ID A0A2S4YPK6_9ACTN Unreviewed; 485 AA.
AC A0A2S4YPK6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:POX50671.1};
GN ORFNames=C3488_14080 {ECO:0000313|EMBL:POX50671.1};
OS Streptomyces sp. Ru72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080747 {ECO:0000313|EMBL:POX50671.1, ECO:0000313|Proteomes:UP000237426};
RN [1] {ECO:0000313|EMBL:POX50671.1, ECO:0000313|Proteomes:UP000237426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru72 {ECO:0000313|EMBL:POX50671.1,
RC ECO:0000313|Proteomes:UP000237426};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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:POX50671.1}.
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DR EMBL; PQSR01000023; POX50671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4YPK6; -.
DR OrthoDB; 9804807at2; -.
DR Proteomes; UP000237426; 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; PF14200; RicinB_lectin_2; 2.
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:UP000237426};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..485
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015733461"
FT DOMAIN 29..338
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 342..425
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT DOMAIN 431..483
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT ACT_SITE 225
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 301
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 30..40
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 90..95
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 180..181
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 485 AA; 49430 MW; 233D940F7C9479C0 CRC64;
MGAVLALVAG ILGGVIATTG TAQAASSLPC DIYAAAGTPC VAAHSTTRAL YASYSGALYQ
VKRLSDNTTL NIGTLSAGGY ANAAAQDSFC SGTECIITEI FDQSGKGNHL TIEGPGGNGG
QDVGAIANAL PVTAGGQHVY GVSIQAGVGY RDNSTNGVAT GSQPEGTYMV TSGHHVDGNC
CFDYGNAETS STDTGNGHMD AVNFGTECWF SPCSGSGPWV MADLENGLFA GGNGTNSNNT
GNSSTFVTAL MKNNGTTTYA IKDGNAQSGA LKTDYNGSLP TTAGYMPMHK EGAIVLGTGG
DDSNWSDGSF FEGVMTAGYP TDAADNAVQA NVVSVGYTQA AQTFPVTGTA YRLTNPNSGK
VLDAVNCGTA NGTSIDIWSS LGNTCQQWKF ASAGNGHYTI TNVNSGTVLD DKNCGINNGT
AVQLWSSLGN TCQEWDVTPA GSHYTITNVN SGMTLDVANC GTGNGTAVRQ WAQLDNACQQ
WDIAP
//
