ID A0A260WWK6_9NOCA Unreviewed; 535 AA.
AC A0A260WWK6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OZF53351.1};
GN ORFNames=CH292_08265 {ECO:0000313|EMBL:OZF53351.1};
OS Rhodococcus sp. 14-2470-1a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2023150 {ECO:0000313|EMBL:OZF53351.1, ECO:0000313|Proteomes:UP000215821};
RN [1] {ECO:0000313|Proteomes:UP000215821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-2470-1a {ECO:0000313|Proteomes:UP000215821};
RA Savory E.A., Fuller S.J., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA Grunwald N.J., Chang J.H.;
RT "Evolutionary transitions between beneficial and phytopathogenic
RT Rhodococcus challenge disease management.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OZF53351.1}.
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DR EMBL; NPFZ01000016; OZF53351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A260WWK6; -.
DR Proteomes; UP000215821; 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;
FT DOMAIN 58..154
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 167..503
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 332..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 58423 MW; 1F31CE8320AB4018 CRC64;
MGQRDVNIGR DISLRGGATR RQFLTWSALV GALAFAPELN PATASAQSGT PSSYPFRLGV
ASGDPLPDSV VLWTRLATDP FAPAGGMTPG VVPVQWQIAA DERFTRVTAQ GVELATEFDG
WSVHVDVRGL EPAREYFYRF LVGPHASAVG RTKTAPAAGR PLARLDFGWA SCQKWEDGYF
GAYADLAASN LDVVFFLGDY IYEYAVKDEG ARAGRPRPES ASRETMQLSD YRDRYAMYKA
DENLAAAHAS APFVSAFDDH EVDNNWASQI SQDDDDPVLF LNRRADAFKA WWENTPVRAN
LKPQGPDMKV YRRLSFGDLV DFSVLDTRQY RSDQANGDKE HAQNAETADP SRTITGPEQE
KWILDGFASP SKWNFLAHQT VISDLAQGLD GDRKVGMDPW SGYEASRHRI LDGARERGTT
NVASIVGDIH RTIVSELRRD YQDQASPVVG VEIATTSIAS GKDGADVDTT GAAIANGSPH
VKYGNARRGY LRSTLTPGEW RSEVRVLDAV STPGASVRTA TTVTVPDGRP EIQLG
//