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Database: UniProt
Entry: A0A182X139_ANOQN
LinkDB: A0A182X139_ANOQN
Original site: A0A182X139_ANOQN 
ID   A0A182X139_ANOQN        Unreviewed;      1285 AA.
AC   A0A182X139;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA003506-PA, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA003506-PA}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA003506-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|RuleBase:RU003694}.
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DR   STRING; 34691.A0A182X139; -.
DR   EnsemblMetazoa; AQUA003506-RA; AQUA003506-PA; AQUA003506.
DR   VEuPathDB; VectorBase:AQUA003506; -.
DR   Proteomes; UP000076407; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_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; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF23; FATTY ACID SYNTHASE 3; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          219..625
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   1285 AA;  143749 MW;  AD9ECC4130FF0CE0 CRC64;
     MFETVFAKAE QFLVIGYSFG SLLALEVVKR LEARSLRGKL MLIDGSPLYL QRFASHHLSG
     FDDEHLQMAI LTLVLRFSLP SVSNEILSSI MGEATYENRV TKMLDIGRES NPFSEDYTRK
     MMRVLLFRLK AAMNMSTEVK EKLASPLVLV RSGTIGDIEE DYGLTEFTSS SMIVKIIDGT
     HQTMLANMEL LEIINKDTFI HLPFTMKTVT NCSEPIDSEN SIVISGISGK YPRSDNVQEF
     ANNLYSKVDL VDDKEERWRH THPDIPKRLG KLNHLEKFDA DFFGYSPKEA HTMDPQHRLL
     LEHCYEAVMD AGLHLDDLRG SKTGVFIGIS MSETETYWTY KKTQMPYRRV MLGFTRSMTA
     LKIAYALDLK GPAMTVDTAC SSSMYALDWA CKAIRQGQCD AAIVAGTNLT LHPYITLQFA
     LLGVLAADGY CRPFDKNASG YSRSEANAVI LLQKAKDAKR IYAHVVNTKT NCDGYKLEGI
     TFPSNKIQKQ LLDELYSEVP YDPKDISYVE AHSTGTVVGD PEECDAIEKV FCPNRTSPLL
     VGSVKSNIGH SEPAAGLCSL TKCIIAMQTG LIPPNIHYTE PRKDVPSLLN GHLKVVDEAT
     PLGGPLVAVN SFGFGGANAH ALLHAHTRKK GHDIRPHDDL PRLVVWSGRT IEAVDQFLEG
     IAKHSFDPEL YALTHNIQRK ELAKMTSRGY AVLARGSDGS TTILQKNISK ANKTLPPFAI
     VFGQMDYEWQ ATLQAFEKFP PFKASVEQCL ALLKEPEHDC IFSKDDYATI LQRAVWTLII
     QIGVYQVLKS IGVKVDQYGG YSIGQITCAY IDGVLSLADA IRVAFTHGVL LSSYQNPETV
     NYRDIITNKE LNTKLTSILE SFLFAKATDR WKTATSVLSF RIYDPKSATQ MFNRIDSNAI
     VLQPLPSIQS TDSLVNSFLA SIGRAFIHGQ HCQLLDLYPT VTFPVSLETP MIGPLIRWNH
     SVDWHVANFQ TKKMVDQGSN QHSVTLAEQE YIAGHCIDGR VLIPATEYLY LVWDSFTSKT
     GTIPNEVAVQ FTEVEFLRAT TIAAGQVITL FVEINDISGH FEVSEGSTLV VKGCIQRLDH
     FQRQPIEQRN QPAITLPTKD FYKELRLRGY HYGGFFKSVM ESAADGSHAK IEWKGNWTAL
     LDCMLQVAII ALDTRSLMIP TRIESIKIDP DVIKPVMDQP TYSDRVEKLM TVARDSNPFS
     DQYARKMMRV LFYRLKVAMN MSTEVKEKIA SPLVLVRSAT IVDVEEDYGL SEFTVASLIV
     KIIDGTHQTM LANPELIEII NKDTL
//
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