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Database: UniProt
Entry: A0A1B1MPN6_STRLN
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ID   A0A1B1MPN6_STRLN        Unreviewed;      1183 AA.
AC   A0A1B1MPN6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Putative secreted glycosyl hydrolase {ECO:0000313|EMBL:ANS70565.1};
GN   ORFNames=SLINC_8341 {ECO:0000313|EMBL:ANS70565.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS70565.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS70565.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS70565.1,
RC   ECO:0000313|Proteomes:UP000092598};
RA   Meng S.C.;
RT   "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT   actinobacteria.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP016438; ANS70565.1; -; Genomic_DNA.
DR   RefSeq; WP_067444125.1; NZ_CP016438.1.
DR   AlphaFoldDB; A0A1B1MPN6; -.
DR   STRING; 1915.SLINC_8341; -.
DR   KEGG; sls:SLINC_8341; -.
DR   PATRIC; fig|1915.4.peg.9188; -.
DR   Proteomes; UP000092598; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd00146; PKD; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 3.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012938; Glc/Sorbosone_DH.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR029010; ThuA-like.
DR   PANTHER; PTHR40469:SF2; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF07995; GSDH; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 2.
DR   Pfam; PF06283; ThuA; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00089; PKD; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ANS70565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1183
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008527354"
FT   DOMAIN          707..789
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          902..1027
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   REGION          725..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1183 AA;  125585 MW;  50058B4622F820FB CRC64;
     MRRIILIFGA IASVLLSLVI AQPASAAPAF RALVFTKTAG YRHDSIPAGL SMFREQAAAS
     NFELVHSEDS SVFTPANLAT FDVLIMFQTS GMVWTTAAQR QAVEGYLASG KGIVAIHNAT
     DMGIENEYPW WDQTINGGAH MPEHSPGVLS GTAVVADKKH PSTAGLPDRW NRSEEWYNFD
     RNPRGDVHVL VTADERTYNP GPRAMGPDHP ISWCRNTGGG RVWATGMGHT SAAYSETHFR
     NHVLGGVKWA AGNEPGDCGG TVWSNFEKRT LDDNTADPMA LAVAPDGRVL YVQRGGQLKI
     FKPTTNRTVT AATLSVYTGG EDGLTGLALD PDFADNGYVY LYHSPAGVPN DINRVSRFTL
     TGDTLNMSSQ VTIIDIPATR DRTFAEPGHT GGYIEFGPDK NLYIGTGDDV PPNLDSNWQG
     YAPLDWRQGK ANLDAARTAG NTNDLRGKLL RIRPSADGGY TVPAGNLYPQ GTAQTRPEIY
     AMGFRNPFRF SIDPANGWVY LADYGPDRNP PTTNRGPEGL VELNVIKAPG NYGWPFCHGD
     NQAYAPYNPS TGVVGAKFNC NAPVNNSPNN TGLTSLKPIV APNMWYGYGV SPNFPELGSG
     GSGPMGGPVY RYDATNPSGT KFPPYYDGVH FFYEWSRHTV KEVHFDSATA VTRTNPFMPG
     AKFLKPMDME FGPDGSLYLL EWGNNFSGGN NDSGLYRIDY NHGGRSPIAK ATGTPTNGDA
     PLNVQFSSAG STDPDPGSTL SHHWTFGDGT TSTAANPSHT YTANGNYTAQ LKVTDNTGKT
     AFANVPITVG NTAPTVTLTI PSNGGMLDFG DRVPYKVSVS DPGGAPIDCA KVLVNPALGH
     DDHQHETTDH PGCSGTIDTT LLGGHPDGAN LYYVLNARYT DDGGPGGANP LTGYAQAILQ
     PKHKQAEFYT DQSGVQIVEQ AGAESGKRVG NISDNDWIAF NPMSLSGITS VKYRLSSPSG
     GGSIELRADS PTGTLLATTP VPSTGGWNNY QSTPAVNTAD LAGSHRLYLV FKGTSNNWFD
     LDSLTFGGNG VGEPGSGGGG VAGRTWTVAA QHSGKFMDVN GASTADGAQV VQWPATGADN
     QKWQAVDAGG GAVHLKAVHS DKCLAVTGGS TAQGAFLQQS TCDNGNPQKF LVTPTTTVGV
     YTVKSLPSGL CVDVNGGSTA DGARLLQWSC HSGTNQQWRF TAV
//
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