Conserved Protein Domain Family
AcNei2_N

?
cd08971: AcNei2_N 
N-terminal domain of the actinomycetal Nei2 and related DNA glycosylases
This family contains the N-terminal domain of the actinomycetal Nei2 and related DNA glycosylases. It belongs to the FpgNei_N, [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This family contains mostly actinomycetes and includes Mycobacterium tuberculosis Nei2 (MtuNei2). Complementation experiments in repair-deficient Escherichia coli (fpg mutY nei triple and nei nth double mutants), support that MtuNei2 is functionally active in vivo and recognizes both guanine and cytosine oxidation products. In addition to this AcNei2_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif.
Statistics
?
PSSM-Id: 176805
View PSSM: cd08971
Aligned: 39 rows
Threshold Bit Score: 114.222
Threshold Setting Gi: 262197858
Author:
Barrantes-Reynolds
Author Information
Name: Ramiro Barrantes-Reynolds
Address: Department of Microbiology and Molecular Genetics
University of Vermont
89 Beaumont Avenue
Burlington, VT 05405
USA
Created: 4-Jul-2009
Updated: 2-Oct-2020
Structure
?
Aligned Rows:
 
Feature 1:catalytic residue [active site]
Evidence:
  • Comment:This catalytic proline is almost perfectly conserved in FpgNei DNA glycolsylases. It acts as a nucleophile in catalysis.
  • Citation:PMID 9030608
  • Comment:Site-directed mutagenesis of this residue renders Fpg proteins defective in catalysis but still able to make the Schiff-base intermediate.
  • Citation:PMID 9654091
  • Comment:Site-directed mutagensis of this residue renders Escherichia coli Nei inactive but still able to make the Schiff-base intermediate.
  • Comment:1KFV_A , is a structure of a mutant Lactococcus Lactis Fpg which has a Gly in place of a Pro at this position.

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1         #                                                                              
ZP_04031420    1 MPEGDTVWLAARRLHRaLAGWALt--VCDV--------RVPRYATTDLRGQRVr-EAVSRGKHLLIRVd----------- 58  Thermomonospora...
ABX10726       1 MPEGDTIHRAAANLRKvLDRQKIv--SASG--------RQEVLSVADLAEATVt-GVEARGKHLLIHFd----------- 58  uncultured plan...
YP_001378913   1 MPEGDTIHRAARNLHGaLAGEVVi--RFETvl----prLARVDEDRPVAGRTVe-SVTARGKHLLLRFs----------- 62  Anaeromyxobacte...
ZP_03712289    1 MPEGDSIYQLSRRLQF-LVGRTVl--AADI--------RVPRHATVNLAGTTIr-RVWPYGKHLFMQLd----------- 57  Corynebacterium...
YP_589459      1 MPEGDTIFRAARTLQRaLAGKVVt--RFETvl----pkLARVDEDAPLAGRTVv-DVEARGKWMLMHFs----------- 62  Acidobacteria b...
NP_939193      1 MPEGDSVFQLARRLSF-MQGRTIt--HTSL--------RVPAYATMRFDGRTIt-KVWPYGKHLFMHIg----------- 57  Corynebacterium...
YP_002754793   1 MPEGDTIFRSARTLHKaLAGTIVtgfVTEFa------qLAAVHDNTPVTGRTIe-QVESRGKWLLIHFs----------- 62  Acidobacterium ...
ZP_01911505    1 MPEGDSLHATAITLRAvLAGRELt--GCELnwsgrrgvALAHGEAWRVPGRRVe-SVEARGKNLLIRCaphpeavgavea 77  Plesiocystis pa...
YP_002515232   1 MPEGDTLHKLAKALQPrLQGQAI---RLTR--------LRGVPPRTPLPEGRVe-SVTAEGKHLLIRFtge--------- 59  Thioalkalivibri...
YP_003461489   1 MPEGDTIHKLARVLGPaLAGAPLe--SVAT--------RARRGAVLVEHGAMTvrRVSARGKHLLIALeda--------- 61  Thioalkalivibri...
Feature 1                                                                                  
ZP_04031420   59 -----gGLSVHVHLKMDGRWLIRPa----GPVPRDHRIRLALGne---rHLALGYR--------LGVVEVLPTA 112 Thermomonospora curva...
ABX10726      59 -----sDLVVHSHMGMTGSWHIYRltdswQKPDTQAVLVLKTAa-----WCVVCFT--------PKLLEIVSET 114 uncultured planctomyc...
YP_001378913  63 -----gDLVLRTHLRMNGSWHLYRpgerwFRPRDAMRVLVETRp-----WIAVGFD--------LPVAELLDAR 118 Anaeromyxobacter sp. ...
ZP_03712289   58 ------DAIIHTHLKMEGTWAIHRvgdrwRRPVHTARLILRVAdpphqpIELVGHS--------LGFVKIFSAK 117 Corynebacterium matru...
YP_589459     63 -----gDLILLTHMLMSGSWHIYRpgeqwQRSRNDMRVVIETSd-----ILAVAFR--------VPVAEFHTEE 118 Acidobacteria bacteri...
NP_939193     58 ------SEILHTHLKMEGTWAVHRagdrwRKPGHTARVVLHLDdaphdpIEVVGHE--------LGFVRVFPDH 117 Corynebacterium dipht...
YP_002754793  63 -----gDLILVTHMLMSGSWHIYRrgerwRRGRSHMRVLLANEt-----YEAIAFD--------VPVARFYTSR 118 Acidobacterium capsul...
ZP_01911505   78 ggraalALTIWSHMGMTGSWHTYRprerwALPPRDAPIVLRTAe-----RVVPCFR--------PHALELLGPR 138 Plesiocystis pacifica...
YP_002515232  60 ---eggAQVLRTHLGLWGGWHQYApgepwRKPARQAWVVLQADd-----AVFVCFN--------AREVEVMSAG 117 Thioalkalivibrio sp. ...
YP_003461489  62 ---agrAWRLRTHLGMYGTWHQYApgaawHKPDHQAWAVLRLAd-----RVLVCFHprelawqlLSEGRADPER 127 Thioalkalivibrio sp. ...

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap