ID A0A074WH43_9PEZI Unreviewed; 705 AA.
AC A0A074WH43;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:KEQ61781.1};
DE Flags: Fragment;
GN ORFNames=M437DRAFT_17118 {ECO:0000313|EMBL:KEQ61781.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ61781.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ61781.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ61781.1,
RC ECO:0000313|Proteomes:UP000030672};
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).
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DR EMBL; KL584836; KEQ61781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074WH43; -.
DR STRING; 1043003.A0A074WH43; -.
DR HOGENOM; CLU_024238_0_0_1; -.
DR OrthoDB; 5471104at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR006693; AB_hydrolase_lipase.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF160; STEROL ESTERASE 1-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KEQ61781.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..348
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT REGION 101..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KEQ61781.1"
FT NON_TER 705
FT /evidence="ECO:0000313|EMBL:KEQ61781.1"
SQ SEQUENCE 705 AA; 80541 MW; 28C2ED052F0EA1D7 CRC64;
DVHSTKSNHK ADAAIEFARQ AERLAQYTTD QERKRNSDST QAVEAKFVTA QDPVIVTANG
SRLPAVPIDE ALKLNRLKDQ LDDRQSDGRI PVKYTSRKAR DGTMHGILEK DGAGPSNDPD
APLREAAAPS RTNPMFPPLP TYGPPSILRT LHCCFFRTTS SILSFLFLLI IVLGAAFTSI
PLAFEHVRLR LMLKNPDKRR PFFEEEQRRK KARAEANRDW AKDKPPTTPA EVETSPPQDG
EFIPTEGGPD PLVCDPAYYA RRVGLDVEIF DVETEDGFII ELWHVYNPRE YRPVSPSAHR
PRGPDIFETT TSDPEFGEAE RAFPSGNKKY PVLMIHGLLQ SAGAYCCTDD DSLAFYLAKS
GYDVWLGNNR CGFKPRHTLL DYSDPRMWSW NIRQMGVLDL PALISRVLSE TGFEKLGLVC
HSQGTTQTLV ALAKEQRPDI GEKISVFCAL APAAYAGPLI GKAYFKFMRM INPNFFRCIF
GIHAFIPFMM RMHTILPAKL YGAMGYRVFS FLFNWTDTRW EMDLRNRLFQ FAPVYVSAES
MRWWLGRECF AKRKCILATR EEGRMEDEED EEEDEVIRRY YEGEHTDTEK SPDRDKSEER
GKYAWFNEQF PPLAMWVAGN DDLVDGRRLL RRFDRGREPH VNVVHKKIIE GYEHLDVIWA
MDMIEKVGKE VKDIIWATAS ETARVQCRTP VGCEDKPQLQ EKADS
//
