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Database: UniProt
Entry: A0A0P8BHX1_9CYAN
LinkDB: A0A0P8BHX1_9CYAN
Original site: A0A0P8BHX1_9CYAN 
ID   A0A0P8BHX1_9CYAN        Unreviewed;       488 AA.
AC   A0A0P8BHX1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Family M23 lectin-binding peptidase {ECO:0000313|EMBL:KPQ33311.1};
GN   ORFNames=HLUCCA11_18940 {ECO:0000313|EMBL:KPQ33311.1};
OS   Phormidesmis priestleyi Ana.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ33311.1, ECO:0000313|Proteomes:UP000050465};
RN   [1] {ECO:0000313|EMBL:KPQ33311.1, ECO:0000313|Proteomes:UP000050465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ana {ECO:0000313|EMBL:KPQ33311.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-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:KPQ33311.1}.
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DR   EMBL; LJZR01000034; KPQ33311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8BHX1; -.
DR   STRING; 1666911.HLUCCA11_18940; -.
DR   Proteomes; UP000050465; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd12797; M23_peptidase; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 1.
DR   SMART; SM00458; RICIN; 2.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Lectin {ECO:0000313|EMBL:KPQ33311.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..488
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006148455"
FT   DOMAIN          34..172
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   DOMAIN          184..315
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   488 AA;  53657 MW;  BDEBD68DB8A4DA59 CRC64;
     MKTIKPNFLS RKTLSLLCFM SASLTMTAFA GSAKALETLT LDSGYALGPD PSLPAIHGQP
     RSTIHRGDVY NSNQQLEVVP KDRGTVMIKH RSTNKCLNAY RPGIETLLNF WPCSDSDGDQ
     RFHLEMDNQG RGIIRREGTN LCVDAPHRST GQSLLQLHVC NSNNANHLWK RNPIFNGPAT
     NLPSTVMLTS WANNLALDSG GANNTDIYGH PNPTTANPWH QWELHRAGNY YLLKNKATGK
     ALDAGGDGGR TVYPHPQPNI HNDFHLWRIE SVGSNRYMII SKATGRALDS GGSNNDIYAH
     PTPMGHNPYH QWKMTSLGGS TTTQGQAFNQ REYLNQLYIN GQGAWSRGPH NHTNAIDTYA
     TGSTQVKALV GGEVLSVRQG TQLSRVSHTS NSGYHPSRGW VKASDYNAEV IIYNPDLNRT
     FTYLHFSSIN VRPGQRVNSG DVIGIEGATG WSDGRHTHLH VQVGRGTSGS RENPLVTLGN
     ARARNIIR
//
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