ID A0A1R1SFD3_9ACTN Unreviewed; 456 AA.
AC A0A1R1SFD3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:OMI36898.1};
GN ORFNames=SPAR_24326 {ECO:0000313|EMBL:OMI36898.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI36898.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI36898.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI36898.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) 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:OMI36898.1}.
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DR EMBL; ASQP01000321; OMI36898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1SFD3; -.
DR Proteomes; UP000186168; 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; -; 2.
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:UP000186168}.
FT DOMAIN 2..130
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 413
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 140..150
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 200..205
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 293..294
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 456 AA; 46651 MW; 2F0931ABC1B9DD9C CRC64;
MSAAPLLSSA SGRCLDVKGN VDTPGTTLDI WDCNGQVNQA FEFTSAGELR ALNGTRCVDA
YDDRTAPGAP VVIRSCDGRA TQVWRQNSDG SVTGVRSGFC LDVNGAGTAN GTAVILWTCN
DQSNQKWSSP TAPPSGSGPC DIYAAGGTPC VAAHSTVRAL HGSYNGSLYQ VRRASDNATR
DIGVSAPGGF VDAAAQDSFC AGTSCVITVV RDQSGHGNDL WYQGSAQVPG SSQSSPAKAT
SESLTAGGTK AYSLYINPGN SYWRDGHLTG VPTGAAPEGA YMVTSGTHVN NGCCFDYGNS
ETSRKADAAG AMDAINFGTE CWFGGCAGSG PWVQADLEWG LYSGGSQSWN PNQRAFPSKF
VTAMLKNNGT SRFALKGGNA QSGGLTTLWD GGLPGGYSPM KKQGAIVLGS GGDCCKPGGG
ANLSAGTFYE GAIVAGYPSD ATDNAVQANV IAAGYR
//
