ID A0A372G449_9ACTN Unreviewed; 362 AA.
AC A0A372G449;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Cellulose-binding protein {ECO:0000313|EMBL:RFS47684.1};
GN ORFNames=D0Q02_03790 {ECO:0000313|EMBL:RFS47684.1};
OS Micromonospora craniellae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS47684.1, ECO:0000313|Proteomes:UP000262621};
RN [1] {ECO:0000313|EMBL:RFS47684.1, ECO:0000313|Proteomes:UP000262621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63014 {ECO:0000313|EMBL:RFS47684.1,
RC ECO:0000313|Proteomes:UP000262621};
RA Li L., Lin H.W.;
RT "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT South China Sea.";
RL Submitted (AUG-2018) 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:RFS47684.1}.
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DR EMBL; QVFU01000002; RFS47684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372G449; -.
DR OrthoDB; 5179374at2; -.
DR Proteomes; UP000262621; 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 Reference proteome {ECO:0000313|Proteomes:UP000262621};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..362
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016894281"
FT DOMAIN 259..361
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 230..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 38008 MW; D7EC9035D26BE1AA CRC64;
MSKLLRNSRA LSLLGVTAGA MLLLSTALVA PASGHGSVAN PVSRNYGCWQ RWGSDFQNPR
MATEDPMCWQ AWQANPNAMW NWNGLLRDGV GGNHQGTIPD GQLCSGGRTE SGRYNALDAV
GAWRTTSVAN SFRLKFYDQA SHGADYIRVY ATRPGYDALT KPLAWSDLEL VGQIGNTPAS
RWQPETGGVS TEIPVNAPGR SGRHVLFTVW QASHTDQAYY ICSDVQFGGG SNPPPTTPPA
SPTPTPTFDP PTTPPPTTAP PATGACSATY RVTSTWSGGF QGEVQVTAGS AAIRSWRVTW
TYASGQQVSQ AWNATVSSSG STVTAQNVSY NGGLGAGTST TFGFLASGSG SSAPTLTCTA
TT
//
