ID A0A1S8AAG4_ROSNE Unreviewed; 2102 AA.
AC A0A1S8AAG4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative polyketide {ECO:0000313|EMBL:GAW27057.1};
GN ORFNames=SAMD00023353_6500350 {ECO:0000313|EMBL:GAW27057.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAW27057.1};
RN [1] {ECO:0000313|EMBL:GAW27057.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAW27057.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF977510; GAW27057.1; -; Genomic_DNA.
DR STRING; 77044.A0A1S8AAG4; -.
DR OMA; ETEFWLH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000054516; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 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; 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; IPR014031; Ketoacyl_synth_C.
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; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; PF16197; KAsynt_C_assoc; 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; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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:UP000054516};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..153
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2015..2095
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2102 AA; 228858 MW; BC139DFE1A630027 CRC64;
MGITHPSAKG QEQVVRMAYQ KANLDPNLTA YAELHGTGTP VGDPIEVRAI SRALNDRRPE
DRPLLVGAVK PNIGHSEAAS GIFAVMKAAL MTESSIIPGV AYFQNLNPAI KEKEWNVKIH
ANTAAWPTDF PVRRTSVSSF GYGGTNGHVI IESIDSLYPW YRHAGKKQKT NSPPSDRAFL
LCLSAHDKPT LLRNVAAVGA VANNYNLTDL AYTLNLRRTK FAHRTYVVAR EGREAESFAL
ATSQAGTAAK KIGSIGFFFT GQGAQWVGMG RLALQEFPVV MDTIQHLDRI LSKVHPKPSF
SLVEMLLGNN EDNAKRINDA DVAQPLSTAI QIAIVDLFAQ WNITPEVSIG HSSGEIAAAY
AAGLISAPEA ILVAFCRGRA VTACSSSGSM LAVGLGADEV GKYLSSFAAE DVCIACENSP
SSITLSGRQK PISQLKDMLT EERIFARELP TGRAYHSPHM APVCDVYDCM LAEALDEVSE
DDLLWRRQRS GMISSVTGEI VDCSSESLLP GYWSANLRNR VLFNTAVQHL GTNSEFESIT
HMIEIGPHSA LAGPFKQIRL SNKNIGNRIT YVSSLKRLEN DADGLLRVAG SLFVAGHAVD
LEAVNMANDG GIKNDAGKQK TKQLLVDLPP YQWNYEKRYW AEPRASAEQR ARVYPRHDLL
GSRVSGLSKK SASWRNVLRQ RDVPWLKDHN LGGTVIFPAA GHLSMAIEAL RQVCEIAGDS
FGGVKLRDVD IKTALVVPED DEGVEVILNL QAPTDASSKW YTFSVESPGE DGEWTVHCKG
RISAVGELES PPSNARVPVD ESALTQRVSG RRWYDAFHRV GFYYGKNFQG LRHARTARTL
HHATGDVTVR ECCAEEMQGE SRYLVHPSSI DACLQLIIIS INAGKHKEMP HGVVPIHFEE
VTLFPARLGE ETDVGHAIAW TDGFEGRRFN TNVQLTGGDD RLLLDIKSMI CTAYEAALPA
KSESMGGEEG KGPEPFSIMA WKPDIGTLRP GDADLLWPNI SNYEKLAKCV DLIAHRDGLS
NVLIIAQTPS RAACELVDAL IRMIPSNTTV TIGFGADGDE QNIPISDSVM PRVQKITLGL
DPENWATTND GSHDLVVVTS NVETSEISLY ESLSGLVGNA GWLVCPSINL PSCSLSPLSL
RIGEYSLLQK TSVNVPENDL QQHFDTRDEI TILSSCQDQS AQSVTKILSG TRSRYTVSEK
VISELPEGFD HPVIVNDLSG AVSASLLESE KHFEAVKKLF SSEAPILWIT RGVRQGRPGN
HSVAGGMTEG LLRVIRSEQA AVKVTLLDID FGEEPCDVSR AITHALSSTA TKDPGCETEF
WLHRSIMFTS RVHAHDELNR ELGQNQPQMM PLSGALKLAN KTAEGQFIFE PQGLVEQNAL
GEDEIEIQVA ASSWPSYSAN SRMVVLGSVI RTGESVWRDL LGKRVLAFAF DGLQTVFTTS
VYTVIDDEFD ESFHDSLLHT VSSLCPLIHM CLGNAKMERG DTVISLPGPE QDIRMLGNLS
RAMGWQLTVV TQDEGDAELY ATRIGLSANQ ILRTNDADVM NAFIQNQRTM SSSRVVTILA
HDFGARLAQE AWRHIPPSCR FLVLDEKPLE TALDPIPFSR GASFMPSSMR HVRESAKAAS
TLLATSLNLI KEHSSILGVE TAQGINCVDI EDARDITAKN VGKDQGISNV VVRYRSQASR
VLIVPKSKQL RLSSDATYLL VGCLGGLGRS LTRWMMEHGA RHFAFISRSG VDKPEAARLV
ADIQLSGAST QVLRADASDE ESIAQLVISL HAQRPIRGVV HAAMVLKDGM FEQMTHRSFA
ECVKPKAQGA LSLHRALQVA NIDPDFFVMT SSISALLGNT GQANYSAANS ALDSLARQRR
TAGLAATSLV LPMVLDVGVV ADNDAIEASL VRKGLYGIDE HEMLRGFAAA MMASRSSPSQ
RMGSNGGDLD NLRSTFTDDS QIIMGMEPRE LAASAVGESA DAYWHGDSRF RHTRAVMDKL
LRGDGSHGSS NKEGNGENNT FARSIKAALS ESHEALVKVI SEHIARRMSS ILMIPCENFE
LNGSASIASY GLDSMIGAEL RTWLFKEFGL DYPFQKLLAS TLTFEKLSGA VVDKMGLLAT
AN
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