ID W6Z7N3_COCMI Unreviewed; 2419 AA.
AC W6Z7N3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EUC45778.1};
GN ORFNames=COCMIDRAFT_5016 {ECO:0000313|EMBL:EUC45778.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC45778.1};
RN [1] {ECO:0000313|EMBL:EUC45778.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC45778.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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DR EMBL; KI963977; EUC45778.1; -; Genomic_DNA.
DR RefSeq; XP_007687651.1; XM_007689461.1.
DR STRING; 930090.W6Z7N3; -.
DR GeneID; 19124466; -.
DR KEGG; bor:COCMIDRAFT_5016; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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; 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; 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; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..452
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2323..2404
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2419 AA; 265241 MW; 413E741F87689D6A CRC64;
MAPFLNGDLS ANNGIDHNDK ADGSMPIAIV GMSFRGPGSA NNIETLFKMI CEKRESRTAI
PKSRWNNKAF YHPNFQRHGS HNVEYGHFFQ DDISKFDAPF FNMTREEAAA LDPAQRLLLE
TTYEALENGG IPLEKIVGTK TSVFVGSFAT DYTDLLTRDP ESVPMYQCTN SGQSRAMVSN
RLSYFFDLHG PSVTVDTACS GSLVALHLAC QSLRTGEANS AIAAGVNVVL NHEFMTTMSM
MKFLSPDGRC YAFDERGNGY GRGEGVGTVF LKPLADALKD GDTIRAVIRG SASNQDGKTS
GITLPNPVAQ EALIRDVYHA ADLDPLDTGI VEAHGTGTAA GDPLELRALT NSFCGTNRPE
DRPLVIGSIK SNLGHLEGAS GIAAVVKAVL MLEQEVILPN QNFEKPNPRI PFADRKLRVP
TEMQPWDSSG PLRVSINSFG YGGSNAHVIL ESTRTYLSSR GLSSAQKVPT HFLRHRYGVA
NASPKLAGAL MYENGDPPVD SVLPNHSRPK LFTLSVFDEP TAQQQIQTLV KHLQERGMSR
QAGFLDDLAF TLNERRTNFI WRASVVAASL KELIGALSRP TKFSRSLKSP TLGFVFTGQG
AQWCGMAKEL LEVYPVFKTT IRRIGKYLHS IGAPFNVEEE ITMDPKVSKI NKALYSQPMC
SAIQIALVEL LASWNIRPTS VTGHSSGEIA SAYAIGALSL EDAMTAAYYR GVCSTKMQEE
HKANGAMMAA GLSEEDATRF LAELKSGKAV VACSNSPSSV TISGDVSAVG ELQKILESKG
IFARMLAVEV AYHSHHMELV AEEYAKAIAG IRIRQGNGAK FYSSVYGREV GTEELGPSYW
VKNLLCQVKF TDAIRQLCLA PAIQSKRRQV KRHGVDVLVE IGPHSALAGP IKETIQSDPK
LKAADITYTS ALVRKMDAVR TVLDLAGKLS AIGYQVNFSA MNRPTADHSA SVLVDLPSYT
WNHSTSYWAE PRRSKAFRNR TFPRVDILGV RDENSDPLQL SWRNHLRTSE IPWLLQHKIQ
SSVVFPAAGF IAMAIEAAAQ RSKERLNKQV SGYQLREVNI GTALLLPEQE SVETILTLKP
IRDSSKRHSN TWSEFHIYSV TNDNHWTEHC HGLISVQHQR QQDSSGGTRL ITQSSTVDEF
RTTLPMPEFY EHLSSIGLDY GEVFQNLVEA HSCPDKLTGV LQLPATTSTM PLDQEHTYVI
HPATLDAILH TVFGALSADT WLQDPAIPVF VSSLFISADM PFQAGHLLKA NATISTRDNQ
TMKTNILVTN DNNNTPVVQF SELDWRFLPT PIEQEDVVDS HHVAYTLDWA ADVEFLEFQD
AQQISHSAAD YIHLLGFKNP EISVLDISAS SSTTLSFLKA LEIGNSAAKQ RCRAYTVANA
QKTKTVLVSD TPNLAYDLVT KKSLDLEIGP QKPDFELESF DVIIVSASLV PSSSPDKALD
HIKSLLRPGG RLIVLHEGAM DQDPILLEWK ISLQQTGFTN HKLTELDYLG ERVDQGSLFV
AYPSQELHPA APEIIVMAED HNQAIDTGYL ASLLGLDPGK VERGTIHDVA PAEKIRIVWD
PAGELLSSPS IEQFEAVKRI FTQSDKLLWV TSGRGQGSRR PESSMIAGLA RTARTENGAA
RLVTLDLDDE DKLSQKDTVN IISAVVKRSF LGNEQQDMAE SEYVERKGIV TIPRLSVDDT
LNQALDSYLN SMAKEIQLLH HKGITFCLRD RPHAQEPFSF QEITVDEELK ENEIQVEVKA
MTLVSGNSVD IFTQDISGVV VKVGGQVLHL SPGDRVFGAV SNRVSNSYKG RASSFRKIPD
GVPFEIAVSY PTAYSTAYHS IHRLANLSKT DKVFVSSAVT PIGRALIDLC SRNGAKVYVG
VSNDKEALFM ESTLHLPKDQ IVYNNEQHSV AALVANTEGH GMDVIFNTLS GEILQTCWNC
IAPYGRFIEL GTQDLIENSR LEMANFRRNT SFSALDFSRL QQERLALADE IWGQTLELIS
NDSFSSAVPN LQLFNSEGIT QAFERLMDEE NTDHVVLTFN PSDRVKVLPT TTEDQLFHAD
ASYLLVGGLG GIGRATASWM VEHGAKNLIF ANRSGMSKQE AKDTVHALKS MGARVHVQKC
DVSNTDSVRK LVDECANQMP PIRGVIQGAM VLRDMLLEKL TLDDWNAVVR PKVHGTWNLH
NHLPKDMDFF VMLSSISGII GNTTQAAYAA GNTFLDAFSG FRNAQGLPAV TLDLGAISGV
GYLASEENKE LSKSMQDQGF SMTDEKLLLA LIRSAIVQPF GQEGKTQTIT GLGTWRSGRS
LSALETSMFS HFRRHSQEAE VVAEKEQTSN GKISVKDALR SSESVDDAAG VICNGLLGYL
ASRSGVSVEN FSSEMSLTEC GVDSIVAVDV RNWIARELES SIPLLELLAN HSLSQLSVDI
ASRSKLVPVE VKSRGATAT
//
