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Database: UniProt
Entry: Q0CNM5_ASPTN
LinkDB: Q0CNM5_ASPTN
Original site: Q0CNM5_ASPTN 
ID   Q0CNM5_ASPTN            Unreviewed;       285 AA.
AC   Q0CNM5;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Acetylxylan esterase {ECO:0000313|EMBL:EAU35156.1};
GN   ORFNames=ATEG_04709 {ECO:0000313|EMBL:EAU35156.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU35156.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH476599; EAU35156.1; -; Genomic_DNA.
DR   RefSeq; XP_001213887.1; XM_001213887.1.
DR   AlphaFoldDB; Q0CNM5; -.
DR   STRING; 341663.Q0CNM5; -.
DR   ESTHER; asptn-q0cnm5; Acetylxylan_esterase.
DR   EnsemblFungi; EAU35156; EAU35156; ATEG_04709.
DR   GeneID; 4319895; -.
DR   VEuPathDB; FungiDB:ATEG_04709; -.
DR   eggNOG; ENOG502QUMZ; Eukaryota.
DR   HOGENOM; CLU_040058_4_1_1; -.
DR   OMA; CPNTREV; -.
DR   OrthoDB; 2726434at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR000675; Cutinase/axe.
DR   PANTHER; PTHR33630:SF13; ACETYLXYLAN ESTERASE; 1.
DR   PANTHER; PTHR33630; CUTINASE RV1984C-RELATED-RELATED; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   SMART; SM01110; Cutinase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..285
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004170462"
FT   DOMAIN          249..285
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
SQ   SEQUENCE   285 AA;  28356 MW;  8846D6BA39D1E353 CRC64;
     MLWTLSILPL LGHAIASAVP AEKRQSCPGV HVFGARETTA SPGYGSSSTV VNLILSAYSG
     STAEAISYPA CGGQSSCGGV SYSASVAAGI DAVASAVNSF NTQCPSTQLV LVGYSQGGEI
     MDAALCGGGV PNQGVTNTAV RLSSSAVNMV KAAIFMGDPL FRAGLPYDVG TCSAGGFDAR
     PAGFSCPSAS KIQSYCDGPD PYCCNGSNAA THNGYGAEYG QAALTFVKSK LSSSSSGGGS
     TGGGSGSGGT VAQYGQCGGQ GYTGATTCQS PYTCTVMNQW YSQCL
//
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