ID A0A177DAF2_ALTAL Unreviewed; 798 AA.
AC A0A177DAF2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=CC77DRAFT_971887 {ECO:0000313|EMBL:OAG15909.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG15909.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG15909.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG15909.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441491; OAG15909.1; -; Genomic_DNA.
DR RefSeq; XP_018381330.1; XM_018535847.1.
DR AlphaFoldDB; A0A177DAF2; -.
DR STRING; 5599.A0A177DAF2; -.
DR GeneID; 29121441; -.
DR KEGG; aalt:CC77DRAFT_971887; -.
DR VEuPathDB; FungiDB:CC77DRAFT_971887; -.
DR OMA; WGFKGHV; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000077248; 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, ECO:0000313|EMBL:OAG15909.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..798
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008059181"
FT DOMAIN 672..742
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 798 AA; 86721 MW; 8B0BD14A513A0F3E CRC64;
MLTSTRSLQV LLVAATGAYA QFVFPDCTSG RLSNETICDA SASPLARAKS LVALYTLEEK
INATSSGSPG VPRLGIPPYQ WWSEGLHGIA GPYTNFSDEG EYSYSTSFPQ PILMGAAFDD
DLITEVAKVI STEARAFNNA NRTGLDFWTP NINPFRDPRW GRGQETPGED PYHLSSYVQA
LVHGLQGDAS DKYKRVVATC KHFAGYDIED WNGNLRYQND VQISQQDLVE YYLVPFQACV
QANVGAFMCS YNAVNGVPTC ADPYLLQTIL REHWGWTNEE QWVTSDCDAV QNVYLPHEWS
ATRGGAASDA LKAGTDLTCG TYMQEHLPAA FQQDLLEESV LDQALVRQYS SLVRLGYFDS
PDNQPYRQIG WDSVATNASQ ALARRAAAEG IVLLKNDGTL PLSLDSSTSI GLFGDWANAT
SQLLGNYAGV STYLHSPLYA LEQLNVTINY AGGNPGGQGD PTTNRWSNLY GAYSTSDILM
YVGGIDNSVE EEDQDRTYLT WTGAQLDVIT ELAETGKPVI VVVTGGGQID STPLVNNPNI
SAILWAGYPG QDGGSAIIDI VTGKTAPAGR LPTTQYPSNY IAKVSMMDMN MRPGENNPGR
TYKWYNGSAV YEFGHGLHYT NFSANITTQM QNSYAISALT QNCNSTGGFL ERCPFAAVDV
EVSNDGDVTS DYVALGYIAG EFGPAPHPKK SLVSYKRLHN ITGGASDTAT LNLTLASLAR
VDEMGNKVLY PGDYTLLIDN HPLASINFTL TGEQAMLDMW PQPPANRTAE GVKGVGDYWY
GGYGSEYAEE PADLQNTM
//
