ID   A0A285CJL7_9BACI        Unreviewed;       712 AA.
AC   A0A285CJL7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=5'-nucleotidase/2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase {ECO:0000313|EMBL:SNX67218.1};
GN   ORFNames=SAMN05877753_101536 {ECO:0000313|EMBL:SNX67218.1};
OS   Bacillus oleivorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1448271 {ECO:0000313|EMBL:SNX67218.1, ECO:0000313|Proteomes:UP000219546};
RN   [1] {ECO:0000313|EMBL:SNX67218.1, ECO:0000313|Proteomes:UP000219546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC228 {ECO:0000313|EMBL:SNX67218.1,
RC   ECO:0000313|Proteomes:UP000219546};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
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DR   EMBL; OAOP01000001; SNX67218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285CJL7; -.
DR   Proteomes; UP000219546; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006146; 5'-Nucleotdase_CS.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR11575:SF24; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF00395; SLH; 3.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR   PROSITE; PS51272; SLH; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362119};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219546}.
FT   DOMAIN          13..76
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          132..195
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
SQ   SEQUENCE   712 AA;  76577 MW;  C243A57C4EE0644A CRC64;
     MTPAVVSVSY AEEAVKFSDV ADDYWAAAEI YSLVERDIIN GFVDGTFRPE QPIIRGQVAI
     LLKGALGLPV PSDLKAFKDV SERSVFAEAV AAVKQAGIFY GSEGKFGVGQ AITHEQMASV
     LVRAFDLKFN PNAEELTVEN VTPAHEKNVE ILAQNGIITK EELDSFEPKA SVSRAEFAVY
     LYRTLVFVEE KGTFELSIMH TNDTHAHLDK VAKRVTAVNE IRAKKPDALL LDAGDVFSGT
     LYFNEFKGLA DLQFMNLMGY DAMTFGNHEF DLGSQPEGHK GLADFIKVAD FPFVSANVDF
     SGDALFNEIY QGGTISSAPE NGNIYGGIIK EVDGEKVGIF GLTTEETVNL SSPGKVSFED
     YAEAAQETVD AFEAQGVNKI IALTHIGFDD NPAVDNDLQL AELVDGIDII VGGHSHTELA
     APFVVGKDEQ GSKKEPTIIV QAYQYGDYLG TLDVEFDENG EIVGYLGELI DVGEKVADPD
     AAKLLETYSA KIKEVQNSET GAVAAKELAN PRLGNGDPIS VRNSETELGN LISDGMLDKA
     KEFNPDTVIA MQNGGGIRAA IDKGPITLGE ILTVLPYGNT LATMELTGAE IIAALEHSVS
     NAPNESGGFL HVAGMKFTYD SSKSAGERVV SVQVEESDGS FSPLDESKTY VVATNNFTAK
     GGDGFDVFAK AYEEGRVTDL GLADWENLRD YVVKIGTVEP VIEDRIVDVA GK
//