ID A0A372M1L4_9ACTN Unreviewed; 1083 AA.
AC A0A372M1L4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acyltransferase domain-containing protein {ECO:0000313|EMBL:RFU84395.1};
GN ORFNames=DY218_22290 {ECO:0000313|EMBL:RFU84395.1};
OS Streptomyces triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU84395.1, ECO:0000313|Proteomes:UP000263094};
RN [1] {ECO:0000313|EMBL:RFU84395.1, ECO:0000313|Proteomes:UP000263094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU84395.1,
RC ECO:0000313|Proteomes:UP000263094};
RA Han C.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from
RT wheat.";
RL Submitted (AUG-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:RFU84395.1}.
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DR EMBL; QUAK01000120; RFU84395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372M1L4; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000263094; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:RFU84395.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RFU84395.1}.
FT DOMAIN 40..467
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 996..1073
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 114133 MW; 5377BC541D812143 CRC64;
MSDSRQSPSD TRQPPSDNQQ PPSDNQQPSS DNQQPPPAHE FSVAVIGMAA RFPGADTVDA
FWDNLVAGRD SLTRLTDADH LAAGGDPALL DDPYHVRVVR EIDGMDRFDA DYFGYRPAEA
ALLDPQQRVF LEVAHHAFEN SGHVPSRNPG PVGVYAGAGL SRYYTANLAP WYAAQPGSLD
QMAALSGNSP GTLSTRVSYL LGLTGPSVNV QTACSTSLVA VHAACQDLLA HRCDLALAGG
VALNPHARLG YRHVEDGPYS PDGRVRAFDA DAAGMSQGDG AGAVVLKRLD DALADGDTVR
AVILGSAVNN DGDRKVGFTA PSAQGQTEVI LAALAEADVD AASIGYVEAH GTGTPVGDPI
ELTALQVAFD QAGGHPGGCL IGSVKSNIGH LDAAAGIAGL VKTVLALEHG TVPATLHHDR
PNPLFDWDDA PFEVATSASP WRLPGPRRAA VSSFGIGGTN AHLVLEQPPT ALEQPPTVLE
QPPSPHPATD REAPPREPAD DEAYTLLTLS ARTPAALDTL ARDTAAHLDT HPELEPQDVA
HTLNSGRLAH PWRRTLVVRD LAQAVEQLRA APRTEPRPAV HRPLGLLLPG GGVHYDGMGA
GLYAREPVFR DIIDDCARIL RPVLGHDLRT ALYGPAGTGP GAGPGLGRGT DPGEHTARID
GVATGLRPAA FPAIVATQYA LAGLLESKGL APAALLGHSL GEYTAACLSG VIALEDVLPL
MAERERLFAE VGGLTLSVRL GEQAVAPLLS PDTAVAAVNS LETCTVSGTA EAVLALEQRL
AAAGVDHHRL RTPSAVHTPL LDPVLGEFRE LVAQLPLRKP QIPYVSNVTG TWMTAQDATD
PDYWVAHCRR TVRFADALRT LGADDPGPLL LEAGPGGGLG KLARQVLGPE AATVTAIRHA
YAEQTDEAFL LEAIGSLWRH GADGARDTWR LGGPPTRRPR PVPLPGYPFE RRRYWIDPPE
QGRTPKGGPV LSTGDPDAPE ARHTRRAPTV PDPTGDDRLH QLHQVVAVWE RLLGIDGITP
DDNFFDLGGD SLLLMRAAAE VRDLLGAQLS VRRLYVNQRL TPAGFLAEAA DTSTAPASTV
PAP
//
