ID X0CYM0_FUSOX Unreviewed; 2351 AA.
AC X0CYM0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXK99226.1};
GN ORFNames=FOQG_01812 {ECO:0000313|EMBL:EXK99226.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK99226.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK99226.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK99226.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH658363; EXK99226.1; -; Genomic_DNA.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_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; 3.90.180.10; 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 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; 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; 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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 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; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2270..2344
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2351 AA; 258391 MW; 5AB3BE686826CC58 CRC64;
MENDIAIVGI GLRFPGDASS PEELWKVLER GESQWSEFPK DRLNIDGYYH PSGDRQGSIS
FRGAHFIKGN FASFDASFFS ISAEDAKAID PQQRILLEAS YEALENAGIR KEDIDGSDAA
VYVGSFVKDY EQVCLRDPDW QPQYAATGNG IAIMANRISH FFNLHGPSMT IDTGCSGSLV
SVHLASQSLR AKETSLAIAA GAGMILTPNT MMPMTALNFL SPDGKCFTFD SRANGYGRGE
GIGVVVMKRL SDAIRDNDTI RAVIRATKVN QDGHTTGITL PSKEAQVANI NSVYESAGLD
FSQTGYVECH GTGTKAGDWR ELKAISESLC TVRDIDNPIV VGSIKPNIGH LEGAAGVAGL
IKGVLTLEHA KIPPNINFEK PNPDIDFKEW KVKVPTELLD WPVSGLRRVS VNCFGFGGTN
AHVIMDEAPR YLSARGLRGN HNSFEAITSS RRTSNTKALF EPQLFVFSSH DKLGVRRIME
SHIPYLESQG EDDTAFLHNY AYTLGSRRSN LEWKHAVVAK SREDLIVKLQ NIDESLFKRT
SKNKQPNICF LFCGQGAQFA QMGKDLLPFE AFHDALEAGS RYMKNKLASE FDLLEEILKD
EAETRISDSR ISQPATTAIQ MALVDLLDSF HVAPNYVIGH SSGEIAAAYA SGALTKEEAW
EVAYYRGLVA SSLAIEHTRT QGSMMVVGLS VLDLDESYDD KTYPCEVACV NGPRSLTLSG
RKENIEGAFR ELSAKGIFCR ILPVKVAYHS SDMLKIEKEY KSALRLINPR QHRKLVTMFS
SVTGEEIDGH ELNNKYWTLN LVSPVVFMSA ISTMLQLPSD KSPDIIVELS PSSTLRSPVL
DIITFFGFPT PPRYSTILDR KVHGAMSLLG TMAELWECGC KFSMEKVVTR GSYQIPLKPL
ADLPPYPWNH TRSYWHESHL GEATRFREFP RQDLIGAPTG DAISFEPRWR GFLRIAENPW
IQDHQIQKTI IYPAAGMIAM ALQGAYQATK GQENVLGYEI INMRIERAMI VPTTAHGLEM
AMNFKSVSCT SVHSLQGAAF DFCIYSKQLN SSWEQNATGR IEVRYMRGQW KIAFQKHREE
YELLKGSCLE PVVPRQLYEL LDIVGMNYGS LFQNIIHIRK SKGACVTKIR IPDTRSKMPA
KFEYDHLIHP ATLDSMFQTP FAIESEPMVP SFIESIFVSA KVSSDINKEF DGYSTATRVG
VRDASADISM AQSGWEQPSV IIRGLRFTGI SGSSREGDGF LPNNRTLCTQ VSWMEDITCS
RTENVEDFVK RLAHKLPGLS ILQVGGTSDT TQKIVSALTS PEGQRPWLSR YTLAEASPDD
RVFDIASVFA GTAAEPFIEK RPVDGSEPLP DYDLILVCSR SEIDIAKLSS HLKRPGYIME
NCPDGNPDLD ETISHDYIEV DGKKVEIKLR VNRKNLAEDW LSVPDVAILL PDNPPSETQW
LAGKLIMERQ SSVQMRTMQL NEVLSDPSRL KNKIVISLLD FSAGSNAGAS IYNWTETEFN
AFHSVHQVVK GILWISRSAH MDPMNPKGAP VIALARTLMS EEPLKTFVTF DLSMSTPLNS
SSVVQNVNKI FLQAFVSDQG SGPRELEYAE RNGVICVPRL VPIGPLNDVV ENGISSEITK
VSFHSYPRHL KLHVSQPGLT DDSLVFTAGT RYAPQPGEVE VIFESAPLDF IDLETAMGKT
LESEVGSEIC GRIGRIGRNV SGFMTGDLVS GLVTSGSVQS NVNIDSRFVS KWSSRLSFSH
FVRAFHCFDK VGRLGPGKSV LIHAGASGVG MAAIVVAFAL SAEVFVTVMG PNSDKQRAFL
EVSGVKKANI VHADSDLFTT VVCNRSGHGV DLVYNATQRH IEDNFKCVRR GGIVVQFSCR
LRSPPPVHVL SSDVSLVNFD LQNMLKYDAD YVAELVNELS RLVESSSDDL GNDLPLPEPI
INIDINRVKE AFGLIEKNPF FGLVSITGGP DATPQVDMAI KKTIKPLHQA LSGTDTYLLA
GGLGGLGRSI CELLVKNGAR HIAFLSRTGT SSEASQRFFK DLCDKGIDAR VYKADLCDAE
ALTKVIKEEI CQEMPPIKGV FQCAATIKDS IFSNMTYSDW TEAIRPKTVG SDNLVRAISA
NSEDPFFIFL ASSAGVIGNR GQANYAAGNC FEDALALNLR LEGKHAVSID LGPVLGAGML
ADDEEILDIL RANGFYGIRH EDFLTMITHA ITAEISPGTP MPGRVIMGIG SGGLVRQNQP
ADPYWSRTAL YSYLNLVDTS NPDLKVVDAS NDFDLKSLLS CCSSTDVAAE IVTTGLSLML
AKAMNMLPEE IDTGKPPNVY GVDSLVAVGV RNWVVTNCGV EVSVFEVLSE RTVAELAREI
ARRGGFGDED K
//
