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Database: UniProt
Entry: Q0H904
LinkDB: Q0H904
Original site: Q0H904 
ID   XYNC_ASPFU              Reviewed;         325 AA.
AC   Q0H904; A3FG82; Q4WPJ5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   20-JUN-2018, entry version 59.
DE   RecName: Full=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; Synonyms=xynf10a;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SL1;
RA   Dabrowski S., Ahring B.K.;
RT   "Characterization of recombinant xylan degrading enzymes from
RT   Aspergillus fumigatus isolate SL1.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MKU1;
RA   Thiagarajan S., Jeya M., Gunasekaran P.;
RT   "Cloning and characterization of xynf10a gene from Aspergillus
RT   fumigatus MKU1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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=EAL89839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DQ156555; ABA40421.1; -; mRNA.
DR   EMBL; EF375874; ABN48479.1; -; Genomic_DNA.
DR   EMBL; AAHF01000005; EAL89839.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_751877.1; XM_746784.1.
DR   ProteinModelPortal; Q0H904; -.
DR   SMR; Q0H904; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   GeneID; 3509139; -.
DR   KEGG; afm:AFUA_4G09480; -.
DR   EuPathDB; FungiDB:Afu4g09480; -.
DR   HOGENOM; HOG000019847; -.
DR   InParanoid; Q0H904; -.
DR   KO; K01181; -.
DR   OrthoDB; EOG092C45ID; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; 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;
KW   Reference proteome; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    325       Endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000393188.
FT   DOMAIN       44    324       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    155    155       Proton donor. {ECO:0000250}.
FT   ACT_SITE    261    261       Nucleophile. {ECO:0000250}.
FT   DISULFID    279    285       {ECO:0000250}.
FT   CONFLICT     14     14       V -> A (in Ref. 1; ABA40421).
FT                                {ECO:0000305}.
FT   CONFLICT     40     40       K -> R (in Ref. 1; ABA40421).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       Y -> C (in Ref. 1; ABA40421).
FT                                {ECO:0000305}.
SQ   SEQUENCE   325 AA;  35221 MW;  BB2D1688371B3F92 CRC64;
     MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL LQKSQNEAIV
     RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN GKKVRGHTLV WHSQLPSWVS
     AISDKNTLTS VLKNHITTVM TRYKGQIYAW DVVNEIFNED GSLRDSVFSR VLGEDFVRIA
     FETARSVDPS AKLYINDYNL DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGAGASS
     SVKGALTALA SSGVSEVAIT ELDIAGASSQ DYVNVVKACL DVPKCVGITV WGVSDRDSWR
     SGSSPLLFDS NYQPKAAYNA IIAAL
//
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