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Database: UniProt
Entry: A0A2D3UVV7_9PEZI
LinkDB: A0A2D3UVV7_9PEZI
Original site: A0A2D3UVV7_9PEZI 
ID   A0A2D3UVV7_9PEZI        Unreviewed;       779 AA.
AC   A0A2D3UVV7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Related to triacylglycerol lipase {ECO:0000313|EMBL:CZT17200.1};
GN   ORFNames=RCC_03032 {ECO:0000313|EMBL:CZT17200.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT17200.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT17200.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT17200.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FJUY01000003; CZT17200.1; -; Genomic_DNA.
DR   STRING; 112498.A0A2D3UVV7; -.
DR   OrthoDB; 5471104at2759; -.
DR   Proteomes; UP000225277; 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:UP000225277};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        149..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          251..342
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   REGION          97..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..779
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  88688 MW;  7851068445E29626 CRC64;
     MRERRSESLH VEFERQSRKL PLLNPDQEDF STGSTQAAEA KFITPLDPVI ETVQGQRLPV
     IPVAEAVKLN KLKNSVEGHE SFYPPQSALR EGKDGSRYGA RIARPGSEKQ SEEADAPLRH
     AIPKSRTNPL FPDLPVYGPP TRLRSLQCWF FRVVSSVLSL CFLIVIVLGA VFTGLXKLLH
     PTKLQVSGKN RPFHAEELRR RQERKAAEKE WVQTKKHLNA QAPSGEKQDL PQDGQFIPTE
     GGPDPLCVDM AYYARRVGLD AECFDVQTED GFIIELWHIY NPREYVRPPQ SSREIRSPDI
     FQTSVSSPCY AETSRAFPEG RKKYPVLMMH GLLQSAGAYC ANDDDSLAFY LAKSGYDVWL
     GNNRCGFDPK HTSLQYEDPR FWAWNVRQMG VMDLPALISR VLAETGFPKL GLIAHSQGTT
     QTLVALAKEQ RPEIGEKISV FCALAPAAYS GPLIKKAYFR FMQLISPGMF RLIFGIHAFI
     PIMGFAHTVL PGRPFSWMGY HVFSFLFSWS DSRWDRDIRN RMFQWAPSYV SAESMAWWLG
     RTGFAKQKCI LSTREEGQIE DEEDEEDDAA LRAYYADKEP HLSEREKLQR SLTAYRRGSI
     AIHQFQNKRG RFAWYDDRFP PLALWVAGAD DLVDGRRLLR RFERGREPHV NIVHQKIIEG
     YEHLDVIWAM DAIEKVGKEV REVIWRTASL ESQKQCRTPI GCDKPHEEEP HPQDVPMVYS
     GGRERMASIS QSASKVGTGE LQIDASKNAK ADQQKYRESR EEARSYADTS DGSETSEKP
//
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