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PKS18_DICDI
ID   PKS18_DICDI             Reviewed;        2999 AA.
AC   Q54TW0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable polyketide synthase 18;
DE            Short=dipks18;
DE            EC=2.3.1.-;
GN   Name=pks18; ORFNames=DDB_G0281475;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=17660200; DOI=10.1093/bioinformatics/btm381;
RA   Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J., Kessin R.H.,
RA   Hranueli D.;
RT   "Polyketide synthase genes and the natural products potential of
RT   Dictyostelium discoideum.";
RL   Bioinformatics 23:2543-2549(2007).
RN   [3]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA   Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA   Ivens A., Martinez J.L., Escalante R.;
RT   "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT   and specific effects from PAO1 and PA14 strains.";
RL   BMC Microbiol. 8:109-109(2008).
CC   -!- FUNCTION: Probable polyketide synthase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated by P.aeruginosa, PAO1 strain and PA14 strain
CC       infection. {ECO:0000269|PubMed:18590548}.
CC   -!- DOMAIN: Modular protein that is responsible for the completion of one
CC       condensation-processing cycle. The beta-ketoacyl synthase region is
CC       responsible for the actual condensation reaction while the acyl/malonyl
CC       transferase region is responsible for incorporating carboxylic acids
CC       units onto an acyl carrier protein (ACP) domain (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC       synthase genes localized in chromosome 3.
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DR   EMBL; AAFI02000041; EAL66719.1; -; Genomic_DNA.
DR   RefSeq; XP_640701.1; XM_635609.1.
DR   SMR; Q54TW0; -.
DR   STRING; 44689.DDB0235183; -.
DR   PaxDb; Q54TW0; -.
DR   EnsemblProtists; EAL66719; EAL66719; DDB_G0281475.
DR   GeneID; 8623087; -.
DR   KEGG; ddi:DDB_G0281475; -.
DR   dictyBase; DDB_G0281475; pks18.
DR   eggNOG; KOG1202; Eukaryota.
DR   eggNOG; KOG1221; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54TW0; -.
DR   OMA; WECLENS; -.
DR   PhylomeDB; Q54TW0; -.
DR   PRO; PR:Q54TW0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 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; IPR013154; ADH_N.
DR   InterPro; IPR013120; Far_NAD-bd.
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; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 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; PF08242; Methyltransf_12; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 3.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2999
FT                   /note="Probable polyketide synthase 18"
FT                   /id="PRO_0000371383"
FT   TRANSMEM        1448..1468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2620..2640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2476..2553
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          168..221
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          651..684
FT                   /note="Acyl/malonyl transferase"
FT   REGION          1066..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2556..2575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        661
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2513
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2999 AA;  339544 MW;  FFD29B5F1927E5F5 CRC64;
     MGFKVNKNLN ETNDNSDNDV AIIGIGFRLP SGNLNKSNDS PIILWDNLMK GFDGMVETSE
     RWSDNFNQLG EISNKSGGLL PLDEWKSFDP LFFGINPSEA QTIDPQQRIL LKCTWEAIED
     SNIDPIKIRG SKTSVYMGGT SVEYKELNKN SNEINPNIFG STFNTIANRI SYCFDLSGES
     MTLDTACSSS LNAIILGYQS IKSGTSNLSI VGGVNLILDS NLSKSYSYLN MLSKKEGKCM
     SFDSRADGFV RSEGAGVFIL KSLKQSIIDG NNIYCVIKGA SSNIDGNGLN DKQNFYSPSS
     SSQAENINRA LSSTKGSVKI DDIVYVEAHG TGTPTGDPIE LEAISRVFKT NNNDNNNQQH
     QNPILIGSFK SSVGHLESAS GSASLVKCCL MFKNQYLTPN VNFKTPNPSI KFDEWNLKVV
     TEPIQFKDVK KSNNFSMILN NFGITGSNCC LILSQYNGNH NDEQENQQQQ QQQGKQYLIP
     FSANSIQSLK QYESLINENQ FKESNDFKEF VKHQIYSKSI SLYQRSVSIA SNWNDFNEGM
     KSTNNNNNKT QTSNSKSSNI SIIPKNPITV MVFAGQGSQY STMAMELYNN EPIFKESMDR
     LDNRLLRYYG YSVLEKFRSS CDSDSIHYPT IAQPSMCMLT ISLFELYKHW GIETSFIIGH
     SLGEIPAAYC SGMISLDTLC FLIYHRSVAQ THTHRNGRML SINISPEEYN SNYSLKYPKV
     EIACYNSPTS IVLGGEETIL NQISNDLKEK GIFSAMLGSL SSFHTSSQRI IKDQVIDLNI
     ECKLAKIPSF STVTTNLFNE TTLFNSEYIF NNMALPVKFS QSISNLFKHI EINNLGSDIV
     FIELAPHPTL QFYLKQMASS YEKVNSNLKI STYSPLHKKK NDIEEIQKTI SQLYCNNGYS
     INFKSQFNND FKINKINSIL PNYQWEDVIH WREDLIHQKH NTQGPPIDQL GLSLIESSPN
     LKSYQTFIDI SRKPFQYLKG HFVNGKYYFP GCGYIDNLLK IYGSQDFTIA SMEFKSPLIF
     TEGVSQCLQT NIFQTGKSEF RVNYHFKDTK SNEWIQSSVA HFQLFNNNNN NNNNNNNNNN
     NNNNNNNDSD DGNSTNKKYN IEDIINNKCN FTKLSNNELY ENIKSKTGIY YTGEFKTVSN
     LYVGENCSLA EIPITIKSYE SSFFSPSILD TCLHGTIGLI DEKSQIVFER VEGFEYHSSN
     IPSQNELSSL KHTKLYSLTE SFKRVGDSYS SSITVMLEDG RVLIEFKKVV CKSLTNVIDS
     LIIQSPLNEL YSTCMQTIDS PIQPSLSSSS LIQLLGNTNE KVKINYSQFI SNQLYYNIIK
     RCPQLNIETI KSKNIEQLKE SYNSLNTKYS KLFKSVFETI QSIGINNEDN SEFNETNIQH
     YKILLKSTRI IAKLLFPLKD DDLSKDTGQS LFENGILDEF NSNYFNNNNQ VISNIIKESL
     LPILNEKMVF RIFGFGGFGS SLSSVVLNKI NELLQEFPNS EIDIEFTHAD ISSSSSSFGS
     STPNFKPNFP QINEKVHIIY KSLDLEKQLS SEQMIKPSYY DFVIMSNVLH FTKDVKSVLD
     QIHQILKPNG QIILVEPINK SILLDNIFGI FDQWWSFTDL NIRRNDCYIS KDTWNSLLLD
     CNFDNSKVLI STKEISNFYI IQTQKPSISN LNTNSTTNGD TVIIYGDELK FISSDSNKEI
     KISNIQQFNE LIEKSIITDE SIIYFTKSTN QLTVDNFKLV TLEYIQINQK LLSNNLKCKH
     VLITLNSDNM NYLSASLIGA TRYFEEFPQL NLFNLDFDQN SINNNELEKT IKLLLDSNQF
     IQKEFFIKNS KVYYERYKRE LNLNNFFKES QSFSNEKNQL YAKLSPNLEY ILKSKKVIKD
     DEIEVEVKAT GINYKDYLIY CGLVSAESIN RYGDVNNPEF GIEYSGIISR IGNNITNFEI
     GDQVYGMGLD TISTHVIVNP NYCYHKPTNI SFQEAASIPC VYLTSLCSIF NIGCLSVSGN
     ESILIHSGTG GVGLSALNIL KWKGHKSHVF VTVGSKEKEK YLLDTYGDFI TGIYSTRNKN
     YVEQIKLKLK QLGSNKNGVD LILNTLSSDY MESNFKCLNT SGRIVDLSVT HLNHNEYINN
     NNFKFNFGYH NFELTFINKF LIQKSLKKIK IGIESGELKL IPITAYSNSN AKEAIEFINQ
     RKHIGKIVLN NDNDILDSLF NNLSNERNSK FTTLKPNYQI NKDHLGSNII VTGQSGIILE
     ILKWIVKFSE NVKNIIILSK SSMKWGLELL IKKNKHINFN FKSIDIGDSN QVDKSIDEIL
     NENSITNIDS IFHFAFEHTI CDVNDIEINH LTKSHGAKTM GAINLHNQSI KRNWKLKQFI
     LSSSVTSMIG STDQCTYVCS NRLLDSLSKY RNSIGLPSIC TNYGSVQSAG IVSRNKSIEK
     LLDAQGLDPL SINMILGSLD SQIQNVNKST NLMVSPFNFN NFFETFKNHS MIHKFDFITN
     LLENNKSKNS NNGNTEGESN IDTLFLNKVS ELLSMELPKI NQDLKLVEYG SDSLLIVQLK
     NWIDKEIFPN LITIQQLQTN TISSSIKIIT NQFNSKSTDG RKKQKQNGIN VSSNKSSLPT
     LEFWKNETKL DEEEFNFILD SSTKSKINHK DQLKDNEKRI LLTGSTGFLG AYLLWHLIQM
     DNCKIVYCLL RNKKLFNNPL NDIIDNLKHH QLYDKQLNES HLSKIVAVVG DLSKIKFGLS
     DDNYSLLSND TNLLLNCGAD INLSSNYEES KQVNVVGTKE MIKISLIGNI KPKPIITISS
     FSVFYNQKLN QEFDESIVTP KLETINDLPA GYIQSKVISE IILTEASSRF NIPSAIIRAP
     SIFSNPETGI GHSADIIQLM LQSCFKLGYY PSGNGVDFDL LCSPITWVAD NTIKIIFNDN
     IINNKEPQQL TSPLKPNIYS VYGKVLDLFE ILQVLKSDEG GNCKEIEINQ WKQMVMDSKE
     KACIKLRTFH TLQFDGRNIL NKGHGISNKQ KSYLQSIGSF GNGGEITNQM IFKNVQSNN
 
 
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