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Database: UniProt
Entry: A0A1H0WZ52_9PSEU
LinkDB: A0A1H0WZ52_9PSEU
Original site: A0A1H0WZ52_9PSEU 
ID   A0A1H0WZ52_9PSEU        Unreviewed;       367 AA.
AC   A0A1H0WZ52;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Chitin-binding protein {ECO:0000313|EMBL:SDP95998.1};
GN   ORFNames=SAMN05421507_12665 {ECO:0000313|EMBL:SDP95998.1};
OS   Lentzea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=641025 {ECO:0000313|EMBL:SDP95998.1, ECO:0000313|Proteomes:UP000199691};
RN   [1] {ECO:0000313|EMBL:SDP95998.1, ECO:0000313|Proteomes:UP000199691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6609 {ECO:0000313|EMBL:SDP95998.1,
RC   ECO:0000313|Proteomes:UP000199691};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNIX01000026; SDP95998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0WZ52; -.
DR   STRING; 641025.SAMN05421507_12665; -.
DR   Proteomes; UP000199691; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd21177; LPMO_AA10; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.70.50.50; chitin-binding protein cbp21; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004302; Cellulose/chitin-bd_N.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR34823:SF1; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34823; GLCNAC-BINDING PROTEIN A; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF03067; LPMO_10; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          266..367
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  38598 MW;  3AD371675DB9D5B0 CRC64;
     MLRFSADVPD RHHRAPGTPA RIGPARGKAA VWRAFAILGA CLTLLTTMLV TFGAGDASAH
     GAVSDPPSRH YGCYNRWPNG PSQQMATEDP MCYQAWQADP SAMYNWNGLF REGVAGNHQG
     AIPDGQLCSG GLTFNGRYAA MDKPGAWVAP NRPSRFTLNL NDTSSHGADY IRVYATKQGF
     NPKTQTLKWS DLELVGQTGR IPTGTRTPVE INAPGRTGHH VLYTVWQASH LDQSYYACSD
     VNFTDGGTTT TTTTTTTTTT TTTTTTGNPS AGCSATFQVI SQWSGGFQAE ARVTAGATAI
     SGWQVSWTFA NGERINSSWN ATLSTSGSTI TARNAAHNGA VGAGAATTFG LVASGTAGAP
     TLTCTAT
//
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