UniProt: A0A166SMV8

Database: UniProt
Entry: A0A166SMV8_9PEZI

LinkDB:  A0A166SMV8_9PEZI 
Original site:  A0A166SMV8_9PEZI

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Ontology (5)   
   GO (5)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (46)   
   InterPro (25)   
   Pfam (11)   
   PROSITE (4)   
   SMART (6)   
All databases (52)   

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ID   A0A166SMV8_9PEZI        Unreviewed;      2548 AA.
AC   A0A166SMV8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Polyketide synthase (Beta-ketoacyl synthase domain-containing protein) {ECO:0000313|EMBL:KZL70949.1};
GN   ORFNames=CT0861_01946 {ECO:0000313|EMBL:KZL70949.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL70949.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL70949.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL70949.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL70949.1}.
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DR   EMBL; LFIV01000081; KZL70949.1; -; Genomic_DNA.
DR   STRING; 708197.A0A166SMV8; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000076552; 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; 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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..438
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2463..2540
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          450..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2548 AA;  278596 MW;  C529B4CAB618EAB6 CRC64;
     MPFIDEPASA SSTNQPIAII GIGLRAPGDA SDPEKFWQML LDARSARSEI PKDRYNVDGF
     YHPDPERLGS IQPRHAHFLK QDFKVFDAPF FSVTPKEAKA MDPTQRMLLE AAYEGFENAG
     LRLEDVSGTQ TSCYIGTFTN DFVNLQAQSN EAPSIYHATG LSSSLASNRL SWFYNLKGPS
     MTIDTACSSS LTAFHLACQS IRTGEAEMSI VAGANLMFGP DMSILLGAAK ILSPEGKSKM
     WDANANGFAR GEGFGVTILK PLDAAIRDGD TVRAVVLASA ANEDGRTPGI SLPNSEAQQA
     LIRTAYRNAG VDPAETGYVE AHGTGTQAGD PLEARAILKT IGDQPGRKSD LYVGSVKTNI
     GHLEGAAGVA GIIKAALAVE RGLIPQNLWF EELNPQIDLL ENVKIPKTLQ VWPHSGPRRA
     SINSFGFGGA NAHVILEDAA SYLFRHGLPG RHSTTPDPKL PTISSTASES GSDMDTSSSV
     SHEEVTSKLF VLSSNDQEGV KRNVERLATY LDGKTSSKPS LLTDLAYTLF SKRTTLPWKS
     FAIASDVTSL RQSLEKIPAV VRSSNSSVPG VAFVFTGQGA QYFKMGKGLS VYKAFRDSML
     RSEFILKALG CPWTLTEELE RDEADCNLRR TDYSQPACTA LQVALVDLSK AWGIKPVAVV
     GHSSGEIAAA YCAGFIDHES AVKIAWLRGQ VSQTVSKNGG MLAVSASAES IAEHLQTLKL
     GKAIVGCLNS PKACTVSGDS VAIDELQEIL KETQVPCTRL PMDVAYHSFH MEAARERYEV
     ALAGIPHGSS DIPMFSSVTG RQVTPEQMTP SYWVDNLVSP VNFVGAVRSL LHHTQGKVRS
     HDRTAFASVF VELGPHSALR SYLLDTFSTE ERFSDLSYTT VLRRKFDGAQ TALEAMGQLW
     CKGCDVDINQ VNEVSDTTNM LVDLPPYAWN HTRTFWDESY LSREYRLREK PRTDLLGYRI
     SGTPDPTWRC HLRCTESPWI REHKVQGDIL YPGAGIVVMA IEAARQLAEE HATEEIYGYE
     LRDVAIDTAL RVPDTEKGIE VMIQLHGRRT GTKAAPSATL NEFSVSSWSE EIKEWTVHAR
     GLVSVTYKSS ISPSMQRELA LENERYAQSF TSAKKICQKP ARNFLYDTVE TIGMQYGPTF
     RNMTELFAGP NASYGVISVP DTKSVMPKGF EYPSVVHPAT LDSVLHLLFP SISGEDQSLN
     EAVVPFSFDR IFVSAKLSGV PGTKLHGCST AQKTSYTTWK SSITISEDLS EPMIIMDGVS
     LASVGEGDAQ KTQETRASCF GQAWHEDADL LEPSQIKELV YKRTLKSKDD ESVLDKLEYV
     CLVHIYRCLA WLESEEGKAF VPQDGFWKLY VEWMYDTIKQ FPPLSASEAE IETELDASRK
     RIILSESGDI TVQMVDRIGE NLKRIFTREV EPLQVMTEGD LLYSFYRGAF GTSFNTNVAE
     YVGMIADKSP GIKILEIGAG TGGTTYHVLE RLRNADGTSK AAKYCFTDIS PGFLAKAADR
     FSNDASIMEF TTLNIENEPT EQGFTPESYD LIVCANVLHA TKSIQETLAH CKSLLKPGGR
     LVLSEVTIKR IFSGFIMGPL PGWWLGEDDG RKGGPLLDVE EWNTALVQAG FSGVDVDIRG
     DREVSKEPVS LILSTKPEKE VSGPSQFVVL STGSEASEKL SHSIQKHLVS AAQDVTIMQW
     NELDTSNNQV GGKYCLSLAE WENPVLSDLT DDNWERLRHV ILGSAGTLWI TGGAAMDCPE
     PMKSLMVGLS RAIRNENAGV RLATLDLETP SSIDFDEAAK NILKVALSHS RSDVFDGEYA
     ARGRTVYVPR VERTLNVDAS LRKYEAKGQP ELVPFKGCGR PLKLTIKTPG LLDTFRWEED
     EVYYEPLPED WIEVEVKAVG LNFKDVLVAL GNLAENKLGV DASGIITRVG SAVSNFKPGD
     RVMTASCDTF ATYVRFPAKG AIAVPEKMSF EEAASMPLIF LTAYYSLVTA GNLVKGEKIL
     IHAAAGGVGQ AAIMIAQRKG AEIFATVGSD EKKKLIMDQY GIPEDHIFSS RDASFAKAVM
     RATNDQGVDV VLNSLAGELL RLSWHCLAKF GRFLEIGKAD LFANTGLDMK PFLDNKAYIG
     VNLLDFENNP TPRAIALWED TAKLIHDGSV KPIAPIQLFS MAEVEKAFRF MQAGKHMGKV
     VVRVDDADMV PAVPRTPRVG IQPDATYVIA GVGGICKEIG RWLAEKGAKH LVLLSRSAAS
     SEENKAFASE LQKTYEATTY AYDCDVGNKS ALQKVLDDLK LKNVPDIKGC VTGAMVLRDT
     LFDKMTADHV RTTVGPKVHG TWNLHELLPK ELDFFVMLSS LAGVMGHRGQ GNYGCGNIFQ
     DYFAAYRRSQ GLRAMTIDIG YLLSVGFVAE HDEYVDHVKA MGLKVMHKSD LHGLMATALE
     GSDAHPPQVM CGLPYNEHDD AWYWILDQRF AGLRKTAAGS GAGGSASVSL RDELVRCGKA
     DDEAVHLITS ALVQRLAKLM MMPEDDVDAG KPLSAYGVDS LVAVEVRNWI AKEVAVEVSV
     FDIMANIPMR QLATDLAGKS KLLTQDAS
//

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