ID   EXOG_DANRE              Reviewed;         343 AA.
AC   Q502K1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 67.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH95666.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC095666; AAH95666.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q502K1; -.
DR   SMR; Q502K1; -.
DR   PRIDE; Q502K1; -.
DR   InParanoid; Q502K1; -.
DR   PRO; PR:Q502K1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
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           ?..343
FT                   /note="Nuclease EXOG, mitochondrial"
FT                   /id="PRO_0000342611"
FT   ACT_SITE        121
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  39053 MW;  7ADB80FDEC0A3582 CRC64;
     MMLFSVRFIS GFVFGAGSGV AALKLYYYEE QQTHTGSSVH RVIGRFGLPE SGAESRFYTN
     HVLSYDQTHR TPRWVAEHLS STRLLGEANR KQCKFRPDPS VPELFTAHNE DYLKSGWSRG
     HMAPAGDNKS SEQAMAETFY LSNIVPQNYE NNAGFWNRLE MYCRELTEKF SDVWVVSGPL
     MKPQITDDGK KTVSYQLIGK DEVAVPTHLY KVILAQKDPS SDALAVGAFV VPNAPIGFQH
     QLQEFQVSVC DLERESGLVF FPALQKQQLS DLCTVDSCQL MDFRRFSLYI SSRKMQSANS
     VYRLEKILAE LQEAGIAPDE HLKQIYQQRR TELERRQDTN THT