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Database: UniProt
Entry: A0A1W0B4V1_9NOCA
LinkDB: A0A1W0B4V1_9NOCA
Original site: A0A1W0B4V1_9NOCA 
ID   A0A1W0B4V1_9NOCA        Unreviewed;      1918 AA.
AC   A0A1W0B4V1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ONM45992.1};
DE   Flags: Fragment;
GN   ORFNames=B0T46_25410 {ECO:0000313|EMBL:ONM45992.1};
OS   Nocardia donostiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM45992.1, ECO:0000313|Proteomes:UP000188836};
RN   [1] {ECO:0000313|EMBL:ONM45992.1, ECO:0000313|Proteomes:UP000188836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1655 {ECO:0000313|EMBL:ONM45992.1,
RC   ECO:0000313|Proteomes:UP000188836};
RX   PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA   Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA   Potter G., Perez-Trallero E.;
RT   "Nocardia donostiensis sp. nov., isolated from human respiratory
RT   specimens.";
RL   Antonie Van Leeuwenhoek 109:653-660(2016).
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:ONM45992.1}.
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DR   EMBL; MUMY01000038; ONM45992.1; -; Genomic_DNA.
DR   STRING; 1538463.B0T36_25625; -.
DR   OrthoDB; 4516163at2; -.
DR   Proteomes; UP000188836; 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; 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; 3.40.50.11460; -; 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   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; 2.
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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188836};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..447
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1720..1795
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1811..1918
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1391..1427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1918
FT                   /evidence="ECO:0000313|EMBL:ONM45992.1"
SQ   SEQUENCE   1918 AA;  200553 MW;  A691EFA4AAF1DD90 CRC64;
     MSVSSEALLE ALRVAARDNA VLRQTHDRLL AELSEPIAII GMACRFPGEV TTPEQLWRLV
     SEGRDAIGPF PEDRGWDVAG LYDPDPDADG KSYVRHGGFL YDAAEFDAGF FGISPREAVT
     MDSQQRLLLE TVWEALEDAA IDPYTLRGSD TGVFAGVMYH DYPFSAGSGS IVSGRVAYTL
     GLEGPAVSVD TACSSSLVAL HQAVRSLRAG DCAMALVGGV TVMATPDTFV GLSRQRVLAA
     DGRCKSFAES ADGTGWGEGA GVLVVERLSR ARELGHEVLA VVRGSAVNSD GASNGLTAPN
     GPSQQRVIGR ALASAGVGAG DVDVVEAHGT GTVLGDPIEA QALIATYGQD RAPESPLWLG
     SIKSNIGHTQ AAAGVAGVIK MVQAMRHEML PRTLHVDAPT PHVDWSGGAV RLLTEQQPWP
     RREDRPRRAG VSSFGISGTN AHVILEEAPP PPPPIDSTDT APVQDSDATP AIRGTVAWVL
     SARDRTALAE QARRLIEHLR SRPDDTPTAI GWSLVSGRAR LEQRTVVLGT GRDDLLAKLA
     VIAADPATAI VSGAPSAPVP TGARARGRTV FVFPGQGTQW VGMGRELLDS APVFAATIAA
     CEVTLTDRVP WSLTAILRAP DDDPTAAALL ERIEVLQPVL FAVMVGVARV WEALGVRPDA
     VVGHSQGELA AAAVAGALSV DDALRIVLER SRLFAEKLTG RGAIASLGMP ADTATEQLAR
     YPGLTLAGVN GPAAVSVAGE LPELDRLVTD LTAAGVRARL IATTVASHSA AVEPLRDELI
     GALSFVRPQR ARIPIYSTVT AAEIDGTELN ARYWYDNCRQ PVRFQDTVRA LRSDGFGIFV
     ETGPHPVLTM PVEQTVAEVD GPEAIVVGSL RRGDGSARQL LDTAARLFVA GAPVDWSALY
     HGREPRRIPL PTYPFQRRRY WLEPTGAGSA AAALGQWEAD HPLLRAVVAA PDSGGVTITG
     RLSLRTHPWL ADHAFAGTVL FPATGFLELA LRAGDETGSP VVDELNLLQP LLLPDDRTIR
     LQTVVGGPDE HGRRPVSVYS SADGEPGGIW VRHAEGRLTP HLAVDGPESG TQWPPAGFAP
     ADIDGVYEDL ADAGYGYGPV FQGLRAVWRR DTDLCAEVAL PDTVTDAERY AVHPALLDAV
     LHALGAVTDP ATGAGPVLPF SWAGVTAQLH GATALRAEIT SAETDAISLR VTDMQGHPVL
     SVRSLTTRPV PLDRLTSPQQ PLLTVAWRGL PHAAAPETEV RYEPWARCAN QNDTAAPVVV
     LDCRWHDGRT VIAETHAATA NVLAVLQTFT GSARFTTSRL LVITHGAVSV AGEDIGDLAA
     TAVWGLVRSA QSEEPGRIVL LDTDTGEPSV ASIAAVLACG EPQLALRGET LYVPRLTRLP
     GIDTTPLVGG TAPSVGGTAP SVGGTASPVG GATPSVGGTA PSVGDIASPA TDTAPALAAD
     ATVLVTGGTG GLGAAVARHL VAAYDVRSLV LASRRGPAAP GATALVDELS AAGARVRVVA
     CDVSDRAAVA DLIAAVPADN PLGGIVHAAG VLDDGVIGSL TPQRLDTVLA AKADAAWYLH
     ECTQDRDLAM FVLFSSAAAV FGSPGQGNYA AANLFLDALA AHRHATGAVA TSIGWGLWTT
     VTDATAHLDA ADTARIRRGG ITGLSAEQGL ALFDAAVRQP QPAVTAVRLD RMVLAEQARA
     GLLPPLLREL APAARQNGSS GGSGALARRL AEADNRDRTQ LLLDLVRAQV AVVLGHDGPA
     AVETERNFQE LGFDSLTAVE VRNRLAAVTE LALPATLVFD HPTPLAVARY LQDRLLGTVV
     RTEPVARAAT SEPIAIVGVG CRFPGGVDGP EALWRLVTDG GDTLSEFPSD RGWEVEKIYD
     PDPDPDAVGR SYVRHGGFLS GAGGFDAGFF GVSPREAVVM DPQQRVLLEV VWEALEDA
//
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