ID   A0A380K7M8_9STRE        Unreviewed;       741 AA.
AC   A0A380K7M8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative 5'-nucleotidase {ECO:0000313|EMBL:SUN61085.1};
GN   Name=sntC {ECO:0000313|EMBL:SUN61085.1};
GN   ORFNames=NCTC12224_01321 {ECO:0000313|EMBL:SUN61085.1};
OS   Streptococcus hyointestinalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1337 {ECO:0000313|EMBL:SUN61085.1, ECO:0000313|Proteomes:UP000254924};
RN   [1] {ECO:0000313|EMBL:SUN61085.1, ECO:0000313|Proteomes:UP000254924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12224 {ECO:0000313|EMBL:SUN61085.1,
RC   ECO:0000313|Proteomes:UP000254924};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; UHFN01000007; SUN61085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A380K7M8; -.
DR   OrthoDB; 9801679at2; -.
DR   Proteomes; UP000254924; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; NF040549; Nt5e_LPXTG; 1.
DR   PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
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; PS00786; 5_NUCLEOTIDASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254924};
KW   Signal {ECO:0000256|RuleBase:RU362119};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT   CHAIN           20..741
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT                   /id="PRO_5039757734"
FT   TRANSMEM        718..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..332
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          409..585
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
FT   REGION          38..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  79323 MW;  865ACA8E7DD72BE9 CRC64;
     MKKKSLLLST VLISTTLLAG QVAADETEVT LAQESNVSQQ ASVLSSEEAT SSAVETSTPL
     AEVAEVTAEP TNQEQEEATA ATTEDASAAD NQSEELGSAS ETNSDYAITV LHTNDMHGRI
     VEESSVIGTP KLAEAVKESR SQGTTLVLDS GDAFQGLPIS NSTKGEDMAT LMNEIGYDAM
     AIGNHEFDFG LDQLKKLKEL LQFPLLSANT YVNGARLFEA STIIDKNKEV VGDEVVVIGV
     TTPETATKTH PRNVVGVTFS DPIAEVTSVI AEIEARAKAE GKSYNKYIIL AHLGVDTTTP
     TEWQGSTLAE ALSQNALLSG KNVLVLDGHS HTAKVDTYGN VTYNQTGSYL NHIGKIVLNS
     ERVLENSLIT TEAGKALKED ETVAALVKTI QEKYAAENAV VVLDKSPVEL NGQRENVRVR
     ETNLGNIVAD ALYDYGQTGF SHPTDLAVTN GGGLRETIQK DKPITKGDII AVLPFGNIIS
     QIEVTGQQIK DMFIKSLGSI NQVDSNGNVV LDENGQPLLE PSGGFLQISG ARVYYDTTLP
     ADQRVLAIQI LDHESQTYKD LVLDKVYYLA TNDFLAAGGD GYTMLGGSRE EGPSMDGVFA
     DFLAKADLTK YAVINPNSRT ISIKASELAT YLTSKETKPT KDNTQQSTQN TTTTTTLELS
     PSGQTQTITV SYQTAAFKSK AQAVHEQNKV KGNIYFGQAL AFADGDLLTL PLTASNRSIA
     AVLVGFVLLL VGLIGVRRKR H
//