ID A0A074XRX6_9PEZI Unreviewed; 454 AA.
AC A0A074XRX6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:KEQ77316.1};
DE Flags: Fragment;
GN ORFNames=M436DRAFT_30086 {ECO:0000313|EMBL:KEQ77316.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ77316.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ77316.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ77316.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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DR EMBL; KL584702; KEQ77316.1; -; Genomic_DNA.
DR RefSeq; XP_013431533.1; XM_013576079.1.
DR AlphaFoldDB; A0A074XRX6; -.
DR STRING; 1043004.A0A074XRX6; -.
DR GeneID; 25408229; -.
DR HOGENOM; CLU_010974_5_0_1; -.
DR OrthoDB; 5474043at2759; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; 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; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF103; STEROL ESTERASE TGL1; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:KEQ77316.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..429
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 423
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT NON_TER 454
FT /evidence="ECO:0000313|EMBL:KEQ77316.1"
SQ SEQUENCE 454 AA; 51220 MW; 9A7625F7DB325577 CRC64;
MPSIPFIGRL HLQEYLALLG SFVLIGLEVI IRGITLALPG PIIRFFYNCS RKLFNQLSGA
QGRRSRNRKK AISSPIAQAS DFVELCELFG YYAEEHIVQT KDGYLLGLHR LGWKRGEEDQ
RVNSGEGSIQ KKVVYLHHGL MMNSEVWVCL TEKERCLPFV LVDQGYDVWL GNNRGNKYSK
KNVHHSPTSA AFWNYSIDQF AFHDIPDTID YILATTSQKA LSYVGFSQGT AQAFATLSIH
PNLNDKVNVF VALAPAMAPP GLAMGIVSSF IKASPEVLFL LFGRKAILSS TTMWQALLYP
GIFSWVIDKA LLYLFGWHAK NITAYQKLAA YPHLFSFSST KSVVHWLQII RNETFQMFDD
EVQAPLSIAS GAKYYKVAKY PTRNIKTPIV LVYGGSDSLV DIKVMLKELP RHTIAKEIPH
YEHLDFLWAE DVHKLVIPHV LQALESHSTD AGRR
//
