ID E5AFF9_LEPMJ Unreviewed; 366 AA.
AC E5AFF9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Similar to alpha-N-arabinofuranosidase {ECO:0000313|EMBL:CBY01948.1};
GN ORFNames=LEMA_P007350.1 {ECO:0000313|EMBL:CBY01948.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY01948.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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; FP929139; CBY01948.1; -; Genomic_DNA.
DR RefSeq; XP_003845427.1; XM_003845379.1.
DR AlphaFoldDB; E5AFF9; -.
DR STRING; 985895.E5AFF9; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR EnsemblFungi; CBY01948; CBY01948; LEMA_P007350.1.
DR GeneID; 13286376; -.
DR eggNOG; ENOG502R8XS; Eukaryota.
DR HOGENOM; CLU_009397_3_0_1; -.
DR InParanoid; E5AFF9; -.
DR OMA; IDIWAPE; -.
DR OrthoDB; 1588416at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..366
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003193760"
FT REGION 223..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 167
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 366 AA; 41847 MW; 570C155A0C24D24F CRC64;
MLKLLLLAAF AAIGICQGYA PPSNTTAPAT FTNPIVDAGA DPWMFRYEDY YYLTYTNNQD
ITLFRSKSLT DWTDADSKLV FSPPPGMNYS TDLWAPEIHN IDGKWYVIFT ADPRNDSPPP
EIEMWCEYNC PAVHHRVFVV EGTGSDPWTA TYQYKSELDT YNQFAIDGTY FQHNDQLYHI
YSCWRRQYDG WPANLCITKM ANPYTVSSPF SERQIISTPE YDWEKTPFGR TSNDRLSSNE
GPQQLTNPTT GQQFLIYSAA RSDNRNYCLA QLELVGDDPM NPGNWRKHPF PIFYQNPSES
AYGVGHASFT TSPDGSENWI VYHGMRDPTN GWSARSIRAQ KFEWNDDGSP KFPRPGYGPY
ETPKGQ
//