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Q8SRB8 (NTH_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endonuclease III homolog

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:NTH1
Ordered Locus Names:ECU08_0880
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Subcellular location

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

Developmental stage

Expressed in late sporogonial stages. 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

Chain1 – 238238Endonuclease III homolog HAMAP-Rule MF_03183
PRO_0000382919

Regions

Domain129 – 15527HhH

Sites

Active site1491Nucleophile; for N-glycosylase activity By similarity
Metal binding2171Iron-sulfur (4Fe-4S) By similarity
Metal binding2241Iron-sulfur (4Fe-4S) By similarity
Metal binding2271Iron-sulfur (4Fe-4S) By similarity
Metal binding2331Iron-sulfur (4Fe-4S) By similarity
Site1681Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8SRB8 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 3D9D7B774187F35B

FASTA23826,755
        10         20         30         40         50         60 
MGSASGEERE GPLGLYLEIK MQRKDIVSPV DTMGCSITPS CRTEEERRFH ILVSLLLSSQ 

        70         80         90        100        110        120 
TKDEVTYEAM ARLRKLLPES AATDGEARGG LTIERVANSD VKHINECIKK VGFHNRKAAN 

       130        140        150        160        170        180 
LKKIAEILRE KGLPREMKDL ISLPGIGNKM ALLYMSHACN RTVGISVDTH VHRISNRIGL 

       190        200        210        220        230 
VRTRDVESTR RELERVVPRK EWKTINNILV GFGQTICVAK RPRCEECCIR GRCPSSLF 

« Hide

References

[1]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.
[2]"Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages."
Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.
Proteomics 6:3625-3635(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590448 Genomic DNA. Translation: CAD26394.1.
RefSeqNP_597218.1. NM_001041827.1.

3D structure databases

ProteinModelPortalQ8SRB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6035.ECU08_0880.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID859640.
KEGGecu:ECU08_0880.

Organism-specific databases

EuPathDBMicrosporidiaDB:ECU08_0880.

Phylogenomic databases

eggNOGCOG0177.
HOGENOMHOG000252209.
KOK10773.
OMAHINECIK.
OrthoDBEOG7PK99N.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_03183. Endonuclease_III_Nth.
InterProIPR011257. DNA_glycosylase.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR005759. Nth.
[Graphical view]
PfamPF00730. HhH-GPD. 1 hit.
[Graphical view]
PIRSFPIRSF001435. Nth. 1 hit.
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNTH_ENCCU
AccessionPrimary (citable) accession number: Q8SRB8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families