ID A0A1E7LD61_9ACTN Unreviewed; 1501 AA.
AC A0A1E7LD61;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OEV14108.1};
DE Flags: Fragment;
GN ORFNames=AN218_00715 {ECO:0000313|EMBL:OEV14108.1};
OS Streptomyces nanshensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=518642 {ECO:0000313|EMBL:OEV14108.1, ECO:0000313|Proteomes:UP000176005};
RN [1] {ECO:0000313|EMBL:OEV14108.1, ECO:0000313|Proteomes:UP000176005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10429 {ECO:0000313|EMBL:OEV14108.1,
RC ECO:0000313|Proteomes:UP000176005};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV14108.1}.
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DR EMBL; LJGW01000020; OEV14108.1; -; Genomic_DNA.
DR Proteomes; UP000176005; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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; 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; 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; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
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 1236..1314
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1335..1501
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 43..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEV14108.1"
FT NON_TER 1501
FT /evidence="ECO:0000313|EMBL:OEV14108.1"
SQ SEQUENCE 1501 AA; 156802 MW; A00A9ECCD5DFFDFC CRC64;
DEPSSHVDWE AGAVELLTEQ KEWPQSDRVR RAAVSSFGVS GTNAHLILEQ PDETAQDRES
TPERGAEPEG ISSAPSGAVP VLASAKSAGA LDGQIERLGE CAAAGPALDV GFSSVVSRSV
FEHRAVLLAS DEGVTEAARG VASSDPGELA VVFSGQGSQR LGMGRELYDR FPVFAEALDA
VLAHLDPGLR EVMWGGDEEL LNRTGWAQPA LFAVEVALFR LAASWGIEPD YLAGHSIGEI
AAAHVAGVFS LEDACRLVSA RARLMEALPE GGAMVAVEAA EAEVVPLLTD GVSLAAVNGP
TSVVVGGVES EVEAISAHFE ASGHRTRRLR VSHAFHSPLM EPMLEDFRTA IENLTFEAPG
IPVAAWGDVS TPEYWVEHVR ETVRFGDSVE WLAQQDVSAY VELGPDGVLS AMAAAIAPDA
TTVPLLRKDR GEEAAVLTAV AQLHVVGHEV AWSRLFDGTG ARRMDLPTYP FQHRRFWPAV
STRGGDAAGL GLSAAEHPLL GAAVELAEGD GVLFTSRLSL RTHPWLADHV VMGQILVPGA
ALVELAMRAG DEVGCDRVED LTMAAPLVVP EQGGVQIQLR VGTADSAGRR TVSIHGRASG
TDDLPWTEHA SGTLGTGTEA TEFDTSVWPP ADAQPVELAD CYERFAEAGF RYGPVFQGLT
AAWRGKDGEL FAEVTLPEET RTGGFGLHPA LLDGALHALL LQDGDQAAVP FSWEGVTLYA
TGASAIRVRL IPGSDDAIAV ALTDTLGAPV AAIESLITRP VQTEQLAGAY SAPRDALFGM
SWTPVPIPSG ENTDLPTVAV VGADPFGLAA CVSGAGTWAE LADVTGLAAV DVSSVPGVVL
VPVSGGADGG VAEAAHGLSV RVLELAQLFL GAEEFAGSRL VFVTRGAVSG VDPAAAAVWG
LVRSAQSEHP GRFGLLDVDD SDASVAALPQ ALAVDEPQLM LCGGEMSAPR LARATSAEGD
GVSWGGVEGS VLVTGGTGGL GALVARHLVS EHGVRDLLLV SRRGQGAEGA DELVAELTEL
GARAEVAACD VADREALASL LAGQPVGAVV HAAGVLDDGV IGSLTPERVD AVLRPKVDAA
WNLHELTRDR DLSAFVVFSS AAGVFGNAGQ GNYAAANVFL DALALHRREL GLPAVSLAWG
AWAQEGMLDE ADAERLARGG MPPLGTGEGL ELFDAALAAD EPLLVPVRLD LPVLRARGEV
PPLLRGLIRT RTRRSVAGAE TVASLVQRLS DLDVDEQHDA VLDVVRGEVA GVLGFGSGAE
VDATRAFQDL GFDSLTAVEL RNRLTATTGL RLPATLVFDY PTAAVLATHL REELVGNDTD
TAALVPSRVL PPVADDPVVI VGMSCRYPGG VSSPEDLWRL VAEGTDAISD FPTDRGWDLD
SLFHPDPDHP GTSYVRSGGF LREAAEFDPE FFGMSPREAL ATDSQQRLLL EASWEALERT
GVDPGALRGS RTGVFAGVMY NDYAQLLEGA XVFAGVMYND YAQLLEGAET EGHQGTGTSP
S
//