GenomeNet

Database: UniProt
Entry: A1CCL9
LinkDB: A1CCL9
Original site: A1CCL9 
ID   BXLB_ASPCL              Reviewed;         771 AA.
AC   A1CCL9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   19-FEB-2014, entry version 36.
DE   RecName: Full=Probable exo-1,4-beta-xylosidase bxlB;
DE            EC=3.2.1.37;
DE   AltName: Full=1,4-beta-D-xylan xylohydrolase bxlB;
DE   AltName: Full=Beta-xylosidase bxlB;
DE   AltName: Full=Xylobiase bxlB;
DE   Flags: Precursor;
GN   Name=bxlB; ORFNames=ACLA_062400;
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: Xylan 1,4-beta-xylosidase 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-xylans, to remove
CC       successive D-xylose residues from the non-reducing termini.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW12276.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DS027050; EAW12276.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001273702.1; XM_001273701.1.
DR   ProteinModelPortal; A1CCL9; -.
DR   GeneID; 4705939; -.
DR   KEGG; act:ACLA_062400; -.
DR   eggNOG; COG1472; -.
DR   HOGENOM; HOG000031216; -.
DR   KO; K15920; -.
DR   OrthoDB; EOG7PGF05; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR026892; Glyco_hydro_3.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30620; PTHR30620; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    771       Probable exo-1,4-beta-xylosidase bxlB.
FT                                /FTId=PRO_0000394085.
FT   ACT_SITE    293    293       By similarity.
FT   CARBOHYD     67     67       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    305    305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    345    345       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    423    423       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    462    462       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    463    463       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   771 AA;  83355 MW;  4EA258993A6B26C1 CRC64;
     MVGLTPQHYG NAIALMTYLA STALADNKFP DCTSGPLSKL AVCDTSRDVT TRAQSLVDAM
     SFAEKVNNTQ YEAPGVPRLG LPAYNWWSEA LHGVAGAPGV HFADSGPFSY ATSFAQPILL
     GASFDDELVK QVATVVGTEG RAFGNAGRAG LDYWTPNINP FRDPRWGRGQ ETPGEDPLHV
     SRYVYHLVDG LQGGIGPARP QIAATCKHFA AYDMEDWNGV SRHEFDARVS TQDLAEFYLP
     SFKSCVRDAQ VDAVMCSYNA LNGVPTCADP YLLQTLLREH WDWDQPGHWV VSDCGAIDDI
     YIGHNYTKTG AEAAAVALNA GTDLDCGTVF PKHLGEAAEQ GLYTNQTLDR ALVRLYSSLV
     KLGYFDPAEK QPYGSIGWKD VDTPAAEQLA HKAAVEGIVL LKNDQTLPLK AKGTLALIGP
     YANATKQMQG NYQGPPKYIR TLEWAATQHG YQVQYSPGTA INNSSTAGFA AALAAAKDAD
     VVLYAGGIDN TIESETLDRT TITWPGNQLS LISELSNLHK PLIVIQFGGG QVDDTPLLTN
     PHVNALLWAG YPSQEGGAAI FDILTGKAAP AGRLPITQYP AAYTAQVPMT EMGLRAGGDN
     PGRTYRWYDK AVVPFGFGLH YTSFEVSWDR GRLGPYNTAA LVNRAPGGSH VDRALFDTFR
     VQVQNTGTVT SDYVALLFVK TEDAGPEPYP LKTLVGYTRV QQVKPGERRS VEIEVTLGAM
     ARTAANGDLV LYPGKYTLQV DVGERGYPTA RVSVHGKEVV LDHFPQPPEG R
//
DBGET integrated database retrieval system