ID   LIP4_ARTBC              Reviewed;         394 AA.
AC   D4AV38;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Probable secreted lipase ARB_00047 {ECO:0000305};
DE            EC=3.1.1.1 {ECO:0000250|UniProtKB:L0TC47};
DE   Flags: Precursor;
GN   ORFNames=ARB_00047;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Lipase that displays broad substrate specificity.
CC       {ECO:0000250|UniProtKB:L0TC47}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000250|UniProtKB:L0TC47};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; ABSU01000012; EFE32960.1; -; Genomic_DNA.
DR   RefSeq; XP_003013600.1; XM_003013554.1.
DR   AlphaFoldDB; D4AV38; -.
DR   SMR; D4AV38; -.
DR   ESTHER; artbc-d4av38; Bacterial_esterase.
DR   EnsemblFungi; EFE32960; EFE32960; ARB_00047.
DR   GeneID; 9519879; -.
DR   KEGG; abe:ARB_00047; -.
DR   eggNOG; ENOG502REH0; Eukaryota.
DR   HOGENOM; CLU_038297_1_0_1; -.
DR   OMA; GNGHMVF; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..394
FT                   /note="Probable secreted lipase ARB_00047"
FT                   /id="PRO_5003053689"
FT   REGION          366..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        206
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:L0TC47"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   394 AA;  44100 MW;  FDE5B63D8C9F9C84 CRC64;
     MVVLPLFFAF FFMVQGNNYQ PRDEIPYVRK YFYVGGQYAD DGNGDHIFRD QMYVEHLVPT
     KGPIKQQPIV LLHGQAQTGT NWLNKPDGGR GWASYFIEHG YECYIVDQTS RGRSPWVPEN
     GTIAAIPAET IQRLFTATAR YKLWPEAELH TQWPGSGVIG DPIFDAYYAS TVQFLKSQIQ
     QETTIQAAGA ALLDRIGRPV ILVTHSQAGA HGWLVADTRP ELVHSIIALE PAGPPFENVI
     YKGPYSRVWG LTNAPLTYSP AVVDPETEIV KQTIDDRPGS HCIIQADSPP PRQLPNLRRI
     RTLVVTAEAS FHRPTDWCVV RYMEQAGISV DHVQLGDIGI RGNGHMLFLE RNSDEIAAVL
     RRWMEEKDTK PAKKAQEAQG AQGAQEAQGK EKEL