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Database: UniProt
Entry: A0A0W0FKL2_9AGAR
LinkDB: A0A0W0FKL2_9AGAR
Original site: A0A0W0FKL2_9AGAR 
ID   A0A0W0FKL2_9AGAR        Unreviewed;       541 AA.
AC   A0A0W0FKL2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KTB36862.1};
GN   ORFNames=WG66_10599 {ECO:0000313|EMBL:KTB36862.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB36862.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB36862.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB36862.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:KTB36862.1}.
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DR   EMBL; LATX01001880; KTB36862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0FKL2; -.
DR   eggNOG; ENOG502RY03; Eukaryota.
DR   Proteomes; UP000054988; 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   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..541
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006901778"
FT   DOMAIN          92..239
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          412..509
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          520..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  58877 MW;  B1D12D92956D0E5D CRC64;
     MGWPTKTLLT SACIFVSLTK CAVSQATWNE SSWLSITPTK NLTWVPCYDG DLECGRFQVP
     LNYSDPEGQS AAIALVRMKA NVSVDSTDYL GPILLNPGGP GGSGVDLILT QVECLGWHHA
     LTIPPGVSRS TPRVTFFETL EERLLWGRGG ILEPNSSLQD NVGSYWSRAK IIGQLAGERA
     GDILPFMNTD YTARDMLRIT EAYGREKIQY WGISYGTVLG STFASMFPDK VERLVIDGVV
     DVQDDYYTGE RRSLVSDTDD AVRWFFKDCH DAGPEKCSFY ESSVESIEER LDKLYQSIIR
     APVPVRNAGI SYGLVDYATL RSVIFSALYA PFDQWSTLAT VLADLEKGNG TALFQMAIDA
     ASPGPTPPLF ESNTFEIQTA IGCNDGDVVP SSLEDAEQHY QEALKVSGWA SMTATLRIRC
     SSWPSIPKNF FRGPITGNTS YPLLLIGNTA DPITPLASAH KVSKLFPGSV VLQQDSSGHS
     ALRSPSLCTA NAVRAYFVNG TLPEPGTVCP IDGNPFLTAP EPVKRSGGKE ARRMGGPFQI
     S
//
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