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Database: UniProt
Entry: A0A0M8YM11_9ACTN
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Original site: A0A0M8YM11_9ACTN 
ID   A0A0M8YM11_9ACTN        Unreviewed;      1689 AA.
AC   A0A0M8YM11;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOX33962.1};
DE   Flags: Fragment;
GN   ORFNames=ADL06_08225 {ECO:0000313|EMBL:KOX33962.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX33962.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX33962.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX33962.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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:KOX33962.1}.
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DR   EMBL; LGEE01000063; KOX33962.1; -; Genomic_DNA.
DR   PATRIC; fig|1519495.3.peg.1738; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000037743; 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; cd08956; KR_3_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 2.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
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:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 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; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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}.
FT   DOMAIN          1..80
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1324..1399
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1417..1689
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          84..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KOX33962.1"
FT   NON_TER         1689
FT                   /evidence="ECO:0000313|EMBL:KOX33962.1"
SQ   SEQUENCE   1689 AA;  174173 MW;  5DF31F38F25ED3C1 CRC64;
     GHAQAAAGVG GVIKTVMALR AGVLPKTLHA REPSPFVEWE GSGVRLLGEQ ETWPERGRPR
     RAGVSSFGIS GTNSHVILEQ APEHDDHVGP AQPGPTADEP GAVSERPAPP VLLSGNTPAA
     LRRQAAALAD HLRAHPDTDA HALAAALARR ARHAHGAAVP FDGDGDPDRL SAALRALADG
     EVHDALITGE RAAGRTVFVF PGQGSQWSGM ARELLDASPV FRDGIEACAA ALAPHTDWSL
     LDVLRGAPDA PGLDRVDVVQ PVLFAVMVSL AGLWRSAGVV PDAVVGHSQG EIAAAYVAGA
     LSLADAAKLV ALRSRALTGI AGDSGMVSVA LDADALAPVL AEHPDELEIA VRNGPRATVV
     AGGDTALGAL LAWCEEHGVR ARRIPVDYAS HTRYVEPLRE HLLELGAGLT PGTAGTAFYS
     AVTGGPVATD TLDAGYWYRN LRETVRFEAA VDSLVDSGHR RFVEVSPHPV LTFAVEEILA
     GRGVAAFTGG TLRRDHGGPD TFRRSLAAAH LGGAPVAWDV PATAPDLPLT YRFAPDRHWL
     VPSGGPAATA LPGLTAEPHP LLGARVELAD GAAVFTGRID LRALPWLTDH GVFGTVLVPG
     TAFAELALHA GAAVDLPAVA DLTVRAPLVP DPDRPTALQV RVAPVDATGA RELTVHARPD
     DTAPWTLHAS ATLRAAAPAA TPAFPAFPPA DAAPVALDDV YAGLFRLGYD YGPAFQGLAA
     ARRTPDGVLH AELDPGLSDG DGDASGTGFA LHPALLDAAL HPVVAGLVGT HAADPERPLL
     PFAFEGLRIT DAAAAAAADR LRVRIEPLAD TRFRLTLADA HGNPVAEIDS LAFRPVGRAE
     LAGRPAVGAT AHHLDWPELP LAGPATGTHL VLAGLGDTGL VTDAETVPDT EALSARATPP
     TAVLVPVTGT VPPTGTAIGT GTAEGTGTGP DPRAVPARAH ELTAAVLALL QRWIATPAWD
     GVPLHVVIRT GDLAAAPVRG LLRTAAAEHP GRFALVETDG PAPAARLAGD HGEPESALRD
     GRVHVPRLAA HDLAPASPPA PDGAGTVLVT GGTGALGALV ARRLAARPNP PHLLLVSRTG
     PAAPGAADLT AELRAAGAGT TVAACDVTDR DALARLLADV PADRPLRAVV HTAGVLADAT
     VTELTPEQLA AALRPKVDAA WLLHELTAEL PLDAFVLFSS AVAVAGVPGQ ANYAAGNTFL
     DALAAHRRDL GLPGVSLAWG LWEETGAMTG HLGAADRTRL ARYGVGPVAT EAGLDALFAA
     ERPHTIVSPL DEGLLRQEAA AGRLRPVFGA LVRVPASAAR RAAGAGGGAW ADRLAAVPAH
     ERLRTVTALL REQAALVLGH DGSDGIGADR PFKDLGFDSL TAVELRNRLG RLTGLTLPAT
     VVFEYPTIAG LAGHLHASLT TDAPEEAAAV VRQRDVEDPV VIVGMGCRFP GGVASPEDLW
     RLVADGTDAT GGFPEDRGWD LEKLYDPDPD HKGTTYTRRG GFLYDAAEFD ADFFGMSPRE
     ALATDPQQRL LLQITWEALE RAGIDPHSLK DSDTGVFIGA MYDDYAARLR TAPEDVEGLL
     LAGNQSSVAS GRIAYVLGLR GPALTVDTAC SSSLVALDLA VRAVRSGECA TALAGGVAVM
     ATPSTFVEFS RQRGLSADGR CRAFGADADG TGWAEGAGIL VVERLSRARR EGHRVLAVVA
     GSAVNQDGA
//
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