GenomeNet

Database: UniProt
Entry: A0A093Z030_9PEZI
LinkDB: A0A093Z030_9PEZI
Original site: A0A093Z030_9PEZI 
ID   A0A093Z030_9PEZI        Unreviewed;       804 AA.
AC   A0A093Z030;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE            EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN   ORFNames=V491_07527 {ECO:0000313|EMBL:KFY10676.1};
OS   Pseudogymnoascus sp. VKM F-3775.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY10676.1, ECO:0000313|Proteomes:UP000029338};
RN   [1] {ECO:0000313|EMBL:KFY10676.1, ECO:0000313|Proteomes:UP000029338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY10676.1,
RC   ECO:0000313|Proteomes:UP000029338};
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:KFY10676.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPJT01004634; KFY10676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Z030; -.
DR   HOGENOM; CLU_320818_0_0_1; -.
DR   Proteomes; UP000029338; 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   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:UP000029338};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368117};
KW   Signal {ECO:0000256|RuleBase:RU368117, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..804
FT                   /note="Alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001890245"
FT   REGION          558..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          672..737
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   804 AA;  88112 MW;  2639BE51D5E00DBC CRC64;
     MIFTTALLIV ALPLVSSQSC DLPSTYTWTS TEALAQPKSG WVSLKDFTAV PYNGQHLVYA
     TFHDQGSTWG SMNFGLFSDW SDMSSASQNT MNSYTVAPTL FQFAPTNTWI LAYQWGPTAF
     SYKTSSDPTN ANGWSEAQTL FTGSISDSST GVIDQTLIGD DTNMYLFFCG DNGKIYRASM
     PIGNFPGSFG SSSTIIMSDT TNNLFEAVQV YTIAGQKKYL MIVEAIGANG RYFRSFTATD
     LGGSWTPQAA TESNPFAGKA NSGATWSNDI SHGDLIRSNA DQTFTIDPFN ANFHIAPLPS
     ATISPLPQST IALPLFAAIC EKTKFVFALQ TILLKPSSSV DKYIGDTETS HTSRCPIPKS
     GEVWDPVIGS GPFRPYMVPK GVLVADGVLV MMRLYYELPF NVSGITLADL QQIHGLDQKG
     RAQRLETKTQ RSHGSTVYDV NNNLMTIDGS TNETNFLKRG GVDNQLWFNR LFNGADNPSP
     GIGAAFAQKC LTDYGYDIHN DDLNSNVRYA DATKQERYKQ YYSTALARRN GPIERILPLT
     PKSVQNLKLR LNLKITENTK PKPGGAPAVL IQSNEDRQSE ESEEDMPIVR KRRRLIPGSE
     LSAKVNNSVA VALRGCIRDK NNKEGNEETV LGSTRVFARL STDKAINMPE LPEPVPINSI
     TPAPVETSAE RAIKVKKELA ARTKEVEEMK REPKEIEERA AAEKAAAEEA AIKKAAAEKA
     AAETAAVEKA AAKLTKENAE LDLKACLPCT ASVEAADKAL VEKLDEELAL YFLDALKIAA
     RKPQKRKFKK EETNDKRPEK VARK
//
DBGET integrated database retrieval system