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Database: UniProt
Entry: C9SY61_VERA1
LinkDB: C9SY61_VERA1
Original site: C9SY61_VERA1 
ID   C9SY61_VERA1            Unreviewed;       505 AA.
AC   C9SY61;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE            EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN   ORFNames=VDBG_09836 {ECO:0000313|EMBL:EEY23726.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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.
CC       {ECO:0000256|ARBA:ARBA00037415}.
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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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DR   EMBL; DS985229; EEY23726.1; -; Genomic_DNA.
DR   RefSeq; XP_003000116.1; XM_003000070.1.
DR   AlphaFoldDB; C9SY61; -.
DR   STRING; 526221.C9SY61; -.
DR   GeneID; 9528948; -.
DR   KEGG; val:VDBG_09836; -.
DR   eggNOG; ENOG502QRW4; Eukaryota.
DR   HOGENOM; CLU_017810_1_0_1; -.
DR   OMA; GETSPKW; -.
DR   OrthoDB; 1574266at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
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; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43576:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   DOMAIN          309..497
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   505 AA;  57012 MW;  2ECABFD0198A33C2 CRC64;
     MTTFTKLTDE QQPVISVNPN HKIAKIEDNT YGGFTEHMGR CIYGGLYDPG SPLSDENGYR
     KDVIEAFQEL KCPVVRYPGG NFIATYHWQD GVGPREKRPK KQELAWHGIE TNEFGTDEFL
     RWCEVVGTEP YLALNFGTGT LDEAMGWLEY CNSTADSHYA NLRRQNGREE PYNVKYWALG
     NECWGPWQVE QMTKEDYAKK AWQWAKALKL LDPNVQLILC GMEGPTSWDA YVTKECINYT
     MHALGDNSAS CLIDMHSIHI YTASPEHLKN ATAPRSAERA IEITASLIDL ARIENKIPNN
     IPRQKICFDE WNVWDPVRAP GWLGAEEKYT LSDALAVAVW LNVFIRQAKY IGMATVAQSV
     NVISPLMTTK NGLLKQPTWW PLLLFSKHMR GQTIGVNVQC GEYEGQTKPE WIRGTIETPW
     LDVSASINDE GIVSLVVVNI HETKRFATKL EGVSGKIDVF TVAGPSIDAV NTEEKEEVGI
     AESSWDGQGL YEFPQASMTM LRWKP
//
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