ID A0A1A9W885_9MUSC Unreviewed; 2400 AA.
AC A0A1A9W885;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:GBRI009807-PA};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI009807-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI009807-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI009807-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR STRING; 37001.A0A1A9W885; -.
DR EnsemblMetazoa; GBRI009807-RA; GBRI009807-PA; GBRI009807.
DR VEuPathDB; VectorBase:GBRI009807; -.
DR OrthoDB; 3378513at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000091820; Unassembled WGS sequence.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:UniProtKB-EC.
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; 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; 3.40.50.1820; alpha/beta hydrolase; 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; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 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; SSF53474; alpha/beta-Hydrolases; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2007..2084
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2400 AA; 268224 MW; 2FD82460AACC1572 CRC64;
MTEFKEKVNS IVKNKSKKFL RIHPETDGDD IVISGMAGKF PNCHNVAEFE YKLYNKVDMV
DDDERRWRHF HPEIPKRCGK IYDLEKFDAT FFGVHFKQSH AMDPQARILV ETAYEAIIDA
GISPKSLRGT KTGVYIGSSI SESEKTWMYD KVSPGGLSMT GCSRAMLANR VSYSLGLEGP
SYLLDTACSS SMYALDNAFT ALRVGEIDAA IIGGANLCLQ PLVTLQFVRL GVLAADGYGK
PFDQNASGFT RSEAVNCLFL QRKRDAKRVY ASIVYSKTNC DGYKPEGITY PSRRLQERLL
REFYQEVDIC PEDLGYLEAH STGTVVGDPE ECQAIDNVLC SQRSKPLLVG SVKSNAGHAE
PASGICSLVK VCFAFETGKI APNINLKDVK SEISALAEGR LIVVKDIMNL EKPYVGVSSF
GFGGANAHAL LKAFDKSKIN NGVPDDNIPR LITWAGRTEE SVNVIFDSIE GKPLDAEFIS
LLHNIQNEDM TGLVFRGYGV FAKNGNTSAK SLVRDVHHYS GIRRPIVWVF SGMGSQWTEM
GSSLMIIPQF RQSIERCHKA LESKGLNLIK ILTSSDATIF DNILHCFVGI AAVQIALVDI
LRSLSMEPDY VIGHSAGEMG CGYADRGFTP EQMILASYYR GKVSLEIEKI KGSMAAVGIG
YKKIVNILPE KIEVACHNAA DSCTISGPVE DVERFVNELK SKDIFAKEVP CSNIAYHSRY
IAHMKPQLLK YLRKIIPNPK PRSSKWLSSS VPQANWQQEG RNLCSAEYHT NNLLNSVLFE
ETFALLPTNS ITIEIAPHGL LQAILKRSMP NGIHIPLTQR GNKGNDVFLL SAIGKLFTNG
VNFPTANLYP KIEFPVSRGT PGISSLIRWD HSEDWFVTKY EDMKTKSKGE RSYTVNLDSD
DEDFLTGHVI DGKVLIPAIC YLRYVWETFS LMYHGPSYMD VPVEFEEVKF LRATSISPGE
NVELNVMIQY GTGYFEITES GALVVTGSIK DIEQPSPPEV YEFTEESDFP KLCQKDFYKE
LRLRGYHYSG SFQAVREGRG DGLYGKIGWN YNWVTFMDAM LQIQILGTDS RTLLLPTKIR
KIRIYGFHHM GLLTAMDPEN RVFEVYVDRK YDRIVSGGIE IVGLHASPVQ RRKSPGIPVL
ERYQFVSHFP APAFSIQDAI RICVQLALEN STVTKIKAVE VDTDGRYPII ENFMEAIEDL
PVVTGDYLFL SSQTPEDISK VVHVENGKLF TQKNCHFIII GGLCGEMNEL SVTQASKCLV
ERGYLVVRNN NSSGTSNLKI PIDFKMIAKL PIENSAEVIL LLQYVGTKKY SPEPILVEVS
DCDKEFKWIA QVQQSINNKT PTIVYAYNEK LNGLIGLVNC LRKEPDGHLI TCFFINDERA
PAFNINEPLY AAQYALGLAI NVYQNGKWGS YRHLQLKQDV EAAPRKDHVY GNVSQRGDLS
SLRWFEGPLK PKDCDIKIAY SSVNFRDLML ATGRLAVELY GDSRLDQSCV LGLEYSGIHR
KTGRRVMSMV AKGGVGSYVE KASRLVWNVP EHWSLKDAAT VPVVYITVYY AFFMLSDIRK
GKSILIHAGT GGIGLAAIRV ALAYNLEIFT TCSTTQKKQF LLDTFPQIKE SHIGNSRDTS
FERMIIRETN GRGVDFVLNS LSEDKLLASI RCLGMRGKFL EIGKFDMAND TKLGMSCFLK
EIKFITALAD QLFLASDEEV AHLKALIDKD IANGIIQPLP ATVFQAHEIE QAFRHMVGGK
HLGKVVIQVR EDPESELTMP VKVVKQVYFN ANLSYIIPGG LGGFGLELAD WMAVRGAKKL
ILNSSRGLSN DYQRHRIALW KTYGCEVLIS TSNICTYEGC CNLLKEAKNM APIGGIFNLA
VKLQDAIFLN QTKEKFVKCF DPKAAATKYL DELSRVMCPE LEHFVVFSSV SCGRGNPGQT
NYGMANSVME RIIEDRLRNG FPAKAIQWGA VGEVGLIADM SEDKIDVDIG GTLQQRISSC
LQELDTLLSA PDAVVGSMVV AEKRLGRSGS ENIIQSIMNI LGARDLKSLS LGTTLSEMGM
DSLMAVEIRQ TLERNFELSL TSQELRALTF QKLQEYDEAR DRKRTETAKI ICDSKTTPQG
IELLLRNLGD ETRCNEAMIE LQSVLDVSQP AALPTIIIPG IEGTAGQVWY NIAKHIKGNV
NILQFHRFAD LTTIKEIAEA CLEDVKAVVK SNRQFYIVAY SYGTFIALEL VSMLEKIGFH
GQLLLIDGAP HFLTKHTRLH LGKHTTNDDV YNLLLSIFVQ MIFPEDVKGK VGQIFNQFPT
VEQKMKQFDK YIAKQNLYSP HYLITMIHTM FKRIRSIITY DLKNFTLVNT PITLVRPAEI
ALQDIDEDYC LREITKEAVV VKVIEGDHTS MLDNPILPEL INDFNPSLVD LRVFQKELKQ
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