ID A0A3N1ASJ1_9ACTN Unreviewed; 592 AA.
AC A0A3N1ASJ1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=O-glycosyl hydrolase {ECO:0000313|EMBL:ROO59608.1};
GN ORFNames=EDC02_1409 {ECO:0000313|EMBL:ROO59608.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO59608.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO59608.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO59608.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
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:ROO59608.1}.
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DR EMBL; RJJY01000001; ROO59608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1ASJ1; -.
DR OrthoDB; 9806701at2; -.
DR Proteomes; UP000275308; Unassembled WGS sequence.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF38; GLUCURONOXYLANASE XYNC; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361188};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW Reference proteome {ECO:0000313|Proteomes:UP000275308};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 45..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017971711"
FT DOMAIN 485..592
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 453..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 62906 MW; 6BC74FEE6C560907 CRC64;
MRLTPRGKIP PSQLRRGAGA TAVLAAATAA VTAAGVLTAP PSIAATPDIT VNTGSTYQTI
DGFGAATPIF SSGGDQWTTS ETQTLVGMGQ GQLGLSIVRT VVSPTSSEWS WPVSSLQTAK
SYGSDVKILT SPWTAPAHFK TNNSRVNGGK LRTDYYDDYA AHLNDYVQYM KSQGVTIDVT
SIQNEPDWHP DYDSMDWTGA EMRNFVRDHG AAIRDTELMV GESLRFARSY SDPTLYDAAA
RNNIGYVGGH LYDTENSGNL SPYPLANQYG KPQWMTEWNL HAADGNGSNI WGDPSNTAVW
NETLDDIMRT VHRSMEVGWS AYIWWYGRRF YSFIGDGESQ YGTTKGAPLR RGYAFSQYAK
YVRPGDQRVA LSKSSRVSGL EVTAYQGRGK VTLVVLNRSN SAVNDAVVQV PQNISAAEYT
VTSRTQSAQS QPVNVSGGQV TVDVPARSIS TITITEGTTT APPTTAPPTT APPTTAPPTT
APPTTNPPAG ACRVTNAVDA WNSGLVDNIT ITNTGTATVN GWSLRFTLAP GQTITAGWNA
TYSPTSGQVT ATNVSYNPTI PPGGSVSIGF QATHTGNSSS PSGFTLNGAA CG
//