ID N1Q1G5_DOTSN Unreviewed; 503 AA.
AC N1Q1G5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU367111};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU367111};
GN ORFNames=DOTSEDRAFT_161792 {ECO:0000313|EMBL:EME48329.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME48329.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME48329.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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:RU367111};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|RuleBase:RU367111}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367111}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family.
CC {ECO:0000256|ARBA:ARBA00006963, ECO:0000256|RuleBase:RU367111}.
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DR EMBL; KB446535; EME48329.1; -; Genomic_DNA.
DR AlphaFoldDB; N1Q1G5; -.
DR STRING; 675120.N1Q1G5; -.
DR EnsemblFungi; EME48329; EME48329; DOTSEDRAFT_161792.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR OMA; WNYPTRY; -.
DR OrthoDB; 2573673at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000016933; 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:0031222; P:arabinan catabolic process; 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-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367111};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|RuleBase:RU367111};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367111};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU367111};
KW Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW Secreted {ECO:0000256|RuleBase:RU367111};
KW Signal {ECO:0000256|RuleBase:RU367111};
KW Xylan degradation {ECO:0000256|RuleBase:RU367111}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT CHAIN 21..503
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT /id="PRO_5027145370"
FT DOMAIN 24..339
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 358..499
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT REGION 102..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 25..35
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 85..90
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 181..182
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 406..444
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 503 AA; 52119 MW; 394E86BD893219EA CRC64;
MPLRSSSLLA FSLATTGAIA ATGPCDIYAS GNTPCVAAHS TTRALYSSYN GALYQIKRGS
DGKTTDIAPL SAGGVANAAT QDSFCASTTC VVTVIYDQSG KKNHLSQAPP GGNGQGPQSG
GYDDPASAIG APVTLNGQRA YGIFISPGTG YRNDVTNGIS TGDVAEGMYA VFDGTHYNDG
CCFDYGNAET SNDDTGNGHM EALYFGTNTF WGTGSGNGPW VMADLENGLF SGENIKQNPA
DPTVTYRFLT ATLKGSADKW AIKGGNAASG GLSSYYNGPR PDASGYNPMS KEGAIVLGIG
GDNSLGAQGT FYEGVMTAGY PSDATESSVQ ANIVAAKYAV TSLMSGPAVK VGSTITIRAT
SPGSNTRYLA HKGSTINTQP ITSSSSSATQ ASAQWNVRTG LGNSDCVSFE SKDTPNSYIR
HNAFVLYLQP SDGSKQFNED ATFCPQTGLQ GSDTSSIRAW GYPTRLIRNY NDLGYIATNG
GPDAFDDASS YNYDVSFVVG SGF
//
