ID A0A0F7NFA7_9ACTN Unreviewed; 521 AA.
AC A0A0F7NFA7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Metallophosphatase {ECO:0000313|EMBL:AKH85377.1};
GN ORFNames=AA958_27615 {ECO:0000313|EMBL:AKH85377.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH85377.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH85377.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH85377.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011492; AKH85377.1; -; Genomic_DNA.
DR RefSeq; WP_047018611.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7NFA7; -.
DR STRING; 444103.AA958_27615; -.
DR KEGG; strc:AA958_27615; -.
DR PATRIC; fig|444103.5.peg.5819; -.
DR OrthoDB; 327733at2; -.
DR Proteomes; UP000034283; Chromosome.
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:UP000034283};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039563048"
FT DOMAIN 51..146
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 157..475
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 498..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 57184 MW; 2FD2EA250CDBD556 CRC64;
MTVDRRTLLK SAAAAGALGA AWPLTAGLSP AQARAAAERL GAAYDTAPFT LGVASGDPQP
DSVLLWTRLA PEPLAAEQDL PDIVEVRWAL AEDPGLRRVV ARGTTPASAT LGHSVHVPVT
GLTPGRTYHY AFSALGRTSR TGRTRTAPGG TVGRVRFAAA NCQAFHDGYY AAHRGIAAEN
VDFVLHLGDY IYEHGQVGGV PEDHVRDHDG PEILTLADYR KRHALYKGDP ALRDAHAAHP
WFLTWDDHEV VNDYSGSTGG APFVRRRAAA YQAWYEHMPH RDSFGDSALP DPEIHRTRDW
GGLVQLAILD LRSHRSAQNL PDGTILGTDQ KNWLKHHIDN APDTWHVWAN SIMLSQLRGS
PGGPYMFTDQ WDGFLAERKE ILQHVHAAGL EDLVVVTGDW HSAFVDDIRT DYDDPESPLV
GTEFTAHSVT SGAYSPDWNR TNGPVMGAAN PHLKYFEGNR YGYDVYDVTP GRFSAHMRVI
GDRRDPDSPV TTLTTFHVDR GSTGSYEDQA TKNSPAQYRR D
//
