ID A0A1F7ZNF1_9EURO Unreviewed; 1761 AA.
AC A0A1F7ZNF1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGM40961.1};
GN ORFNames=ABOM_010478 {ECO:0000313|EMBL:OGM40961.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40961.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM40961.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM40961.1}.
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DR EMBL; LYCR01000125; OGM40961.1; -; Genomic_DNA.
DR STRING; 109264.A0A1F7ZNF1; -.
DR OrthoDB; 20296at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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: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 CDD; cd05274; KR_FAS_SDR_x; 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; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF46; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..430
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1683..1757
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1659..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1761 AA; 190704 MW; 6CA9183E8C7059B3 CRC64;
MEDNDISHDV AVVGMGCRLP GKINTPEELW RSILKKVDAS SEIPSLRWAP YQRNAQDARS
IGKVPRRGYF VENLENFDAS FFSISPKEAE QMDPQQRLAL EVAWEALENA GIPLSSLSGS
DTAVFMGVNS DDYGKLLLQD LPHVEPWMGI GTAYCGVANR ISYHLNLMGP STAIDAACAS
SLVAIHLGRQ AILGGESKVA IVGGVNAIFG PGLTSVLDKA GALSSDGRCH SFDDAASGYG
RGEGAAVVIL KNMAEAVKDG DHILAALKGT AVAQDGRTNG IMAPNQKAQE LVARKALEVA
RVGASTIDYV EAHATSTPVG DPTEVSAISA VYGKGRSPDK PCYIGSVKPN VGHLEAGAGA
VGFIKAVMSV QKGILPPQAN LKTLSTRVDW SEGVRVVQDI EDWPSSGNPR RAGVCSYGYG
GTVSHGIIEQ YIQTDPPINS KGQWPKGTQV LLLSAPQRRS LEAQAATQAE WMSTVGKLND
LRCVAATLGT RRSHLKYRAA FVVESHDDAA EKLNAFARQT PIKWATSGRL PEGDDRPVVW
VFSGHGAQWT DMAKDLLQCP VFRDVIESVE TLIQDEMGFS AIQAMEMGVL NGSDQVQVLT
YLMQIGLSAV LRSLGVSCGA VIGHSVGEIA ASVAAGCITP VEGTLIVTRR AKLYRRFMGA
GAMVLVRAPF EQVTSEISTQ HVNHLVAAIN SSSSSCVVSG PREEIEAFAL NLNNKGVKTF
RVDTDIAFHH PMLSELMDPL EEALDGCISP SQSKVTIYST STSDPRSTMD RGIRYWLDNM
VNPVQLTSAI AAAAEDGMRL FLEVSSHCIV SHSISETLLN IGVEDYTVTN TMLRDTPAER
TILYSMAQLH CQGAKIDWSQ YMQGAWAPNV PTTTWNHRPI CRQVNAWSEQ PTRMHDVDKH
NLLGHRTSIA GDNTIIYETR IDEQTKPFPG SHPVRGCEII PAAVLVNTFL QGTGAQVLYN
FCLRVPVATS EPREVQFVVQ SNQSRLCSRL VKGNGTEGDS GWLTHTTSCW TVEQDEQPTT
RKVDIEAVKP RINNKLEDNF SIDYLASVGV SAMGFPWVVT EHHGNLDEMV ARVDVSPNNG
SGEIPWDKSS WAPILDSATS VASTLFFDNP RLRMPAHVKE VKILVEQPPP KIAWLYVKKA
TDSDYAAHIS ICNEDGTVLL QVNSMRFSEI DGTPEDRGGL EGLVHQLAWP PATYSESPLA
ISHVILISRD ESLANEYAAS INRDTQTVII LISPEELAKL AEDANVLHQK DTIVTYIPGC
VSSLDSITSA SQEYTSDLVN IMKLISSSAF SIKVFVLTHR VAKAETATSL AQAPLHGLSR
IISSEVPDNW GALIDLETPV FPLAIMKYVQ NGDIIRISDG IPRVARLRPL PRTKALRPSG
QNSLLPRPSG TYLITGGLGD LGLATADFLV QKGARRIILV SRRALPRRKD WAALVHSASP
LAPTIKKILS MESRGATIQA IAVDISSHNA ASQLSSRIDD LCLPPVQGVV HAAGVLHNEH
VLSVTPDSFE RVLAPKIAGS LTLNMLFPPK TVDFMVLFSS CGQFFGFPGQ GSYASGNAFL
DALATYRRSQ GDNTVAMQWT SWREIGMAAG SEFVKAELAT KGITDISQDE AFQAWMHVSK
YDVDHAVVLR SRALEKHEPL PSPLLIDIAI QKVSSILTPP PSPPLSASGD SLTPPQTPAD
RFDSLTRQVR ECVASVLQME TDEVASQELL SNMGMDSVMT VHLRGRLQKS LGVLVPPNLT
WCHPTIDHIV KWLMEKAGGN E
//
