ID   A0A0A2G9S7_9PORP        Unreviewed;       476 AA.
AC   A0A0A2G9S7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=5'-nucleotidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HQ36_01445 {ECO:0000313|EMBL:KGN99150.1};
OS   Porphyromonas gingivicanis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=266762 {ECO:0000313|EMBL:KGN99150.1, ECO:0000313|Proteomes:UP000030134};
RN   [1] {ECO:0000313|EMBL:KGN99150.1, ECO:0000313|Proteomes:UP000030134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-022 OH1391 {ECO:0000313|Proteomes:UP000030134};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas gingivicanis strain:COT-022_OH1391 Genome sequencing.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
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:KGN99150.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JQZW01000002; KGN99150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2G9S7; -.
DR   STRING; 266762.HQ36_01445; -.
DR   eggNOG; COG0737; Bacteria.
DR   Proteomes; UP000030134; 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   CDD; cd00845; MPP_UshA_N_like; 1.
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   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; PS00786; 5_NUCLEOTIDASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030134}.
FT   DOMAIN          25..222
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          304..430
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
SQ   SEQUENCE   476 AA;  53578 MW;  E5B7B868FA4F7452 CRC64;
     MIAFVAFFAF CTVQTTVAQE KKVVFLSVND MHAAIDQFPR FGYMVDSLRQ IYPDMLLIGA
     GDNHSGNPIN DLFTPRGYPM THLMNMVRFD YSVLGNHEFD TRADLGLLTQ VAQFPFLAAN
     VFPAPQRGIR LLPSAIHTLP NGVRVGLVGL LQLEKSGLPA TNPTWVEHVR FAPAQKEIKK
     YQELREVCDA VVLVSHLGVE EDQIVARDNN WIDLIIGGHS HTLLTEPIKE GKCTITQAGS
     RLRNCYLTTL TLSDSSEVQV TTQLLSIDAQ AGEESATIRA VVDDFNSNSF FKQVVGEASD
     DFTSGEELGF FMADAHYSTL GVDITLQNRG GVRMSRLPKG PITNHNVYSL DPFGNEMVVI
     ELTPEELSRL LLKNWSKEFE SPIYAAGLYA VYHVDKKSKK CFSVELFTPN KKPLKKDYKY
     RVAYNNYIAN AYEFEHTSSY KETGYTSVES ILAYLKKVQK VPSYRKSKKR WKVVYH
//