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Database: UniProt
Entry: A0A166KS21_9AGAM
LinkDB: A0A166KS21_9AGAM
Original site: A0A166KS21_9AGAM 
ID   A0A166KS21_9AGAM        Unreviewed;       533 AA.
AC   A0A166KS21;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU361235};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361235};
GN   ORFNames=PENSPDRAFT_741445 {ECO:0000313|EMBL:KZV76028.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76028.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV76028.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV76028.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000256|ARBA:ARBA00005964, ECO:0000256|RuleBase:RU361235}.
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DR   EMBL; KV424467; KZV76028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166KS21; -.
DR   STRING; 1314672.A0A166KS21; -.
DR   ESTHER; 9homo-a0a166ks21; Fungal_carboxylesterase_lipase.
DR   InParanoid; A0A166KS21; -.
DR   OrthoDB; 1552062at2759; -.
DR   Proteomes; UP000077086; 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; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   PANTHER; PTHR43142; CARBOXYLIC ESTER HYDROLASE; 1.
DR   PANTHER; PTHR43142:SF8; CARBOXYLIC ESTER HYDROLASE; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU361235, ECO:0000313|EMBL:KZV76028.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT   DOMAIN          19..296
FT                   /note="Carboxylesterase type B"
FT                   /evidence="ECO:0000259|Pfam:PF00135"
FT   REGION          73..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  59279 MW;  3915765EDFCE1354 CRC64;
     MSDPTRHLDT ELVESKETVV VQTRYGPVRG RRAANGAACF LEVPYALPAE RWKDPRPLPE
     DYRYEDKEYI RESKYGYQPS KNGQAAGSAP RDGLGYGVPS EDPLFVNIVA PPSFSTRSET
     TTKYPVKVYI HGGFLQFGSP HGLSSQAQYV AAERNELWIN VGYRLSAFGF LASDAPDVSG
     NFGFKDQWVA LEWVRANAAA FGGDLDDIEL NGLSAGAHSV HQLLHHASRL PEGVRAPFTS
     AALQSNAIAT DPKTPSELHA QFEALCEALE LDPAASDVLD SLRTTSWKRI ADLIDAEKVG
     PLGTYGTFRG TSDGAWMGID PGAMRWQRSG GFARGLKAAG VRAVLLGDLT EEWYLYGLAH
     EVSSVDEIQS NLARYYPASV VDTMMELYKG RIRNDLTKDE LFRLLGDMLS EGQVHLPVRL
     LHRDLLAANF SVARYQIRWT PEQGRPLGYV THATDRPLWA FRKPALNEDQ VPVAREWLNT
     IATELARLQS GGAPRGEREI LTLKEDRTIG WTEDARWEEY MRIRRALPGE DVE
//
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