ID G0WB91_NAUDC Unreviewed; 669 AA.
AC G0WB91;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF00561};
GN Name=NDAI0E01950 {ECO:0000313|EMBL:CCD25011.1};
GN OrderedLocusNames=NDAI_0E01950 {ECO:0000313|EMBL:CCD25011.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD25011.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD25011.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE580271; CCD25011.1; -; Genomic_DNA.
DR RefSeq; XP_003670254.1; XM_003670206.1.
DR AlphaFoldDB; G0WB91; -.
DR STRING; 1071378.G0WB91; -.
DR GeneID; 11498901; -.
DR KEGG; ndi:NDAI_0E01950; -.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_5_0_1; -.
DR OMA; SDIWCCQ; -.
DR OrthoDB; 5474043at2759; -.
DR Proteomes; UP000000689; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF103; STEROL ESTERASE TGL1; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
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:UP000000689};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..405
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 556..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..636
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 76608 MW; 1BB7929916684537 CRC64;
MLVPFIGRIS LADYLIIISL YIEFIMSFFL KLIPQPIINF LSSIINYTTN LDDSTREQKL
RLAPTIHEMC AQFDINIEDH LVRTEDDYIL TLHRIPPKTN ITGSGTGKIV YLHHGLLMCS
DIWCCQLDKN KNLPFVLHNL GYDVWMGNNR GNKYSTAHLY EMPKSKKFWD FSIDEFAFFD
IPNSIDFILN HCQRDKLICI GFSQGSAQMF ASFSINEYLN SKVSQFIAIA PAMTPKGLHN
RIVDTFAKSS PALMYLFFGR NILLPSATTI WQKTLHPKIF NLCIDIGNRI LFNWTSKNIS
EQQKLICYSK LYSTTSVKSV VHWFQILKSQ KFQMFEASDN MFNSITRPYQ ISRFPTRTNI
KIPILLIYGG MDSLVDIKVM KKNLPQTGVF DIKVENHEHL DLIWGEDTDT LVISKIIKFI
DFFDGVSRRN SLLQKTLNKR IMSTKNYNTS GISTNEEQHH PYVMDLEDNT PIIPYSNETL
IINDNVSQKD ESVMLENQFA STSSIGNTPS MLRHVKTRSK TKLNSDKPVI TSTMRNYINN
TRSIINELDK KSLAENKNNN ISNNNDNHEY SIGLSPTASS YNGEDDIVGK NDQGIYVEEL
EASPSNVKAT LDNEFALNND TCTDDEDEDD DDGDESNSID RINSNEKLKN KIQQRKLSKY
LSNEVQANT
//
