ID F9FMB7_FUSOF Unreviewed; 2530 AA.
AC F9FMB7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGU81944.1};
GN ORFNames=FOXB_07547 {ECO:0000313|EMBL:EGU81944.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU81944.1};
RN [1] {ECO:0000313|EMBL:EGU81944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU81944.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU81944.1}.
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DR EMBL; AFQF01002281; EGU81944.1; -; Genomic_DNA.
DR STRING; 660025.F9FMB7; -.
DR PaxDb; 5507-FOXG_11954P0; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
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; IPR020843; PKS_ER.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF54; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_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; PF08242; Methyltransf_12; 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; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 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; SSF50129; GroES-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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..421
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2451..2528
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2530 AA; 274976 MW; D6DDEE52B8E77C28 CRC64;
MACRLPGGID KPLDLWDHVR AGRSSATAIP KDRFNAENFL SMDPNQKGAQ AFRGAHFVKR
DIKQFDHKFF GISKDTATAM DPQQKQLLEV VYECLESANI SMETISKSKI GCYCAMFVSD
YHDMLMQDPE YLPTFIAIGT TRTMLANRIS HALDLGGPSV TIDTACSGAL VALHLACQAL
QAGECDGAVI GASNLFLSPD YALSLTRLGA IAADGQCKTF DASANGYGRG EGTNAVYVKR
LSDAIRDGDS IRAVIRGTSS NSFSSGATPA ITEPSGRAQA DTILQAYAQA GINDFSETGY
FECHGTGTPV GDCIELGAVG SVFSESHKTQ DALWVGSTKP NVGHSEAASG LSSLIKVVLA
LEKGEIPPNT NYKTPNPKID FDGWRVRVPT APQPWPSKSI RRASVNSLGI GGSTAHAVVE
FYEPPHLTNG STNGANGVNG THSINGTNGV NGVNGVNGHH EEGEKSNDPY FLLFTSGASK
SSRETNEQNL LEFLKTHEEC KSLTSPLVKA LNARSQINIR PWKSFAVAQS VDDLIQQLET
NALKVGTGPT SGDSPRVLFT FTGQGAMWSQ MGKRLLDAFP VARNSLYNLE EVLRELQSSK
TPTWSLIDKL TTELSQEEID SPALAHPLSM AVQIALTDVL SSWGVHPDGV VGHSGGETAA
AYACGALTAK EAITVAYYRG IACQNAPSGA MLATRSAPKA KELQDALKRN DVQIACFNGP
QNLTLAGSSE GVKNVAAELS THGIVSRAVA VTRAYHTRAM KTVVDEYVGQ LKGVIQPKTG
RVPMYSSVTG LELKGTEVDA DYWGANLVSP VLYTDAVTLA LTSSDRKFDL CVELGPHSLL
SRPTSEIVKS LPNSPQLPFF ATMLRNADSS QQLMSLAGDL VLNGKKLDLD QVNKIAGKTG
RLPNHLQDNL PAYAWDYSST PWTEPRNSQE WRFRKSPRHE ILGSRCRGVN PSAPTWRNKV
SIEDAPWLVD HQVNGIVTFS FTTGIAMVVE AMMQVQEENK EIDWANHSFE LQDFVFSNSI
ILPDESPIDL FLTLIPDNDN AKSEETWYDF TISSLRGDVD IRHCHGRAAV LQTSKDNVAL
RRRTSWHHMP LRVPLKSYYK TLERVGYGYG PKFQLLNEVR VRPSLSACSA KIDMTSTAQS
PVPGQRYLLH PAMMDAALQT PALANRSGYF QEIDTLLLPS KMKRISIRMP AENTDVASCT
TNTSPVGFSR IQGSVECYDS LSRPFFVVEG LQMDRATSDD NTTLPWLRLT WKPDIGDISS
SDPMLSSIKI QSLPAEKKLV NLENLVKELI PLIVENGIEK GKDLAPHLLS YHSWFLDQAE
LHKDLLAARH KQQNGFATVQ DAIMNVVANS GISQTVDASI VSQLAINMSR IFRGEVEALA
VWLENDLLYR FYEESIFTTS MNQKLLSIAE LLAHKNPNMK ILEIGAGTGG ATTELLRGFS
KAGGKNAYQS FTFTDISAGF FDKAKKKFAQ WDRIEFKTLD VEKDIAEQGF TEKYDLVVAA
NVLHATADLP FAMKNIRSLL RDDGYLLVGE LSEDLTSANF LWGPLTGWWL RPRSPGRSGP
GLTLDEWRDE LAADFDSVSE IEAKHDKSDT DQLSSTIVMM ARAKPVEYTP PKPLSEEKVH
IAGVGGDLST RDHFQKYLGT RGISASSSTL EDLASREWSG EWLILVDETE GSFLASLQQE
QLTALKSWLT KPIKCIWVTR KVYLDPQNTT GGLVTGFART LRGENSQCQL YTLDLSSDGD
ITANVIYHVL ERAHYSHDDP ISRLDYEIAE KDGQLWTCRL VNDALLENAY GPARKMDAPS
TQVVKAPHHL IMGEVGILES LTMAQDDAYT AIPDGHVLVE VKAVGLNERD GFIAQGSLPA
TSFGRECSGV VTSCGANVAS FSPGDRVAVI GQGTFTTPYL APSNCCRKIP DWLSFEDAAA
IPTSFVTALY ALTTPARVST GQKILIVNAS STQGVALIKI ATALKLDVYA AISDATDKPL
LTRLGLHSAK IFVNPTNTGR SSVSRSTTFQ AYKLVLNTKS GQYADFAHLV ANRGTYIEIA
SGETSGDEVY LAPNKNVMFA SVDLVDAYQE NKQDLGDLLD QVIDWVEKRE IDVDTSVSVT
GLDSIQSAFS SLVEGNQQKQ VVSLTNSDDQ QLIKTRPKTS RFNPHKTYII TGGLGGLGRA
ISVWMASYGA RHIILATSSV ARASESGDLL QQLSSYGCNG RVEVCDVGDS EAVERLVASI
DTPVGGVIHS ALKLSDCFFE DITLEDFDAV FGPKVNGSLN LHNSLINQDL DFFVMLSSGC
GVLGNEGQSN YAASSTFLDT FARYRQSLGL PASSVDLGFV EDVGNISERP EIQASLLSRG
LRPITVRDVL RVVEGAIATG SPKNPNINDS TYDSFIQSQI VLSFGMIDKA TAEYQSWAQD
AKFGLLRSRA ADNAALDSDA DSGESAVQTA VKAFRNTLGR LGDAPEGKEA ALQPFVCTAL
VAKLAQVLSI KVADIQPSRS AIQYGMDSLI AIEVRSWARY AFQIDLPIND LTNPYSIQDL
SARVSRMIVG
//
