ID A0A3D8QVW7_9EURO Unreviewed; 1946 AA.
AC A0A3D8QVW7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RDW65922.1};
GN ORFNames=DSM5745_09661 {ECO:0000313|EMBL:RDW65922.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW65922.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW65922.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW65922.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW65922.1}.
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DR EMBL; PVWQ01000013; RDW65922.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8QVW7; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000256690; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 3.10.129.110; 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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256690};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 414..841
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1743..1820
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1698..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1946 AA; 210128 MW; BDEFBE41C531A769 CRC64;
MQVIFFSNKF PVENPCELFR RLRQQSKAPQ HLVLRQLLDE TTAAIRDEIR LLPADLRSLL
PPFQSILDLA EGYDWQRCPL AGTFECVFLC LASLGLWSHC IQPELQMHAK QADAKRCRDY
ETRPHAFRFS RDDATVTGLG LGFLAATAIV ASPALTDVPA AAADVIRIAM RAGIVVYQRA
QDLEPQSLDA PLQSWTTLVK GLGEEAVQRE LDGFNATVRA SFLLTRQTRL TVQETPRAGL
SRIYISVVEP DGGVFINGPP SRMRQLFSSP GPLKSAPRAP LPVHGGPCHA AHLYDRADVS
WVVEHVRPEV GRRECASAPR LLSMADGQPL RAQTGFELFE EATHILLTQI IRWGEVIAAL
ELSDEERNGL VVESCGRPGV IDGLVQALRG AAVHDLTAWL ADDHGGGDVA ASSDGKIAVV
GMSCRLPGAD DLQRFWELLE QGRDLHQRVP PDRYNVETHT DSTGTRMNTS QTPFGCFIDS
PGLFDTGFFD MSPREAGQTD PTHRLALLTA YEALEQSGYV PERTSSTTRA TVGTIYGQCS
DDYREANAGQ EIDMYFIPGN YRAFAPGRIS YFFKLAGPSF SCDTACSASL AAVQIACAVL
SRGEANMVVA GGLNVLTSSD SFAGLSRAHF LSKTGGCKVF DDAADGYCRG DGVASLVLKR
LADAQSDNDN ILGVILATAT NHSSAAVSIT HPHAPTQEAL YRTVLRQAGV SPLEVDLVEM
HGTGTQAGDA AEMESVTNVF TSPRRTERLY ISSVKASLGH GEAAAGVTSL IKALLIFQHN
AIPRHIGIKT ALNSRFPDLQ KLNVHIPAET VSWPVGTGRK RYALVNNFSA AGGNTALLLE
EPPQRPPPSA NACPATSYVV AVSAKHPLSL KRNIERLVAF LRRHPTTHLG SLAYTTTARR
MHHVHRIAIQ GSSIAEIIKG LELSSQPQGM ALRMPSIAFV FSGQGIYYAG IGHDLLENWP
PYAREMHRLD ALCVRHGFPS ILPAFHPTRP AGGRLANISS SLNPDPLMAQ LASVCVQMAL
VYLWKSLGVT PTLVIGASLG EYAALHAAGA LSASDTIYLV GQRAKLMMEL CTPNTHAMLA
VQATEEELAQ CVASARVKDG DSDGPASAYK YDYEVACINA RRSLTIAATR PATASIKAAL
EAQGYRGTEL NLPYAFHSFH MDPILPQWRE ITQQVPLRPL SVPLLSPLLA HTLPQHAQLP
PSYLADATRG SVRFAAALER AQQEALIGAH TVFVEVGIHP TYSGAVRATV NTADTDTATA
PTIVSSLRSD QDNWHTLAGS MATLYEAGVL LDWNEWFKPF EPQLRLLDLP GYAWHLKNYW
IQHNGDWLLW KDKAVEKGTE TSMFAGLSFR APLLHRMVEE TFWDAGGRVV MESDVHSDEL
VALAEGHKMC GRPVMSVFSY PDMALSLARY MLAKITNASN KANSATAAMN FGNVRILEGL
LPRKDRSRAQ HLRIHMEATS PAHMEVSFQR VAPGESAGTT LLATGTVSTG DAYSWLTEWA
RMAHLVRSRI DALHEFAQQG RADRLTGETV YRLFKSSIVD YAAAYRGIQA AVVCGTEAVA
EVVVSPAESW WTAPPHHVDS IAHVAGFVMN AGAGRAQGID IDNVNTAYVM EGWGSMRFGR
ALVPGRRYRS YVRMAARTAD DAGAAGLFSG DVYVLDVDDD STIIGVVGGV TLRPLPRILM
RRFFDPPDEV EDVHKENMPT ARSSQAIASG GAPDSSSSSV TSSTASSSSI VTSPTPDSDP
SACKPNSKAS KALALLAAET GIPVAELTDE TCLASMGIDS LLSLVLVEKF ALELGVHLPA
SFFIEFPTVP SSLRSITYLR KLATTTKDMA HTEPPISRSA QRPVPSSPIP PSKLLAALRC
IAKWISSHAS NENATALAFG GKGGVVVNNL GDRGLSGTGS HAAGRLALQS SCLFTCFMPS
RKPWSGPHWG RIMARADSDG ASDCSD
//
