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Database: UniProt
Entry: M0MEC0_HALMO
LinkDB: M0MEC0_HALMO
Original site: M0MEC0_HALMO 
ID   M0MEC0_HALMO            Unreviewed;       290 AA.
AC   M0MEC0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Alpha/beta hydrolase fold protein {ECO:0000313|EMBL:EMA42999.1};
GN   ORFNames=C448_10182 {ECO:0000313|EMBL:EMA42999.1};
OS   Halococcus morrhuae DSM 1307.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA42999.1, ECO:0000313|Proteomes:UP000011568};
RN   [1] {ECO:0000313|EMBL:EMA42999.1, ECO:0000313|Proteomes:UP000011568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA42999.1,
RC   ECO:0000313|Proteomes:UP000011568};
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:EMA42999.1}.
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DR   EMBL; AOMC01000123; EMA42999.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0MEC0; -.
DR   STRING; 931277.C448_10182; -.
DR   PATRIC; fig|931277.6.peg.1991; -.
DR   eggNOG; arCOG01648; Archaea.
DR   Proteomes; UP000011568; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43798:SF31; AB HYDROLASE SUPERFAMILY PROTEIN YCLE; 1.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Hydrolase {ECO:0000313|EMBL:EMA42999.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          44..282
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
SQ   SEQUENCE   290 AA;  30901 MW;  03DDA50F27D908C1 CRC64;
     MPSLVRDVGM NEGLVGVESK RIGIDVGDES VGIRYLAAGE GECVILLHGI GLDAASVSWK
     HTLPALAEEH RVIAPDFPGH GESDEASEYT MESYCAVLAG LFDALDIEQA SLVGVSMGGA
     VALGHALDHE DQVERLVLAD SYGLGRDAVW RPGGAALLNT PGIDGWLGAG LATPGLIASS
     LAGLTVTPSA EFVADVERAV GPSAASALAA WQRDEFRACG LRTCYLDRLD ELAVPTLLIH
     GREDPIFPIA WAERAAERIP DSEFVPFERC GHWPPREHPE KFDRVVSDFL
//
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