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Database: UniProt
Entry: A0A1Q5D4H0_9ACTN
LinkDB: A0A1Q5D4H0_9ACTN
Original site: A0A1Q5D4H0_9ACTN 
ID   A0A1Q5D4H0_9ACTN        Unreviewed;       345 AA.
AC   A0A1Q5D4H0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN   ORFNames=AMK10_28075 {ECO:0000313|EMBL:OKI90786.1};
OS   Streptomyces sp. CB02058.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703921 {ECO:0000313|EMBL:OKI90786.1, ECO:0000313|Proteomes:UP000185610};
RN   [1] {ECO:0000313|EMBL:OKI90786.1, ECO:0000313|Proteomes:UP000185610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02058 {ECO:0000313|EMBL:OKI90786.1,
RC   ECO:0000313|Proteomes:UP000185610};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(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:OKI90786.1}.
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DR   EMBL; LIPG01000006; OKI90786.1; -; Genomic_DNA.
DR   RefSeq; WP_073751158.1; NZ_LIPG01000006.1.
DR   AlphaFoldDB; A0A1Q5D4H0; -.
DR   OrthoDB; 5289372at2; -.
DR   Proteomes; UP000185610; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR14969:SF13; AT30094P; 1.
DR   PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          105..220
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          284..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  37230 MW;  4613E9EB86232E72 CRC64;
     MRTDIFARLD REPEPPKIET PRMSRHRIAL FGGTLAFYVA IVVAVLVSSW LVALDWKVML
     FRPYQQWPEL HAFLDYYVVL GQRGPTAVMV ASWLGWRSWR QHTLRPLLTL GASLLLLNLS
     VGAVKLGLGR LGPHYATQIG SAELFAGGDI FPSGHTANAV VTWGILAYLA TTPRARRYLS
     ALSAFVSLGV GLTTVYIGTH WLSDVLLGWA AGLLILLALP WFEPLITRAE VLVLSVREQW
     RARRRLRASA PAAPAAPEPV LLPQSLSGGT GAEGALEAVS VEPAPEGQGA IGHPGARARA
     HQGHPLRSER TPVTPAGSRR PPHADRAPRS NGTQARPVTG GSVAP
//
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