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
//