ID A0A0F8X013_9EURO Unreviewed; 2996 AA.
AC A0A0F8X013;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKK23055.1};
GN ORFNames=ARAM_004821 {ECO:0000313|EMBL:KKK23055.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK23055.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK23055.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK23055.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:KKK23055.1}.
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DR EMBL; JZBS01001361; KKK23055.1; -; Genomic_DNA.
DR STRING; 308745.A0A0F8X013; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR013120; Far_NAD-bd.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000034291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 388..779
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1589..1663
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2454..2503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2996 AA; 329603 MW; 2D8FD3728BE233B1 CRC64;
MAIARQLHPP AGGNAVLLFG CQWLSFDADD FRQLRTTVLD NPEYHWMLDV LAELPRYYRL
ASTEHLPSLQ CISGEQKLRD LERWFRCDDL STAKFPLAYI QLAPLLMMTH FTQYGQYLRF
THPQYVEDGT ITTDESPVVE IVGFCIGFLS AAVASAADTR DQLQALEAVA MRLSMLLGAI
GDMKEFEEGY TSLATMWKTP ELEGRLPELL HAHPGSYITV RYDENRVTVM TRRQSVASLQ
HALQSAGFSA NRVDFNGRYH WPGHQDTLPA LFSLCDAHCE LQLPDAKSLV RPLRENTTGE
PVRCGPPLHQ LVLRAVLAQP CVWLKTFSSV HQAYLTNPES IVIEFGPERC VPPTFLPQLP
QGVVHFADLD LSQTLSRDHE LSGRPPAETD IAVVGMACRV AGADDLNEFW QLLCKGESQH
REMPRERHAD YETPWRPDAS KKPDPQQRLI LQVAYQALEQ GGYFTHPLPT SKNIGCYIAS
CTVDYEHNVN CYPASAYAAT GLLRSFLAGK LSHYFGWRGP SLCIDTACSG SAVALHHACR
AIMNGDCTAA LVGGANAITS PLAYDNLAGA SFLSPTGACK PFDANADGYC RGEGFAAIYI
KKLSDAIADG DPVLATIAGT AVEQNDNCTP IVVPDAPSLA GLFEKVTRCA RLYPRDITVV
EAHGTGTQAG DPAEYRGVRE VLGGPRRPGK LALGSVKGLV GHTEGVSGMI ALCKVVLMIQ
EGQIPPQPGF HSLNQHIKVS PDDHIDIATT LKSWDSGFRA ALINNYGACG SNASIVLTQG
PKSIVEVTGG VHDNDVPLPF RFCASEKARL QEYAVKFREF LAHQTETKGV SLANLAFHVA
RQSNPSLNCQ GVFCAKSLTQ LDSTLAALGD GDEKPLVRVQ KTVRPVILCF GGQVGRCVGI
DRSLYDAFPL FRSHLDACDS LLTAMGEKSI YPGIFSATPV SDTVQLQTQL FSLQYACARS
WIDSGLNVTA VVGHSFGELT ALCISGVLSL PDALTVILRR AVLIRDSWGQ DPGAMLAVEG
DKAGLKQHME GSSASIACFN GPRSFTIAGP TRAVDTLQET LESDPNVRVK RLSITNAFHC
SLVDTILPAL YQVTDGLKLN TPRITLERAT AMAENGIPPS TVIGDHLRQP VHFEDAVRRL
ATQHGPSIWL EAGSNSTIAS MVRRALDSSG SEHAFHSLNM STGSSLQSLT DATIGLWKDR
ISCMFWAHHP LQSREYTPLV LPPYQFEKSR HWLENKPLPI TASSMNDKSE SPEDEPRFSF
VGYQDSLQRR AKFLIHTNHP WYIESVSGHC AAKTAPIAPA SLLLDYAVEA LRSLPDNKGR
IPSMHDVGSE APLRLNPNRE VWLELTAEPD SKYTWSLKFQ SQDRQPGPGC SLLLHCTGRV
TMHDPSDGKL KAEFTRYSRL VSHSRCKELL SDPDVDDILQ GQNVYRTFSE IVEYSQPYRG
VQKLVGKGNE SAGRVIKRYS GQTWADAFLC DSFSQIGGFW VNCMTDRPDD EIYIASGIEQ
WMRSPRYANL DTPRPDTWEV FAKHQRADGW YTSDVFVFGA DGDLAEVFLG LRYSRVAKNL
FIRLLGGSVP KREEGPKEEK RPQENSSSAD LVERVKAVVA EFCALDPDEI QNDSHLANAG
VDSLMAMELA RELEEAFHRT LSVEELLEAE TFADLVRCVQ AAVGVVVPEN GSLYSIDSAT
VISSTSSDRK PSSPTESLTS VSDTADLSLP FEVRVEAFRG TKAFTDRFLE ENQCSGRLHE
FTPLQVKLCV VLTLEAFETL GSNIRSAQVG ECLRRIPFGS QHQSLVDYLY NRLEEACLIS
LDGMTAVRSE ISAPTESSTS ILSQIESEYP EYAGASKLAF YTGSQLASVL RGEQDGLHLI
FGTPEGQQLV SWMYGEEPHN VAGYKLMAEY IRRVVEKVVS SAAGGCGPLK ILEMGAGTGG
GTKWFLPLLA ALPVPVEYTF SDISPAFLAQ ARRKFKDYPF IRYCVHDIEK PPAAELQRTQ
HIIIASNAVH ATSNLQESTR NMRQALRADG VLMMLEMTQP VFAIDLVFGL FRGWWVFNDG
RRHAITSEKR WEEDLHAAGY GHVDWSDGES KEVSIQRVIF ATAQGEQGER LPSPVLKHIE
RMQVVEKYAQ EAIQGFTAPG MSLHEHSTES DKTCVLVTGA SGSLGSHVVA HLATLSTVDT
VVCLNRISGE DPLRRQQKSF AEKGLSLSAA EEAKLVVLEV NSQCTELGLA PDQYKFLQTS
VTHIIHNAWP MNGVMPLSSF EPQFRVLRNL LDLARDAAEM RARPLRFVFV SSIGTVGGGG
ALEKRTQIEQ VMANGYNEAK FVCERMVQET LQRYPERFQA TVTRPGQIAG SAQTGYWNTP
EHFPAMVKSS QTLGVFPTLQ GEMGWTPVDV AAHVLSELLL AESEPEEIYH IDNPVGQNWS
TVVGIIAEEL NATTVPFKEW IQRVRQEESN RGENPARVMA NCYLYMEIRR KPVPASSPTQ
YGVVQRPLTP NPRPPPHPLQ NSQPPTSLQP PHSIPRYRSH PNLGASYHAA ATPAIPRAET
SIPASSEKPS FYEDTRHFLG GLIHHPSEST KHYSILRHSP GVIFYRGPTT SVTVSIFADT
RIPADRSLWL QPKGWTGKTG MRAKAVLHLH DDWINIPPPL ALRAHQVEPA TERAWQRDIS
KFRKKAAARI RDTHRLRETV VARIPADAGD GYFQLVLCHG QKKVLCRSPV FRLFSTSKDP
SSVRGASLAS MPLEVGALVL GSYARTAAQT VLAPVTTAAQ SAVAPYKPGW LKQTAATTVA
STAYSCSGLA DRIARDTADP NIPDTAQPSL ENGPQPPFPI EFTARPTHAL DASRIALKIP
SDVEAKFHGV FFVGWARCAS DHPWQAVIFS MRTWDAAHTT GPVSLSQTTR KVAALRFLDD
PVPTPLPATI NIRVLGFLRP DIAPPTPRTE RELVSARQTA AEAAVLAEQC DMECARGILE
HPLWGPDSTS SPKGWMERTK EGYENVRTRG WKMAERVGVR SGLEHESGGG FYIVRD
//
