ID W3WY57_PESFW Unreviewed; 2583 AA.
AC W3WY57;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETS78082.1};
GN ORFNames=PFICI_10144 {ECO:0000313|EMBL:ETS78082.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS78082.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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DR EMBL; KI912115; ETS78082.1; -; Genomic_DNA.
DR RefSeq; XP_007836916.1; XM_007838725.1.
DR STRING; 1229662.W3WY57; -.
DR GeneID; 19275157; -.
DR KEGG; pfy:PFICI_10144; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; W3WY57; -.
DR OMA; IATNFMA; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
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; 1.
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; 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:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2496..2577
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2583 AA; 283566 MW; DBFCF9BB99CCBD05 CRC64;
MATTMEPMAI IGFSFRLPQD AQDEARFWEV MQNRENLAGE WPETRLNVGS LHDDDSPKRP
STLAARGGHF YKEDIAGFDA PFFSITANEA MAMDPQQRWA LELAYLSFEN AGLTMPKLKG
SRMAIYASTI SDDYSKILSK DPDDLPRMSA TGLAPSTLPA RISWYFDLQG PSFHLDTACS
GSMVSLDLAF QSFRNGETDC ALIMGSSMFL TPETSMMLGQ MNFLSPDSRC YSFDHRANGY
ARGEGLIGLV VKPLSAAIRD GNTIRALVRS TGTNQDGRTP TLTQPSTEAQ ERLIRSVYKK
ANLDFTKTRY FEAHGTGTPT GDPIEMESIG KVFKSSRSKT EPLYVGTVKA NIGHLEGGSG
LAGILKSVMI LERGIIPPNA LFEKINPRID PDALHIAVPT ESIDWPTNDL RRISVNSFGI
GGTNGHAVLD DACHYLHDHQ LQGHHNCFRD RETPFRNGVD AHIGSTQATQ NGGTQSHDHV
NGHVNGHDTT LNSVSASEPP KLLVWTAFDE ATIRQVTERY SEYLKGYIGS DKNLLSNLAH
TLSERRDHLR WRSFAVADSG SNVSDSDAFR VAKPTRALSG SYGINFLFTG QGAQYAGMGM
GLMKYAVFKK TLQDFDDALA RLGCPWSLFG SIDKLQDGQS IDQPEYSQPL CTALQIALVE
LLKTFGITPT AVVGHSSGEI AAAFTAGALS FDSACQVAYH RGRLACKLRT ATSDAPGAML
SANISPDQVS EYLDKADQET VHVACVNSPL NITLSGSALT IDKLKQSLDR EGIFAQKVNT
GIAYHSPAMQ AIAEEYAEVL ESIRPPVGES SCTGVPMASS VTGHIIPANL LSTPRYWVDN
LVSQVKFSDA IQTASELLGA GRFGASNGGF LEIGPHAALR RPVNDTLRQS SSHVSDAENI
IGYHSALYRS KPAVQSLMEM AGQLFSVGYP VIVSAVNQEL ESKPSMLTNC PSYPFNHSRK
YWSESRLSKD FRLRGDSTWS VLGRRATDWN PLDPRWRNVL TLDSAPWLGD HVVNNNIVVP
GTAMLVMSLQ AVHQLATPER PLAGFLIKSA RFSSPIMLAN ADSKTETMVQ VHPVRKSYEK
EVRSFDVKIY AYSNERWTEC FEARVMLQYA TDLSNLDGDS EQMIDHERVK EQCQETAAAC
TRKITPRAFY TFLNEYIGLK YGKTFQLLED IRWDGKNSAV ASVGTSTTEP LMAGDYPQPT
VLDAAIHLCL AQLSRGLTLT GATLVPHEIS NAWISATGWK CSSVQLLSEA AYRSDSTSAE
MAVKILDSEG TPLCSVGQLK LAAVSKSGNS QSQEKVHLYK IASDAQLSML SPEKLQALCL
APTAPEPQYL GYAKALGPAL LFFANKAMSQ LGPQDLVNAP PHMEKYLSSL KPLLAENKHE
IMLTESDYFN VLEQYAGKTE SWRLLPAVAQ NLVPLIKGEV DVLELFFDDG MVEDYYASIF
KELLDDRLRR FLRLVSHEKP ALRILEVGAG TGAMTRGILD TLHQFEIEEG SMRFAEYVYT
DISPGFFDHA KTKFQQFEDR ISFQKFDLEK SAQSQGLVAG SFDLIIAGSV IHAVSELNTT
LQHLRGLLND NGRLVLLEIV SPQNPCVAVP WGLLPGWWLA KEKWRSTNPL ITEVQWDHVL
KEAGFTGTDL VLRDHEDPKH GICSIMISKA DAQHSLSNGS TLQGTTQSSS THLVVLFDEQ
SSLQAELAGK LVHSHGGRLL PFSKLGEAKI DSRDVVISLL EIDRPLLSII QEEEFSGLKS
VLTQAKDIMW ATAVNPESPA YALYSCAKGF LRSLRSEAIE KHIVTLSIET SDPAANSAHY
LEYIQESLRV SFEGERARDT EYIVRDGVFY TERLAQEIEL ENRTQSSGQL QPRIEPWSGG
SPVKLDIPVP GLLDTLRFVE DTEYVNDLSP EDVEIEAKAW PLSFRDIFIA LGRLEGETPG
FECAGVVTRV GTNVTDFRPG DRVALASPGC IKTYPRAHMD YVQHIPDDAS FEDAASGVNP
AMTAYHALIN QARLEEGEKI LIHSAAGSTG QMAIWIAKSV GAEIFVTVGS DEKKQLLIDR
FGIAADHIFY SRNTTFAGGI MRATDNRGVD VVLNSLSGDG LIASWDCVAP YGRFIEIGKA
DISENTPLPM SGFKKNVSFC AIDLHHMALT NRALVKKLFA KVTDLFSRNI MQKPYPRHVY
TIWDIEEALR YMQSGKHIGR IIITADCEKS GTKLVRNSTS WTFDANASYV IAGGFGGLGR
SMGLWLATRG AKNLVILSRS GTSSATSQSL VEELKELGSN VYAPRCDVSS STDLANVIEE
CGRNMPPIKG VLNAAMVLQD AIVENMTHAQ FRTAVQTKVQ SSWNLHNLLP PNLDFFIMLS
SLSGIYGSAA QSNYAAGCTY QDALAKYRIA RGQKAVSFDV GWMRTIGIIA EKEDYRRTRE
VTRDMVPIEE KDFLALLEVY CDPSRTLQSL DKAQLLIGAR TPAEYKERGF ASSRRYAMPL
FMGFEQSFGS TSGAASGGQR DMALMDDFSV LFQKATSAEE KSAIVVKGLA GMLARALMIP
ADDISQTRSL SDYGVDSLMA VELRNWISNK FDTNIGVFDI MGGKPIHAIG DLVVSRSIMD
ISG
//