ID A0A0F4GJZ1_9PEZI Unreviewed; 689 AA.
AC A0A0F4GJZ1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 22-FEB-2023, entry version 21.
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=TI39_contig466g00002 {ECO:0000313|EMBL:KJX97744.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97744.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX97744.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97744.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KJX97744.1}.
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; LAFY01000458; KJX97744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GJZ1; -.
DR STRING; 1047168.A0A0F4GJZ1; -.
DR OrthoDB; 1097767at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000033647; 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; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..689
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002468957"
FT DOMAIN 496..668
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
FT REGION 101..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 75227 MW; 884D90955A6B00F2 CRC64;
MVQLKLSIFA LASSLASTFA VDIVVSSAPG NQTGSQGHPY GYGFLHEDIN NSDDGGIYAE
LIRNRAFQSS LRYPVSLDGY TALNGAHLSI QNLTDPLSDA LPSSMRVSTS NSTSAPGYGP
KGRPGRPGRH DHHGGQMIGF QNDGYWGMDV KCQPYTGSFW VRGEYHGKFV ASLQSNLTDE
VFGSVDIASK AVSGDWVEHE FVLVPGKDAP STNNTFAVTF DPKGTKDGFL DFNLISLFPP
TYKGRKNGLR IDLAEALEEI NPTYFRFPGG NMLEGNTNET YWDWKDSLGP LRNRPGFEGV
WGYQQTHGLG LMEYLYWAED MKMNSILGVW AGLALNGDIT PEADLQYYID DALNQIEFIR
GPASSPWGSK RAALGHPEPF VLQYVEIGNE DWLAGFPSGW NSYRAYRFPL FYAAITAAYP
DIQVIASSAT SDPEEGEPLT YPKGAIGDYH PYREPDELVD EFSRFDNDIG HIVGEVAAIH
PNGGTAWDGE LQPLPWWQGT VGEAVSMIGY ERNSDRIPGT FYAPVMRNTN RWQWAVTMLQ
NDAGSVTRST SWYVWSLFAH HPISETSAVQ GDFGPVYFGA GVDEARGGAR VWKGAMYNTT
DGVDVEVRVK FEGLEGATKA ALTVLTNLGE NGYAANDPAT GVNVVGVNTT VLTADGEGTF
VFELPELSVA VLDTDVEAKT IGRYPGDGK
//
