ID A0A0W7W110_9HYPO Unreviewed; 378 AA.
AC A0A0W7W110;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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=TGAM01_v204742 {ECO:0000313|EMBL:PON26266.1}, TGAMA5MH_10101
GN {ECO:0000313|EMBL:PNP38002.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON26266.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON26266.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON26266.1,
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:PNP38002.1, ECO:0000313|Proteomes:UP000236546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5MH {ECO:0000313|EMBL:PNP38002.1,
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:PON26266.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T6085 {ECO:0000313|EMBL:PON26266.1};
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:PON26266.1}.
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DR EMBL; MTYH01000115; PNP38002.1; -; Genomic_DNA.
DR EMBL; JPDN02000014; PON26266.1; -; Genomic_DNA.
DR RefSeq; XP_018665352.1; XM_018801559.1.
DR AlphaFoldDB; A0A0W7W110; -.
DR STRING; 398673.A0A0W7W110; -.
DR GeneID; 29981642; -.
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:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368117};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368117};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..378
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014528289"
FT DOMAIN 352..369
FT /note="CBM1"
FT /evidence="ECO:0000259|Pfam:PF00734"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 39361 MW; 3626754A7CC2525C CRC64;
MLSSMKKGGR KLWAGLALLA LPAIASASCA LPSTYKWTST GPLANPKSGW VSLKDFSQVP
YNGQHLVYSS TVNTAGSYGS MNFGLVSNWT SLSTASQNTM NLGTVAPTLF YFSPKKIWVL
AYEWAATPFA YVTSSDPTNA NGWSSSQPLF SGSVGGSTGP IDPALISDGT NMYLFFAGDN
GNIYRSSMPI GQFPSSFGTS FTTIMTAATN DLFEAIQVYT VSGQKQYLMI VECIGSVGRY
FRSFTATSLS GTWTPQAATE SNPFAGHANA GATWTNDISS GDLIRSTNDE TMTIDPCNLQ
LLYQGLPVGS SGDYNSLPWR PAVLTLSNPG SSTGNGTGSG GSGGSGSGEA AEYAQCGGLG
YAGPTVCQAC SPSSNLGK
//
