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Database: UniProt
Entry: A0A0M9ZL50_9ACTN
LinkDB: A0A0M9ZL50_9ACTN
Original site: A0A0M9ZL50_9ACTN 
ID   A0A0M9ZL50_9ACTN        Unreviewed;       471 AA.
AC   A0A0M9ZL50;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:KOV62368.1};
GN   ORFNames=ADL01_29880 {ECO:0000313|EMBL:KOV62368.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV62368.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV62368.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV62368.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV62368.1}.
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DR   EMBL; LGDW01000446; KOV62368.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9ZL50; -.
DR   PATRIC; fig|1519490.3.peg.6509; -.
DR   Proteomes; UP000037738; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0031221; P:arabinan metabolic process; IEA:InterPro.
DR   GO; GO:0019566; P:arabinose metabolic process; IEA:InterPro.
DR   CDD; cd00161; RICIN; 1.
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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR   PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR   Pfam; PF09206; ArabFuran-catal; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..471
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005842970"
FT   DOMAIN          14..142
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          238..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        353
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT   ACT_SITE        428
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT   DISULFID        155..165
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT   DISULFID        215..220
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT   DISULFID        308..309
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ   SEQUENCE   471 AA;  48186 MW;  0C25A70FF47B7CF5 CRC64;
     MLLASAPTWS APASAAALVS SASGRCLDVK GNVDTSGTAL QIWDCNDQVN QAFEFTSAGE
     LRAMNGTRCV DAYDTRTAPG APVVIRPCDG RPTQVWRHTS DGPVTGTASG FCLDVNGAAT
     ANGTALILWT CNGQSNQKWT SPSSPPPVPG GSGPCGIYAA GGTPCVAAHS TVRALYGSYN
     GSLYQVRRAS DNTTRDIGLL APGGFVDAAA QDAFCAGTSC VITVVRDQSG HGNDLWYQGS
     AQVPGSNQSS PAKATSESLT AGGTKAYSLY INPGNSYWRD GHLTGVPTGA APEGAYMVTS
     GTHVNGGCCF DYGNSETTRK ADAAGAMDAI NFSTQCWFGG CSGRGPWVQA DLEWGLYSGG
     SQSWNPNQRA FTDKFVTAML KNNGTSRLAL KGGSAQSGNL TTLWDGGLPG GYSPMKKQGA
     IILGSGGDCC KPGGGANLSA GTFYEGAIVA GYPSDATDNA VQADITAAGY R
//
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