ID   XYNC_ASPTN              Reviewed;         326 AA.
AC   Q0CBM8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   22-FEB-2023, entry version 65.
DE   RecName: Full=Probable endo-1,4-beta-xylanase C;
DE            Short=Xylanase C;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE   Flags: Precursor;
GN   Name=xlnC; ORFNames=ATEG_08906;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
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.
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expressed in presence of xylan and repressed by glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; CH476606; EAU31038.1; -; Genomic_DNA.
DR   RefSeq; XP_001217492.1; XM_001217491.1.
DR   AlphaFoldDB; Q0CBM8; -.
DR   SMR; Q0CBM8; -.
DR   STRING; 341663.Q0CBM8; -.
DR   GeneID; 4323089; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   OrthoDB; 548101at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..326
FT                   /note="Probable endo-1,4-beta-xylanase C"
FT                   /id="PRO_0000393194"
FT   DOMAIN          46..325
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        156
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..286
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  35374 MW;  CA861B13624D37FE CRC64;
     MVRLTVLAGF LLTSAACSAC VIGERQAAAS INNAFKAKGK KYFGTCGDQG TLSDSTNSAI
     VKADFGQLTP ENSMKWDATE PNRGQFSFGG ADYLVNYATS NGKMIRGHTL VWHSQLPGWV
     QGITDKNTLT SVLKNHITTV MQRYKGKIYA WDVVNEIFNE DGSLRKSVFY NVLGEDFVRI
     AFETARSVDP QAKLYINDYN LDNANYAKTK GMADHVRKWI SQGIPIDGIG SQTHLGSGGS
     WTVKDALNTL ASSGVSEVAI TELDIAGASS TDYVNVVNAC LSVSKCVGIT VWGVSDKYSW
     RSNDKPLLFD SNFQPKAAYN AIISAL
//