ID S3CLS7_GLAL2 Unreviewed; 331 AA.
AC S3CLS7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN ORFNames=GLAREA_02066 {ECO:0000313|EMBL:EPE26154.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE26154.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE26154.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. Releases L-arabinose from arabinoxylan.
CC {ECO:0000256|ARBA:ARBA00025637, ECO:0000256|RuleBase:RU368117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462,
CC ECO:0000256|RuleBase:RU368117};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU368117}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family.
CC {ECO:0000256|ARBA:ARBA00007396, ECO:0000256|RuleBase:RU368117}.
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DR EMBL; KE145371; EPE26154.1; -; Genomic_DNA.
DR RefSeq; XP_008087473.1; XM_008089282.1.
DR AlphaFoldDB; S3CLS7; -.
DR GeneID; 19461124; -.
DR KEGG; glz:GLAREA_02066; -.
DR eggNOG; ENOG502QR18; Eukaryota.
DR HOGENOM; CLU_041805_0_0_1; -.
DR OMA; WSKDISH; -.
DR OrthoDB; 1772551at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd08987; GH62; 1.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR40631:SF2; ALPHA-L-ARABINOFURANOSIDASE; 1.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU368117};
KW Hydrolase {ECO:0000256|RuleBase:RU368117};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368117};
KW Signal {ECO:0000256|RuleBase:RU368117, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..331
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004507308"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 36328 MW; 370EE0779996EB59 CRC64;
MVRLSNSITA ALLAVTTFAQ RLPTPPTPPS PPSPPSPPSA LPSTFEWVST GPLVGPKNDG
RGIDGIKDPS VVLIDGKYHV FASTASEKDG YNLVYFSFTD FNKANASTFY YLDQSPIGTG
YRAAPEVFYF TPHKLWYLIY QNGNAAYSTN KNISDPAGWS APSNFYNGTP AIVTANIGDG
YWVDMWVICD EAECHLFSSD DNGHLFRSST SLAKFPQGMS DPVIHLSAPK YDLYEASLMY
KVGPKKYLLI VECIGKAGFR YFRSWTSESI AGMATPLAAT EENPFAGLTD VTFNGPVWSK
DISHGEVIRT QVDQTLSIDP SNMRFLYQGK E
//
