ID A0A3E2GW81_SCYLI Unreviewed; 2389 AA.
AC A0A3E2GW81;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RFU25348.1};
DE Flags: Fragment;
GN ORFNames=B7463_g10989 {ECO:0000313|EMBL:RFU25348.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU25348.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU25348.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU25348.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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:RFU25348.1}.
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DR EMBL; NCSJ02000340; RFU25348.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2GW81; -.
DR OMA; SPGGMFM; -.
DR Proteomes; UP000258309; 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:InterPro.
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; 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; 3.
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; 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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 55..483
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2310..2386
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU25348.1"
FT NON_TER 2389
FT /evidence="ECO:0000313|EMBL:RFU25348.1"
SQ SEQUENCE 2389 AA; 258492 MW; B4637DC2C0D066BE CRC64;
MAISSSPRNA SGRSGDTSTI VSSSSFVIDR SDTTSDCSSS NGPPEEPNST PHRIQVPIAV
IGMACRLPGH SNSLRNLWEF LERGGVAENQ PPASRFSLSG HHDKDRRPRT MKSPGGMFME
DVDPELFDAQ FFNISRVDSI AMDPQQRQLL EVTYECLENA GIPMEKISGK KIGCLVGANA
VDYEAIQARD PEDRPDSATI GVARSILSNR ISHFLNIRGP SMTIDTACSA SLVSLDVACR
YLDTNQADGM IVAGANLWIN PEHNQETGMM RMTQSASGRC HTFDAKADGY VKAEGINAVY
IKRLNDALRD GDPIRAVIRG TSTNSAGRTP GIASPSAEAQ ADAIRAAYAN AGIKDFAETG
YLECHGTATL VGDGVELNGA ASVFAANRGE GQELVIGSIK SNIGHSEAAA GISGLIKAIL
AVERGVIPGN PTFLEPNPKI DFQSLRVRAT RTAIDWPAGP TLRRASVNSF GFGGANAHVV
LEAADYSRHV SSYIEKVGSD FFSADDEDTE VEGTPRVLVF SANDEQSLKN NVTSLSGHLL
NPAVSLDPGD LAYTLSERRT HHYHRGFVVT TTSSFSVESV IYGKSQASTE VGFVFTGQGA
QWSQMGLELI DTFPTAKRTI QHLDDVLKAL PLPPSWSLLS ELTEARKPEA LRLPEFSQPL
VTALQLALVA VLNEWDITPK SVVGHSSGEI AAAAAAGLIT PEDAIKIAFF RGQAPNKFTR
RIPLGMLAVG VGVEDVQKYL EPSGGKVQIA CYNSPTSLTL SGPTSELEKV KNSLTSDGYF
ARMLLVDLAY HSTYMAGIGD EYYEMLLDHN IGVLAPTIAS KEAKTSSIKM FSSVTGEVVT
NALDAAYWQK NMISSVRFAQ ATSVLLNDPE APNFLIEVGP ANALAGPISQ IKKSLTGAAA
DVKYASALKR GSQAITPLFE VAGRLFLSGG LPNLKAVNSQ NSTRRAAIIH ETTASKDWRF
KKFILHDLLG SKMIGTPWNA PTFKRTLKLA DLTWLKDHKL GEQIVFPGAG YVAMAVEAIY
QTAFMTTWKE EVPDRFRYRL RDVKFSRAIV IEEDAEKRIM LTLTPVSGST RSWYEFKIYS
LREETWTEHC TGLIRVETDY KDDVAPATAI QPLKYPTSGR AWYKAMAEAG YNFGASFRNH
LMVESITGKR ESRSTVSLKP PPSSYGQSFY PMHPACIDGC FQTVSPSLWK GDRTDVGAVL
VPSVLGSLII SGRTEQPDEA ISVASAHWMG LGRTDSPRNY GTNCSVYDPK DRALILEMKD
LKFAELETSE EEGPSHTFTQ ISWDADISML LSVQNTKLGK FLTERVSSSK SSDDTKSTMQ
ETLVHELLDV AAHKNPILKV AEVNLDAKDQ SSLWLQRPSP KRSASSLYHF ASSDSSTVVS
AQEKYSPSAP NAGFTWFDLA KAEPILTEVK FDVVLIKIRQ SVSEEALNVA VDSISASIQD
GGLVLVAGSD KLSIQTTLER IGKVHNLNES LFICVAASPA DFEEPAQPIT CLVSLSNQTP
PAGLLNSLGK WNIKTIQPLT EIETNQIILV LDELSSSSMD RLDEKSWGIL QELVQKEAKI
LWVTTGAQLD VTEPTRAAIN GFFRVLRAEE PLLNLVTLDV GQATGPATAT AIDACLELIS
KPKPKQRADS EFVERNGIIY ISRLIPEENL TKYQNDDLSS LKTEIVDLHA SYTPIRLRAE
ILGNIDSIHY GEISPVPLAL RKGCLEVELF AAGMNYKDVV VSMGIVPGNE HTLGGEGAGI
VTRVSAEIDN FKVGQRVVVF DKGTFANRIQ TTPGRCYAIP DDMSFEEAST LSAVYLTSIY
GLFDLATLSK GQTVLIHSAA GGVGIAAIQL CQYAGAELFV TVGTTEKRDF LKSTFGLADD
HIFNSRNTDF ASGILTATNG KGIDVVLNSL TGDMLDESFR LLANGGKMIE IGKKDILDRN
SLAMEPFDRN ISFMAVDMSH ERAPDHLVQR LLVRLFELIK GGHVKPIAPI HTFSFSDVPS
AIRFLRAGKH IGKIVIADGL EPEVKVPVRR ALKTMKFRDD ACYLIVGGLK GLCGSLAVYM
AKNGAKHLAV ISRSGHSDEK SQGVVKEIKA LGSKIDLLST DVAVASDVEK AFRAATVPIA
GIIQGAMVLR DRTFSSMDVA DYHGALTCKI QGTWNLHNVS EKLGLKLEFF TMLSSISGVV
GQKGQANYAA GNSFLDAFAS YRHSLGQPAC SVDLGVIEDV GYIAERDGMQ SNLDTSIWTG
INERLLRKIL YFSILQQQEK TAKAASSTQI ITGIPVPQPE DSGLIHDARF APLFTNSGNA
NGGGDSKSSA SKDVQAVLLL LKSKTADAAT QLAATIDIVN KCFVRVLRLP EPMDIGRPIS
VYGIDSLAAV EVRNWLRGEL GALVTTLDIV NATSLVDLCK KIVAKVTGA
//
