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Database: UniProt
Entry: W6ZJZ2_COCMI
LinkDB: W6ZJZ2_COCMI
Original site: W6ZJZ2_COCMI 
ID   W6ZJZ2_COCMI            Unreviewed;       523 AA.
AC   W6ZJZ2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU361235};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361235};
GN   ORFNames=COCMIDRAFT_81951 {ECO:0000313|EMBL:EUC50385.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC50385.1};
RN   [1] {ECO:0000313|EMBL:EUC50385.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC50385.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KI963923; EUC50385.1; -; Genomic_DNA.
DR   RefSeq; XP_007683051.1; XM_007684861.1.
DR   AlphaFoldDB; W6ZJZ2; -.
DR   ESTHER; cocmi-w6zjz2; Fungal_carboxylesterase_lipase.
DR   GeneID; 19125963; -.
DR   KEGG; bor:COCMIDRAFT_81951; -.
DR   eggNOG; KOG4389; Eukaryota.
DR   HOGENOM; CLU_006586_10_7_1; -.
DR   OrthoDB; 4829785at2759; -.
DR   Proteomes; UP000054032; 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   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   PANTHER; PTHR11559; CARBOXYLESTERASE; 1.
DR   PANTHER; PTHR11559:SF360; CARBOXYLIC ESTER HYDROLASE; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361235};
KW   Signal {ECO:0000256|RuleBase:RU361235}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU361235"
FT   CHAIN           18..523
FT                   /note="Carboxylic ester hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361235"
FT                   /id="PRO_5005151164"
FT   DOMAIN          21..499
FT                   /note="Carboxylesterase type B"
FT                   /evidence="ECO:0000259|Pfam:PF00135"
SQ   SEQUENCE   523 AA;  57158 MW;  7AB77073BC50299A CRC64;
     MLRLLLCVAF FLHSALALDE VVDLGYAKYR GKSIGNGVMR WAGMRFARSP SRKEGLRFAA
     PQDPVKEEGI VDASSFGPLC IGTRSDLNAE TGGTHSEDCL FVNVFSPSTA NDTSNLPVYV
     FIQGGGFNMN GNADYNGADL IDAADNGIVV VNFNYRVGPY GFLASDEIAT NQNFSLNNGL
     KDQRQALKWV QANIQKFGGD PKHVTIGGAS AGGGSVVFQL TAYGGKDEGL FHAAAAESAA
     FPSLRDVKDS QWQFNELLRE TGCKDLNCMA TMETVQFQKA VRALQKPFPG GGGPPVYFWN
     PTLDGDFIKD FTFNELRAGH YVHVPTIFGT ATHDGINFTP QNVVSVAKAE SFLIDNYPGM
     KWSTISRIWG SDTAIAAGNN DRWRAVTADI YGAIRYACPG LNISATFASD KEHSTWHYRW
     NVGTASHVGE LLPIWNNATS AAGVFVQAYW ASFIRTYDPN KFAAEFLVGK GSELKSPNWE
     PFDAKDPKRL VFNDDNNVAM EKVSEVEQKR CDDVDALGLH LKQ
//
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