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Conserved domains on  [gi|1485532251|emb|SPR43324|]
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endonulease [Bordetella pertussis]

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 ...
27-244 3.43e-73

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: 222.81  E-value: 3.43e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  27 AVGHRDFRHAKKVLPRVYQNLERDFYCGCP--YQDKR--IDLQACGYEPRKQLRRAQQLEWEHVVPAWTLGHQRQCWQQr 102
Cdd:PRK15137   22 AEGINNFSQAKAAAVKVHADAPGTFYCGCKinWQGKKgvVDLQSCGYQVRKNENRASRIEWEHVVPAWQFGHQRQCWQD- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 103 vngkpGGRKHCSRtDPSFARAEGDLVNLMPSVGEVNGDRQNFRYAVWaDRPAPMYGQCETIVDFKTRRIQPRKYVRGRIA 182
Cdd:PRK15137  101 -----GGRKNCAK-DPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQW-NGGEGQYGQCAMKVDFKNKLAEPPARARGAIA 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485532251 183 RIQFYMVERYRLKLSREDRRVLCVWARAYPVDDWERARDQRIRTLQGNGNHYVTDpaAIQRQ 244
Cdd:PRK15137  174 RTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECERDERIAKVQGNHNPYVQR--ACQAR 233
 
Name Accession Description Interval E-value
PRK15137 PRK15137
DNA-specific endonuclease I; Provisional
27-244 3.43e-73

DNA-specific endonuclease I; Provisional


Pssm-ID: 185091  Cd Length: 235  Bit Score: 222.81  E-value: 3.43e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  27 AVGHRDFRHAKKVLPRVYQNLERDFYCGCP--YQDKR--IDLQACGYEPRKQLRRAQQLEWEHVVPAWTLGHQRQCWQQr 102
Cdd:PRK15137   22 AEGINNFSQAKAAAVKVHADAPGTFYCGCKinWQGKKgvVDLQSCGYQVRKNENRASRIEWEHVVPAWQFGHQRQCWQD- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 103 vngkpGGRKHCSRtDPSFARAEGDLVNLMPSVGEVNGDRQNFRYAVWaDRPAPMYGQCETIVDFKTRRIQPRKYVRGRIA 182
Cdd:PRK15137  101 -----GGRKNCAK-DPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQW-NGGEGQYGQCAMKVDFKNKLAEPPARARGAIA 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485532251 183 RIQFYMVERYRLKLSREDRRVLCVWARAYPVDDWERARDQRIRTLQGNGNHYVTDpaAIQRQ 244
Cdd:PRK15137  174 RTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECERDERIAKVQGNHNPYVQR--ACQAR 233
EndA COG2356
Endonuclease I [Replication, recombination and repair];
67-238 8.82e-54

Endonuclease I [Replication, recombination and repair];


Pssm-ID: 441923  Cd Length: 165  Bit Score: 170.84  E-value: 8.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  67 CGYeprkqlRRAQQLEWEHVVPAWTLGHqrqcwqqrvngkpggrkhcSRTDPsfarAEGDLVNLMPSVGEVNGDRQNFRY 146
Cdd:COG2356    13 CGY------QRADRWNREHVVPASWFGH-------------------GKSDP----METDLHHLRPADGEVNSDRSNFPF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 147 AVWADrPAPMYGQCETIVDFKTRRIQPRKYVRGRIARIQFYMVERYRLK---LSREDRRVLCVWARAYPVDDWERARDQR 223
Cdd:COG2356    64 GEVGG-AASKYGQCGMKVDFKGRVFEPRDEVKGDVARAYFYMATRYELRisvLSRGQLQLLLAWHKQDPVDAWERERNNR 142
                         170
                  ....*....|....*
gi 1485532251 224 IRTLQGNGNHYVTDP 238
Cdd:COG2356   143 IASIQGNRNPFIDHP 157
Endonuclease_1 pfam04231
Endonuclease I; Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli ...
82-238 2.61e-35

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: 125.69  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  82 EWEHVVPAWTLGHQRQcwqqrvngkpggrkhcsrtdpsfaRAEGDLVNLMPSVGEVNGDRQNFRYAVWAD---------R 152
Cdd:pfam04231  76 NREHIVPASVFGGQRQ------------------------PMESDAHHVVPTDGEVNADRSNFPYGEVNTatwtstngsK 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 153 PAPMYGQCETIVDFKTRRIQPRKYVRGRIARIQFYMVERYRLKLSREDRR-----------------VLCVWARAYPVDD 215
Cdd:pfam04231 132 KPNNLGSCNSAVGYKSRVFEPIDEFKGDIARAYFYMATRYELQISRWQSNdmfdgtsdqvfsnwflnLLLAWHAQDPVSA 211
                         170       180
                  ....*....|....*....|...
gi 1485532251 216 WERARDQRIRTLQGNGNHYVTDP 238
Cdd:pfam04231 212 KEIDRNNAIYGFQGNRNPFIDHP 234
 
Name Accession Description Interval E-value
PRK15137 PRK15137
DNA-specific endonuclease I; Provisional
27-244 3.43e-73

DNA-specific endonuclease I; Provisional


Pssm-ID: 185091  Cd Length: 235  Bit Score: 222.81  E-value: 3.43e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  27 AVGHRDFRHAKKVLPRVYQNLERDFYCGCP--YQDKR--IDLQACGYEPRKQLRRAQQLEWEHVVPAWTLGHQRQCWQQr 102
Cdd:PRK15137   22 AEGINNFSQAKAAAVKVHADAPGTFYCGCKinWQGKKgvVDLQSCGYQVRKNENRASRIEWEHVVPAWQFGHQRQCWQD- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 103 vngkpGGRKHCSRtDPSFARAEGDLVNLMPSVGEVNGDRQNFRYAVWaDRPAPMYGQCETIVDFKTRRIQPRKYVRGRIA 182
Cdd:PRK15137  101 -----GGRKNCAK-DPVYRKMESDMHNLQPAIGEVNGDRGNFMYSQW-NGGEGQYGQCAMKVDFKNKLAEPPARARGAIA 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485532251 183 RIQFYMVERYRLKLSREDRRVLCVWARAYPVDDWERARDQRIRTLQGNGNHYVTDpaAIQRQ 244
Cdd:PRK15137  174 RTYFYMRDQYQLTLSRQQTQLFNAWDKQYPVTDWECERDERIAKVQGNHNPYVQR--ACQAR 233
EndA COG2356
Endonuclease I [Replication, recombination and repair];
67-238 8.82e-54

Endonuclease I [Replication, recombination and repair];


Pssm-ID: 441923  Cd Length: 165  Bit Score: 170.84  E-value: 8.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  67 CGYeprkqlRRAQQLEWEHVVPAWTLGHqrqcwqqrvngkpggrkhcSRTDPsfarAEGDLVNLMPSVGEVNGDRQNFRY 146
Cdd:COG2356    13 CGY------QRADRWNREHVVPASWFGH-------------------GKSDP----METDLHHLRPADGEVNSDRSNFPF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 147 AVWADrPAPMYGQCETIVDFKTRRIQPRKYVRGRIARIQFYMVERYRLK---LSREDRRVLCVWARAYPVDDWERARDQR 223
Cdd:COG2356    64 GEVGG-AASKYGQCGMKVDFKGRVFEPRDEVKGDVARAYFYMATRYELRisvLSRGQLQLLLAWHKQDPVDAWERERNNR 142
                         170
                  ....*....|....*
gi 1485532251 224 IRTLQGNGNHYVTDP 238
Cdd:COG2356   143 IASIQGNRNPFIDHP 157
Endonuclease_1 pfam04231
Endonuclease I; Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli ...
82-238 2.61e-35

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: 125.69  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251  82 EWEHVVPAWTLGHQRQcwqqrvngkpggrkhcsrtdpsfaRAEGDLVNLMPSVGEVNGDRQNFRYAVWAD---------R 152
Cdd:pfam04231  76 NREHIVPASVFGGQRQ------------------------PMESDAHHVVPTDGEVNADRSNFPYGEVNTatwtstngsK 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485532251 153 PAPMYGQCETIVDFKTRRIQPRKYVRGRIARIQFYMVERYRLKLSREDRR-----------------VLCVWARAYPVDD 215
Cdd:pfam04231 132 KPNNLGSCNSAVGYKSRVFEPIDEFKGDIARAYFYMATRYELQISRWQSNdmfdgtsdqvfsnwflnLLLAWHAQDPVSA 211
                         170       180
                  ....*....|....*....|...
gi 1485532251 216 WERARDQRIRTLQGNGNHYVTDP 238
Cdd:pfam04231 212 KEIDRNNAIYGFQGNRNPFIDHP 234
 
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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