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Database: UniProt
Entry: A0A0B1PD67_UNCNE
LinkDB: A0A0B1PD67_UNCNE
Original site: A0A0B1PD67_UNCNE 
ID   A0A0B1PD67_UNCNE        Unreviewed;       711 AA.
AC   A0A0B1PD67;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Putative alpha beta hydrolase fold-containing protein {ECO:0000313|EMBL:KHJ34866.1};
GN   ORFNames=EV44_g2450 {ECO:0000313|EMBL:KHJ34866.1};
OS   Uncinula necator (Grape powdery mildew).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ34866.1, ECO:0000313|Proteomes:UP000030854};
RN   [1] {ECO:0000313|EMBL:KHJ34866.1, ECO:0000313|Proteomes:UP000030854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX   PubMed=25487071;
RA   Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA   Walker M.A., Cantu D.;
RT   "Adaptive genomic structural variation in the grape powdery mildew
RT   pathogen, Erysiphe necator.";
RL   BMC Genomics 15:1081-1081(2014).
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:KHJ34866.1}.
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DR   EMBL; JNVN01000633; KHJ34866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1PD67; -.
DR   STRING; 52586.A0A0B1PD67; -.
DR   HOGENOM; CLU_005757_2_0_1; -.
DR   OrthoDB; 1387681at2759; -.
DR   Proteomes; UP000030854; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; 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; PTHR42886:SF61; HYDROLASE; 1.
DR   PANTHER; PTHR42886; RE40534P-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KHJ34866.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030854}.
FT   DOMAIN          368..447
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  78663 MW;  2716E2259B3A1D6C CRC64;
     MSTEQSHRSV QSPITSVNVN THSISVGNSN GRLDSRSQPS GRYERDYVIR ERPTNSQPSS
     DLDIDYSSCS HHEKNLLTAN SRTASKDSNV KERKSIGNLS VVSAQTHSES RVKLPDARDK
     KQRRIIYKSS LEKLRNKELE RRKKTKDSND DRPTFEPSSS AVNKTISSEL KSTSNNLVNK
     AMGSSKFTLE SCGKHDSYIE KGSLNEATKD SLPVTSENYG GLLANASNIS SAHAMENYTS
     SLAFKPDKAR KNNYPKESGA HVSERIYSNH RNRLSISTSS PVNIGSSRLS YNGRISIDER
     SSSIESIDEA VEAYLCAPRL SQKIRHPLTG RIISFSEVGD PEGFAVFCCV GMGLTRYVTA
     FYDELALSLK LRLITPDRPG VGDSEPYNDG TTTPLSWPDD IYTICQFLRI TKFSILAHSA
     GAIYALATAL RMPQHIRGRI HLLAPWIPPS QMSVVGGRVG LPPNSSIPTS QRILRVLPTT
     ILKAANSSFI SATSNSLTSS ISKQRKSKRK SIGREAIAAS ARNTLSSGIE EEILRRNGSL
     FLETSNTNVN QNEDVQLNSE AEILAAAAYS LATKERQVNY ESRLTHAIWN YATQGANPAV
     DLLVCLERRH TIGFRYVDIT RAVVIHHGSK DTRVPLENVL WMGKTMKRCE VNVLEGEGHS
     LMASASVMSS ILTEIAREWE DWMRLTASTV AHRNEGIRRN LIERASIGAF R
//
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