GenomeNet

Database: UniProt
Entry: Q0CFS3
LinkDB: Q0CFS3
Original site: Q0CFS3 
ID   XYNA_ASPTN              Reviewed;         231 AA.
AC   Q0CFS3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JAN-2019, entry version 61.
DE   RecName: Full=Probable endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xlnA; ORFNames=ATEG_07461;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., 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
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:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; CH476604; EAU31723.1; -; Genomic_DNA.
DR   RefSeq; XP_001216082.1; XM_001216082.1.
DR   ProteinModelPortal; Q0CFS3; -.
DR   SMR; Q0CFS3; -.
DR   STRING; 33178.CADATEAP00002779; -.
DR   EnsemblFungi; EAU31723; EAU31723; ATEG_07461.
DR   GeneID; 4322746; -.
DR   EuPathDB; FungiDB:ATEG_07461; -.
DR   HOGENOM; HOG000179135; -.
DR   OMA; NMQNHFN; -.
DR   OrthoDB; 1306131at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    231       Probable endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000393163.
FT   DOMAIN       43    231       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    127    127       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    218    218       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     34     34       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   231 AA;  24752 MW;  4707D257787EDDCE CRC64;
     MVSFLRLAVA CFAAVGALAA PVESLEERSD ELFNSTLHEF AERSTPSSTG WSNGYYYSFW
     TDGGGSVTYT NGAAGQYSVQ WSNVGNFVGG KGWNPGSART INYGGSFNPS GNGYLAVYGW
     TTNPLVEYYV VESYGTYNPG SGGTYKGTVN SDGGTYNIYT ATRYNAPSII GTATFTQYWS
     VRTSKRTGGT VTMANHFNAW ASHGMNLGTH NYQIVATEGY QSSGSSSITV Y
//
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