ID   ABFC_ASPFN              Reviewed;         504 AA.
AC   B8NIX4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Probable alpha-L-arabinofuranosidase C;
DE            Short=ABF C;
DE            Short=Arabinosidase C;
DE            EC=3.2.1.55;
DE   Flags: Precursor;
GN   Name=abfC; ORFNames=AFLA_070020;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of
CC       arabinoxylan, a major component of plant hemicellulose. Acts only on
CC       small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By
CC       similarity). {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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; EQ963479; EED50180.1; -; Genomic_DNA.
DR   RefSeq; XP_002380561.1; XM_002380520.1.
DR   AlphaFoldDB; B8NIX4; -.
DR   SMR; B8NIX4; -.
DR   STRING; 5059.CADAFLAP00008426; -.
DR   EnsemblFungi; EED50180; EED50180; AFLA_070020.
DR   VEuPathDB; FungiDB:AFLA_070020; -.
DR   eggNOG; ENOG502QRW4; Eukaryota.
DR   HOGENOM; CLU_017810_1_0_1; -.
DR   OMA; SKYMRGW; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..504
FT                   /note="Probable alpha-L-arabinofuranosidase C"
FT                   /id="PRO_0000394612"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   504 AA;  56118 MW;  096372DC005819B6 CRC64;
     MTTFTKLSDQ DTPSIAIHPS RRISKINPNI YAGFTEHMGR CIYGGIYDPG NPLSDENGFR
     KDVLEALKTL DIPVVRYPGG NFMATYHWID GVGPKDQRPA RPELAWLGTE TNQFGTDEFL
     KWCEVLGTEP YFCLNFGTGT LDEALAWVEY CNGTGNTYYA NLRRKNGREE PYNVKYWALG
     NETWGPWQVE QMTKEAYSHK AYQWAKALKL LDPSLVLILC GQDGTASWDY YTLKHCLLPV
     NSPLSTSAVP LIDMHSIHLY TSSSSHLPNA TAPLAAERAI EITSSLIDLA RIENGVPPEQ
     ARPTICFDEW NVWDPIRAEG SKGAEECYTL SDALAVAVWL NVFVRKSKDL GMACIAQTVN
     VISPLMTTKE GITKQTTWWP LYLFSKYMRG WTISAHLASA TYEGETSPKW IRGVKETPWL
     DVSAVLGEDG YVNVAVVNIH EEKAIETTID GASGEVTVFT VTGDSVAATN MKGKEEVAVV
     ESTWDGQGPY AFPKHSLTLL RWKA