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Database: UniProt
Entry: A0A0W7W494_9HYPO
LinkDB: A0A0W7W494_9HYPO
Original site: A0A0W7W494_9HYPO 
ID   A0A0W7W494_9HYPO        Unreviewed;       325 AA.
AC   A0A0W7W494;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE            EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN   ORFNames=TGAM01_v202157 {ECO:0000313|EMBL:PON29049.1}, TGAMA5MH_02408
GN   {ECO:0000313|EMBL:PNP46372.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:PNP46372.1, ECO:0000313|Proteomes:UP000236546};
RN   [1] {ECO:0000313|EMBL:PON29049.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON29049.1,
RC   ECO:0000313|Proteomes:UP000054821};
RX   PubMed=26893428;
RA   Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT   "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT   Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL   Genome Announc. 4:e01747-15(2016).
RN   [2] {ECO:0000313|EMBL:PNP46372.1, ECO:0000313|Proteomes:UP000236546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A5MH {ECO:0000313|EMBL:PNP46372.1,
RC   ECO:0000313|Proteomes:UP000236546};
RA   Gardiner D., Kazan K., Vos C., Harvey P.;
RT   "Genomes of Trichoderma spp. with biocontrol activity.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PON29049.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON29049.1};
RA   Baroncelli R.;
RT   "Trichoderma gamsii strain T6085, whole genome shotgun sequencing
RT   project.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PNP46372.1}.
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DR   EMBL; MTYH01000016; PNP46372.1; -; Genomic_DNA.
DR   EMBL; JPDN02000005; PON29049.1; -; Genomic_DNA.
DR   RefSeq; XP_018666523.1; XM_018800381.1.
DR   AlphaFoldDB; A0A0W7W494; -.
DR   STRING; 398673.A0A0W7W494; -.
DR   GeneID; 29980464; -.
DR   OrthoDB; 1772551at2759; -.
DR   Proteomes; UP000054821; Unassembled WGS sequence.
DR   Proteomes; UP000236546; 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; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   PANTHER; PTHR40631:SF1; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW   Glycosidase {ECO:0000256|RuleBase:RU368117};
KW   Hydrolase {ECO:0000256|RuleBase:RU368117};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054821};
KW   Secreted {ECO:0000256|RuleBase:RU368117};
KW   Signal {ECO:0000256|RuleBase:RU368117, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..325
FT                   /note="Alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014528259"
SQ   SEQUENCE   325 AA;  34618 MW;  52B990301EBF3D8A CRC64;
     MRLFETGALL LASAGVVSAR VAAAAACALP STYRWNSTGA LANPKSGWAS LKDFTHVTYN
     GQHLVFGSFH DTGSTWGSMN FGLFSDWSNM GSASQNKMSP GTVAPTLFHF APKNIWVLAY
     QWGPTTFSYI TNSNPSSVSG WSSPQPLFSG TISGASAIDQ TVIGDSSNMY LFFAGDNGKI
     YRASTPIGNF PGSFGTASTV VLSDSTNNLF EAVQVYTVSG ANQYLMIVEA IGANGRYFRS
     FTSNSLSGSW TAQAASESKP FAGKANSGAT WTNDISHGDL IRSNPDQTMT IDPCNLQFLY
     QGRATNSGGT YDLLPYRPGL LTLQH
//
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