ID A0A136IKP0_9PEZI Unreviewed; 2580 AA.
AC A0A136IKP0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXJ85338.1};
GN ORFNames=Micbo1qcDRAFT_223400 {ECO:0000313|EMBL:KXJ85338.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ85338.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; KQ964285; KXJ85338.1; -; Genomic_DNA.
DR STRING; 196109.A0A136IKP0; -.
DR InParanoid; A0A136IKP0; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000070501; 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:0008270; F:zinc ion 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; 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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; PF08240; ADH_N; 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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 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:UP000070501};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..432
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2489..2566
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2580 AA; 281033 MW; 96FECEC8199F653C CRC64;
MSDSAIAIVG VACRFPGGAE SPDEFYDMLV QGRDAWSKIP STRYKGEAFT HANRDRPGSL
VTDGGYFLKR DVSKWDAPFF ATSAVEATAI DPQQRILLEL AYESLESAGI PIEDISDTEA
ACFVGGFTHD YKNIVSRDIH ATPQYGITGC AQSLLSNRLS WFFNLRGASV SVDTACSSSL
AALHLACETI RSGSNKTRVA LVGGTNLILD PDDPTQLNQM GFLSPDGRCF AFDSRANGYA
RGEGICMMVV KHIDDAIRDG DPIRAVIRAT GLNQDGKTAG IVLPHQDAQM ELIKTTYELA
GLDPADTQYV EFHGTGTKAG DPTEMGAIAR TISKARTSKV PLYCGSVKTQ IGHTEGTAGI
AGVLKCALAL ERGLIPPHLN LIKPNPRLQL DAWNIVLPNK AIPWPESETG LHRASVNNFG
FGGTNAHCIL DDAPSYLRSR GVAVEKHVRL TDGAWSTARH PRIFALSAPE QEATARQRKG
LSEYLKMSPE NIDDLAHTLA SRRSKFQWRH TVVARDLDEL RGTLEDDAIK PAKVLAQNNV
AYVFTGQGAQ WYAMGRELLA YEVFAASVTE SAAMMMQMGA SWNALKELLA SETSSKINQA
EFSQPLCAVL QIALTDLLAD WGVKPHAVLG HSSGEIAAAY ASGGLSKLDC LKLGYHRGIV
SKHAKALHPD GGMMAVGLSP ADVHAYLDQV EGIVVVACVN SPASVTLSGD KTALLQLQKI
FNDKSVFNRL LQVETAYHSP HMRSVAEEYR NAIADIKPRT DATTSFYSSV YSRLITPAEL
GPDYWVANLC SPVEFVGALD AALYKDAAKR VVKPKSKGVQ TLLELGPHSA LAGPIKQYKN
MRTDFDTVVY ETALLRGKDA AVTAVTLAGK LWARGVPVNL AMVNEPSGKP AAHNTLHTLP
SYPWNLATSY WHESRRSKNH RAPPAPRHDL IGARIDDSNP LEPIWRNYLR VNELPWLRDH
KINGDIVMPA AGMICMAIEA ARQIAETDGT ADTVKGFALR DVCINKPLVI PEAADAGVTG
GIEVLLNLKR RKLGMGSGAG IWHEFALYSA GSGGDANFVE HACGLIELQQ SRGATEVDGG
REQVLEIQAR RAKYKDFGLV CNDPVATASH YGFCDSQGLQ IGPLFRGLTS LAKRDNNVIF
QATVQDSKAM MPAQAESEML VHPATLDALL QVMLVAIPRQ EDVPKQVWIP SKIKEINISH
DVLRKPGEVL HGTCESSRSG FREMVGTIMT GDDKFDSTAG ISMEGVTFTG LGSAQSMPHG
VEQGEQARLK LCSELQWKPD LDTLTPENEY SVLSEGNNLA GEDLARFCTQ SHKVIQVLCR
RSLEKLSTID RASLPGYLVQ FADWMRTRSE MGDTTALSRS QEDDLLADFA ASYPFDGKFC
MHVFDSLEAI FKQETTGIAT LMQDDMLNRF YRETYACDLS IRIFQNWFDL KGHKQPGMKV
IEIGAGTASM TIPALKTLGG QDGETPRFAS WTFTDISAGW FENAKKVLED WGSRVEYKRL
DVETDPAEQG FELGQYDVVL AVNVLHATKD LKRTLEHCRS LLKPGGKILL GENTNVMDLS
SFIFGTVPGW WVSEDGRKDG PLISEAEWDV ELKKAGFTGT DIAAQDHNDP VAHRMSMLVS
TRLDKDSKTT PPKDLIILEP STASSHVRHL AQLLSKKLQA LGHKTQVQTL EEASRSEEGK
SFGKGKSFVS LLEYDESFFE ELQEQQFEHV KEVLLHCAEM LWVTRSDVKD GPAHPSKRIV
SGLLRCIKTE DATRHVYELH LTRDRLGEAG LESTAEAINT RLSSIWSAAV LSDNRGRDES
ETVERDGVLC IPRYFPQKTL NRSLLLKETG ASPEVDSLVQ PNRDLKLTIG TPGMLDTLHF
IDDDAPTKAL GEEEVEIKTQ ACAMNFLDLM IAMGQVQHPI LGYEAGGLVT RVGSKVNRFK
KGDRVLYMGL GAMRTTIRAH QLSVHAIPSK LSIEEAVTIP IAYTTAYQSL IEVAHVRKGE
TVLVHAAAGG LGQALVQICK LLGATVLATV GNNDKKQAVV DLGVAPEHIF SSRDLTFAQG
VKRVTGGKGV DVVVNSLAGE GLRKSWECLA PYGRFIEVGK KDILGNSGLD MRPFLSNTLF
AGVNLEHMMS HDPQRGAELV AKVLRLFQHG DIDLIKPISV YDFSDMESVF RQMQRGTHIG
KLVLKITPES QVPVMPQLNI PCSLNPNATY LLVGGLGGLG RAQAMLLAEH GAKHIAFISR
SGDAKPEARE LIARLREMGI NAHSYAADVA NKSQLKEVTD SLASTMPPVR GVMQGAMVLQ
DSLFHRMTYQ QWVGATRPKI QGTWNLHELL PKDLDFFISL SSLAGIIGSI SQSNYAAGNA
YQDALMHYRK AQGLAATSLD LGLMRGIGYV EENEDAAAHT SSLKFTAVQA DQFYHIVRAA
MTGSTTGGDR AANPMPTQLL LGGGSGGSQE ASHAAGISGD YYWLRTLAHF AYMQLMDVRL
DSASGSAAAG QGKGNVLIAQ LRASANIDQA TETVTQILLE KIAKSIMTSA SDIDTSKPVY
SYGVDSLVAV ELRNWVGMEL QSEINIFDLT SSAPITDVCR KIANRSAIVA EALRHQLESH
//