ID A0A0M2RX17_9ACTN Unreviewed; 373 AA.
AC A0A0M2RX17;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Chitin-binding protein {ECO:0000313|EMBL:KKJ99529.1};
GN ORFNames=LQ51_22930 {ECO:0000313|EMBL:KKJ99529.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ99529.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKJ99529.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKJ99529.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) 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:KKJ99529.1}.
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DR EMBL; JTGL01000179; KKJ99529.1; -; Genomic_DNA.
DR RefSeq; WP_046571001.1; NZ_KQ058892.1.
DR AlphaFoldDB; A0A0M2RX17; -.
DR STRING; 1538294.LQ51_22930; -.
DR PATRIC; fig|1538294.3.peg.5998; -.
DR HOGENOM; CLU_063855_0_0_11; -.
DR OrthoDB; 5179374at2; -.
DR Proteomes; UP000034330; Unassembled WGS sequence.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..373
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038727683"
FT DOMAIN 269..373
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 223..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 39034 MW; C64AAB06285DB2A0 CRC64;
MAALLTAVAT LALGVFALAS NPDPAAAHGA AMKPGSRTYL CWKDGLSPQG DIRPNNPACA
AAVAESGTNS LYNWFSVLRS DAGGRTVGFI PDGKLCSGGN PNFTGYDAAR TDWPLTHLTA
GRTMEFNYSN WAHHPGTFYF YVTKDSWSPT RPLAWSDLED QPFLTVTNPP QSGAVGTNDG
HYYFNGTLPS NKSGRHIIYS RWVRSDSQEN FFGCSDVTFD GGNGEVTGVG SGGTTPTTPG
TTPTTPGTTP TTPGTTPTTP GTSPSTPNTS PGTNSCMAVY KVVTAWGGGF QAEVTIMNHS
TRTYAGWTAT WSWANGQTIT QLWNGQLSAN GSAVTVNNAA YNGTISPEGS TTFGFTANVS
GTNSLPTVSC TGR
//