ID A0A3D8SGD5_9HELO Unreviewed; 2636 AA.
AC A0A3D8SGD5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Reducing type I polyketide synthase {ECO:0000313|EMBL:RDW85333.1};
GN ORFNames=BP6252_02923 {ECO:0000313|EMBL:RDW85333.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW85333.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW85333.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW85333.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDW85333.1}.
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DR EMBL; PDLM01000002; RDW85333.1; -; Genomic_DNA.
DR STRING; 1849047.A0A3D8SGD5; -.
DR Proteomes; UP000256645; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; 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; PS00606; KS3_1; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..453
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2545..2626
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 499..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2636 AA; 287889 MW; F0D231C6D9AD6AF2 CRC64;
MSSGNGALQM PTDTAIAIVG MSCRFPGAAT SPEKLWELCS NAKSAWSEIP PDRFNKDAFY
HTDGGRTGTT NARGGHFLSQ DIGLFDAPFF NVSAEEAKFD LLTNGCAVNN PETAGIPLDQ
IAGSKTAVFS GIFTRDYSES MMRDIETLPR YSATGTGGAM LANRVSYFFD LKGPSLTVDT
GCSTSLVALH LACQSIRAGE SEAALVGGSN IILNPDMLIT LSNMGFLSSE GRSFAFDHRA
NGYGRGEGAA CIVIKRLNKA MSDGDYIHSI IRQTAVNSDG KTDGITQPSA VAHEHLIRRA
YHEANLDPLD TDYVEAHGTG TQAGDPLELK TVASIFGSTR KNSNPIYVGS VKTNVGHLEA
ASGLAGIIKA SLAMQKGVIP PNINFEKLNE KIVLDKYYFK VQIILFNVSV SGITNPKQIP
SQPTPWPTKT GPRRASVNSL GYGGTNAHVI LEDANELNRR PKGYSNGNIN GFTNGTGRGV
INGTVNGVTD ASSNGISARD VDEVSNGTSS ETTDGTFRSI NGCSGTKNAP FDRKKTETGN
IANKWRFFTL SAKDEDSLKD TIASMRDHLE SYRNKDSLNE ESFLDNLAYT LCERRSSFRW
MQAFTSQSLD GLISTLGSRK PAFNTRRRAE SPRIGFIFTG QGAQWHAMGR ELLHAYPVFR
RTLELADAFL RIQNCPWSLL EELNRDAETT KVNSATIGQP LCTAVQIGLV NLLEAWNIRP
TAVTGHSSGE IASAYAAGAL TLESAMLVAY HRGANAERSA SLSGIKGSMI AVGLSRERAE
DYIERLKTGK VVVACINSPS SVTVSGDLVA IEEIQKLLDA DEVFARRLKV DAAYHSHHML
LAVDGYVDQL SGMEMATQMS PNILCVSSVT GKPVQSAQEF GPSYWEQNAV QPVLFSDALI
CLCQGGASEK NPQNTEAFVD ILLEIGPHGA LAGPVRQILQ ASSLKQTSVS YLSCLMRKQD
AHESMMNVAA SLLCKGAQVN LEEVNFPCGK GIVSVVPDLP SYPWAHEIRH WHEPRINRQQ
RLRQHARHDL LGILIPGQNP AASTWRHFVR LSDQPWVRDH VVDSNILYPA AGFIAMAIEA
VSQKHHDLIA EGARYHLQEL NLVSALAVPD TADGVELQLS LFPTSEQLLK AQKYYEFRIL
SVGEKDEWHE HCSGRIGLQI PSAATSWKLS DRESTMTASA FETSERLCTK TIDVKKYYEG
VHRLGITYGQ SFQNLVKIQQ GPSCSLTTVQ VRDTGALMPS HIEQRHIIHP TTLDAILQSI
YPALSDNGTE HKTIMIPTYI KSLSVSQAIS HAPGSQLRVN TNAERNLRNG AKASLTVIHE
NEADRTPVIR IEELILTSIG TSVEDMKGDS GRELCFNISF DRDISFMTSH EFSAISATSV
DPAEQQIFTD LQRACFHMVE RALKQLTEAD ISHFTGPQLA MFNWMKTQSE LGQQDLLDFQ
ASPSLKISDK EQDNLITAVE TQTVNGEMCV RVGKYLVQIL RKEIEPLQVM MEDGLLYKYY
ENALGMKRIY AHMSSILRLF AHKTPGANIL EIGGGTGGCT VPALQALTSG DQKTSRFAHY
TFTDVSSGFF EKAREKLVKW EDRVSYKRFD VEMDPESQDI QCGSYDLVIA CNVLHATVDM
EKTMSNVRKL IRSGGRLLII EGTRDTLDIS LVFGVLPGWW LGQEKERRLS PKLSLTAWDS
LLKRTGFSGQ QALMLDSPTE LDHVYSVFLA NAASDIKTKE HPQTSIVLGK EKPPEIWLAH
LVSSLQAATG HGPIISSFES PAVDGKVAIF VGEMNKSFLA RLGQDDFLAL RKMLTTAKGV
LWMTVGGSME CNSPESAMVT GLMRTLRGEN AGIRLATLDL DPTRQPFTIQ TTKTITKVFQ
SVFDPELESA NVDLEYSERG DQIFIPRVLP DPQANQALQQ TSGQTILDNQ EFYQEDRPLC
LEVSTAGLLD TMRFVDDVNY HEALPADFVE IAPKAFGLNF RDVMIAMGHL NETTMGYECS
GLITRVGSNV THLQPGDRVA AMMQGHYANY IRLLGIAVSK IPDDISFEEA TSMPMVFTTA
YFSLYETARL QKGETVLIHA AAGGVGQAAI MLAQLVGAEV YATVGSNEKC RLLIENYGIP
EDHIFSSRSD SFTTDIRAAT NGRGVDVALN CLSGSLLHAT WKCMAIFGRL VEIGKRDIET
NTFLDMGGFQ GNVSFSAIDL TYVGRFRPAY LASILEKCMQ LFSEGKIRAV KPITVFPISE
IERAFRYMQA GKHTGKVVIK PNEGDVVKAL APRVKTLFRA DSSYVIVGGL GGLGQSVARW
MIKLGAKYLI ILSRSGRRHA LAASLSADAE QSGCKALILE CDITKEFQVR QSLDDAAQTM
PPVRGIIQGA MVLNDCVFEH MSFEQYQNAI LPKVQGTWNL HNALLQNKLD FFVMLSSAVG
VVGNSSQANY SAGSSFLDAF AQYRRSLGLP AISLDLGIIS SVGYVAENEA VAKRLARMGH
DAISEEKMLG LIQIAVTDSY QTQQSQSPSQ ILTGLSLREF DADWIQDTKF SIIRQSQASS
IRASSNQSSQ RGLKMSLQDH LNTIKSETDA VTVICDAIIS KLAINLMVSE ADIDPEQAIS
ACGVDSLVAV ELRNWLGGQA GAEISVVDIL QCKSLVGLSA SVARSSKVVA KVIGSA
//
