 9.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399   2 MFRFSTLLCTTLLITASFSAQAQAPRTFSEAKKVAWGLYAPQSTEFYCGCK--YTGNR--VDIAGCGYVPRKSAKRASRI 77
Cdd:PRK15137   1 MYRNLSIAAVLLSAAFSGPALAEGINNFSQAKAAAVKVHADAPGTFYCGCKinWQGKKgvVDLQSCGYQVRKNENRASRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  78 EWEHIVPAWQIGHLRQCWQNGGRKNCTKtDAVYKRAEADLHNLVPSIGEVNGDRSNFSFGWVPEQKGQYGSCLTQVDFKA 157
Cdd:PRK15137  81 EWEHVVPAWQFGHQRQCWQDGGRKNCAK-DPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKN 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492049399 158 KKVMPRPSIRGMIARTYFYMSKQYNLRLSRQDQQLYQAWDKTYPPQAWERQRNQQVACVMGRGNDFV 224
Cdd:PRK15137 160 KLAEPPARARGAIARTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECERDERIAKVQGNHNPYV 226
 
Name Accession Description Interval E-value
PRK15137 PRK15137
DNA-specific endonuclease I; Provisional
2-224 9.67e-87

DNA-specific endonuclease I; Provisional


Pssm-ID: 185091  Cd Length: 235  Bit Score: 256.71  E-value: 9.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399   2 MFRFSTLLCTTLLITASFSAQAQAPRTFSEAKKVAWGLYAPQSTEFYCGCK--YTGNR--VDIAGCGYVPRKSAKRASRI 77
Cdd:PRK15137   1 MYRNLSIAAVLLSAAFSGPALAEGINNFSQAKAAAVKVHADAPGTFYCGCKinWQGKKgvVDLQSCGYQVRKNENRASRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  78 EWEHIVPAWQIGHLRQCWQNGGRKNCTKtDAVYKRAEADLHNLVPSIGEVNGDRSNFSFGWVPEQKGQYGSCLTQVDFKA 157
Cdd:PRK15137  81 EWEHVVPAWQFGHQRQCWQDGGRKNCAK-DPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKN 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492049399 158 KKVMPRPSIRGMIARTYFYMSKQYNLRLSRQDQQLYQAWDKTYPPQAWERQRNQQVACVMGRGNDFV 224
Cdd:PRK15137 160 KLAEPPARARGAIARTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECERDERIAKVQGNHNPYV 226
EndA COG2356
Endonuclease I [Replication, recombination and repair];
63-232 4.46e-63

Endonuclease I [Replication, recombination and repair];


Pssm-ID: 441923  Cd Length: 165  Bit Score: 193.95  E-value: 4.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  63 CGYvprksaKRASRIEWEHIVPAWQIGHlrqcwqnggrkncTKTDAvykrAEADLHNLVPSIGEVNGDRSNFSFGWVPEQ 142
Cdd:COG2356   13 CGY------QRADRWNREHVVPASWFGH-------------GKSDP----METDLHHLRPADGEVNSDRSNFPFGEVGGA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399 143 KGQYGSCLTQVDFKAKKVMPRPSIRGMIARTYFYMSKQYNLR---LSRQDQQLYQAWDKTYPPQAWERQRNQQVACVMGR 219
Cdd:COG2356   70 ASKYGQCGMKVDFKGRVFEPRDEVKGDVARAYFYMATRYELRisvLSRGQLQLLLAWHKQDPVDAWERERNNRIASIQGN 149
                        170
                 ....*....|...
gi 492049399 220 GNDFVGPVDLKAC 232
Cdd:COG2356  150 RNPFIDHPELADR 162
Endonuclease_1 pfam04231
Endonuclease I; Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli ...
47-224 5.12e-39

Endonuclease I; Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli endonuclease I (EndoI) is a sequence independent endonuclease located in the periplasm. It is inhibited by different RNA species. It is thought to normally generate double strand breaks in DNA, except in the presence of high salt concentrations and RNA, when it generates single strand breaks in DNA. Its biological role is unknown. Other family members are known to be extracellular. This family also includes a non-specific, Mg2+ activated ribonuclease precursor.


Pssm-ID: 398077 [Multi-domain]  Cd Length: 235  Bit Score: 134.94  E-value: 5.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399   47 FYCGC---KYTGN---RVDIAG-------CGYVP-------RKSAKRAsrIEWEHIVPAWQIGHLRQcwqnggrknctkt 106
Cdd:pfam04231  27 LYCGCdwdNYYENdgsILDMYSenptgpdYSFTYgtnqcgsYSQEGRC--YNREHIVPASVFGGQRQ------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  107 davykRAEADLHNLVPSIGEVNGDRSNFSFGWV----------PEQKGQYGSCLTQVDFKAKKVMPRPSIRGMIARTYFY 176
Cdd:pfam04231  92 -----PMESDAHHVVPTDGEVNADRSNFPYGEVntatwtstngSKKPNNLGSCNSAVGYKSRVFEPIDEFKGDIARAYFY 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492049399  177 MSKQYNLRLSRQD-----------------QQLYQAWDKTYPPQAWERQRNQQVACVMGRGNDFV 224
Cdd:pfam04231 167 MATRYELQISRWQsndmfdgtsdqvfsnwfLNLLLAWHAQDPVSAKEIDRNNAIYGFQGNRNPFI 231
 
Name Accession Description Interval E-value
PRK15137 PRK15137
DNA-specific endonuclease I; Provisional
2-224 9.67e-87

DNA-specific endonuclease I; Provisional


Pssm-ID: 185091  Cd Length: 235  Bit Score: 256.71  E-value: 9.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399   2 MFRFSTLLCTTLLITASFSAQAQAPRTFSEAKKVAWGLYAPQSTEFYCGCK--YTGNR--VDIAGCGYVPRKSAKRASRI 77
Cdd:PRK15137   1 MYRNLSIAAVLLSAAFSGPALAEGINNFSQAKAAAVKVHADAPGTFYCGCKinWQGKKgvVDLQSCGYQVRKNENRASRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  78 EWEHIVPAWQIGHLRQCWQNGGRKNCTKtDAVYKRAEADLHNLVPSIGEVNGDRSNFSFGWVPEQKGQYGSCLTQVDFKA 157
Cdd:PRK15137  81 EWEHVVPAWQFGHQRQCWQDGGRKNCAK-DPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKN 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492049399 158 KKVMPRPSIRGMIARTYFYMSKQYNLRLSRQDQQLYQAWDKTYPPQAWERQRNQQVACVMGRGNDFV 224
Cdd:PRK15137 160 KLAEPPARARGAIARTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECERDERIAKVQGNHNPYV 226
EndA COG2356
Endonuclease I [Replication, recombination and repair];
63-232 4.46e-63

Endonuclease I [Replication, recombination and repair];


Pssm-ID: 441923  Cd Length: 165  Bit Score: 193.95  E-value: 4.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  63 CGYvprksaKRASRIEWEHIVPAWQIGHlrqcwqnggrkncTKTDAvykrAEADLHNLVPSIGEVNGDRSNFSFGWVPEQ 142
Cdd:COG2356   13 CGY------QRADRWNREHVVPASWFGH-------------GKSDP----METDLHHLRPADGEVNSDRSNFPFGEVGGA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399 143 KGQYGSCLTQVDFKAKKVMPRPSIRGMIARTYFYMSKQYNLR---LSRQDQQLYQAWDKTYPPQAWERQRNQQVACVMGR 219
Cdd:COG2356   70 ASKYGQCGMKVDFKGRVFEPRDEVKGDVARAYFYMATRYELRisvLSRGQLQLLLAWHKQDPVDAWERERNNRIASIQGN 149
                        170
                 ....*....|...
gi 492049399 220 GNDFVGPVDLKAC 232
Cdd:COG2356  150 RNPFIDHPELADR 162
Endonuclease_1 pfam04231
Endonuclease I; Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli ...
47-224 5.12e-39

Endonuclease I; Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli endonuclease I (EndoI) is a sequence independent endonuclease located in the periplasm. It is inhibited by different RNA species. It is thought to normally generate double strand breaks in DNA, except in the presence of high salt concentrations and RNA, when it generates single strand breaks in DNA. Its biological role is unknown. Other family members are known to be extracellular. This family also includes a non-specific, Mg2+ activated ribonuclease precursor.


Pssm-ID: 398077 [Multi-domain]  Cd Length: 235  Bit Score: 134.94  E-value: 5.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399   47 FYCGC---KYTGN---RVDIAG-------CGYVP-------RKSAKRAsrIEWEHIVPAWQIGHLRQcwqnggrknctkt 106
Cdd:pfam04231  27 LYCGCdwdNYYENdgsILDMYSenptgpdYSFTYgtnqcgsYSQEGRC--YNREHIVPASVFGGQRQ------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492049399  107 davykRAEADLHNLVPSIGEVNGDRSNFSFGWV----------PEQKGQYGSCLTQVDFKAKKVMPRPSIRGMIARTYFY 176
Cdd:pfam04231  92 -----PMESDAHHVVPTDGEVNADRSNFPYGEVntatwtstngSKKPNNLGSCNSAVGYKSRVFEPIDEFKGDIARAYFY 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492049399  177 MSKQYNLRLSRQD-----------------QQLYQAWDKTYPPQAWERQRNQQVACVMGRGNDFV 224
Cdd:pfam04231 167 MATRYELQISRWQsndmfdgtsdqvfsnwfLNLLLAWHAQDPVSAKEIDRNNAIYGFQGNRNPFI 231
 
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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