ID A0A421DEN6_9EURO Unreviewed; 2566 AA.
AC A0A421DEN6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RLM00572.1};
GN ORFNames=CFD26_108216 {ECO:0000313|EMBL:RLM00572.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLM00572.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLM00572.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM00572.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-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:RLM00572.1}.
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DR EMBL; NIDN02000014; RLM00572.1; -; Genomic_DNA.
DR STRING; 1245748.A0A421DEN6; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
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 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; IPR011032; GroES-like_sf.
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; 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; 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:UP000215289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2468..2545
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1097..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2432..2451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2566 AA; 278323 MW; DBFFC0CDEA25ED99 CRC64;
MIAADESSRE GMTSSVNGLA FAAGTAMESA EPQTMPIAII GMSCRFPGDA TTPEKLWDLC
ARGKSAWSPI SRSRFNREAW YHPNKGHIGT SDVKGAHYLT EDVTLFDASF FNFSAEIART
MDPEVRLQLE TVYEALENAG IPMEEVAGTN TSVFAGTSFR DNHDSHMRDP STMDDAFFVT
GNGAAMVANR VSHFYDLRGP SVMVDTGCST SLTLLHLACQ SLRTGESTMS IVGGSNVLLN
PDMFIAGTKL GIFSAEGKCF TFDSRAAGYG RGDGIATIII KPLSDALRDG NPIRAVIRNT
AANQDGKTTT ITSPSQEAQQ QLFRECYQKA GLDPVHTAYV EAHGTGTQTG DTIEAHAIGT
VFCEKRDSTN PLWIGSVKTN IGHTEATSGL AGVIKAVMAI EKGYIPPSIN FEKVNPKISL
DNLKLKIPLL LEPWPSNALQ RVSVNNFGYG GANAHVIIEH PDYLLAGGHH GASRTGFLSN
PKNRSRVFVW SAKDETAAKA IGPRLREYLN DAAAAGKEPE EVLDRLALTL GQHRSHFAWN
VACSAESLDR LVSQLGTPEL LKPRRTSRVP RLGFVFTGQG AQWFAMGREL IGLYPVFRDT
LRQAEAYLHQ FGASWSLIEE LTRSESESRV NEVTFSLPLS VAIQLALVDL LRSWGIHPTG
VTGHSSGEVG AAYAAKAIDL KSAMAIVYSR GHLTTQYGKT FERNGGMIAV GLSREEAQEK
IARVQSGQLV VACVNSPVSV TVSGDVPAIL ELEQLMAEEK VFARRLKVNA AYHSHHMVPV
AEPYRETLAR YISADPDFKG DVIYSSPTTG DRMSSADEIA SPEHWVRNMV QPVEFLDSLQ
NLCLDRGNEN ARSIDMLIEV GPHGALGGPI RQTLMLPELK EAGISYATCL KRGESAVQSM
HNLVCTLVQQ GYRPDLGAVN FPYGHHGHRI LTDLPPYPWN HQTSYWKEPR INKALREKTF
APHDLLGRTT TDFSPLTPTW RHIIRPRDIP WVCDHVVQSS IIYPGAGYIC MAIEAVRQMA
ADPSAIAGYK LEAIDIISAL VLEANAEGVE VRLSLLPPSD SVLRAQSWQV FHIQSLDLSG
KWVLNCEGRI CVITNNSDRS SPRDEVSESA GEPQKGSSKE DGEDGFGRRV DAAETYQALN
ALGLSYGKMF QNLVSSRTAP GRSSSILKVA DTAASMPYQY EQSHVVHPTT LDTVFQAVFL
NLPPAGSKQR NAMVPKTIKS LYVSADISSQ PGHLFEVRSH LTKSSSQGFE SCATILDAGQ
PDQASSPVLT IDGLFCQSVG SAAPTAAEMD KLCFKTVWKP DVDLIQLADL SSTHPVDPVL
LKMGQDIRAA ALGFMADAVQ ALAGDREPDA RQSQYLEWIQ NTIGQKNPEV LPISEPLETI
EHQTELGALV CQIGRSLPAI LTGQLDPMEI VSQHGLNTQD PEAEEDPLWL AGCLSQIRAF
VDLFGHKKPR ANILEIGAGR GRCTKVILEA LSAETEPSAL FARYDATDPL SEVIEATGAR
LEGSERVRFQ PYDIESDPTT QGFEANSYDL IVASPVLYTV QDVEQALARV RSLLKPGGKL
LIWGPVLDSL AMRMVYGTLS GWQNHSLSSL LQRAGFEEST IGLADSDDQE SRLMSITVAT
AKSELPPIPP SEVVLVHSTS CPPEAWLNCL REAIVARMAS CKVSVQGLTE TEDLSGKFVL
FLGDLTEPVL DQPTPEQFES LKSLLSYSQG VLWVSQGSQM DSPKPFASLH HGLLRTLRCE
NTAMRYLSLD LDPTVSVWDP STAGQIARIL STGSDFQEYS EDLREAEYAI RAGVVQIPRV
RENLQENNAV AGAGAALTPE LCPFFKAGRN IKLGVTTPGL LESLTFIDDP RADETLPEDY
VEINPKAFGL NFRDVLVALD QLEETRMGFE CSGVISRVGS KAAANGFKIG DRVYAFAFGC
FTTTVRVSYL GISHIPEGMD FETAASIPLV YGTAYYGLHD VARLAPGETV LIHCASGGVG
QAAIMMAQYI GAEIFVTVGT AEKRQFIMET YGIAADHIFS SRNSSFASKI MAKTGGRGVD
VVLNSLAGPL LRETWRCIAT FGRFIEIGKR DIEMNNSIEM APFARQVSFS SLDLVKLGEQ
RPHEIARILS AIFTLLSEKK VRAVTPINVF PLSDAERAFR IMQEGKHLGK IILSPEAGDL
VKVLPSTKSV KLSPEASYLI VGGLGGIGKS VSNLLVERGA RHLILLSRNA ASPKPESEAF
VRQLRMAGAN VVLKSCSIAD QAQLSEVIAD CARSMPPIKG VIQSAMVLRD SIFEHMSWSD
YNTAIQPKVQ GTWNLHKEFE NAALDFFVIL SSISGFGGNS GQANYAAGGT FQDALARYRA
SLSLPAVSLD LGMVKSVGVV AETKQLAEHL SRLGLRPLEE DEVLRLIESA IRDPQRNVHL
SQVTTGIPPS FVRNNDSPSF WNRDIRFAAL ERAEDSGSSS PNPNGGGAGV GTHAHTKALI
AAATTFPDAI QRIQDAFIKK LADTFARPES EIDPALPLTA VGVDSLIAVE LRNWLVSALE
ADCSIFDVMQ SPSLAKLAEK VASKSRLVRL EAQPKNGANG TNGTAA
//
