ID A0A127W1U3_SPOPS Unreviewed; 599 AA.
AC A0A127W1U3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Endonuclease {ECO:0000313|EMBL:AMQ07530.1};
GN ORFNames=AZE41_17185 {ECO:0000313|EMBL:AMQ07530.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ07530.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ07530.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ07530.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014616; AMQ07530.1; -; Genomic_DNA.
DR RefSeq; WP_067211996.1; NZ_CP014616.1.
DR AlphaFoldDB; A0A127W1U3; -.
DR STRING; 1476.AZE41_17185; -.
DR KEGG; spsy:AZE41_17185; -.
DR OrthoDB; 9770276at2; -.
DR Proteomes; UP000071057; Chromosome.
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 GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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 InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR13966:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:AMQ07530.1};
KW Hydrolase {ECO:0000313|EMBL:AMQ07530.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2};
KW Nuclease {ECO:0000313|EMBL:AMQ07530.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 375..578
FT /note="DNA/RNA non-specific endonuclease"
FT /evidence="ECO:0000259|SMART:SM00892"
FT DOMAIN 376..580
FT /note="Extracellular Endonuclease subunit A"
FT /evidence="ECO:0000259|SMART:SM00477"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ SEQUENCE 599 AA; 68308 MW; 2AFBA5BBFA125F18 CRC64;
MSIKRLDKFQ SLHVDLVDLH QQQALKRYIA RSSERERIAS ELQTKNPFEV DTPERVATRK
AIIDPRDGLA IERIIGRDDL FPVSYLEAGQ QAATPVCRIE IRDRLGRVLG HATGFLVSPS
LLLTNNHVLE NYNTAQFSVA QFNYEVDLDL NERPMKSFRF TPERFFITDK KLDFTLVAIE
EVSADGTKVS DFGFLPLISQ TGKGLVGECV SIIQHPSGAP KAVAIRENQI MDVFEDYIHY
STDTMPGSSG SPVYNDEWIV ISLHHAGVPD PKNRTEFIAN EGIRISSIVQ FVAEQGSSLS
NDQKLLLYDI VKGWDVPDYT PEEMEVEKLS DSWYESSRGY DTQFLGVDYE VPHPIFPSDL
EQDIAQLKDG SNVLHYTHFS IVMSKSRRLA YYTVVNIDGN QLMKIGRKDK WYLDSRIEME
YQCGAELYKN NSLDRGHLVR RLDPVWGDSA KKANEDTFHF TNCAPQESKL NQKSWLDLEN
YILHNAENLN LKVTVFTGPV FRMDDIIYRG VQIPAEFWKI AVIVKKDGNL SATAYLQTQK
NLIEDLEFVY GEYKTYQVPI SKIEVITGLD YEELRNFDPL NQLESTIGYV IDAPGDIKL
//