ID R1EGF8_BOTPV Unreviewed; 636 AA.
AC R1EGF8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=UCRNP2_6392 {ECO:0000313|EMBL:EOD46868.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD46868.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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; KB916378; EOD46868.1; -; Genomic_DNA.
DR RefSeq; XP_007585657.1; XM_007585595.1.
DR AlphaFoldDB; R1EGF8; -.
DR STRING; 1287680.R1EGF8; -.
DR KEGG; npa:UCRNP2_6392; -.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR HOGENOM; CLU_010060_1_1_1; -.
DR OMA; PYFIGEY; -.
DR OrthoDB; 1097767at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000013521; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..636
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004358943"
FT DOMAIN 449..629
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 636 AA; 67626 MW; D59ECD58B588F6C0 CRC64;
MYQLRSAVTR LAAVAALATR VAGINLTVST SGGNATSPLM YGFMFEDINY SGDGGIHGQL
LRNNGFQGDD QTTTAYGTVG DVDLTVDSDN PLSSAIPYSL AVAVPDGTTG DVGFSNEGYW
GILVNADQYS TSFWVKGDYS GNVTIKLVGN YSGTEYASTT LDVSSNSSAY GYYETSFESE
QAPDGNNLWT LTFDGESTAG STLYFDLITL YPTTFKSRAN GLKPAVANVL DDVGASFLRF
PGGNNLEGYS LDNRWKWNET IGPLQDRPGR QGTWGYPNTD ALGLIEYLDW CTDMGLAPIL
GVWDGFALES GEGTPITGDA LTPYIDDVLN ELEFILGDSS TTYGSLRASL GYSDPFTLTH
VEIGNEDYLG GGCDTYPERF TAFYDAIHAA YPDITIIASA AEALAPTCLP SPLPAGVMQD
YHTYASETDL VANFSQWDHQ NRSLPIFVGE FSCYSNAAGD RNVLPFMACS VAEAVYMLGF
ERNADAVLMS TYAPLLQLFN ATQWTPDLVG YTQAPGGVVR STSYFVQQMF AQNWGSSTRA
VDSDAAFGPV YWAASGEDGG ATYLKVANYG ADEQSVSVSV EGAAGATLTT LAGAQTAENS
EEAGEVVVPV TSTPDGSNGT FAFTLPAWSV AVLATS
//
