ID I1RDS5_GIBZE Unreviewed; 2465 AA.
AC I1RDS5; A0A098D4V3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Chromosome 1, complete genome {ECO:0000313|EMBL:CEF73979.1};
GN Name=FG01790.1 {ECO:0000313|EnsemblFungi:CEF73979};
GN ORFNames=FGRAMPH1_01T04345 {ECO:0000313|EMBL:CEF73979.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF73979.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF73979, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF73979};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF73979, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF73979};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:CEF73979.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF73979.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4] {ECO:0000313|EnsemblFungi:CEF73979}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF73979};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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DR EMBL; HG970332; CEF73979.1; -; Genomic_DNA.
DR RefSeq; XP_011317630.1; XM_011319328.1.
DR STRING; 229533.I1RDS5; -.
DR EnsemblFungi; CEF73979; CEF73979; FGRRES_01790.
DR GeneID; 23549206; -.
DR KEGG; fgr:FGSG_01790; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G04345; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; I1RDS5; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000070720; Chromosome 1.
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; 3.40.47.10; -; 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; IPR013149; ADH-like_C.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000070720};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..470
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2381..2458
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2465 AA; 270330 MW; F67CACD42F1DFC29 CRC64;
MINDTGPEAI KQNGYAATNG SQTNGGHSFE TTGNVAVNGN STNTPPAEPI AICGMSVRLP
GGLHSPQDLW EFLVSKGDAR GPVPESRYNA SSYWSEKMKP GTVKTQYGYF LDESIDIASV
DTSFFTMRKD EVGKADPQQR QMLEVARECL EDAGEFDWKG RPIGCFMGSF GEDWVEMFAK
EAQQYGIYRV MGYGDFMLSN RVSYELDLMG PSQVVRTGCS ASLVALHEAC LALSRGDCEG
AIVGGANLIM APGMTVAMTE QGVLSPDGSC KTFSADANGY ARGEAISAIF VKPLSAAIRD
GNPIRAVIRS TASNSDGRGT AGGIQVPNDI AQETLIRRAY KMAGIDDYSQ TAFVECHGTG
TAIGDPIETK AVGRVFGPSG GVLIGSVKPN LGHSEGASGL TSLIKAVMAL ENRTIPPNIK
LSQPNPAIPW TSCGLSVPTE PTTWPSSKHE RISVNSFGIG GTNAHVIIDS ACSFNIAHPV
GRSATAPQLL VFSANGTDSL RQMITNYENY AEKNPEKIDD LAFTLGHKRE YLPHRAFAVA
SPLGPITVSP VSKVGNKPNI IMVFTGQGAQ WPQMGSDLMH SPQFPTFRKA IAALDAHLHS
LEDGPDWTIE EELQKSPKIS RLGSAELSQP LCTAMQVALV DTLASIGVRP EAVVGHSSGE
VAGAYAAGAI TATEAIKIAY YRGLVTKRQT KPGSMAAIGM GAKSVEQYLQ SGVVIACENS
PSSVTIAGDT EAVESTIGAI KASKPDVMAR LLQVDMAYHS HHMKEIGDDY FALMQDKISP
KKPTKLFYSS VTGNTLTESH QFGPRYWQTN MESRVCFSPA VSEIINQGTI KNAMFLEVGP
HSALAGPLRQ IQTQRSSSFP YVSVLTRHKN DVECFLTCAG SLFNLNARVD LTKVIAKGSV
LPDLPRYPWN HSERHWYESR LTNEWRHREY KYHDLLGIRI PESTDSNILF RNLFHLDNAP
WIRDHMVGDD IIFPFAGYAG MIGEAIRQVT HVEEGFKMRA VRVSTALVLN EGKPVEIMST
LRRKRLTDSL DSEWWEFTIA SYNGTSWTKH CSGEATSQRE KLATAGTHKR FLRKVDIGRC
YESLARSGLN FGPDFQLLSE IRSDTVDQKA QSKVLGKSGE EVDYHLHPTV IDASLQLLSV
AVSRGFADRF DKTMVPTHID EMCVYRPTIT DSFDIRANAC YTSTGSVTGG GQIADSKGQL
VLTISDIKLT TVGDQNGGKP VEPTARSEWA HHVDFLDPKT LIKPAIDRSD HMPDLTRLSN
LCMVHTKRSI SELDSTTEHM HKYKAWVDRQ IKIDDIGSLE SLSNDEIESQ IDAMMTSLKQ
TSAKDAAIAI EKVFANTSDM FTGSKESLDI LLSDGTLNRL YTFMDQCDES ELFKYLAHSK
PNLRVLEIGA GTGGSTSQLL KYLAPVGKVL FSNYTYTDIS SGFFESAKKR FNEFPNMEFA
TLDISRDPSE QGFDGREYDL ILATNVIHAT KSLNESLKNV RKLLSSDGRF LLHELTPTSK
WINYIFGTLP GWWYGEADGR RHEPYISVER WGVELQAAGF EVPDAAVLDT AEPNQLNAMI
LSRPAIKRDS TKAVELLTIS DVETEGEVTL RKSLEKRGHS VSRRTIFDQP ITTGHSIIAL
LDEDEPFFEN IDNERFEAFK LLTSNLKDIS LLWITHVSQM QCSDPRFGQI MGISRVLRSE
MLLDFGTCEV DDVVASSEKI VDVFERFQTR KEDESLKPDY EYAIVNNTVH VGRIYPFSAQ
DNLLMSSQDD PVALRTSKPG RLDALHWARY QSPTLTGDDV EIKVQAAGLN FKDVLCAMGI
VDGENGFGLE GAGVVNRIGP NVSDLQVGDR VFFIAHDSFA THVTMSENLC EKIPDDLSYE
DAATMPCVFA TSYHSIFNMG NLKKGQSMLI HSACGGVGIA TIQLAQMVGA KIYATVSSEE
KIKYLQDNFG LDRSCIFNSR DDSFVQQLMH KTGGEGVDLA LNSLSGELLH ATWKCIAEFG
RMVEIGKRDL IGSGKLDMSP FLDNRTYSCV DLDQLCYKRG RVAKELLKDV IRLYKDGHIH
PIRPIKVYRP DNILDSFRFM QQGVHLGKIV VSMDTTSGPS LKVESRKQIV TMDPSASYLL
VGGLGGLGRS ISRWMIQRGA RHLIYLSRSA GTNEKHRDVQ QELESLGCKV DFVQGSINDL
DNVNAAVARA DGRLKGVLQM SMVLADQSFG RMTIDEWNTA VDPKITGTWN LHNATMSVNA
DLDFFILFSS LSGVIGQPGQ VNYAGANTFL DAFSKYRKGL GLPACSIDIG AVEEVGYLAE
NNSIMQKLKV TGFNGTVSEH EFLDALGAAM AKTSDDFCLG FRPDVSLSDP SNRSLWKKDI
RMAAFHNNGG TTGASTGATN DELKSFISKA KQDPSILKQA ESAHLLAREI GKKVYGLLLK
PVEDLQTASS LSELGMDSLV AIEVRQWWKT IFQFDISVLE MMAMGSLDML GAHAAKGLQH
VFGST
//
