ID G4UJY2_NEUT9 Unreviewed; 2628 AA.
AC G4UJY2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGZ72587.1};
GN ORFNames=NEUTE2DRAFT_106406 {ECO:0000313|EMBL:EGZ72587.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ72587.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ72587.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL891217; EGZ72587.1; -; Genomic_DNA.
DR STRING; 510952.G4UJY2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; LRPQWRN; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 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 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; IPR011032; GroES-like_sf.
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; 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:SF50; HIGHLY REDUCING POLYKETIDE SYNTHASE SRDA; 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; 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; PS00606; KS3_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..436
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2548..2623
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2628 AA; 283997 MW; 60155DE822E214BA CRC64;
MSSTFKHDTH EPVAIVGMAC RWPGGVHDPS QFWEFLRNKV NGWKEFDDPR FSSTGFHHPN
SDRPGSMSMK GAFLAEQDAR LFDHTFFGMT GLEVETMDPS QRKLLEVAYE AIENAGETWE
SVSGTRTGVF VGNFCLDHWM IQSRDWDNPR PYAFTGAGTS ILANRISYIF NLQGPSLTVD
TACSSSMYAL HLAVNAIRAG DCDSAIVASA NWIADPGVQI ALDKLGALSA SARCHTFDAR
AEGYARGEGF GAIYLKRPSL AIANMSPIRA MIRGTAINSN GRTGGITRPS ANGQETVIRE
AYRNAGNLPF RDTSYFECHG TGTYVGDPIE VAALGRVFAP ERSSDDPLLV GSVKSNVGHG
EGASALASIM KVVLALEHGA IPPIYDLQTR NPNIDFEGAK VQPVTEVTPW PKDRLQRASI
NSFGYGGANG HCIIDHVNIV LPDYVAPGIY KRSTRDTTNG VNGHINGRSG TPSHRPIIQR
PKMTASPNAN TRSLVLLPLS AHNENSLELN LKALSQVVDK LPLADVAYTL GARRSKFAQR
SFCIVEKDKV VEGLAAKSRV VRAPLQPTNV GFIFTGQGAQ WHAMGAQLFE YRVFSTAIQY
LDHVLSSLPN GPDWSLEKIL SGDCDAALIQ RAEISQAVCT AVQVGLVDLL ASWSVRPHGV
AGHSSGEMAA AYAAGRITAA EAIVAAYFRG QAVSRNRQTG AMLAVGLGPE AVAKYLSGLE
DQVKLAAINS PGSVTLSGDP AAVDSISKAL AADSVFNRKL QTGGNAYHSH HMLPIGREYI
EMLSQGLQHI QKLGLASPEQ RYPKALWVSS VKPNKDTTGS FDDPSAYWRA NLELPVQFSE
AVASLVRNEN VTIHALVEIG PHPALKSPVE QIVKAAGKAV AYASTLKRQE DARLSMLQLA
GTLFTLNTPI DLAAVNAVDG EAGHSEGLEH GSTCLDLPPY QYTYNGLNYH ESRASKEYRY
RSVLRHDLLG SKVVGNAKLR PQWRNILRMK DVPWLGDHRL VPDAVLPGAA YIAMAVEAAL
RIYDEFAKPF EVKGFSLRDV VIKKSLVIPE DDYSVEILTS MELVDFATAQ SPAWATFSIS
SVGRETNEWT EHCTGRVKVV IQETGYDIDV EHGRVAAPYA PRAVDVKAWY KKFLDIGLGY
GPVFQPLSDI RVDAASNLAV ATVHLQPGIG VMKGGESRYA VHPASLDGAI QLGLVACHGG
RPSEATTAFV PVQFSGLYID SSLAHGGETC TVVARGQRRG IRSAHLDLQF LGADGKLLLD
VESLRCVSFS SEAKPVDRAF SSPYTRLVWK PDIRKLSNSQ ARQIYPPPTK NVDKAPLWGI
TNKVAHFIVY SMYETFGRQA DRPQPSGEVG HFFDWIIRKG ESDHSEMMEE ARELAAKGAL
LQQIEELVAQ APDIMEVKIA KLLHDNAADI LYERKTGMEV IIGENLLTPL YQEGLLMTGI
YPQLSIVLAG LAHAKPNLRV LEIGGGTGGA TRIAMKAFNG PNGIKAYRDY TFTDISPGFL
SAAKESMADL RDMNFSVFDI EEDPVAQGYE EQTYDLIIAC QVLHATSNMT KTLSRCRRLL
KPGGRLVLVE TTENFIVPGV VVGTFTGYWA GIPDGRVDAP FQSLKDWDRS LREAGFAGLD
LVLDDFPEPH NTTSVILAKV PEQEPEPLPE TQSATTVHVV HGGSNGTPVL VDHICQELQQ
RGTNVKAITF NDVTKELSPG SRVVALLDES HLLIKANEEN LATMQYLARS ATSLVALTSC
GTIKGRAAEG ALISGLLRVL QTENPSSQYM SIDIDVDNFE VEDAAEANEL ARSIVDGECD
LFRQASGSAS VFVDGESNGG DPADREFAWQ NGCLWVSRHV PDAGFHSQYG LETRSMKPEL
RPIGSPSQTG GVRAAFETPG VLNSLYFIPY KDLLQPLPAD FIDVAVDAVG VNSRDLEHWA
GRVDGDYLTS EYAGVVTAVG SRVHDIQVGD RVYGVGKGQF GSVTRVPAAF ATKLQPKDDM
IRMASMPLAY TTALYALDHV AHVREGQSIL IQSGAKDLGL AAITLAKAKR SQVFATVETA
EQGMFLVEEL GLPASHVISI LDSKQLQRAA QETRKGKFEV VMATAARGEL LSLFLQVLAP
LGCLVDIGGV DGQTTPVVGQ MSLPHNATYA SIDPFAVFDS DPLLGAELMQ SVDDYYRQGV
IGPVPRITAA DVGQLSSALG DFGTMSGKLV VSFKNPESLV RMAPYAPTVK FDPEASYVVT
GGLGGLGQSL VRWMVGRGAR HLALLSRRTA SSVPSVQELL NGLAGRGVEI QCFACDVSKE
DEVTSAIKAI SAVRPIKGIV HAAVSYRDLT FDKLSPERWN EGLSAKVAGT KNLHKATLSM
SLDFFVMTTS ALSVYGFATQ SAYTAANNFQ DAFARYRRQL GLPASTVSFS LIKDVTDVGS
SGITVDMFER NKALTLDESQ FLALLEPAFL NNRTVTEETS AGQWSGQDDD GLSVANLHTY
LDPRAMAAKR REEMASEASS SSSTVPPRWY SDGRVSLMMR AFADAQRHSG RSQDAADEGS
NKNTIAHLRA ELEAAVREGE AGRGRTVALV QDAITKVVAE MLFVDVESID PAKSVAELGV
DSLIAAELRN WFIQALGTNI SMLDLLDPSV SISTRASTIA DKALSATA
//
