ID A0A5N6DQV4_ASPPA Unreviewed; 797 AA.
AC A0A5N6DQV4;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=BDV34DRAFT_211541 {ECO:0000313|EMBL:KAB8207518.1};
OS Aspergillus parasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5067 {ECO:0000313|EMBL:KAB8207518.1, ECO:0000313|Proteomes:UP000326532};
RN [1] {ECO:0000313|EMBL:KAB8207518.1, ECO:0000313|Proteomes:UP000326532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117618 {ECO:0000313|EMBL:KAB8207518.1,
RC ECO:0000313|Proteomes:UP000326532};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
RL Submitted (APR-2019) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML734956; KAB8207518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6DQV4; -.
DR VEuPathDB; FungiDB:BDV34DRAFT_211541; -.
DR OMA; ILRQHWG; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000326532; 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: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:UP000326532};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 691..762
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 797 AA; 86437 MW; A0A8C2223D1692BA CRC64;
MPLICIVYFL QYLDKIAISY ASVTGLRESA NLHGNQFNWV STSTESIFPD CSTGPLSKNN
VCDTSLDPVS RAKSLVAAMT LEEKINNTKY DSSGAPRLGL PAYNWWNEAL HGVAEGHGVS
FSDSGNFSYA TSFPMPILLG AAFDDDLVKQ VATVISTEAR AFANGGHAGL DYWTPNINPF
RDPRWGRGQE TPGEDPLHLS RYVYHLVDGL QDGIGPERPK VVATCKHFAA YDLENWEGIE
RYAFDAVVSS QDLSEYYLPP FKTCTRDAKV DAVMCSYNSL NGIPTCADRW LLQTLLREHW
GWEQTGHWVT GDCGAIDNIY ADHHYVADGA HAAAAALNAG TDLDCGSVFP EYLGSALQQG
LYNNQTLNNA LIRLYSSLVK LGYFDPADDQ PYRSIGWNEV FTPAAEELAH KATVEGIVML
KNDGTLPLKS NGTVAIIGPF ANATTQLQGN YEGPPKYIRT LIWAAAHNGY KVKFSQGTDI
NSNSSAGFAE AISAAKEADI VIYAGGIDNT IEKESQDRTT IVWPGNQLDL IEQLSDLKKP
LIVVQFGGGQ VDDSSLLAND GVGALLWAGY PSQAGGAAVF DILTGKSAPA GRLPVTQYPA
SYVDEVPMTD MTLRPGSNNP GRTYRWYDKA VLPFGFGLHY TTFNVSWDHD EYGPYNTDSV
ASGTTSAPVD TELFDTFSIT VTNTGKLTSD YIALLFLTAD GVGPEPYPIK TLVGYSRAKG
IEPGQSQQVQ LDVSVGSVAR TAENGDLVLY PGSYKLEVDV GQDFPTATFT VSGKEKVLDE
FPAPQQNATS AVTRRGR
//
