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
//