ID A0A1Y0FSH3_9GAMM Unreviewed; 338 AA.
AC A0A1Y0FSH3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Endonuclease {ECO:0000256|RuleBase:RU366055};
DE EC=3.1.30.- {ECO:0000256|RuleBase:RU366055};
GN ORFNames=CBR65_00735 {ECO:0000313|EMBL:ARU26074.1};
OS Cellvibrio sp. PSBB006.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU26074.1, ECO:0000313|Proteomes:UP000196143};
RN [1] {ECO:0000313|EMBL:ARU26074.1, ECO:0000313|Proteomes:UP000196143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB006 {ECO:0000313|EMBL:ARU26074.1,
RC ECO:0000313|Proteomes:UP000196143};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU366055};
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000256|ARBA:ARBA00010052, ECO:0000256|RuleBase:RU366055}.
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DR EMBL; CP021382; ARU26074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0FSH3; -.
DR KEGG; cell:CBR65_00735; -.
DR OrthoDB; 9811262at2; -.
DR Proteomes; UP000196143; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW ECO:0000256|RuleBase:RU366055}; Hydrolase {ECO:0000256|RuleBase:RU366055};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2,
KW ECO:0000256|RuleBase:RU366055};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU366055};
KW Reference proteome {ECO:0000313|Proteomes:UP000196143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..338
FT /note="Endonuclease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013208516"
FT DOMAIN 124..324
FT /note="DNA/RNA non-specific endonuclease"
FT /evidence="ECO:0000259|SMART:SM00892"
FT DOMAIN 125..324
FT /note="Extracellular Endonuclease subunit A"
FT /evidence="ECO:0000259|SMART:SM00477"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ SEQUENCE 338 AA; 38411 MW; 9F3E38F75E584ECD CRC64;
MKRRIYLLLL GCLFSVEPAL ADYIDARRSM HLKEQPSVNG ISLTKIEVGE RVEVLEGSRQ
TNGYYYVATQ DGYEGYVYRT VGRITVTDET TFVEDTDHSP LAMDMGCEKH LVYGMPQPAD
QVLCREGYAA GYSYTYKIPL WVTYRITREQ ILTTGSDRQG ISFRQDKTIP SDFRSKNSDY
LNSGYDRGHM APNASMDFSV NAQLESFLFS NIAPQLPDFN RDSHGSTGVW GRLEKYERRW
IEQRGELVII MGAFPGEEAL TIGQGVAVPS HFYRVIVDPA TLESIAFWMP QEKNTAHQIT
RYLASIDEIE QQAKIDLLSN ITPAIQDIIE AERQTALW
//
