ID A0A109FI09_9BASI Unreviewed; 1605 AA.
AC A0A109FI09;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=RHOSPDRAFT_17311 {ECO:0000313|EMBL:KWU44842.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44842.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44842.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44842.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) 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; KQ954476; KWU44842.1; -; Genomic_DNA.
DR OrthoDB; 1424726at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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.
DR SUPFAM; SSF52047; RNI-like; 1.
PE 4: Predicted;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1225..1375
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 175518 MW; D7A04339BEE88BBE CRC64;
MAALAPTYSR EETDELLALY DPHLFTPRHV RRREPNKPSP VQTGSTSLAA TDALFGKEQS
LHRRTASIAS SVRSYFADRV AAAATPRQIT VVGQTPPPPP TSTSRPGSIR SLASRGTTQQ
LAPLLCLPSE LLLHILDFAF PTEPHSRWTS SERNHLLRTL ALVHPVLRGW AQQALFGGAP
VYLTTDLAIE RLGKLTSASP GTRGHALASR ITHVRVYGRH DTGDGGKALA KVVHQLSGLE
QLHLEDLDGL ELRQFAIHRP LRKLSVTRCG FRSRFRLVAA ARPSHLQSLS LTRCTGHHDS
FSGFSLPYLQ DLTVWNLSLP PPSPLATLEG SEAFRLLAHD VAPRLRSAVV DEQHFHYLFP
IALSEGGQVS GPQLETLTIV RLGHLPTILD QLRFRAPASS VRVQSIKQLR LVPPPSFVPG
ATSPERASAH FQALVAPFLA TSHATAGQDE CPAALKGVEM IVLDWRYGAW LALGPSKSDE
SIKLAEFVAK CERAGIRRAA HDLRWRVVRS DANGNGRGLS TDEDSDGAAD EALVLPPPFL
TTDSPRESFD GLLGARSARR QSRIARQHER LFAQGRAPPP PFPHNVVRAA VKVARLLGPP
GGFDENGRRI GAAEAAQRRR ARTGEHDTTR KGKSRGLSLD EAAQLVEQDD MTGRQIERQR
RRVKRAESGI KVYELGAKVG RQVAGRLERH RSQRAVTATA EFPESASSDC DRTTAAGSPL
AAVSPAHLLG TPPSPEASTS NSPEQCDLLP LDTEVPLSPP SAPPLRPMNL ADPLPTVSTP
FLLEDAALAP DYFGMRHRST ISSRRGSLPR AEVGKPASGR DFAAAAALIP ERPFQLKANP
SRFSKTRHIV VDWIIWILIG SPPDPATAGL DTSIAFVGGL LGIAIHLVAF VFFIVYHTSA
LLVASCIALR ATAVFLYWLV LNFSGRTEVS RSVLEYWRTC RREWDKVYGE EGERPIGPWS
VVRGLAELAV LQSMTYERWL QEGPGDLVLL NGLEEDGAAL GTPRFGPVRR RASQERLRPS
VTQRMDSYRW SGDDGAEEDG EGLVLTRSVD GVLEGSIISR DSPRQPPSPR RRPSPVLPSP
TPSIGQVLDD EPPPFDLDLA GSEDGTSTPP SGIPSSPPLQ PIADPLEPLE EFVSLVKRHC
RLCTASYGLH TLLPSPPTPL LTPSGQTLPH RLFAHLGGLN DHRNVLHVAL QKRYDGVPAS
EEDEIEATYA PQFYVLRDDV RGEIVCVIRG TQSLADVRTD LDGSLIPLDL PPVDGESPAH
SRNYRIHSAI LSAARYLLSP SSSSPLYSNL SRILAEHPRY ALVFTGHSLG AALASTLALL
VGMYDPVERR WVVDPLSSLG HGEEEEAGPR RPVRAVCFAH PTTLNVPLAE RCAIPKQALR
SQEELLAADD SNRGTPLVVN VSLGADVICR MGVPQVREIR RTLGRLDRMR TSTYTNDKAG
PPGIFSSWRR WRKVVGSLRT ITEGDASSSA AAATAAKVSH EEEEEELAAL EWSRAELEAR
AWHWRSEAEG WDRQRSGTLP EEADVEVAIP AGHCFHLDSL PPRVLEARKR QEVAKERDEE
DEEEDELLGF YEVRDPTRFY AMPILSADLL GAHMPKAYLE ATQSL
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