ID S8AHF6_DACHA Unreviewed; 2198 AA.
AC S8AHF6;
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:EPS42294.1};
GN ORFNames=H072_3762 {ECO:0000313|EMBL:EPS42294.1};
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:EPS42294.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS42294.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42294.1,
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 -!- 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:EPS42294.1}.
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DR EMBL; AQGS01000125; EPS42294.1; -; Genomic_DNA.
DR RefSeq; XP_011109727.1; XM_011111425.1.
DR STRING; 1284197.S8AHF6; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; QWDFTDI; -.
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: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; cd05274; KR_FAS_SDR_x; 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; 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.
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 13..432
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2119..2193
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2198 AA; 240309 MW; D8C81B4AF0803663 CRC64;
MAIKSDAPSP AAAEPLAVVG FAFKLPAGID HSDSFWKMVV NGETGLRPIP ENRLNLEAFR
NLATLKPKGY FIKDRISAFD APFFSITAEE AVAMDPQQRL LLETAYHAVE NAGITLEELG
GSKTSVHVGC LSQDFKLANA KDPEIAAKYA ATGGELSILA NRLSWFFNLK GPSLSIETAC
SSSLVAMDLA CQLLRNGETD MGIVAGSSLM HAPDFYIYLD NMGFLSPDNR CHSFDSRANG
YARAEGLGVI MIKRLSDAIR DGNTIRAVIR SSGSNSDGHT AGITQPCGDS QLALIKETYQ
KAGLSMEPTR YCEAHGTGTI LGDPIESHAI GAAFRSVRTA DEPLYIGAVK ANIGHLEAAS
GIAGVIKTIL VLENGMIPPI ADLQELNPAI DHAYYKLKFP TRATPWPGQG LRRASVNSFG
FGGSNAHIVL DDAYHYLAEH GLKASHNTTP LPMGDSGITN EPMTPSDTRF GPYLLTFSAA
DRDGVKRMGQ LYSDYLANCS ARNPKTIANT SEILAELSIP KRPFAKPSLA FVFTGQGAQW
ARMGIELMKF PVFALSIDRS SKYLDSVGCP WNLKDELSKD AINSRIHSPD ISQPLCGAVQ
IALIDLLEHI NIKPDLVIGH SSGEVPAAYS KGALSHESAI RLAYYRGLGG AAAAGDPDQN
GTMMSVGLGE SDIAPLMADL STKGYNDLHI GCINSPNNVT VSGDTTQMNI LKSILDERGI
FARMLKVACA YHSPHMAKAA RKYIQQAGVL HPRPGKPNST LMISYLTGEE VSNEKLRELD
YWVNNLCGTV NFTKNVGAID NLASLAKGRK YLDLRHRKGM SITNLLEVGP HSALKGPLRD
ILKTFQFAQD IQYDCTLIRG LSALNPFLKA VGNLQSSGFK PDIFYLNSLG KLKDSTSLVN
LPCYPFSRSR EYWVESQRSK NERFRRHKPS ELLGTPTPDW HPLFATWRNF LNRSKSEWVE
DHNINDSIIY PGAGMVTMAI EAMNQYASGH LHIQPAGFSL RDVDFIAAMR IPDSPAQLET
QTHLRVVGDD NTTQNSWFEF SIYSCEDGKW KKNCKGKIRV EADPDSSETS SREPGPLLNP
TILPVDQFYN SIRNAGYLFG PSFRSIESLQ WSEPQKIQAR VKVYEKSSAG SQGSARAMDS
THVIHPVTLD ALLQLGIANS FRMSPNSIPT YIPTRLKRMW ISAEGLNTPK STLSATSCLN
FHGYRGSEQS VSAFGSDNKL KVELFGYEMT RVSGGDALSA QSLPITELHT CWTPDWKPLA
SLKPSQQQLN MRSSSPQEGR QSAIEIHVLD KISTLTELSQ VLKSDLESKG NLVCQIVDSS
KTTSLTSSTA DLKIILWDID ESSILSDMSS DEFKMVKDVL NTNTQVLWIQ STGIISSRYP
SQHLIDGLSR VIRQEQSMAG FATLSTVVTT LSGRVNAICQ VCEILLSNTD GDILHIPQTY
RQTSAGNVEF CLLEEAPMAT RKVQSANSLS TPVPIPWDIK TPLQLAVGSP GVLDSLHFVE
DSSYGSRLLE NEVEVEVKAV GLNFKDCLIA LGALNENSLG HEISGIVNRI GIDTEGHGLL
PGDRVCGFSV DGYRTFFRNK GHSFSKLPET LDFVEAAAIP INFATAWHSL RYVAQIGEGE
TILIHSAAGG TGQAAIQIAQ YLGAKVFATV GTKDKRELLT RQYGIPEDHI FNSRDADFAK
QVRHLTGGKG VDVVFNSLSG EMLFSSWESL APFGRFVEIG KKDIQSQNGL PMGQFEKNCS
FNAVDLGHMF LQRPKQVTKI VDEVLGLFES GDLRSVHSIH TFGISKIIDA FRLMQGGKST
GKIVVKTEPM ATVQATLALK ERLSFESDAS YVIAGGFGGL GRDIVRWMAE RGAKNLVLLS
RSGPRTESAK LLISQLMAMG VNCITPRCDI SDRESVDQTL KSLAAVIPPI KGCIQTSMVL
RSTLFAEMTH KEWTEAIASK VAGTWNLHEL LPINLDFFLL LSSVQGLIGS RTQGNYAAAN
TYLDALARHR VAQGLKAVSL QLGVMDTDGY LAEHEDEKQL LLGQNTYLPI QRPDFHALLE
RYCDPKLQLE AGEANLAVGL RLLYVDPDFD PLGTSWGRDP MFQGLRRLTE ANDVSKVSTG
KDIQLRIRNA RSPQEAIDIV MAALMERLAS TIAGMDPEDM DPSKGVQAYG VDSLQTMELR
SWFLKYFRSD VPTFEILGSP SLTALALVIV ERSVLRHK
//
