ID M0BH97_9EURY Unreviewed; 289 AA.
AC M0BH97;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=PA-phosphatase-like phosphoesterase {ECO:0000313|EMBL:ELZ08994.1};
GN ORFNames=C480_02553 {ECO:0000313|EMBL:ELZ08994.1};
OS Natrialba aegyptia DSM 13077.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1227491 {ECO:0000313|EMBL:ELZ08994.1, ECO:0000313|Proteomes:UP000011591};
RN [1] {ECO:0000313|EMBL:ELZ08994.1, ECO:0000313|Proteomes:UP000011591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13077 {ECO:0000313|EMBL:ELZ08994.1,
RC ECO:0000313|Proteomes:UP000011591};
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:ELZ08994.1}.
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DR EMBL; AOIP01000012; ELZ08994.1; -; Genomic_DNA.
DR RefSeq; WP_006664048.1; NZ_AOIP01000012.1.
DR AlphaFoldDB; M0BH97; -.
DR PATRIC; fig|1227491.4.peg.523; -.
DR OrthoDB; 329477at2157; -.
DR Proteomes; UP000011591; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..256
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 289 AA; 32773 MW; 8CE9022AB4D66171 CRC64;
MLTQVLVQLV VVVTLMIAVS VALFVGRRRL QVTRTEWRTR LRATAPALAV LTVALLFNSI
ARQLVPDLSW MIGWNLTWAI YDIEGQFILW LQSFETPAVT AYFSFIYIYG YVFALTFPVV
AYFALADTRP LRELLAAYTL NYTLGLVLYV FVIAFGPRNM MPELVEALLY DTYPQYQHLT
RQVNRNTNVF PSLHASLATT VTLLAYRTRD QYPTWFYVTL GLGTSIALST MYLGIHWAID
VLAGLGLAYI SVSLARVLVD RWSVSAWIAS IRGRDADDDR EMDSSSDHT
//
