ID A0A093Y596_9PEZI Unreviewed; 1053 AA.
AC A0A093Y596;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN ORFNames=O988_06459 {ECO:0000313|EMBL:KFX94139.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX94139.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX94139.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX94139.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFX94139.1}.
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DR EMBL; JPJR01001403; KFX94139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Y596; -.
DR STRING; 1391699.A0A093Y596; -.
DR HOGENOM; CLU_320818_0_0_1; -.
DR Proteomes; UP000029329; 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 SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000029329};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1053
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001893985"
FT DOMAIN 17..53
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 729..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..922
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 971..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 114148 MW; B9533ECEEDF491F8 CRC64;
MIYAAAVLFV ALPLVSGQAA VWGQCGGTGW TGATTCASGS CCTVSNAWYS QCIPCTGGGG
GGATTAVTPP ATGVATSSAP GATCDLPSTY KWTSTTALAQ PKSGWASLKD FTAVPYNGQH
LVYATFHDTG STWGSMNFGL FSDWSNMASA SQNTMSGYTV APTLFQFAPK NIWVLAYQWG
PTAFSYKTSS DPSNANGWSG AQTLFTGTIS DSNTGVIDQT LIGDDTNMYL FFCGDNGKIY
RASMPIGNFP GSFGSSSTII MSDSTNNLFE AVQVYTVKGQ KKYLMIVEAI GANGRYFRSF
TATSLGGSWT PQAASESNPF AGKANSGATW SNDISHGDLI RSNPDQTFTI DPCNLQLLYQ
GRAVGSDTDY NLLPYRPALL TLKNLSNSAT TSPLPPRHSD LEVAFLELPC EQYKSHCGEK
QTLCFYCLNN TSQISQRYIA ICLLIGKFDC LFLSTWRYLM WVNSEMVENM DCSRFFMCNT
SLNSGALKVI ASEVEQWKLV EFEKTPLGCP VPKEGEVWDP VIGAGPFRPW MVPKGVAVAD
GVLLMMRLYF ELPSKTSGVT LADLQKIHGF TQRGKIQRQA AKTPGDNGST VYDVDGNLIT
IDEAVMRGNN PSDATRYPGR VNETNFLKQK GPGHNLWFNR LFNGADTQCP AYGAIFAQHW
LANCGYDITT PDGHPVLVRR AGATGQEQYK QYYLEALARR EKLRESTSPA KPSPAPSIKL
RLNIKKTQNL NPQPLEAPAN LTEPSKEIST DVSEDGMPSA QMLGNMFPCE EVSVRVRNSP
VIVLGEPDGD KCNKDTNEGV ASALTKTFAE LAFGKALTVL ETPAPVPLNN IVAAPAETSA
EKAAKVKLKL EERKKELEEI TRELEEIEEK AATEKAAAEE AAAAKAAAEK EAMEKAAAEK
TAAKLAKEND ELNRKMATKS LKHMAASIKH SISAYLAQRK AEVSEKGVVS KLDEELVFYF
WDALNSTASE PQKRKFKEEE TDGQRPAKIA KTSGEDGMMR KAPRETDDGE GAMRGLSELY
QAREEGRWTA SIKRPEFNDA VVGLGSLVGI YCA
//
