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Database: UniProt
Entry: E8LXN4_9VIBR
LinkDB: E8LXN4_9VIBR
Original site: E8LXN4_9VIBR 
ID   E8LXN4_9VIBR            Unreviewed;       655 AA.
AC   E8LXN4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Chitin-binding type-3 domain-containing protein {ECO:0000259|SMART:SM00495};
GN   ORFNames=VIBR0546_07232 {ECO:0000313|EMBL:EGA64645.1};
OS   Vibrio brasiliensis LMG 20546.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA64645.1, ECO:0000313|Proteomes:UP000004371};
RN   [1] {ECO:0000313|EMBL:EGA64645.1, ECO:0000313|Proteomes:UP000004371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA64645.1,
RC   ECO:0000313|Proteomes:UP000004371};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGA64645.1}.
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DR   EMBL; AEVS01000081; EGA64645.1; -; Genomic_DNA.
DR   RefSeq; WP_006880576.1; NZ_AEVS01000081.1.
DR   AlphaFoldDB; E8LXN4; -.
DR   STRING; 945543.VIBR0546_07232; -.
DR   eggNOG; COG3468; Bacteria.
DR   OrthoDB; 6018988at2; -.
DR   Proteomes; UP000004371; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   CDD; cd12214; ChiA1_BD; 1.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR22595:SF208; CHITINASE; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..655
FT                   /note="Chitin-binding type-3 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003224478"
FT   DOMAIN          601..651
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000259|SMART:SM00495"
SQ   SEQUENCE   655 AA;  71296 MW;  5005DA0B8800AB83 CRC64;
     MIKKRSVPLA VGVMATGLVP SIALAETYDI NLSQLQADEQ EIIAQAPEGL ALVQESIETL
     DNDVVEAITV NSPSNPENVK RVESIVSEQQ WEFLFPERHQ NYTYLNFLKG VGKYPAFCGT
     YSDGRDSDAI CRKSLATMFA HFTQETGGHN AYSENPQWRQ GLVYLREIGW DENTPGGYGI
     CDSGLWQGQA YPCGTFPDGS NKSYFGRGAK QLSYNYNYGP FSYSIYGNVE KLLNEPELVA
     DTWLNLASAV FFYLYPQPPK PSMLHVMDGT WQPNQEDLNN GLVPGFGVTT QIINGGVECG
     GSSEHQQSLN RIEYYREFAS YLGVDVPEDE VLGCASMKQF TESGAGALQV YWEQDWSWTP
     DTPSGEVYKC QLVAYQGPFS AFIDGDYVKC VDNKFDVNII DDSGPQPPVA DAGSDVTLYS
     DNSNVTLDGS GSQNGSSESV TYQWTQVSPS APTLTITNAD QASASVVVPP VDSDVRFEFS
     LTVTNSDGVS DSDTMAINAQ PMPGNFPPEV TLNAPESATA GGVAQLSVSI DDVDDSSFNI
     VWNSAESIQL VVADDNLSAS FTAPDVAEVT SATVSVEVTD SANNVVTESK TITLQPQGGA
     YPAWQLGHAY NEGDLVTEQG VNYECKKWPV TGWCGANEVY KPGEGLYWQE AWIQH
//
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