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Database: UniProt
Entry: A0A291QF93_9ACTN
LinkDB: A0A291QF93_9ACTN
Original site: A0A291QF93_9ACTN 
ID   A0A291QF93_9ACTN        Unreviewed;       512 AA.
AC   A0A291QF93;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Ricin B lectin domain-containing protein {ECO:0000259|SMART:SM00458};
GN   ORFNames=KY5_5169 {ECO:0000313|EMBL:ATL30187.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL30187.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL30187.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL30187.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP022685; ATL30187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291QF93; -.
DR   KEGG; sfk:KY5_5169; -.
DR   Proteomes; UP000221011; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   CDD; cd00161; RICIN; 1.
DR   CDD; cd01823; SEST_like; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR037460; SEST-like.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR37981; LIPASE 2; 1.
DR   PANTHER; PTHR37981:SF1; SGNH_HYDRO DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR637460-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..512
FT                   /note="Ricin B lectin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012810063"
FT   DOMAIN          387..511
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-1"
FT   ACT_SITE        343
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-1"
FT   DISULFID        108..131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
FT   DISULFID        188..199
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
SQ   SEQUENCE   512 AA;  54631 MW;  7FBA0C22F3FD6827 CRC64;
     MKRIRRSGRG RLRGSFAAAV AMAAVLGTAA AVPAQAADGG AAKAPASTPL PPELEKIRAD
     EATKLYGSPG ERPMADRKTG LISLGDSEIS GEGVGTYEPG TDGPDNWCHR SPDAAIHRTG
     IPADVTYNVA CSGAQTVNIK IGGQKQYADE LVQSDNLAIK ARNTKIKTIL LVIGANDDLN
     FSGVMTDCVT RFLLSQGACA GKYNDGWQAR VDGLVPKVEQ SIRDLKTVMK DAGYQAGDYK
     LVAMGYPSPI GPDFRDNPTF PGKLVCGGLG YDSDTEWGRN YAVPTFATGM RKAAKNAGAT
     YLDNSRLFQG HEVCMEDTWA RGLYIDVSNP FPPDSNSVRQ SFHPNARGHA AFASCLTQIY
     NSGYGEGSCA DPASTGSPKL YKGAWDDAYK PLKNEGTGTC VDVDASKSRN GTKVQGWDCT
     GNRNQTWWYD DTQKSLHTGL TQDRCVDVPE GSYKEGTAVT LWNCHGGDNQ KFVRQSGTVR
     PAAEGGLCLT LAGAKEPVRL QKCTGAANQR FA
//
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