ID S8BJN7_DACHA Unreviewed; 2292 AA.
AC S8BJN7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS35452.1};
GN ORFNames=H072_11126 {ECO:0000313|EMBL:EPS35452.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS35452.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS35452.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35452.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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:EPS35452.1}.
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DR EMBL; AQGS01001130; EPS35452.1; -; Genomic_DNA.
DR RefSeq; XP_011116496.1; XM_011118194.1.
DR STRING; 1284197.S8BJN7; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; PELLWPV; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000015100; 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:0008270; F:zinc ion 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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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 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; IPR013149; ADH-like_C.
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; 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; 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; PF00107; ADH_zinc_N; 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; 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.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2212..2286
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1100..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2292 AA; 251172 MW; AB6DE2C61A43765B CRC64;
MSDLSEGANS EPLAIIGFAF KFPSGIESPE AFWEMMMHGE TGLSDIPSDR LNLQAFLDIS
GERANENRSR ASTGYFMGNP VDQFDAPFFT ITSEEAMAMD PQQRLLLETT YHAFENAGLP
LSQVQGSRTS VHVGCLSYDY RLAISRDAEA ATKYSVTGTE VSILANRLSW YFNLKGPSIS
VETACSSSLV ALDLASQLLR SKNTNMAIVA GTSLTLMPDL FLYLDNMGFL SPDSRCHSFD
SRANGYARSE GLGVIVVKRL DDAIRDKDII RAVIRSTGSN SDGFTPGITQ PSELSQLSLI
RDTYEKAGLS MEPTRFCEAH GTGTLLGDPI EANAIGTAFR ASRKTDDPLY IGASKANIGH
LEAASGIAGI IKSILVLERG VIPPIADLVE LNPNIDDVYY KLKFPTIAVP WPGTGLRRAS
VNSFGFGGTN AHVVLDDAHG FLTERGRNAE ANYIHFDGSH QYENSLTRVQ TERPYLLTIS
ASDRNGIQRL ENVYSSYFAG LESIDTDFCQ RLAFTLSNRR TSLPWKSCTI VKSTDSLPSS
MSELSIPKRH SSGITPHLAF VFTGQGAQWA RMGVELLQYS AYAESIHRSS EYLESLGCPW
SLEEEMNKNA AISRMNEPEI SQPVSCALQI AIVDLLERAN LRPSVVLGHS SGEVAAAYCK
GALSHRSAIK IAYFRGMGGA AASRGEGRHT MMSVGLSEAD AIAILGDISA MHNDIHIACI
NSPSNVTLAG DEGHLDALKL ILDGKGTFAR KLKVPCAYHS PHMIPIAKEY FSRAGELEAR
YQDTSGTKNI PMLSYLDGKE VSKERLLDLE YWITNMCSAV RFPDSVSGID RLASLANGRK
ILDLSHKKSV RVTNILEIGP HSALKGPLRE IMKGFKYARD IEYDAALIRG NSGLESFLRA
AGSLYCSGFE PDIAYLNGYE ERGSKITPLV DLPPYPFAHT RSYWKESRRS KSERLRSCRP
NELLGNPSPD WHPFSASWRN FLNRSKSDWL EDHCINDSVL YPGAGMLTMA IEAANQYSRE
TLSTIPKGFS LKHIEFLSTI QIPEGSGDLE IQVNLRPLDE GTLKLGWFEF EVFSSDNEQW
KKSCKGLIRP ETSDRHKALL SPPAKYKRDA LQHSDTPPNE EKDTNRNSSI PGSPYVLIDA
TIFNSTTPTP DSATIPIRPA EGFTDIDAVE YFNPTGSGLQ TLPTDKFFQK IRMAGYNYGP
SFQRIDCIQY KNPGEVTAIV ETYEPITSSH KGHGTRLIDP ASVIHPATLD AFFQLPLANI
LRDHSSMPSM IPSKIKSLWI SASGLGNDAP PLSATAWYNF SSYRGSEHTV SAVDADNNLK
IELSGYEMTR VAGGEDTVAQ INPIDLHHCW KFKWESITTL PQHGGNRSLE PTLVEVHVHN
PTKTTLELAS ALTSALEISG YLTCTINSSG KEIKDSANLR VILWDTDQES LLSKLDEENL
IMLQRTLNTS NNVLWIQTAA YNSAEFASQH LVDGLSRVVR QEHSMVNFAT VSLSSSQHEI
PGRVRAISQV CDLLLSGADA LYLPQTFRET NPGCIEFYRL TEAAELTEKV QSVKLAPVPT
QAVWGRCGPL KLAVTSPGVL DTIHFVEDLE YNHQQWLQDN EVEVEVKAAG VNFKDCLIAL
GALNENKIGS EISGVVRRVG RDIEGHGLVP GDSVCGFAGD GYRTFYRTKG SSLSRIPSSA
SLTHVEAASI PVNFATAWHA LKHIARLEPG EKVLIHSGAG GTGQAAIQIA KFLGATIFTT
VSTQEKRGLL TTKYNIPPSH IFNSRDSKFA DEIKHMVGGV DVVLNSLSGD VLFSSWECME
PFGRFVEIGK KDIQSQGRLP MAQFEKNISF NAVDLGHMAI ARPKYVAQLV DEVLALFKQK
GGFTTVHEIQ RFDISDIVPA FRLIGSGKST GKIVVEMTSD SQIPVLLPSK LSSNFPPNAS
YIIAGGLGGL GRVAARWMAE RGAKHLVLLS RSGARAEDAK AFVKELQDMG VNCLAPACDI
SNKDTLKETL DSLQIPPIRG CLQSSMVLRS ALFADMKHSE WKEATKAKVA GSWNLHELLP
RNLDFFILLS SVQAVFGART QSNYNAANTY MDGLALHRVS KGLKAVSVML GVVTTDGYLA
EAEHQDERDL LLAQNTYHGV ETPDFHALLD YYCDASMPLL PVEEAQVTLG MMLLYEDPDL
DPLGTIWGRN PMFRALRRLK GTDRSTDSKD SGKKDIASLI AAAKTSEEAA EAVMVALTTR
LASTIAGMDP EEMDQSKPIQ AYGVDSLQTM ELRSWFLRYF KADLPTFSIL GAPSLTALAN
SIVEKSTLRA KA
//
