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Q2KID2 (NTH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endonuclease III-like protein 1

EC=3.2.2.-
EC=4.2.99.18
Alternative name(s):
Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase
Short name=DNA glycoslyase/AP lyase
Gene names
Name:NTHL1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines By similarity. HAMAP-Rule MF_03183

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. HAMAP-Rule MF_03183

Cofactor

Binds 1 4Fe-4S cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand By similarity.

Subunit structure

Interacts with YBX1 By similarity. HAMAP-Rule MF_03183

Subcellular location

Nucleus By similarity. Mitochondrion By similarity HAMAP-Rule MF_03183.

Sequence similarities

Belongs to the Nth/MutY family.

Contains 1 HhH domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 305277Endonuclease III-like protein 1 HAMAP-Rule MF_03183
PRO_0000244406

Regions

Domain192 – 21625HhH

Sites

Active site2131Nucleophile; for N-glycosylase activity By similarity
Metal binding2831Iron-sulfur (4Fe-4S) By similarity
Metal binding2901Iron-sulfur (4Fe-4S) By similarity
Metal binding2931Iron-sulfur (4Fe-4S) By similarity
Metal binding2991Iron-sulfur (4Fe-4S) By similarity
Site2321Important for catalytic activity By similarity

Amino acid modifications

Modified residue641Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KID2 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 9318553C857F500C

FASTA30533,645
        10         20         30         40         50         60 
MNAAGVRMVV TRARSRGTGA SLRRRGEKAA PLRSGEAAAE ERKSYSPVKR RRKAQRLSVA 

        70         80         90        100        110        120 
YEASEGEGGE GAEHLQAPSW QPQDWRQQLD NIRTMRSGKD APVDQLGAEH CFDPSASPKV 

       130        140        150        160        170        180 
RRYQVLLSLM LSSQTKDQVT AGAMQRLRAR GLTVDSILQT DDSTLGALIY PVGFWRSKVK 

       190        200        210        220        230        240 
YIKQTSAILQ QRYDGDIPAS VAELVALPGV GPKMAHLAMA VAWGTVSGIA VDTHVHRIAN 

       250        260        270        280        290        300 
RLRWTKKATK SPEETRRALE EWLPRELWSE INGLLVGFGQ QTCLPIRPRC QACLNRALCP 


AARGL 

« Hide

References

[1]"A whole-genome assembly of the domestic cow, Bos taurus."
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.
Genome Biol. 10:R42.01-R42.10(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GJ062847 Genomic DNA. Translation: DAA15605.1.
BC112681 mRNA. Translation: AAI12682.1.
RefSeqNP_001039862.1. NM_001046397.2.
UniGeneBt.6550.

3D structure databases

ProteinModelPortalQ2KID2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000046623.

Proteomic databases

PRIDEQ2KID2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000049780; ENSBTAP00000046623; ENSBTAG00000006272.
GeneID535203.
KEGGbta:535203.

Organism-specific databases

CTD4913.

Phylogenomic databases

eggNOGCOG0177.
GeneTreeENSGT00510000047513.
HOGENOMHOG000252209.
HOVERGENHBG052675.
InParanoidQ2KID2.
KOK10773.
OMAWRNKVKY.
OrthoDBEOG76MK8Z.
TreeFamTF314967.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_03183. Endonuclease_III_Nth.
InterProIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20876660.

Entry information

Entry nameNTH_BOVIN
AccessionPrimary (citable) accession number: Q2KID2
Secondary accession number(s): M5FK15
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families