ID   XYNC_NEOFI              Reviewed;         314 AA.
AC   A1CX14;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=NFIA_106540;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027685; EAW25166.1; -; Genomic_DNA.
DR   RefSeq; XP_001267063.1; XM_001267062.1.
DR   AlphaFoldDB; A1CX14; -.
DR   SMR; A1CX14; -.
DR   STRING; 36630.CADNFIAP00009419; -.
DR   EnsemblFungi; EAW25166; EAW25166; NFIA_106540.
DR   GeneID; 4593532; -.
DR   KEGG; nfi:NFIA_106540; -.
DR   VEuPathDB; FungiDB:NFIA_106540; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_2_0_1; -.
DR   OMA; PENQMKW; -.
DR   OrthoDB; 829814at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006702; 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   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 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..314
FT                   /note="Probable endo-1,4-beta-xylanase C"
FT                   /id="PRO_0000393195"
FT   DOMAIN          23..313
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        154
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        250
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..274
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34254 MW;  1CA184D0E5D274F7 CRC64;
     MVVLSKLISS ILFASLVSAA VIERQATSIN QAFTSHGKKY FGTASDQRLL QNSQNEAIVR
     KDFGQLTPEN SMKWDATEPS RGSFNFAGAD FLVNYAKQNG MKVRGHTLVW HSQLPSWVSA
     ITDKNTLTSV LKNHITTVMT RYKGQIYHWD VVNEIFNEDG SLRDSVFSRV LGEDFVRIAF
     ETARSVDPSA KLYINDYNLD SASYGKTQGM VSHVKKWLAA GIPIDGIGSQ THLALTALAS
     SGVSEVAITE LDIAGASSQD YVNVVNACLG VPKCVGITVW GVSDKDSWRS SSSPLLFDSN
     YQPKAAYNAI IAAL