ID A0A0N0T8N5_9NOCA Unreviewed; 655 AA.
AC A0A0N0T8N5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KOV83228.1};
GN ORFNames=ADL03_21845 {ECO:0000313|EMBL:KOV83228.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV83228.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:KOV83228.1}.
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DR EMBL; LGDY01000102; KOV83228.1; -; Genomic_DNA.
DR RefSeq; WP_053735365.1; NZ_LGDY01000102.1.
DR AlphaFoldDB; A0A0N0T8N5; -.
DR STRING; 1519492.ADL03_21845; -.
DR PATRIC; fig|1519492.3.peg.4692; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000037746; 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; cd09001; GH43_FsAxh1-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KOV83228.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037746};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..655
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005859272"
FT DOMAIN 25..134
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 70955 MW; 69A35BFE6A43E6FD CRC64;
MRRAPLAAGL AALTLVAAGL AATTAAHAAP GCSVTYTKTS EWQGGFGASV SITNTGDALN
GWTLEWTYAS GQQVGQHWNA TITQSGDQVS ARNVSYNGSV PTGGKVEFGF NATVTSTNPD
PVSFRLNGTT CDDTGTPTTT TTTTTTTTTT TTSTPRPSSF TNPVLWQDFA DIDIIRVDDA
YYYSASTMHY SPGAPVLRSY DLVNWEFAGH SVPRLDFGSK YDLNGGRGYV RGIWASFLQH
RKSNKTFYWG GCVDFAQTHI YTATAVDGQW SKHATIPKCY YDAGMLVDDN DTMYVAYGNT
TISVAQLSAD GKSEVRSQQV FQTPSNIGTL EGSRFYKRGG NYYIWLTKPA NGQYVLKSSS
PWGPYTVQQV LLNMPTPIQG GGVPHQGGLV QTQNGDWYYM AFVDAYPGGR VPVLAPVTWT
SDGWPRITTV NGGWGANYPM PNLPAPPRQV KPMTGVDTFQ GTQLGPQWEW NHNPDTTKYS
VNNGLRLSTA TVTNDLYNAR NTLTHRVQGP TSTATVELDV SAMRDGDRSG LAMLRDSSAW
IGIKRDSGRN RVVMVNGLTM DSNWNTTGTG TEVASANFTG TRIWLRANAD IRPGSGRQAR
FSYSTDGVNF SSLGSGFTLK SDWQFFMGYR FGIFNHATQA LGGSVGVSRF ALTTP
//
