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Q8NTL4 (Q8NTL4_CORGL) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate By similarity. HAMAP-Rule MF_00942

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. PIRNR PIRNR001435 HAMAP-Rule MF_00942

Cofactor

Binds 1 4Fe-4S cluster By similarity. PIRNR PIRNR001435 HAMAP-Rule MF_00942

Sequence similarities

Belongs to the Nth/MutY family. PIRNR PIRNR001435 HAMAP-Rule MF_00942

Contains 1 HhH domain. HAMAP-Rule MF_00942

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain125 – 15127HhH By similarity HAMAP-Rule MF_00942

Sites

Metal binding2121Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942
Metal binding2191Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942
Metal binding2221Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942
Metal binding2281Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942

Sequences

Sequence LengthMass (Da)Tools
Q8NTL4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 823BACDBDE55190F

FASTA26028,918
        10         20         30         40         50         60 
MGSITPQKRP RVGSHIANKG QETDIGRKRR ARRINRTLTV AYPDAHCELD FTNPLELTVA 

        70         80         90        100        110        120 
TILSAQCTDV RVNQVTPALF KRYPTATDYA NADRTELEEF IRPTGFYRNK ATSLIGLGEA 

       130        140        150        160        170        180 
LISLHDGQVP GTLEQLVELP GVGRKTANVV LGNAFGVPGI TVDTHFGRLV RRLKLTDEED 

       190        200        210        220        230        240 
PVKVEKVMNE LIEKPEWTMF SHRLIFHGRR ICHSRRAACG ACMLAADCPS FGLEGPSDPF 

       250        260 
EAQKLIKSDD REHLLKMAGM 

« Hide

References

« Hide 'large scale' references
[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 and DSM 20300 EMBL CAF18863.1.
[4]Kalinowski J.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 20300 EMBL CAF18863.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB97686.1.
BX927148 Genomic DNA. Translation: CAF18863.1.
RefSeqNP_599545.1. NC_003450.3.
YP_224592.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NTL4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg0353.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB97686; BAB97686; BAB97686.
CAF18863; CAF18863; cg0353.
GeneID1021358.
3343750.
KEGGcgb:cg0353.
cgl:NCgl0288.
PATRIC21492650. VBICorGlu203724_0297.

Phylogenomic databases

HOGENOMHOG000252208.
KOK10773.
OMANNKSKHL.
OrthoDBEOG6H4KC5.
ProtClustDBCLSK632780.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_00942. Nth.
InterProIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR023170. HTH_base_excis_C.
IPR005759. Nth.
[Graphical view]
PfamPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
PIRSFPIRSF001435. Nth. 1 hit.
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
TIGRFAMsTIGR01083. nth. 1 hit.
PROSITEPS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ8NTL4_CORGL
AccessionPrimary (citable) accession number: Q8NTL4
Secondary accession number(s): Q6M869
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2002
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)