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Database: UniProt
Entry: A0A1E5L265_9ENTE
LinkDB: A0A1E5L265_9ENTE
Original site: A0A1E5L265_9ENTE 
ID   A0A1E5L265_9ENTE        Unreviewed;       838 AA.
AC   A0A1E5L265;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OEH84131.1};
GN   ORFNames=BCR26_00635 {ECO:0000313|EMBL:OEH84131.1};
OS   Enterococcus rivorum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=762845 {ECO:0000313|EMBL:OEH84131.1, ECO:0000313|Proteomes:UP000095256};
RN   [1] {ECO:0000313|EMBL:OEH84131.1, ECO:0000313|Proteomes:UP000095256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25899 {ECO:0000313|EMBL:OEH84131.1,
RC   ECO:0000313|Proteomes:UP000095256};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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:OEH84131.1}.
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DR   EMBL; MIEK01000001; OEH84131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5L265; -.
DR   STRING; 762845.BCR26_00635; -.
DR   Proteomes; UP000095256; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   CDD; cd20174; GH18_LinChi78-like_UFR; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR032179; Cry22Aa_Ig-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF16403; Bact_surface_Ig-like; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095256};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..838
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009180739"
FT   DOMAIN          40..458
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          697..785
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          179..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  91093 MW;  73EEAB5D172A57FF CRC64;
     MATIIASSTL AMGAVGMFAS LPTKAFAEET IKNKAEQVPY RNVMYYGDWS IWGGQDNFYP
     KNFDASLYTH LNYAFIAMDA NGELILTDKD AAFGAPVGNA DVGWDNALSG LIPAFTAIKS
     KNKNLKIGIS LGGWSKSANF SLIAANPEKR KNYINNILKF IKYTGMDFVD VDWEYPNSQR
     EPDKVDNKND DGTPHAGPAD KQNFITLMRE LRAGLDKQGS ELSKRYELTC ALPGTPAQLE
     QGIDVEELFK IIDFGNMMTY DMNGAWSEKS SHQTALYANP KAPNNYSVET VINYLQSKNV
     PSNKIVIGAA MYSRGWNTVE KGNNPEQPGL FQDAAITNKD ADLTPSRGAN NELPLANGDG
     GRAGGVWSYR KIDELKKKVP DLKEYWDDAA KAPYLYSEST KQFFTFDNVK SIQYKTAFVK
     EKQLGGVISW MASQDKDGTG SGKRNELSSA IKQGLYGDQK IPEVVTLDKS QLKIDVKTNV
     VKTDSGKDGY GISIANQESL LSGNVALGAA SKFYFTVKKP TFVITMKDGS TLEKGDYKSG
     EVTEKDGKTY VNIATQYDGR YIAPGASAEF KLATKGGAEV NISNIKKIEL LQYFDNDTLL
     ASQTIFGDDT PGVSVPTISG VQDVTIKLGD TFDPKAGVKA VDKTDGDLTN KITIAGSVDT
     NKVGTYPLTY SVKNSSNQEN VATRKVFVVE SESKPSTPQN VNIANVTKDS ATISWDASQS
     ASGIKEYQLK ISGGGQTIDF VTSKTNQLVT GLRANTAYTI EVTAVSVLGQ VSDIAKGSFN
     TQKEEASGSQ EWSATKVYNG GEIVTYKGAQ YKAKWWTQGN VPDDAASTES GSNPWQKL
//
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