ID NTH_EMENI Reviewed; 443 AA. AC C8VC05; Q5AVM7; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 2. DT 09-JUL-2014, entry version 31. DE RecName: Full=Endonuclease III homolog; DE EC=3.2.2.-; DE EC=4.2.99.18; DE AltName: Full=Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase; DE Short=DNA glycoslyase/AP lyase; DE Flags: Precursor; GN Name=nth1; ORFNames=ANIA_10978; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL OS 194 / M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [2] RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., RA von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., RA Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G., RA de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., RA Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., RA Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., RA Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., RA Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., RA Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., RA Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., RA Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., RA van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., RA Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., RA de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., RA Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a RT community effort."; RL Fungal Genet. Biol. 46:S2-13(2009). CC -!- FUNCTION: Bifunctional DNA N-glycosylase with associated CC apurinic/apyrimidinic (AP) lyase function that catalyzes the first CC step in base excision repair (BER), the primary repair pathway for CC the repair of oxidative DNA damage. The DNA N-glycosylase activity CC releases the damaged DNA base from DNA by cleaving the N- CC glycosidic bond, leaving an AP site. The AP lyase activity cleaves CC the phosphodiester bond 3' to the AP site by a beta-elimination. CC Primarily recognizes and repairs oxidative base damage of CC pyrimidines (By similarity). CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster does not appear to CC play a role in catalysis, but is probably involved in the proper CC positioning of the enzyme along the DNA strand (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Mitochondrion (By CC similarity). CC -!- SIMILARITY: Belongs to the Nth/MutY family. CC -!- SIMILARITY: Contains 1 HhH domain. CC -!- SEQUENCE CAUTION: CC Sequence=CBF79828.1; Type=Erroneous gene model prediction; CC Sequence=EAA61839.1; Type=Erroneous gene model prediction; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AACD01000130; EAA61839.1; ALT_SEQ; Genomic_DNA. DR EMBL; BN001304; CBF79828.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_680922.1; XM_675830.1. DR STRING; 162425.CADANIAP00000774; -. DR EnsemblFungi; CADANIAT00000774; CADANIAP00000774; CADANIAG00000774. DR GeneID; 2869384; -. DR KEGG; ani:AN7653.2; -. DR eggNOG; NOG290273; -. DR HOGENOM; HOG000252209; -. DR OMA; NKWHEIN; -. DR OrthoDB; EOG7PK99N; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 2. DR HAMAP; MF_03183; Endonuclease_III_Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR SMART; SM00478; ENDO3c; 1. DR SUPFAM; SSF48150; SSF48150; 2. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; KW Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion; KW Nucleus; Reference proteome; Transit peptide. FT TRANSIT 1 40 Mitochondrion (Potential). FT CHAIN 41 443 Endonuclease III homolog. FT /FTId=PRO_0000428804. FT DOMAIN 297 321 HhH. FT ACT_SITE 318 318 Nucleophile; for N-glycosylase activity FT (By similarity). FT METAL 386 386 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 393 393 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 396 396 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 404 404 Iron-sulfur (4Fe-4S) (By similarity). FT SITE 337 337 Important for catalytic activity (By FT similarity). SQ SEQUENCE 443 AA; 48637 MW; FCAA1786A6FD8861 CRC64; MCIEAMRTSR ASRETAKVLQ ALSPPARRQT RSTSHSALLK GFAYNAGKTE ADPDDGEDDG SSLTSVDTVD IEDILEPSAK RRKTKASSAA KTTSNSTRRT PEKKVEKLVK KENSQPKARR VPARKVKNED GSFTVEAPSN WDAIYSIVKK MREDNPTAPV DTMGCAELYW RASSPRDRRF QTLIALMLSS QTKDTVTAVA MQRLHTELGE GGAPAIKLET EHAESIVKQE AENGEPAIKQ EAKDGVPPAN PSHDSTLNLE NILAVSPERL NSLIGTVGFH NNKTKYIKKA AEIIRDQYNS DIPSTPAELM KLPGVGPKMA YLCMSAAWGK HEGIGVDVHV HRITNLWGWH KTKTPEETRM SLESWLPKDK WHEINKLLVG LGQTVCLPVG RRCGDCGLAG TKLCKSEIKG MAPKNNGRGL PKKEIVVETF SLTGEPKIKV EGE //