GenomeNet

Database: UniProt
Entry: E4ZNM6_LEPMJ
LinkDB: E4ZNM6_LEPMJ
Original site: E4ZNM6_LEPMJ 
ID   E4ZNM6_LEPMJ            Unreviewed;       658 AA.
AC   E4ZNM6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Endo-1,5-alpha-L-arabinanase A {ECO:0000256|ARBA:ARBA00042202};
GN   ORFNames=LEMA_P041460.1 {ECO:0000313|EMBL:CBX93245.1};
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|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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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; FP929105; CBX93245.1; -; Genomic_DNA.
DR   RefSeq; XP_003836610.1; XM_003836562.1.
DR   AlphaFoldDB; E4ZNM6; -.
DR   STRING; 985895.E4ZNM6; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   EnsemblFungi; CBX93245; CBX93245; LEMA_P041460.1.
DR   GeneID; 13287497; -.
DR   eggNOG; ENOG502SM7B; Eukaryota.
DR   HOGENOM; CLU_010779_2_0_1; -.
DR   InParanoid; E4ZNM6; -.
DR   OMA; MWSEDDT; -.
DR   OrthoDB; 2719402at2759; -.
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; cd08983; GH43_Bt3655-like; 1.
DR   CDD; cd18828; GH43_BT3675-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 3.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CBX93245.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..658
FT                   /note="Endo-1,5-alpha-L-arabinanase A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003194798"
FT   REGION          334..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        366
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        538
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            489
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   658 AA;  72218 MW;  0F8A7ABD70262D24 CRC64;
     MFFTSIFSLL TLGAVSSVSA QAAVNEGYVF AYFTNNSRAG EKIYLAASNG NNALDWTELN
     NGQPILTSTK GTTGLRDPFL IRSNDGSKFF LIATDLSIGS GTSWGAAVRT GSRYLEVWES
     PDLRTWSEQR HILVSPPEAG NTWAPEAYFD TDLNEYVVFW ASSLYAANDP NHTGSTYHRM
     LYATTKDFVT FSPTKIWQDA GTSRIDSTVL KAGDVFYRFT KDEGGVTGCA DIIQESSTSL
     LAPLDGWTIG ASCIGRNAGL GAVEGPTAFK SNPGDVHGEK YYLFVDEYSG RGYVPLETAD
     MSRPEWKVSP NYKLPASPRH GTVVPVTAAE LAGVTGRSTT NSRRKKSELA TRQASGNPVL
     PDFYADPNAI IFDDTYYIYA TTDGFPGWGG KVFYTWQSKD LVNWSRAETP FLTLNGTNGN
     VPWATGNAWA PTIIEREGTY SFYFSGHNPE FNRKTIGVAT ASSPEGPFTA QPTPMITNNE
     AIKTGQAIDP HAFFDPATGK YWLSWGNGTP LMAELNDDMI SIKQETLHKV EGLVNFREGS
     FLNYRKGLYH FTYSIDDTGV SGYRVGYATS EDIMGPWTYH GLILEKDESQ GILATGHSSI
     INVPNTDEWY IVYHRFAIPG GDGTHRVTCI DKLTIDEETG LMQPVKPTLT GVDPRPLQ
//
DBGET integrated database retrieval system