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Database: UniProt
Entry: C9Z0D2_STRSW
LinkDB: C9Z0D2_STRSW
Original site: C9Z0D2_STRSW 
ID   C9Z0D2_STRSW            Unreviewed;       616 AA.
AC   C9Z0D2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Putative hydrolase {ECO:0000313|EMBL:CBG68065.1};
GN   OrderedLocusNames=SCAB_8831 {ECO:0000313|EMBL:CBG68065.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68065.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG68065.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG68065.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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DR   EMBL; FN554889; CBG68065.1; -; Genomic_DNA.
DR   RefSeq; WP_012998797.1; NC_013929.1.
DR   AlphaFoldDB; C9Z0D2; -.
DR   STRING; 680198.SCAB_8831; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   GeneID; 24308107; -.
DR   KEGG; scb:SCAB_8831; -.
DR   eggNOG; COG1595; Bacteria.
DR   HOGENOM; CLU_018974_0_0_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CBG68065.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          384..515
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  64615 MW;  9B0886FEA6CC0E39 CRC64;
     MHTPHPPRPA YAPAPGPVPG ESDETLASRL RGWPDGGTGD PVALLMARHW QPTYDYAAIC
     LATQSGVASM VTATAFHRVL DGLMRGESGV ALRPRLLVAA RDTVKEWSAE EGVSQVLSDL
     RKPAGGRGMR AAKSMTPENR KLVERSFQAL PAVAQCLLWH TEVEAETITI PTGLLGLDAD
     NAVATLEQAR DKFREGCVRA HRELAPSKDC RFYNRLLDVP IRRGGALLPD VQQHLLECRY
     CRYAAEQLSH FEGGLGGVIA EAVLGWGARR YLDSRPGRMP EKGASRRPGS GGRHRLLSQI
     PAQRRKLTSG ARSPRALLTV GVSSGALLAA VLGAAFLSDD GGAADPAAST SATGGVATAP
     DTGNETTTDT GSPTPPASDG RPTGPVQTRL RNQAADLCLD VKGGKAQKGA ATELAACDTG
     WTQKWSYEED GLLRSVANPE LCLDSQVDAG VVVLGKCADE DSARGDDVRY DFTVQGELLP
     RWGEGLAVAP IGSEPKADIV IKVRDHSGRQ HWLTDGVTAS PDSLSVSGSE APTPETEPVT
     RRPEARTSPS PGPGDSGSPE AGAPPGAEAE QNGSIRSVAD GTTTENDPGT EPGPGTGPVR
     PLTTVDIPHL LSGLGL
//
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