ID A0A0M2S302_9ACTN Unreviewed; 369 AA.
AC A0A0M2S302;
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=Cellulose-binding protein {ECO:0000313|EMBL:KKK07376.1};
GN ORFNames=LQ51_02940 {ECO:0000313|EMBL:KKK07376.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKK07376.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKK07376.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKK07376.1,
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:KKK07376.1}.
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DR EMBL; JTGL01000021; KKK07376.1; -; Genomic_DNA.
DR RefSeq; WP_046565743.1; NZ_KQ058814.1.
DR AlphaFoldDB; A0A0M2S302; -.
DR STRING; 1538294.LQ51_02940; -.
DR PATRIC; fig|1538294.3.peg.2849; -.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..369
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039625101"
FT DOMAIN 264..369
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 232..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 38734 MW; 30768EABBB237224 CRC64;
MSTPYRRRAL VAAALLSVGA VVAALLNLTL AGPASAHGSV VDPASRNYSC WQRWGSDFQN
PAMATQDPMC WQAWQADPNA MWNWNGLFRE GVAGNHQAAI PDGQLCSGGR TQSGRYNALD
TVGAWKTTSI SNNFRIKLFD QASHGADYIR VYVTKQGFNA LTSPLRWSDL ELVGQIGNTP
ASQWTQETSG VSIQVPANAP GRSGRHIVYT IWQASHLDQS YYLCSDVDFG GGSTTPPTTT
PPTSTPPTST PPTSTPPTST PPTTPNPAGG CTATYKITGQ WGGGFQADVQ VTNGGSPIRG
WSVSWTFPNG QQVTSAWNAT VSTSGTLVTA RNAAYNGSLG AGASTTFGFT GSWSGSNAVP
GNISCTTSA
//
