ID A0A0F4Z0W2_TALEM Unreviewed; 979 AA.
AC A0A0F4Z0W2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=T310_1860 {ECO:0000313|EMBL:KKA24129.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA24129.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA24129.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA24129.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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:KKA24129.1}.
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DR EMBL; LASV01000074; KKA24129.1; -; Genomic_DNA.
DR RefSeq; XP_013330741.1; XM_013475287.1.
DR AlphaFoldDB; A0A0F4Z0W2; -.
DR STRING; 1408163.A0A0F4Z0W2; -.
DR GeneID; 25314211; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
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 Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..979
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482090"
FT DOMAIN 513..682
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 979 AA; 106322 MW; EB0D375B3192C5F6 CRC64;
MIFLASPRLL FGATVVVALC QAQLFPNGFS FNPQLTSKKC PRDAKAVERD AFLDQLVANL
TVPELVLQMH LMFADNIIGP KSDNGLYDYT MRLAPTAPIG IIHDWYPTNK SQYNDLQRLN
SQKARIDIPF LQTGECLHGV GSFKQSMLPQ SIGMAASFDT NLVHRVGRAI GTEASSIGIH
ACFAPVLDLG KDPRWGRVQE AWGEDMVLTS HMGVAYASGL SKNGSLSDPD AVVPVMKHFA
AHGSPQAGHN AAPFMGYGVR EVLQELLVPF KAAVDLGGVK GVMMAYSELD EVPCSVNPIL
YQALESWGYD GYVTADDGGL SMLYETHRVT SSVTDTIAQW HNAGGMVQYY DFPLETTVDL
VANGTLSKST LQSLVRRILG VKYDLGLFEN RYIADDVDSE AITQSHVPLT LEAAQKSIVL
LENRNVTLPL KPKEKGIKRI ALVGPFGDTF NYGDYSGQWG GYPVANASTI RQAMSQYLAV
NASGTELVSS WGANSWLYNG QYNIPPYHLS ANGTSGGLLA TYYADTNFTD ARFQKLETPS
LDWGLYPPNG LPSNNFSVTW EGDLTVPVDA EVDGWLGVAV YANTTAKLYV DGQFLVEAEA
TPSGNILSNI MPLSYSMANG TMAPPGSAPF TFRKGARHHI RLEYQAWNYV QKFENVNSLN
AQVLLFWNLV DRNDPVGKAV DIAKSSDVIV LAVGANWNSD GESGDRATLG LSPNQTALAD
AIFALEKPVV LVLQGGRPFA IPQYYRQAAA VLNTFFPGQS GGQAISDAIF GITNPGGRVP
LSVPYDVGTL PVYYNYKPSY PRDYTDIPYT PIVSSLPLSP LNDQMILTIS RVTKQYPFGY
GLSYTNFSVS NFRATATSPN STTTASTNSS FTPTSTITFS VDITNTGDIA GSYVPQVYLL
GRVSSITRPV RQLVAFTRVY LSPGETATAT MDLDVARYLT VLDRAYQWVV EPGAYTFALM
ENGGSQASTA MNVTMSCCR
//
