ID M0BTV0_9EURY Unreviewed; 321 AA.
AC M0BTV0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Phosphoesterase PA-phosphatase-like protein {ECO:0000313|EMBL:ELZ14461.1};
GN ORFNames=C477_20019 {ECO:0000313|EMBL:ELZ14461.1};
OS Haloterrigena salina JCM 13891.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ14461.1, ECO:0000313|Proteomes:UP000011657};
RN [1] {ECO:0000313|EMBL:ELZ14461.1, ECO:0000313|Proteomes:UP000011657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ14461.1,
RC ECO:0000313|Proteomes:UP000011657};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ14461.1}.
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DR EMBL; AOIS01000063; ELZ14461.1; -; Genomic_DNA.
DR RefSeq; WP_008896260.1; NZ_AOIS01000063.1.
DR AlphaFoldDB; M0BTV0; -.
DR STRING; 1227488.C477_20019; -.
DR PATRIC; fig|1227488.3.peg.4012; -.
DR eggNOG; arCOG03951; Archaea.
DR OrthoDB; 329477at2157; -.
DR Proteomes; UP000011657; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
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; PF14378; PAP2_3; 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 Reference proteome {ECO:0000313|Proteomes:UP000011657};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..256
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 283..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 321 AA; 36239 MW; BF3909626ECC3DCA CRC64;
MLAELLTQVT AIIVVLLVGF VPVCIGRRRL RATRREWRDR MREAAPVAGV VLVVLLANRF
TRQRLPDISW AIDWNLTPTF YAIEGEAIIW FQQFASPLVT QYFSFVYIYG YVFILVFPVI
AYFALSDTRP LRELLSAYAL NYLIGLFLYL LVIAYGPRNI MPTAIETVLY DFRPQYQYLT
QEVNHNTNVF PSLHTSLSAT IAIFAYRTRD EYPIWFAVAV PLAASIAVST MYLGIHWAID
VVAGIALAVG TVYAADRFVG RWSLSEDFGI EIDEYVDRIR RTAGMRTPAD PSPSADDEYG
EADGTDVEDP SSDEPSTGQR S
//
