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Database: UniProt
Entry: A0A1G0XGP8_9BACT
LinkDB: A0A1G0XGP8_9BACT
Original site: A0A1G0XGP8_9BACT 
ID   A0A1G0XGP8_9BACT        Unreviewed;       461 AA.
AC   A0A1G0XGP8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=PhoD-like phosphatase metallophosphatase domain-containing protein {ECO:0000259|Pfam:PF09423};
GN   ORFNames=A2523_13245 {ECO:0000313|EMBL:OGV32759.1};
OS   Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV32759.1, ECO:0000313|Proteomes:UP000177243};
RN   [1] {ECO:0000313|EMBL:OGV32759.1, ECO:0000313|Proteomes:UP000177243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGV32759.1}.
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DR   EMBL; MHBA01000034; OGV32759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0XGP8; -.
DR   STRING; 1798454.A2523_13245; -.
DR   Proteomes; UP000177243; Unassembled WGS sequence.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   PANTHER; PTHR43606:SF6; ALKALINE PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G03860); 1.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..461
FT                   /note="PhoD-like phosphatase metallophosphatase domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009569405"
FT   DOMAIN          119..384
FT                   /note="PhoD-like phosphatase metallophosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF09423"
SQ   SEQUENCE   461 AA;  52477 MW;  FAD7661CF626E1FA CRC64;
     MKTKLILVLV FTFSTLSFAQ LNLGPLVGGV THNSAIILVK TYKPQTVQIE LFSESNPHPS
     VYSETFVSDT NNYNYVKIPV QNLSPNTNYF YRAIVDGIKS KRWHSFKTFP LEKYHSFSFG
     FGSCQQSSYS KWNPEVFPVV AQDSLRFFIQ IGDWTYPDTT EKKYGYRFNT SLALIEKTYQ
     AKYNYNYPFA GEVLSQMPVV YAYDDHDFAA NNPDGTDPAK QNSLWAYKAF FPHYPLKNPD
     NGIWQSFAFG DVEFFVLDCR SQRNPNKNSL DGNGNFNPPE KHSLLSGFAI SGENQLDWFL
     NALKNSTAKW KVIVSTVLFN PAYSKVFTNT ELLKKYPWMK EDAMDKWAGF PNDLNLLMKT
     IKDNNIKNVL VVSGDSHSSY IDDGKNSLIP EISASNLDVN NSLLHKKLEE GGINIWNQGT
     YDEKGHTYGK VSFIFGEEDY ALLEVIDEKG KIAASYRLIA E
//
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