ID A0A0T1QIF1_9ACTN Unreviewed; 514 AA.
AC A0A0T1QIF1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Sugar hydrolase {ECO:0000313|EMBL:KQX17176.1};
GN ORFNames=ASC82_02875 {ECO:0000313|EMBL:KQX17176.1};
OS Streptomyces sp. Root431.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736535 {ECO:0000313|EMBL:KQX17176.1, ECO:0000313|Proteomes:UP000051818};
RN [1] {ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|Proteomes:UP000051818};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX17176.1, ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|EMBL:KQX17176.1,
RC ECO:0000313|Proteomes:UP000051818};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX17176.1}.
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DR EMBL; LMEI01000001; KQX17176.1; -; Genomic_DNA.
DR RefSeq; WP_056640911.1; NZ_LMEI01000001.1.
DR AlphaFoldDB; A0A0T1QIF1; -.
DR OrthoDB; 99456at2; -.
DR Proteomes; UP000051818; 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; cd06543; GH18_PF-ChiA-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KQX17176.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006658797"
FT DOMAIN 35..145
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 220..514
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 145..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 51902 MW; AE2132F1DB118D8A CRC64;
MGTSSHRRRA STRTKAVGAV VAAAIAGGTA FALSGTAQAA GVGAAYTRTS AWTGGYTGQY
VVTNGSSTTQ TDWTLEFDLP AGTTIGSLWN GEYTVSGGHV TVRPASWNKQ LAPGQSVTVG
FVTSAAGAAG DPADCLINKA ACSAGGPAPT PSGRPTEQPT ATASPSATAK PTPTSTATAT
ATVKPTPTAT ATATVKPTPT ATATTPTPTP TATGAPSTAA KYAPYVDTSL YPAYDLLATA
DATGVKEFNL AFITSGGSCA PLWGGVTDLA NDKVAAQIGA LRAKGGDVRV SFGGAAGHEL
ALNCSSSSAL AAAYGKVIDQ YKLTKVDFDV EGAALPDTAA NTRRSQAIAQ LQKTHPGLDV
SFTLPVMPEG LTQPGVALLA DAKKNGVRVD AVNIMAMDYG PAYSADMGTY AIQAATATQA
QVKGVLGLSD AAAWKAVAVT PMIGVNDVTS EIFRVDDATQ LVDFAKSKGL GWLSMWSSTR
DKQCAAGAVN HADATCSSIL QQPLAFTKAF AAYK
//
