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 23-FEB-2022, entry version 64. DE RecName: Full=Endonuclease III homolog {ECO:0000255|HAMAP-Rule:MF_03183}; DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03183}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_03183}; DE AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_03183}; DE Short=DNA glycosylase/AP lyase {ECO:0000255|HAMAP-Rule:MF_03183}; DE Flags: Precursor; GN Name=nth1; ORFNames=ANIA_10978; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / OS M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Nidulantes. 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., Batzoglou S., RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., RA Denning D.W., 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., von Dohren H., RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K., RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J., RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., RA Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a community RT 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 step CC in base excision repair (BER), the primary repair pathway for the CC repair of oxidative DNA damage. The DNA N-glycosylase activity releases CC the damaged DNA base from DNA by cleaving the N-glycosidic bond, CC leaving an AP site. The AP lyase activity cleaves the phosphodiester CC bond 3' to the AP site by a beta-elimination. Primarily recognizes and CC repairs oxidative base damage of pyrimidines. {ECO:0000255|HAMAP- CC Rule:MF_03183}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'- CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3- CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho- CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA- CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03183}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03183}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a CC role in catalysis, but is probably involved in the proper positioning CC of the enzyme along the DNA strand. {ECO:0000255|HAMAP-Rule:MF_03183}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}. CC Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183}. CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP- CC Rule:MF_03183}. CC -!- SEQUENCE CAUTION: CC Sequence=CBF79828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=EAA61839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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 SMR; C8VC05; -. DR STRING; 227321.C8VC05; -. DR EnsemblFungi; EAA61839; EAA61839; AN7653.2. DR GeneID; 2869384; -. DR KEGG; ani:AN7653.2; -. DR eggNOG; KOG1921; Eukaryota. DR HOGENOM; CLU_305877_0_0_1; -. DR InParanoid; C8VC05; -. DR OrthoDB; 1322642at2759; -. DR Proteomes; UP000000560; Chromosome IV. DR Proteomes; UP000005890; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central. DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central. DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central. DR CDD; cd00056; ENDO3c; 1. DR Gene3D; 1.10.1670.10; -; 1. 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; IPR023170; HhH_base_excis_C. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR030841; NTH1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR SMART; SM00478; ENDO3c; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; KW Lyase; Metal-binding; Mitochondrion; Nucleus; Reference proteome; KW Transit peptide. FT TRANSIT 1..40 FT /note="Mitochondrion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT CHAIN 41..443 FT /note="Endonuclease III homolog" FT /id="PRO_0000428804" FT DOMAIN 297..321 FT /note="HhH" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT REGION 1..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 97..126 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 318 FT /note="Nucleophile; for N-glycosylase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT METAL 386 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT METAL 393 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT METAL 396 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT METAL 404 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" FT SITE 337 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183" 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 //