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Database: UniProt
Entry: A0A2K8SKI1_9NOSO
LinkDB: A0A2K8SKI1_9NOSO
Original site: A0A2K8SKI1_9NOSO 
ID   A0A2K8SKI1_9NOSO        Unreviewed;      1590 AA.
AC   A0A2K8SKI1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Non-ribosomal peptide synthetase component F {ECO:0000313|EMBL:AUB35345.1};
GN   ORFNames=COO91_01223 {ECO:0000313|EMBL:AUB35345.1};
OS   Nostoc flagelliforme CCNUN1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB35345.1, ECO:0000313|Proteomes:UP000232003};
RN   [1] {ECO:0000313|EMBL:AUB35345.1, ECO:0000313|Proteomes:UP000232003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB35345.1,
RC   ECO:0000313|Proteomes:UP000232003};
RA   Shang J.;
RT   "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT   its photosynthetic adaptation to extreme terrestrial habitat.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP024785; AUB35345.1; -; Genomic_DNA.
DR   KEGG; nfl:COO91_01223; -.
DR   OrthoDB; 499075at2; -.
DR   Proteomes; UP000232003; Chromosome.
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; cd08955; KR_2_FAS_SDR_x; 1.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR049490; C883_1060-like_KR_N.
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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
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; PF21394; Beta-ketacyl_N; 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; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 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; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232003};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..424
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1457..1534
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1590 AA;  173695 MW;  EA863947625B9014 CRC64;
     MEAIAIVGIG CRFPKAKNPE SFWHLLRDGV DAIAQVPPER WDINAFYESK PATPGKMNSR
     SGGFLDQVDL FDPNFFGISA REAEHLDPQQ RLVLEVAWEA LENTGLVPKT LADSQTGVFI
     GVTNADYHKL IYKDSSQIGA YSATGTTPCI AANRLSYLLN LRGPSIAIDT ACSSSLVAIH
     LACQSLRNGE SNLCLAGGVN LMLAPEPAIS CSQAQMMAPD GRCKTFDASA DGYSRGEGCG
     VVVLKRLEDA LRDGDNILAL IRGSAVNQDG TSNGLTAPNG PSQQAVIRQA LEQAGVAPAQ
     ISYVEAHGTG TSLGDPIEVK SLKAVLMEGR SPEQPCWIGS VKTNIGHLEG AAGMAGLIKV
     VLQMQQREIA PHLHLKQLNP YISLEGTPFA IPVELQPWSS PGSRLAGVSA FSFGGTNCHI
     ILEEAPLPTP VASEVERPQH ILTLSAKTAP ALAELAQEYQ DFFASHPEVS LADVCFSGNT
     GRSHFEHRLA VVGESAVQMC QQLSAFGAGE DTAGLKSEQL KKKKLPKLAF LFTGQGSQYV
     GMGRQLYNTQ PIFREAIDKC AQILHPYLKQ PLFEILYPEA GKSSPLDETA YTQPALFALE
     YALFQLWESW GIKPDAVMGH SVGEYAAACI AGIFSLEDGL KLIAERARLM QALPQDGEMV
     AVIASEALVT SIIEPYVQVA IAAINGPKNI VISGDRHVIE TVTNILRTQG ITTKKLQVSH
     AFHSPLMEPM LGEFEQVAKN ITYSSPKISL ISNLTGQPIT DEMATPEYWC NHVRQPVRFA
     DSMESLYQRG YKIFVEIGPK PILMGMGRYC LPEGEGTWLP SLRTGRDDWK QILDSLAALY
     ISGAIVDWNG FDRDYARRQV VLPNYPFQRQ RYWFEQAKNG NSKTESLSQD RIQTQIFNLL
     HQGETQELAK YLQTATQFSQ EEIKVLPKLL DILAKQHQQQ LTAASYKDWL YEVSWQPKPR
     QLTQISAQEP GSWLILADKR GVGQALAHLL QEQGESCFLV YPGEGYEVKQ PGTWSVNPSN
     PADFERLFQE VVGTNKLPLK GVVHLWSLEA GLTSELTVPL IEKIQVLGCA STLHLVQALA
     SRLASPRLWL VTRGAVPAVS SLQAPAQASL WGLGKVIALE HPKLWGGLLD LAADAPTDEA
     VNLLAEIWDS QGENQIAFRE GRRYVARLIR SEVPEARSIS LQSDSTYLVT GGLGALGLKV
     AQWMVEQGAR HLMLTGRKQA SAEVLQAIAQ MENLGAKVAI AQADVAHWSD MVRVFEEIKT
     SMPPLGGIIH AAGMLHDGIL RQQEWKSFEQ VMAAKVKGTW ILHTLSQQLQ LDFFVTFSSA
     AALLGSPGQG NYAAANAFMD ALTDYRRASG LPGLSINWGL WKDAGMATSL GNRDQARLAA
     QGMESIPLEQ GLQILGNLLG QDRSQVGVLP VNWSKFCEQF PEGVVSPFLE SFIARDKKPS
     LQRTQLLQQL EASPVNERQT LLIAHIQTEL VKLLGIDASE LEPQQGFLDL GMDSLMAVEL
     KNRLESTLSC SLPSTLVFDY PTIEALVDYL LKDAIPSVSF ANASLISDES AVESQETNHE
     EQVVTDSYLD DLSDSEAEEL LLGKLNSMRY
//
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