ID   A0A2X0PA30_9BASI        Unreviewed;       630 AA.
AC   A0A2X0PA30;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   SubName: Full=BQ5605_C007g04702 protein {ECO:0000313|EMBL:SGY62513.1};
GN   Name=BQ5605_C007g04702 {ECO:0000313|EMBL:SGY62513.1};
GN   ORFNames=BQ5605_C007G04702 {ECO:0000313|EMBL:SGY62513.1};
OS   Microbotryum silenes-dioicae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY62513.1, ECO:0000313|Proteomes:UP000249464};
RN   [1] {ECO:0000313|EMBL:SGY62513.1, ECO:0000313|Proteomes:UP000249464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQNC01000045; SGY62513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0PA30; -.
DR   STRING; 796604.A0A2X0PA30; -.
DR   Proteomes; UP000249464; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249464};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        200..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          256..312
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  72284 MW;  5D1C75DB9AE2357A CRC64;
     MSDFVDYSRK AQAGATNKGP FDDEPPRPLS RGSRSGKSSA SQRRKVNYGD MSRADLEAEA
     RDERQHPVGD FMSRQQVISK EGDEEAYIGG TSAFGVSGSG RPGQNDYNEK DGVAYGNYPQ
     QQDAASYYGA VQQPGFFSEK SQQKRQYADP RQHIDARPQR NQPEDLGYDP EDHHFLNDHI
     VPDYPTQTFF RKCVLTGFQI GSFIGTTAGF NLIAVMAIAT YVFKFINPFY KFKKRKDVDK
     EWELRITGER FSSRAEYYAE FFGHECEALD VETEDGFVLR VHHLIHKKFK GRGHPVILQH
     GILSNSVTFM VNEEKSLAFW LLDQGYDVYV SNIRTNFKMP HRHFKRSDPR YWAWSIKEIG
     MYDLPAIVDF VVGRTGVKPA YIGHSQGTGT MFLALSRGIR PDIGNKLSSF IALGPSVYAG
     PVLRTFPFSV MRKFKSRGLW SLVFGVREFL PFLSILQNVL PSWLFGHVAV PVFQFLFGFG
     TQQWLWRQVP KFFRTVGLPN SSELLYYYMS NFSYTNCIFN THSAEPWFPR SFPPLAIFYG
     TADTLVLGKP LVERIREYEP NVRLVKVVAL DDYEHMDMIW GVNAVPECFL GIRDMIEETK
     NGYTPVRRTK RSNSKRSRRS SSQNRETRDY
//