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Database: UniProt
Entry: A0A2A4J2W6_HELVI
LinkDB: A0A2A4J2W6_HELVI
Original site: A0A2A4J2W6_HELVI 
ID   A0A2A4J2W6_HELVI        Unreviewed;      2162 AA.
AC   A0A2A4J2W6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PCG65733.1};
GN   ORFNames=B5V51_8757 {ECO:0000313|EMBL:PCG65733.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG65733.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG65733.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG65733.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG65733.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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:PCG65733.1}.
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DR   EMBL; NWSH01003873; PCG65733.1; -; Genomic_DNA.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000218220; 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:UniProtKB-UniPathway.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; IPR013149; ADH-like_C.
DR   InterPro; IPR049391; FAS_pseudo-KR.
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; 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; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF23; FATTY ACID SYNTHASE 3; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 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; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          23..428
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2057..2134
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2135..2162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2162 AA;  238888 MW;  7152B2C4809492D4 CRC64;
     MAPTTIAEDR LTSGHRLSHP PPGDEVLISG VSGYFPDSDS VNHLQENLFN KVDLISGDAR
     RWKLAHPEIP QRTGKINNVN KFDASFFGVH YKQAHTMDPM CRILLEKAYE AVIDAGVNPK
     ELRDTKTGVF VGACFSESEK TWFYEKMQVN GFGITGCSRA MLANRISYWL GVTGPSYTVD
     SACSSSLYAL EHAFRAIRDG HCDAAIVGGS NLCLHPYVSL QFSRLGVLSP DGRCKSFDNS
     ANGYARSEAI VVVFLQKAKD SRRVYAQLLH AKTNCDGYKE QGITYPAGHI QKLLLSEFYE
     ECSIPPSILE FVEAHGTGTR VGDPEELLAI DEIFCTGRKA PLRIGSIKSN LGHSEPASGL
     CSIAKMCIAY STGYLPPNLN YNVPREGVAA LAENRLQVVT DKTPWGRGMS GVNSFGFGGA
     NAHALLKNVA RDKVNNGIPF DDLPRLVCVS GRTESAVARI LDDLESRTVD AELVRLYHAI
     HDDDIAGHVV RGYTLLGSTP TKSVSLAREI QYFSGVRRPV WFVYSGMGSQ WAGMGKELMR
     IPVFAAAIEK CHKALEPKGV NLTKIITDPD PKIYDNILNS FIGIAAVQIG LTDVLKTIGV
     EPDYIIGHSV GELGCAYADG CFTAEEMILS AYSRGLASIE TPFIKGSMAA VGLGYNQIKS
     MCPPEIEVAC HNGPDSSTIS GPADIMKVFV AKLSSQGIFA KEVPCSNIAY HSRYISQAGP
     TLLKYLKQVI KDPKPRSEKW VSTSLPQAQW KDAKAALSSA EYHTNNLLSP VLFEETARLI
     HPNAITIEIA PHGLLQAILR RSLKKDVINI ALTQRNHKDN VQVLFTAFGK LYESGLNPHL
     ANIYPHVPFP VSQGTPMISH LVEWEHSEDW YVTSYKAQEK MKSGERTIRM SIVDEDCEYM
     AGHVVDGRNL YPATGYLVLV WETLGMMMGE LFTEVSVVFE NVRFQRATNI PKEGNLEFII
     MIQKGSGNFE IVESGASIVT GRIYAKKNVG QDYRVIPSLP EVSGPNIKHM LTKDFYKELR
     LRGYQYSGLF RGVLGCNVEG TRGRLAWVNN WVTFMDCMLQ MKIIGQDTRG LFVPTRIEKL
     SIDANMHYNA ISKMNPDSTK NSFEIRVYPD VDVIRGLFVP TRIEKLSIDA NMHYNAISKM
     NPDSTKNSFE IRVYPDVDVI RAGGVEVRGL HATPITKRLP LGVPVLEKNE FIANFGKSKM
     KLEDILRANI QLVLENIQTY KVKSIELVDE EYKKNEIEPI LETVGEMLGD LPLVQAELLM
     ISEEPIEVSS NITVENKKLS GESNTILFIG ANLLSRPEVL QSAVGTLRDK CFLISREKVR
     PNPKDYSDKY DIVTIHDTGV EYLVLFRKRV GARPAKFVRI LAADLEFSWI DKVKEELKEG
     QKVVLYTQDE PINGLLGLVN CLRKEPGGEV VYGLLISDPS APAFNPDLEF YEEQLDKDLA
     INIYQDGQWG TYRHLLLGDL ETVRANHAYV NTLTIGDLSS LSWVEGPIRE NHVFKSKEKV
     LVSVYCAALN FRDVMTATGR VTVDAVARGR LAQECVQGFE IVGKTPNGSR VMGMIRNRGM
     ANLAEGDKAL LWAIPDEWSF EEAATVPVAY GTVYYSMVMV GQIKHGESIL IHAGSGGVGQ
     AAINVALHYG CEVFTTVGTA EKRAFIKKLF PQLKDSHIGN SRDASFEDMI RRETNGRGVD
     MVLNSLSDEK LQASVRCLAY RGRFLEIGKF DISNNTPIGM YFFLKETSFH GIMLDYIFDQ
     TYAFRKRLQD LLLSGIENGA VRPLTYCTFE AKEVETAFRY MAAGKHIGKV IVKIRDEERS
     NRPVRPVVTP IQAVPRYICH EDHVYIVAGG LGGFGLELAD WLIMRGGRKI LLTSRRGVTN
     GYQSSRLRAW ASYGADVQIS THDITTEEGC EAMLQQALKM GPVDAIFNLA VVLRDSIFQN
     QTPETFKTSY GPKALATIYL DKLSRKLCPG LKDFVIFSSV SCGRGNAGQT NYGLSNSVME
     RICEWRKKLG LPALAVQWGA VGDVGLVADM QDDDVQLEIG GTLQQRISSC LSALDKFMKQ
     DAAIVSSIVV AEKKAGGSGC GNIVDAVAQI MGIKDLKTVS QQVSLAELGM DSMMAVEIKQ
     TLEREFEIFL TAQDIRTLTF ARLVELTAQR EAAASTSASR PVNVEGAAAR SRTQGRDLGP
     DG
//
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