NUCG_CAEEL
ID NUCG_CAEEL Reviewed; 308 AA.
AC Q95NM6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Endonuclease G, mitochondrial;
DE Short=Endo G;
DE EC=3.1.30.-;
DE AltName: Full=Ced-3 protease suppressor 6;
DE Flags: Precursor;
GN Name=cps-6; ORFNames=C41D11.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11452313; DOI=10.1038/35083608;
RA Parrish J., Li L., Klotz K., Ledwich D., Wang X., Xue D.;
RT "Mitochondrial endonuclease G is important for apoptosis in C. elegans.";
RL Nature 412:90-94(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Endonuclease important for programmed cell death; it mediates
CC apoptotic DNA fragmentation. {ECO:0000269|PubMed:11452313}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11452313}.
CC -!- MISCELLANEOUS: The active site contains 1 hydrated magnesium ion that
CC has only 1 direct interaction with the protein; all other interactions
CC are via water molecules. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {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; AF390558; AAK72007.1; -; mRNA.
DR EMBL; FO080509; CCD64257.1; -; Genomic_DNA.
DR RefSeq; NP_491371.1; NM_058970.4.
DR PDB; 3S5B; X-ray; 1.80 A; A/B=63-303.
DR PDB; 4QN0; X-ray; 2.74 A; A/B/C/D=64-302.
DR PDB; 5GKC; X-ray; 1.89 A; A/B=63-305.
DR PDB; 5GKP; X-ray; 2.30 A; A/B=63-305.
DR PDBsum; 3S5B; -.
DR PDBsum; 4QN0; -.
DR PDBsum; 5GKC; -.
DR PDBsum; 5GKP; -.
DR AlphaFoldDB; Q95NM6; -.
DR SMR; Q95NM6; -.
DR BioGRID; 37514; 9.
DR IntAct; Q95NM6; 2.
DR STRING; 6239.C41D11.8; -.
DR EPD; Q95NM6; -.
DR PaxDb; Q95NM6; -.
DR PeptideAtlas; Q95NM6; -.
DR EnsemblMetazoa; C41D11.8.1; C41D11.8.1; WBGene00000787.
DR GeneID; 172045; -.
DR KEGG; cel:CELE_C41D11.8; -.
DR UCSC; C41D11.8.1; c. elegans.
DR CTD; 172045; -.
DR WormBase; C41D11.8; CE29488; WBGene00000787; cps-6.
DR eggNOG; KOG3721; Eukaryota.
DR GeneTree; ENSGT00940000160987; -.
DR HOGENOM; CLU_055174_0_1_1; -.
DR InParanoid; Q95NM6; -.
DR OMA; YVMPNQV; -.
DR OrthoDB; 933605at2759; -.
DR PhylomeDB; Q95NM6; -.
DR PRO; PR:Q95NM6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000787; Expressed in larva and 4 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:WormBase.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:WormBase.
DR GO; GO:0004519; F:endonuclease activity; IDA:WormBase.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:WormBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IDA:WormBase.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:WormBase.
DR GO; GO:0006401; P:RNA catabolic process; IDA:WormBase.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
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 SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Nuclease; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..308
FT /note="Endonuclease G, mitochondrial"
FT /id="PRO_0000019920"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10047"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:3S5B"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3S5B"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3S5B"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3S5B"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:3S5B"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 235..246
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 249..260
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:3S5B"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:3S5B"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3S5B"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:3S5B"
SQ SEQUENCE 308 AA; 34511 MW; 9BAE5813E178CEB3 CRC64;
MIGKVAGTAA IAGISFLAGK YSNDDLPIFR NVQSATNVPM NQIQVSEPMT VKPASLNADA
MGPSRSAEIM KHGYPGFTNV RTYEDFVLSY DYKTRTAHWV CEHLTPERLK HAEGVDRKLC
EFKPDITFPQ KFLSQNTDYK CSGFDRGHLA AAGNHRKSQL AVDQTFYLSN MSPQVGRGFN
RDKWNDLEMH CRRVAKKMIN SYIITGPLYL PKLEGDGKKY IKYQVIGDNN VAVPTHFFKV
ALFEVTPGKF ELESYILPNA VIEDTVEISK FHVPLDAVER SAGLEIFARL DPKSIVKENG
AKKGGLLW
