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Database: UniProt
Entry: A0A1X7EAQ9_9ACTN
LinkDB: A0A1X7EAQ9_9ACTN
Original site: A0A1X7EAQ9_9ACTN 
ID   A0A1X7EAQ9_9ACTN        Unreviewed;       560 AA.
AC   A0A1X7EAQ9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alkaline phosphatase D {ECO:0000313|EMBL:SMF30592.1};
GN   ORFNames=SAMN02745830_02764 {ECO:0000313|EMBL:SMF30592.1};
OS   Streptomyces sp. Amel2xC10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF30592.1, ECO:0000313|Proteomes:UP000192930};
RN   [1] {ECO:0000313|EMBL:SMF30592.1, ECO:0000313|Proteomes:UP000192930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF30592.1,
RC   ECO:0000313|Proteomes:UP000192930};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWZW01000005; SMF30592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7EAQ9; -.
DR   OrthoDB; 327733at2; -.
DR   Proteomes; UP000192930; 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   InterPro; IPR032093; PhoD_N.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   Pfam; PF16655; PhoD_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000192930}.
FT   DOMAIN          59..155
FT                   /note="Phospholipase D N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16655"
FT   DOMAIN          168..525
FT                   /note="PhoD-like phosphatase metallophosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF09423"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  60174 MW;  1C1C7C02C3FD9226 CRC64;
     MTNSRYRSTE STGAPLGGGT PLAPRRRTVV KAAAATAVLA GPLAAALPAR AAEAPVFQHG
     LASGDPLPDG VLLWTRVTPT AEATPGSGLG PDTRVDWVVA RDKALTNIVA KGSLTTTAAS
     DHTVKADVRG LAPATDYWFR FSANGTDSPV ARTRTAPAAD AAVPGLRFGV VSCASWEAGY
     FSPYRHLAAR GDLDAWLHLG DYIYEYGTGE YGARGTVVRQ TSPTHETLSL ADYRIRHGKY
     KTDPDLQALH AKAPVVAIWD DHEIANDAWS GGAENHTEGA EGTWAARQAA AKQAYFEWMP
     VRPALAGTTY RRLRFGKLAD LSLLDLRSFR SQQVGIGKGS VDDPERTLTG RAQLDWLKAG
     LKSSDTTWRL VGNSVMISPF AVGSLPASLL RPLAKLLGLP QEGIALNTDQ WDGYTDDRRE
     LLAHLRSNAI GNTVFLTGDI HMAWANDVPV DAGTYPLSAS AATEFVVTSV TSDNLDDIVK
     VPEGTVSAIA SPIIKAANRH VHWVDTDRHG YGVLDITAAR AQMDYYVVSD RTKANATSSW
     SRSYRTRTGT QKVERTYDPV
//
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