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Database: UniProt
Entry: A0A136IKP0_9PEZI
LinkDB: A0A136IKP0_9PEZI
Original site: A0A136IKP0_9PEZI 
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
//
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