ID A0A2I0SSH3_9ACTN Unreviewed; 630 AA.
AC A0A2I0SSH3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:PKT72865.1};
GN ORFNames=CW362_11235 {ECO:0000313|EMBL:PKT72865.1};
OS Streptomyces populi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT72865.1, ECO:0000313|Proteomes:UP000236178};
RN [1] {ECO:0000313|EMBL:PKT72865.1, ECO:0000313|Proteomes:UP000236178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A249 {ECO:0000313|EMBL:PKT72865.1,
RC ECO:0000313|Proteomes:UP000236178};
RA Wang Z.;
RT "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT isolated from stems of Populus adenopoda Maxim.";
RL Submitted (DEC-2017) 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:PKT72865.1}.
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DR EMBL; PJOS01000016; PKT72865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0SSH3; -.
DR OrthoDB; 9804807at2; -.
DR Proteomes; UP000236178; 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; 2.
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; 2.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000236178}.
FT DOMAIN 373..502
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 503..630
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 56..66
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 116..121
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 208..209
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 630 AA; 64161 MW; BB8C7427A11D4072 CRC64;
MRRSRSASSR LIPSPAAGPG SRLRHALLSV AAVLGLLVTV LVGMPGVARA AGSQPCDIYA
GAGTPCVAAH STTRALFSAY NGPLYQVTRV SDGASADIGL LTAGGYANAA QQDGFCANTT
CSISKVYDQT SRHNDLFPGP AGTAGMGADR GADAGELSVT AGGHKVYGIW ISPGVGYRSH
GAASGTAVNG QAEGAYMVAS GTHVGSACCF DYGNAEATPA DTGNGHMDAV SIATTCYFAP
CSGSGPWVEA DLENGMFQGD NGSNTANKGN NSTYVTAVLK NNGQTTYALK GGNSQSGSLT
TWWDGALPTR GGYRPMQQEG GIILGTGGDN SNWNMGTFFE GVMVIGYPTD AAENAVQANI
VSVGYSGQTN VPNGPQGTIG GPGGQCADVA ADDTGVNGAA VQLWNCQSYA EDQHWTHNAN
GSLGTIGRCL DIIGNGTANG TNVELWDCNG VGGQKWVQRA DGSLFNPQSG RCLDSPNGAT
ANGTRLRIWD CNGSAAQKFA VNAGAPVIGP GGACADVAGD DNGSNATAVQ LWSCQSYAVD
QHWFHSSDGR LHTLGRCLDI NGNGTAGGTQ VELWDCNGAG GQVWQQQADG SLLNPQSGRC
LDSPDGATAN GTRLRIWDCN GSAAQKFALG
//
