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Database: UniProt
Entry: A0A1E7FR82_9STRA
LinkDB: A0A1E7FR82_9STRA
Original site: A0A1E7FR82_9STRA 
ID   A0A1E7FR82_9STRA        Unreviewed;       793 AA.
AC   A0A1E7FR82;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=FRACYDRAFT_234313 {ECO:0000313|EMBL:OEU20682.1};
OS   Fragilariopsis cylindrus CCMP1102.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC   Fragilariopsis.
OX   NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU20682.1, ECO:0000313|Proteomes:UP000095751};
RN   [1] {ECO:0000313|EMBL:OEU20682.1, ECO:0000313|Proteomes:UP000095751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU20682.1,
RC   ECO:0000313|Proteomes:UP000095751};
RG   DOE Joint Genome Institute;
RA   Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA   Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA   Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA   Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA   Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA   Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA   Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT   "Extensive genetic diversity and differential bi-allelic expression allows
RT   diatom success in the polar Southern Ocean.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC         acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:28868; EC=3.1.1.116;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KV784354; OEU20682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7FR82; -.
DR   EnsemblProtists; OEU20682; OEU20682; FRACYDRAFT_234313.
DR   KEGG; fcy:FRACYDRAFT_234313; -.
DR   InParanoid; A0A1E7FR82; -.
DR   OrthoDB; 373802at2759; -.
DR   Proteomes; UP000095751; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45792:SF8; DIACYLGLYCEROL LIPASE-ALPHA; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OEU20682.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095751};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          485..622
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   793 AA;  89940 MW;  720EBC40019A2C9F CRC64;
     MPALQLFGQR TFFAGDDICT FLVLHALFRA FQIAVALSLI GITVFYNHNQ EIILLENGMN
     CTVEGSTEDR MTYIYSSVSI VVAGMSIYLV VPMFHYSRKG TPTEPTLREP LRRLCYFDTT
     VMNVLRIIVF VLGSRDIKGV MAYCRCISND ISVDTFVEVH ESCPRHAGFM TAVITLFCTH
     IFDACMTILT FLYFTFCHEN LFINSQIEFV SSEQRCSICL RCCIGWASIF TCCLFGGDKA
     VRGDYANFSM LLANYVNGKG ILDVTASDIS VGLHMLRKVR KRNRLETTNR LVREHSEISK
     QKVVSSRHGS SDRLSLNDDK NYENKIVVKM STDGNSVDLV HDNCNSEDTK EEIYDNRARP
     QNLPEHRQKL EILSSVYTRD VNLINEAAHF MIYAQAAYTV VSYMMENPVT GFVSLQLQML
     RNWCVCHFPS RKESIVGDNF WQIQTIAFKA LSGLAVKDIV YANFCDTITE IPYIILLDHE
     WKSVVVTIRG TITLESVLTD MNVAPEALTR LGEECGFDGD GLYCHTGMLA STEWLYRDMK
     RHGKLNKILA EYEGYKLRIV GHSLGAGIAA ILSVLLRPKY PDLRCLAFSP PGCVMSENLA
     DDISTFTTAF VVNDDIVART SIEGFEELRN SILEMICRIK IPKHMVTKVS KNYDDTTVDG
     LSEAIDHILY DKDDINDSKF KQEIDEFQKH QIELKEKNKE SYIKLCPPGN IIQLFLTADV
     RQSECITTHN GEEIGQYTAR WANRSDFEKI NISSHLISDH NTNGVKYKLH ELAIGKFGLH
     PPFKPISDPD REI
//
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