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Database: UniProt
Entry: A1CU59
LinkDB: A1CU59
Original site: A1CU59 
ID   XYNB_ASPCL              Reviewed;         221 AA.
AC   A1CU59;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   16-JAN-2019, entry version 60.
DE   RecName: Full=Probable endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE   AltName: Full=Endo-1,4-beta-xylanase G1;
DE            Short=Xylanase G1;
DE   Flags: Precursor;
GN   Name=xlnB; Synonyms=xynB, xynG1; ORFNames=ACLA_085410;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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:
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW06846.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; DS027060; EAW06846.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001268272.1; XM_001268271.1.
DR   SMR; A1CU59; -.
DR   STRING; 5057.CADACLAP00007756; -.
DR   PRIDE; A1CU59; -.
DR   EnsemblFungi; EAW06846; EAW06846; ACLA_085410.
DR   GeneID; 4699767; -.
DR   KEGG; act:ACLA_085410; -.
DR   EuPathDB; FungiDB:ACLA_085410; -.
DR   HOGENOM; HOG000179135; -.
DR   KO; K01181; -.
DR   OrthoDB; 1306131at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006701; 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; 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; 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; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    221       Probable endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000393165.
FT   DOMAIN       33    221       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    117    117       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    208    208       Proton donor. {ECO:0000250}.
SQ   SEQUENCE   221 AA;  24058 MW;  45E7DBA2FEEFBAD8 CRC64;
     MVSFSSLALA LSTVVGVLAA PGSEKYVELA KHQLTHSQTG TKNGYYYSFW TDNRGQVSYT
     NGKGGQYSVN WKDCGNFVAG KGWNPASAKT VTYSGNWKPS GNSYVSVYGW TQNPLIEFYI
     VESFGSYNPS TGATELGTVE SDGGTYKIYK TKRVDAPSIE GKKTFDQFWS VRTSHRVGGT
     VTTKNHFNAW AKSGLKLGTF NYMILATEGY HSSGSATMTV S
//
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