ID A0A495JUL5_9ACTN Unreviewed; 379 AA.
AC A0A495JUL5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Lysophospholipase L1-like esterase {ECO:0000313|EMBL:RKR92511.1};
GN ORFNames=BDK92_6952 {ECO:0000313|EMBL:RKR92511.1};
OS Micromonospora pisi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR92511.1, ECO:0000313|Proteomes:UP000277671};
RN [1] {ECO:0000313|EMBL:RKR92511.1, ECO:0000313|Proteomes:UP000277671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR92511.1,
RC ECO:0000313|Proteomes:UP000277671};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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:RKR92511.1}.
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DR EMBL; RBKT01000001; RKR92511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495JUL5; -.
DR OrthoDB; 468550at2; -.
DR Proteomes; UP000277671; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01833; XynB_like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR30383:SF2; CELLULOSE-BINDING PROTEIN; 1.
DR PANTHER; PTHR30383; THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000277671};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..379
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019821924"
FT DOMAIN 276..379
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 243..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 39278 MW; D91A973B212233EC CRC64;
MLRKPLGQAA LAALAVLLGL VITTPSLRAA STPATTLAPV RVMPLGDSIT GSPGCWRSML
WNRLQSTGYT NIDFVGTLGP QGCGQAYDGD NEGHGGALVT NVANQNQLPG WLAATRPDIV
LMHFGTNDVW SNVAPATILA AYGKLVDQMR VNNPAMKVLV AQIIPMAPSS CAECGQRVVA
LNNAIAGWVG SKNTAQSPVV RVDQWTGFST GSDTYDGVHP NASGDQKMAD RWYPALTAAL
GGITPTTSPT VDPTPTRPPT VSPTPTRTPT TAPPTTAPPI GGCTATYRVI GQWQGGFQAE
VTVRNGSTGT FAGWAAYWSF GAGQRVSQSW NATVSQSDTN VSARNVAWNG NLAPGATATF
GFIANGDGAN PVPTVTCTA
//