ID A0A060SLF1_PYCCI Unreviewed; 757 AA.
AC A0A060SLF1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=BN946_scf185007.g108 {ECO:0000313|EMBL:CDO73054.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO73054.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO73054.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO73054.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:CDO73054.1}.
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DR EMBL; CCBP010000119; CDO73054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SLF1; -.
DR STRING; 5643.A0A060SLF1; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OMA; WGFKGHV; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000029665; 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; PF14310; Fn3-like; 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:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDO73054.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..757
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001587534"
FT DOMAIN 664..734
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 757 AA; 81634 MW; A99536C54D188375 CRC64;
MANGIRRLLP FIGVVTVGAA TVRAYGFPDC ANGPLRNTTV CDVTKDPITR AAALISLWTD
QELLNNTVNA SPGVPRLGLP AYNWWSEGLP ILMGAAFDDA LIQQVASIIS TEGRAFNNAG
HAGLDYWTPN INPFKDPRWG RGQETPGEDP FHLSQYVYNL IVGLQGGLDP KPYFKVVADC
KHFAAYDMDN WEGNVRYGFN AIVTQQDLSE FYLVPFQTCV RDAKVASVMC SYNAVNGIPS
CANSFLLQNI LRDYWGFAED RWVTSDCDAV QNIYSPHNYT NDPAQAAADA LLAGTDIDCG
TFSSTYLPDA LQRGLVHVTD LRRAATRQYA SLVRLGYFDP VDAQPYRQLG WSDVNTPQAQ
KLAYTAAVEG IVLLKNDGVL PLAKHIKKLA LIGPWANATT LMQGNYFGVA PYLISPLLGA
QQAGFDVEYV LGTNVTTRND TSGFPAAIAA AKRADAVIFA GGLDETVERE EIDRLNVTWP
GNQLELVAEL ERVGKPLVVA QFGGGQLDDS ALKSSPAVNA IIWGGYPGQS GGTALFDILT
GNVAPAGRLP ITQYPAIYAD QVPMTDMTLR PSASNPGRTY KWYTGTPVYE FGFGLHFTTF
DFSWAAPGAA ADATNVTDFG GPPSTYSISD LVQRGQKSAA FLDLAPLDTF SVRVTNTGKA
TSDYVALLFV SGSFGPSPHP NKQLVSYTRV HGLAPRKSAI AKLPVTLGAI ARADQSGDQW
IYPGTYTIAL DTDGVLKHTF RLTGSAAKIA TWPTDAS
//
