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Q8SRB8

- NTH_ENCCU

UniProt

Q8SRB8 - NTH_ENCCU

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Protein
Endonuclease III homolog
Gene
NTH1, ECU08_0880
Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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.UniRule annotation

Cofactori

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 1491Nucleophile; for N-glycosylase activity By similarity
Sitei168 – 1681Important for catalytic activity By similarity
Metal bindingi217 – 2171Iron-sulfur (4Fe-4S) By similarity
Metal bindingi224 – 2241Iron-sulfur (4Fe-4S) By similarity
Metal bindingi227 – 2271Iron-sulfur (4Fe-4S) By similarity
Metal bindingi233 – 2331Iron-sulfur (4Fe-4S) By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
  3. hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. base-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NTH1
Ordered Locus Names:ECU08_0880
OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Taxonomic identifieri284813 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
ProteomesiUP000000819: Chromosome VIII

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU08_0880.

Subcellular locationi

Nucleus By similarity. Mitochondrion By similarity UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Endonuclease III homologUniRule annotation
PRO_0000382919Add
BLAST

Expressioni

Developmental stagei

Expressed in late sporogonial stages.UniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi6035.ECU08_0880.

Structurei

3D structure databases

ProteinModelPortaliQ8SRB8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 15527HhH
Add
BLAST

Sequence similaritiesi

Belongs to the Nth/MutY family.
Contains 1 HhH domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0177.
HOGENOMiHOG000252209.
KOiK10773.
OMAiHINECIK.
OrthoDBiEOG7PK99N.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth.
InterProiIPR011257. 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]
PfamiPF00730. HhH-GPD. 1 hit.
[Graphical view]
PIRSFiPIRSF001435. Nth. 1 hit.
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8SRB8-1 [UniParc]FASTAAdd to Basket

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MGSASGEERE GPLGLYLEIK MQRKDIVSPV DTMGCSITPS CRTEEERRFH    50
ILVSLLLSSQ TKDEVTYEAM ARLRKLLPES AATDGEARGG LTIERVANSD 100
VKHINECIKK VGFHNRKAAN LKKIAEILRE KGLPREMKDL ISLPGIGNKM 150
ALLYMSHACN RTVGISVDTH VHRISNRIGL VRTRDVESTR RELERVVPRK 200
EWKTINNILV GFGQTICVAK RPRCEECCIR GRCPSSLF 238
Length:238
Mass (Da):26,755
Last modified:June 1, 2002 - v1
Checksum:i3D9D7B774187F35B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL590448 Genomic DNA. Translation: CAD26394.1.
RefSeqiNP_597218.1. NM_001041827.1.

Genome annotation databases

GeneIDi859640.
KEGGiecu:ECU08_0880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL590448 Genomic DNA. Translation: CAD26394.1 .
RefSeqi NP_597218.1. NM_001041827.1.

3D structure databases

ProteinModelPortali Q8SRB8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6035.ECU08_0880.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 859640.
KEGGi ecu:ECU08_0880.

Organism-specific databases

EuPathDBi MicrosporidiaDB:ECU08_0880.

Phylogenomic databases

eggNOGi COG0177.
HOGENOMi HOG000252209.
KOi K10773.
OMAi HINECIK.
OrthoDBi EOG7PK99N.

Family and domain databases

Gene3Di 1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPi MF_03183. Endonuclease_III_Nth.
InterProi IPR011257. 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 ]
Pfami PF00730. HhH-GPD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001435. Nth. 1 hit.
SMARTi SM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view ]
SUPFAMi SSF48150. SSF48150. 1 hit.
PROSITEi PS00764. ENDONUCLEASE_III_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiNTH_ENCCU
AccessioniPrimary (citable) accession number: Q8SRB8
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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