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Database: UniProt
Entry: A0A1Q4DED1_9PSEU
LinkDB: A0A1Q4DED1_9PSEU
Original site: A0A1Q4DED1_9PSEU 
ID   A0A1Q4DED1_9PSEU        Unreviewed;       176 AA.
AC   A0A1Q4DED1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN   ORFNames=BGP03_28100 {ECO:0000313|EMBL:OJY42720.1};
OS   Pseudonocardia sp. 73-21.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY42720.1, ECO:0000313|Proteomes:UP000186163};
RN   [1] {ECO:0000313|EMBL:OJY42720.1, ECO:0000313|Proteomes:UP000186163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-21 {ECO:0000313|EMBL:OJY42720.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJY42720.1}.
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DR   EMBL; MKVV01000070; OJY42720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4DED1; -.
DR   STRING; 1895809.BGP03_28100; -.
DR   Proteomes; UP000186163; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd03392; PAP2_like_2; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 2.
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        20..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..165
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   176 AA;  18543 MW;  0E79AEE27060CBE2 CRC64;
     MDGPALGESI ENRSPALTAV AVVVTTVGNT AAMAVLAVLV GAFCWWRGRR ADAVLAVVAM
     ATASLVFTTI KNVLDRPRPP VADRLVTVGN ESLPSGHATM SIVVIGTIVV LAWRFLAVRG
     RAVLVVLGAA WVGSVGATRV YLGVHWFSDV IAGWLVGAAW LAVCATVWSR WRARQA
//
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