ID A0A3N0EI94_9ACTN Unreviewed; 1295 AA.
AC A0A3N0EI94;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyltransferase domain-containing protein {ECO:0000313|EMBL:RNL87504.1};
GN ORFNames=EFW17_01440 {ECO:0000313|EMBL:RNL87504.1};
OS Nocardiopsaceae bacterium YIM 96095.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae.
OX NCBI_TaxID=2487137 {ECO:0000313|EMBL:RNL87504.1, ECO:0000313|Proteomes:UP000269198};
RN [1] {ECO:0000313|EMBL:RNL87504.1, ECO:0000313|Proteomes:UP000269198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 96095 {ECO:0000313|EMBL:RNL87504.1,
RC ECO:0000313|Proteomes:UP000269198};
RA Tang S.-K., Chunyu W.-X., Feng Y.-Z.;
RT "The genome draft of YIM 96095.";
RL Submitted (NOV-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:RNL87504.1}.
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DR EMBL; RJMB01000001; RNL87504.1; -; Genomic_DNA.
DR OrthoDB; 4537517at2; -.
DR Proteomes; UP000269198; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:RNL87504.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000269198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RNL87504.1}.
FT DOMAIN 286..711
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1222..1295
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 245..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 136332 MW; 9682D169574500E4 CRC64;
MDRNEPSPWL ARSPRHSAKV RLFCFPHSGG GPSAFRDWPT LVPPWVDIVP VQLPGRERRA
DEAPPSSLDS IVTAVTAAVA PHTDRPFALF GHSLGALLAY EVARHLHREG LPSPERLLVA
GVGAPHQGPA DRSAAPSSDE ALLSEIEELG GVPPQLHENR DLLRAALPGL RADVALFTSY
THQPGPLLDC PVTVLVGEED PLTRESDTSA WSEVTRGEST VHTFPGGHFF VDEHARAVSR
TVLAELRRSS SPEPPSRGVS GTSEGPTSMS GTAGHGDAPD IRPAGGEPVA VVGIGCRFPG
ASGPEAFWRL LLDGVDAVTD VPDSRSGDHG VFAELPPLLG GAAHPRQGGF LDDVDGFDPT
FFDISEREAA RMDPQQRILL EVAWEALEDA LVPPTSLGGS RTGVFMGQMG RDYWDLQSRQ
TSVDVHSLVG SGLSSFTSGR LSYDLDLRGP SVSLDTACSS SLLAVHLACQ SLRTGESTLA
LAGGVNLVLV PELAAVYEQV GLMSRSGRCR FGDASGDGFV RSDGAGVVVL KPLARARADG
DRVYAVVLGS VANNDGRSGS SLTAPGQEAQ ERLLADAVEI AGVRPSDVDY VEAHGTGTEV
GDAIELRALA NALGTGREPE RPCRVGSAKS NIGHPESAAG IAGFIKAALS VHHREIPGNP
LLRDPHPVLA DQRRSLDIPV APVPWPSDRD PVAGVTSFGL SGTNVHALLG AAPTAPVPEP
SGQPLVLPIS ARDPAAAEAL ADSLADRIDG TGAAEAEWIC AAAARGRSHH QWRAAVAAND
GAGLATALRE VRRGAVDPVG ERPRIAFVFG GHGGQWHGMG RALLATSPAF RDALHECDAA
IRAESGWSVT ELLTGDAPGA LRGSETIQPA CWAMHMALAA YWRSWGVRPD SVLGHSFGEV
AAACVSGAIG LTDGARLICR RAELTSHADG RGGMLAVGLP EGEVAAEITE YGDRVAVAAH
NGPRSTVVSG DSEALELLLD TFDGRGVRTS RVRIPFAAHS AHMDPLRRPL VDSLGALAPR
PTTASFRSTV TTRVMAGADL GAAYWGDNLR EPVRFRDAVT AECAQGRTVF LEISPRAVLS
PVLRQCLAAH QDERHSVVAG PTREEPESSG VARATSDLYN AGVDLDWGAR YPAVPAPEDM
PRYPWQRRSV WFTPSPRART SAHDQPTIRV DVRRDGSGWS CAVTGSHPAR VEIGPADDDG
TRSDGARQGD VSVADRPTST APLPSDTATE LAKEIADVLG VPPSGVSREK PLRLLGTDSL
AAGEVRVRIE RRWGVNVPAT TVLESTIEEI AANHL
//
