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Database: UniProt
Entry: A0A066X8M6_COLSU
LinkDB: A0A066X8M6_COLSU
Original site: A0A066X8M6_COLSU 
ID   A0A066X8M6_COLSU        Unreviewed;       728 AA.
AC   A0A066X8M6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   03-MAY-2023, entry version 33.
DE   RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE            EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN   ORFNames=CSUB01_10947 {ECO:0000313|EMBL:KDN65282.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN65282.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC         Evidence={ECO:0000256|ARBA:ARBA00024574};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN65282.1}.
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DR   EMBL; JMSE01001048; KDN65282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066X8M6; -.
DR   STRING; 1173701.A0A066X8M6; -.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   HOGENOM; CLU_004542_5_3_1; -.
DR   OMA; NYVVSDC; -.
DR   OrthoDB; 366914at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000027238; Unassembled WGS sequence.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KDN65282.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   DOMAIN          613..684
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   728 AA;  78623 MW;  18EA5A0717F5A3DA CRC64;
     MSVEEKVRNL VDASAGVKSL GLPPHGWWNE GLHGVGFSPG VLFADDSEPF GHATSFPLPV
     LTAASFDDDL FNAIGQVIGK EGRAFSNYGY AGFNFWTPNM NAFRDPRWGR GQETPGEDVL
     VVSNYVQSYV TGLQGGDPTD KVIIAACKHF AAYDIETARR ANDYNPTQQD LQDYYLPAFR
     RCVRDSHVGT VMCSYNSVNG IPSCSSEYLL KEVLRDTWGF TMDYQFVVSD CDAVKDVWLL
     HNFTNTEQDA ASVSMAAGTD LECGSSYLHL NGSLADNQVT QERVDEALTR LYKALFTVGY
     FDGSSHSSLG WSDVSTAGAQ QVAYQAAHAG MTLLKNDGVL PLASGEYKSV ALIGPFANAT
     TQMQGNYYGR APFVRSPLWA FTQQSSLQVN YAAGTDVNST SDSGFADALA AAKDSDLVIF
     CGGIDTTIEA EALDRVSITW PGNQLDLISQ LSMLGKPLVV AQFGGGQVDD TALVENANVN
     ALFWAGLPGQ AGGLALYDLV VGKVSFAGRL PITQYPASYT DSVSIFNINL RPNGTFPGRT
     YKWYTGEPVF PFGFGLHYTK FDFTWKDTLE PTYDISSIIS AAQSNARGYV TDTSTFASVN
     ITVENVGNVR SDYVGLLFLS SKNAGPAPRP NKSLASYSRA RDIEAGDSDQ LTLKLTLGSL
     ARSDAQGNLT IFPGDYTLEL DNDKSLTFDF TLTGDPVVID SLPAPKASYE FAVPVHIEPP
     SDRPLGPA
//
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