NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034599331|ref|XP_016880002|]
View 

endonuclease V isoform X21 [Homo sapiens]

Protein Classification

endonuclease V( domain architecture ID 3329)

endonuclease V selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA

CATH:  3.30.2170.10
EC:  3.1.21.7
SCOP:  4004835

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Endonuclease_V super family cl00653
Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine ...
1-53 1.42e-15

Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine bases; Endonuclease_V (EndoV) is an enzyme that can initiate repair of all possible deaminated DNA bases. EndoV cleaves the DNA strand containing lesions at the second phosphodiester bond 3' to the lesion using Mg2+ as a cofactor. EndoV homologs are conserved throughout all domains of life from bacteria to humans. EndoV is encoded by the nfi gene and nfi null mutant mice have a phenotype prone to cancer. The ability of endonuclease V to recognize mismatches and abnormal replicative DNA structures suggests that the enzyme plays an important role in DNA metabolism. The details of downstream processing for the EndoV pathway remain unknown.


The actual alignment was detected with superfamily member cd06559:

Pssm-ID: 469860  Cd Length: 208  Bit Score: 70.99  E-value: 1.42e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034599331   1 MALRSHDRsTRPLYISVGHRMSLEAAVRLTCCCC-RFRIPEPVRQVHLLlcSRR 53
Cdd:cd06559   158 AALRTRDG-VKPVYVSPGHRIDLETAVELVLKCCkGYRLPEPTRLADLL--SRE 208
 
Name Accession Description Interval E-value
Endonuclease_V cd06559
Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine ...
1-53 1.42e-15

Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine bases; Endonuclease_V (EndoV) is an enzyme that can initiate repair of all possible deaminated DNA bases. EndoV cleaves the DNA strand containing lesions at the second phosphodiester bond 3' to the lesion using Mg2+ as a cofactor. EndoV homologs are conserved throughout all domains of life from bacteria to humans. EndoV is encoded by the nfi gene and nfi null mutant mice have a phenotype prone to cancer. The ability of endonuclease V to recognize mismatches and abnormal replicative DNA structures suggests that the enzyme plays an important role in DNA metabolism. The details of downstream processing for the EndoV pathway remain unknown.


Pssm-ID: 143472  Cd Length: 208  Bit Score: 70.99  E-value: 1.42e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034599331   1 MALRSHDRsTRPLYISVGHRMSLEAAVRLTCCCC-RFRIPEPVRQVHLLlcSRR 53
Cdd:cd06559   158 AALRTRDG-VKPVYVSPGHRIDLETAVELVLKCCkGYRLPEPTRLADLL--SRE 208
Endonuclease_5 pfam04493
Endonuclease V; Endonuclease V is specific for single-stranded DNA or for duplex DNA that ...
2-47 7.04e-15

Endonuclease V; Endonuclease V is specific for single-stranded DNA or for duplex DNA that contains uracil or that is damaged by a variety of agents.


Pssm-ID: 427979  Cd Length: 198  Bit Score: 69.02  E-value: 7.04e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034599331   2 ALRSHDRStRPLYISVGHRMSLEAAVRLTC-CCCRFRIPEPVRQVHL 47
Cdd:pfam04493 153 VLRTRKNV-KPIYVSPGHRISLDTALELVLrCLRGYRLPEPTRLADL 198
Nfi COG1515
Deoxyinosine 3'-endonuclease (endonuclease V) [Replication, recombination and repair];
1-48 2.90e-14

Deoxyinosine 3'-endonuclease (endonuclease V) [Replication, recombination and repair];


Pssm-ID: 441124  Cd Length: 221  Bit Score: 67.85  E-value: 2.90e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034599331   1 MALRSHDRsTRPLYISVGHRMSLEAAVRLT-CCCCRFRIPEPVRQVHLL 48
Cdd:COG1515   166 AVLRTRDG-VKPLYVSPGHRISLETALELVlACTPGYRLPEPTRLADRL 213
PRK11617 PRK11617
deoxyribonuclease V;
2-53 7.63e-08

deoxyribonuclease V;


Pssm-ID: 236937  Cd Length: 224  Bit Score: 50.32  E-value: 7.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034599331   2 ALRSHDRsTRPLYISVGHRMSLEAAVRLTCCCCR-FRIPEPVRQVHlLLCSRR 53
Cdd:PRK11617  163 VWRSKAR-CNPLFISTGHRVSLDSALAWVQRCMKgYRLPEPTRWAD-ALASRR 213
 
Name Accession Description Interval E-value
Endonuclease_V cd06559
Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine ...
1-53 1.42e-15

Endonuclease_V, a DNA repair enzyme that initiates repair of nitrosative deaminated purine bases; Endonuclease_V (EndoV) is an enzyme that can initiate repair of all possible deaminated DNA bases. EndoV cleaves the DNA strand containing lesions at the second phosphodiester bond 3' to the lesion using Mg2+ as a cofactor. EndoV homologs are conserved throughout all domains of life from bacteria to humans. EndoV is encoded by the nfi gene and nfi null mutant mice have a phenotype prone to cancer. The ability of endonuclease V to recognize mismatches and abnormal replicative DNA structures suggests that the enzyme plays an important role in DNA metabolism. The details of downstream processing for the EndoV pathway remain unknown.


Pssm-ID: 143472  Cd Length: 208  Bit Score: 70.99  E-value: 1.42e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034599331   1 MALRSHDRsTRPLYISVGHRMSLEAAVRLTCCCC-RFRIPEPVRQVHLLlcSRR 53
Cdd:cd06559   158 AALRTRDG-VKPVYVSPGHRIDLETAVELVLKCCkGYRLPEPTRLADLL--SRE 208
Endonuclease_5 pfam04493
Endonuclease V; Endonuclease V is specific for single-stranded DNA or for duplex DNA that ...
2-47 7.04e-15

Endonuclease V; Endonuclease V is specific for single-stranded DNA or for duplex DNA that contains uracil or that is damaged by a variety of agents.


Pssm-ID: 427979  Cd Length: 198  Bit Score: 69.02  E-value: 7.04e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034599331   2 ALRSHDRStRPLYISVGHRMSLEAAVRLTC-CCCRFRIPEPVRQVHL 47
Cdd:pfam04493 153 VLRTRKNV-KPIYVSPGHRISLDTALELVLrCLRGYRLPEPTRLADL 198
Nfi COG1515
Deoxyinosine 3'-endonuclease (endonuclease V) [Replication, recombination and repair];
1-48 2.90e-14

Deoxyinosine 3'-endonuclease (endonuclease V) [Replication, recombination and repair];


Pssm-ID: 441124  Cd Length: 221  Bit Score: 67.85  E-value: 2.90e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034599331   1 MALRSHDRsTRPLYISVGHRMSLEAAVRLT-CCCCRFRIPEPVRQVHLL 48
Cdd:COG1515   166 AVLRTRDG-VKPLYVSPGHRISLETALELVlACTPGYRLPEPTRLADRL 213
PRK11617 PRK11617
deoxyribonuclease V;
2-53 7.63e-08

deoxyribonuclease V;


Pssm-ID: 236937  Cd Length: 224  Bit Score: 50.32  E-value: 7.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034599331   2 ALRSHDRsTRPLYISVGHRMSLEAAVRLTCCCCR-FRIPEPVRQVHlLLCSRR 53
Cdd:PRK11617  163 VWRSKAR-CNPLFISTGHRVSLDSALAWVQRCMKgYRLPEPTRWAD-ALASRR 213
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH