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Database: UniProt
Entry: M0DE19_9EURY
LinkDB: M0DE19_9EURY
Original site: M0DE19_9EURY 
ID   M0DE19_9EURY            Unreviewed;       227 AA.
AC   M0DE19;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=HAD-superfamily hydrolase, subfamily IA, variant 1 {ECO:0000313|EMBL:ELZ33023.1};
GN   ORFNames=C473_07504 {ECO:0000313|EMBL:ELZ33023.1};
OS   Halorubrum terrestre JCM 10247.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum; Halorubrum distributum group.
OX   NCBI_TaxID=1227486 {ECO:0000313|EMBL:ELZ33023.1, ECO:0000313|Proteomes:UP000011572};
RN   [1] {ECO:0000313|EMBL:ELZ33023.1, ECO:0000313|Proteomes:UP000011572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10247 {ECO:0000313|EMBL:ELZ33023.1,
RC   ECO:0000313|Proteomes:UP000011572};
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   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00007958}.
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:ELZ33023.1}.
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DR   EMBL; AOIW01000048; ELZ33023.1; -; Genomic_DNA.
DR   RefSeq; WP_007345103.1; NZ_AOIW01000048.1.
DR   AlphaFoldDB; M0DE19; -.
DR   PATRIC; fig|1227486.3.peg.1415; -.
DR   Proteomes; UP000011572; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   PANTHER; PTHR43434:SF1; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G00760)-RELATED; 1.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   Pfam; PF13419; HAD_2; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ELZ33023.1}.
SQ   SEQUENCE   227 AA;  24623 MW;  4C262F9F6E086F66 CRC64;
     MYDAVVLDND GVLVGRTPFD TLREAAWDAF VSLGVEDPDL AHVDDVAVGV DPATLTDICE
     RYGVDPAEFW RVRDETAAAA QIDAARKGRK TPYDDIDALR ALDASLGVVS SNQQATVDAL
     LDHFGLAGRF EVAYGREPSV ASLSRKKPSP YYIERALEDL GAETALFVGD NESDVRAADN
     AGIDSAFLRR PHRRSTELSC HPTYEIDDLH DLVSICGRAP ADTDGEV
//
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