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Database: UniProt
Entry: B0Y6E0
LinkDB: B0Y6E0
Original site: B0Y6E0 
ID   XYNC_ASPFC              Reviewed;         316 AA.
AC   B0Y6E0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   10-MAY-2017, entry version 44.
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=AFUB_066600;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)
OS   (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expressed in presence of xylan and repressed by
CC       glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP50325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DS499598; EDP50325.1; ALT_SEQ; Genomic_DNA.
DR   ProteinModelPortal; B0Y6E0; -.
DR   SMR; B0Y6E0; -.
DR   HOGENOM; HOG000019847; -.
DR   OrthoDB; EOG092C45ID; -.
DR   PhylomeDB; B0Y6E0; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001699; 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; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; Complete proteome; Disulfide bond;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    316       Probable endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000393189.
FT   DOMAIN       44    315       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    155    155       Proton donor. {ECO:0000250}.
FT   ACT_SITE    252    252       Nucleophile. {ECO:0000250}.
FT   DISULFID    270    276       {ECO:0000250}.
SQ   SEQUENCE   316 AA;  34476 MW;  4FDDF1F05E93AF30 CRC64;
     MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL LQKSQNEAIV
     RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN GKKVRGHTLV WHSQLPSWVS
     AISDKNTLTS VLKNHITTVM TRYKGQIYAW DVVNEIFNED GSLRDSVFSR VLGEDFVRIA
     FETARSVDPS AKLYINDYNL DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGALTAL
     ASSGVSEVAI TELDIAGASS QDYVNVVKAC LDVPKCVGIT VWGVSDRDSW RSGSSPLLFD
     SNYQPKAAYN AIIAAL
//
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