ID   EXOG_XENLA              Reviewed;         358 AA.
AC   Q0IH72;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Nuclease EXOG, mitochondrial;
DE            EC=3.1.30.-;
DE   AltName: Full=Endonuclease G-like 1;
DE            Short=Endo G-like 1;
DE   Flags: Precursor;
GN   Name=exog; Synonyms=endogl1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endo/exonuclease with nicking activity towards supercoiled
CC       DNA, a preference for single-stranded DNA and 5'-3' exonuclease
CC       activity. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site contains 1 hydrated divalent metal
CC       cation that has only 1 direct interaction with the protein; all other
CC       interactions are via water molecules. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; BC123280; AAI23281.1; -; mRNA.
DR   RefSeq; NP_001090384.1; NM_001096915.1.
DR   AlphaFoldDB; Q0IH72; -.
DR   SMR; Q0IH72; -.
DR   DNASU; 779295; -.
DR   GeneID; 779295; -.
DR   KEGG; xla:779295; -.
DR   CTD; 779295; -.
DR   Xenbase; XB-GENE-981842; exog.L.
DR   OrthoDB; 933605at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 779295; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.570.10; -; 1.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR041003; Exog_C.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR040255; Non-specific_endonuclease.
DR   PANTHER; PTHR13966; PTHR13966; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   Pfam; PF18026; Exog_C; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SUPFAM; SSF54060; SSF54060; 1.
PE   2: Evidence at transcript level;
KW   Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Nuclease; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..358
FT                   /note="Nuclease EXOG, mitochondrial"
FT                   /id="PRO_0000342612"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  40494 MW;  748C613E773C5BB7 CRC64;
     MVASFSWRLL SPRFLGGFVL GAAASSASCV AALQLYDKRE PELAPVAPEE KDPLEEYGFP
     LTGTEARQYI NHALAYDPAK RTPKWVIEHL SRTKTVGSAD RKHCKFKPDP NIPKMFSATN
     EDYLGSGWTR GHMAPAGDNK FSTEAMAETF YLSNIVPQNY ENNAGFWNRM EMYCRDLTKR
     FEDVWVVSGP LELPTSHEDG KKRVTYEVIG ADEVAVPSHL YKVILVREKG SEQPLAIGAF
     VVPNSPIGFD HQLPEYKVQL EDLEKMSGLL FFPQLDRDKG LKPLCDVDSC RLIQLHEFKL
     YIAARRVGGA RNLQKLERIL SELKEEGITP DGYLLDLYEK KRKEFSLKSG TDRDERKG