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Database: UniProt
Entry: A0A2U1E3R7_9FIRM
LinkDB: A0A2U1E3R7_9FIRM
Original site: A0A2U1E3R7_9FIRM 
ID   A0A2U1E3R7_9FIRM        Unreviewed;       379 AA.
AC   A0A2U1E3R7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Endonuclease YncB(Thermonuclease family) {ECO:0000313|EMBL:PVY94349.1};
GN   ORFNames=C7381_10552 {ECO:0000313|EMBL:PVY94349.1};
OS   Ezakiella coagulans.
OC   Bacteria; Bacillota; Tissierellia; Ezakiella.
OX   NCBI_TaxID=46507 {ECO:0000313|EMBL:PVY94349.1, ECO:0000313|Proteomes:UP000245793};
RN   [1] {ECO:0000313|EMBL:PVY94349.1, ECO:0000313|Proteomes:UP000245793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20705 {ECO:0000313|EMBL:PVY94349.1,
RC   ECO:0000313|Proteomes:UP000245793};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVY94349.1}.
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DR   EMBL; QEKV01000005; PVY94349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1E3R7; -.
DR   Proteomes; UP000245793; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR036582; Mao_N_sf.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR   PANTHER; PTHR12302:SF3; SERINE/THREONINE-PROTEIN KINASE 31; 1.
DR   Pfam; PF07833; Cu_amine_oxidN1; 2.
DR   Pfam; PF00565; SNase; 1.
DR   SMART; SM00318; SNc; 1.
DR   SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR   SUPFAM; SSF50199; Staphylococcal nuclease; 1.
DR   PROSITE; PS50830; TNASE_3; 1.
PE   4: Predicted;
KW   Endonuclease {ECO:0000313|EMBL:PVY94349.1};
KW   Hydrolase {ECO:0000313|EMBL:PVY94349.1};
KW   Nuclease {ECO:0000313|EMBL:PVY94349.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245793};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..379
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015513386"
FT   DOMAIN          149..287
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
SQ   SEQUENCE   379 AA;  42305 MW;  70692B58D139F868 CRC64;
     MKKYRKILMV TAFLMLVPLT ASAKDVKLWI DGNYVTGDVA PQIVNDRTVV PLRMISESLG
     LTPVWNEHEQ SVTIEAQNIS VVFKINDMNY VLNGEKKQMD VAPQIISDRT FVPLRVIAEV
     FGKKVDWDQK NETAIVGEGY VPPAATEISF EKATVKNVVD GDTIVVDIDG AEKKVRFVGI
     DAPEMSTPNG NTSKKFTEDA ILNKTVYLEK DVSEVDKYDR LLRYIWLVSP NGIEINENTV
     RENMLNGKMV ASGMAASKTY APDTKYQNIL DKLQTDAINN KLGMWAPAPT GAVVSTHKVE
     GWGLQFGTFV PENRTKIERK QNGKTYFADT TQGYIKGNAS SKKYHLPGMQ GYDKISVVNV
     CFFRTEEEAI ARGFVKAKK
//
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