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Database: UniProt
Entry: A0A136J229_9PEZI
LinkDB: A0A136J229_9PEZI
Original site: A0A136J229_9PEZI 
ID   A0A136J229_9PEZI        Unreviewed;      2177 AA.
AC   A0A136J229;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Melanin synthase {ECO:0000313|EMBL:KXJ91143.1};
GN   ORFNames=Micbo1qcDRAFT_148260 {ECO:0000313|EMBL:KXJ91143.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ91143.1, 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.
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DR   EMBL; KQ964251; KXJ91143.1; -; Genomic_DNA.
DR   STRING; 196109.A0A136J229; -.
DR   InParanoid; A0A136J229; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          381..813
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1656..1733
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1787..1864
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1625..1644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1736..1791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1736..1752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2177 AA;  235944 MW;  6FDC145D3845CD13 CRC64;
     MTDHLSFLLF GDQSLDTHGF LADFLKSGRP GVLAREFLRQ VEGALRDEVD SLPRSERASI
     PVFRTLPQLN EKYHAQATKT PAVDSALLCV SQLVHYIDLS EKDHETPTPV TNRILSGLCT
     GLFAASAIAS SPSLSTLLPV AVQVVLMAFR TGNYVSSMAE RLRSASNGQE SWTYVLPGVK
     DTEACSSLLA FHQAEKIPAA TQVYISAISG SNVALSGPPA TLKLLFSKIS FDSRPTSIPV
     YGPYHATHLH QFADIRRILR LDDEITKNAL ASSRPQSCII SSVTGVAFPQ KDTSQLLAAV
     THEILNEPLY FQKALNGCVE YAKSFNGSRA VIIPCGPTQA ASTLANAITS QTGLSVELRS
     PPQVNRQDGG ATIGNHGSLG RCKLAIVGMA GRFPDSASHE ALWDLLKKGI DAHRVVPGDR
     FPHETHVDPT GKALNTSHTP YGNWIENPGH FDPRFFNMSP REAYQTDPMQ RMALITAYEA
     LEMSGYVPNR TPSTRLDRIG TFYGQTSDDW REINAAQEVD TYYITGGVRA FGPGRINYHF
     GFSGPSFNVD TACSSSAAAL NVACSSLWNK DCDTAIVGGL SCMTNSDIFS GLSRGQFLSK
     SHNCNTFDND ADGYCRADAC ASIIIKRLDD ALSDKDNILA VVLGTQTNHS AEAISITHPH
     GPTQSVLSSS ILDEAGVDPL DIDYVEMHGT GTQAGDGTEM ISVTDVFAPR NRVRPADRPL
     YLGSIKSNIG HGEAASGVTA LIKVLLMLKK NAIPPHIGIK KEINKTFPSD LGARGVNIAF
     HTTPFARSDG RARRVFVNNF SAAGGNTGLL LEDAPKQRAA STDARTHHVV SITAKSKGAM
     IRNAENLIRF MEENPQTPVA HVAYTTTARR IQHYWRMNVS ATSLVEAKDN IQERLKATFV
     PVPPGQPQVA FMFTGQGSHY AALGVDLYTH HSVFRAAMDD FDHLAQIHGF PSFMPLINGS
     EKDVQKLSPV VVQLGLASFE MSMAQLWASW GIKPSVVLGH SLGEYAALHV AGVISASDAI
     YLIGVRAKIL AEKCTAGTHA MLAVQGSVDS LITLGACTGN VNIACINGPR ETVLSGPTRE
     IAQAATLLSS EGLKCTQLMV PFAFHSAQVE PILDDFEDFA RSVQFQPAQV PIISPLLGKL
     VEDETIDSSY LRRHARDTVN FLGGLVHAQQ AGVIDERTIW IEVGPHPVCA NMVKAAFGAT
     TLAVPSLRRN ETTYKTLAST LCALHSAGLN LDWQEFHRDF DASVRLLDLP AYAFDLKNYW
     LQYTGDWCLT KNRGSLGASS VKAIEPAKPK LSTTSVQKIV KEEVDGDCAV LETESEMTEE
     NLRKVCAGHM VNGTALTPSS LYGDMAITIC EYAYKLLRPD AADIGVNVAH MECPKSLIFN
     TKADSQILRM RATVDVAACK ADVVWTTGEG AQLVEHAMCK VSFGKKQEWL SEFERIGYLI
     KSRIDLLHAA ESRGDASKIG RGLAYKLFAA LVDYDRRYRG MESVILLSES CEATAKVVFQ
     TTPEDGTFRV APYWIDSLCH ISGFIVNGTD AVDSREQVYI SHGWGSMRFA EDFDVSTPYR
     TYIRMQPIKG SKMMSGDAYI FNGDKLVGIT GDIRFQAIPR KILNIVLPPQ GAAASAVSAR
     PERTAAVSRS TQQRQVPGKA RKQLTSSNLK AVSKTLAKTS VAEQVMEIIS KETGVGHDEL
     DDNIAFSDLG VDSLMSLTIS GRLREELELD ISSHAFLDYA TVGLFKKFLA QFDSTASSSS
     DPGSSGTSGL SDTDEEGGLG ECDSDITTPP GESEEGSVNC DEGMPGSGNS ELRRIVRETI
     CEEMGVEMEE VVAAPDLAAL GMDSLMSLAI LGTLREKTGL SIPSDLLGHN PSLKDIERTL
     AIEDKPVPRT APVKEVKIET EIAVKSSSVV NSNTKTIVAT VPPAKTPTTY GDAYELRKAT
     SVLLSGNHRT ATKQLFMVPD GSGSATSYTE IADLGLDTAV WGMFSPFMRT PNEYKCGVYG
     MAAKFIEEMK RRQPHGPYAL AGWSAGGVIA YEMVNQLTKA DEEVSQLIII DAPAPITIEP
     LPAGLHAWFA SIGLLGDGDS PTSARKIPEW LLPHFAASVT ALSNYTGDPI APEKCPKVLS
     IWCEDGVCKE PTDPRPDPYP TGHALFLLDN RTDFGPNRWD EYMPLDKMTF RHMPGNHFSM
     MHGELAKQLN GFLKECF
//
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