ID E6JBT3_9ACTN Unreviewed; 423 AA.
AC E6JBT3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative lipase/esterase {ECO:0000313|EMBL:EFV90953.1};
GN ORFNames=ES5_13493 {ECO:0000313|EMBL:EFV90953.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV90953.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV90953.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV90953.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV90953.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEKG01000317; EFV90953.1; -; Genomic_DNA.
DR AlphaFoldDB; E6JBT3; -.
DR Proteomes; UP000004165; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 173..373
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ SEQUENCE 423 AA; 43440 MW; BE4DC5AD57A75B44 CRC64;
MRSAGRLRSA RGSRPTPPTS SHSPPTPHGG ANGRARSRSG GCTGTWAAPR SARVPAAAEN
SSGACRRGPP LAPAAGSTAI LSLLARRLVA EADRRIAVTR RPSLSSRFQR AGLQLVVRPV
LTIAPFDEKW IRALRAVATT ASRATGSRRR TRPAHGAPVP GLWIDGADDA PGLLVLHGGG
YVAGSPDTHA TMAKALARLA GTTTYVPDYR LAPEHRYPAA LDDAEAAFRH LAERVGGAER
VAIAGDSAGG GLALGLLDRL RGGGERPAAL ALISPWVDLT EPLGGERSGG ALDPLMPPSI
AADCRDAYAG DTPVDDPGIS PARRPLDASA PAVSIVCGGD DFVVDDVRAF VDASTARGAT
VDLRVWPGMV HCFPVVAGTP EGASALAVLA GHIRTAVTAT AVDADTVGPR DPGDNRGPET
TDR
//
