ID A0A218Z0D6_9HELO Unreviewed; 738 AA.
AC A0A218Z0D6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Partial AB-hydrolase lipase domain-containing protein {ECO:0000259|Pfam:PF04083};
GN ORFNames=B2J93_2818 {ECO:0000313|EMBL:OWP01408.1};
OS Marssonina coronariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Marssonina.
OX NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP01408.1, ECO:0000313|Proteomes:UP000242519};
RN [1] {ECO:0000313|EMBL:OWP01408.1, ECO:0000313|Proteomes:UP000242519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:OWP01408.1,
RC ECO:0000313|Proteomes:UP000242519};
RA Cheng Q.;
RT "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT blotch.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWP01408.1}.
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DR EMBL; MZNU01000279; OWP01408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218Z0D6; -.
DR STRING; 503106.A0A218Z0D6; -.
DR InParanoid; A0A218Z0D6; -.
DR OrthoDB; 5471104at2759; -.
DR Proteomes; UP000242519; 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:UP000242519};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..344
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT REGION 97..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..738
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 83087 MW; 9DDE5AD0060CC065 CRC64;
MSTTSSHTAP ATVLPTTAIK YAHQAERLSL AALGQDSDGS GMAVEALYIT PQDAIVITGN
GGRLPAVPLA EAAKLNRLKA AVEGDPNETL EAAMMEKSVS EDGRPDSQNW NPMQKTGEGS
LRRAMPPSRT NPLFPPLPLY GPSSVSRDLQ CMVFRASSFI LSGCFLGLIV FGAAVTSLRP
MFTHVWLRLT WRSPDARRPF HEDEKRLKRL RKEEEKEWSK KQKTWTDSAV KMHAINDDEA
DQSEFIPTEG GPDPLVCDVG YYARRVGLDM EAFKVQTEDG FIIDLWHIYN PSEYTPMSDV
EHSARGPDLF ASAGPCRSPT TQKPKFPILM IHGLLQSSGA YCTNDDRSLA FYLCKSGYDV
WLGNNRCGFN PDHTLLSSPD PRMWAWNIRQ MGVMDLPALT SRVLSETGFS KLGLIAHSQG
TTQTLVALAK EQRPELGDKL TVFCALAPAA YAGPLIGKAY FKFMRMISPA FFRIIFGIHA
FIPLMMTMHS IIPGKLFGAM GYVVFHFLFN WSDFRWDRGL RDRCFQFSPV YVSAESMRWW
LGRECFAKHK CILATREESH AEDAEDDMED SCIRSEQEAN SSSPRDRPSQ AQRSLEARKK
HERRPRGATA WYNEQVPPFA FWVTGSDDLV DGRRLLRRFE RGREPHARIV HSNVIEEYEH
LDVIWAMDCI EKVGREVKEV LWKTCDVRHQ VRTPKGCEDV EAWHDPKFDE KVDSDVGADG
ASEEKEEDDQ SSSESPGE
//