UniProt: A0A2S6GTC4

Database: UniProt
Entry: A0A2S6GTC4_9PSEU

LinkDB:  A0A2S6GTC4_9PSEU 
Original site:  A0A2S6GTC4_9PSEU

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Ontology (4)   
   GO (4)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (38)   
   InterPro (21)   
   Pfam (8)   
   PROSITE (4)   
   SMART (5)   
All databases (43)   

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ID   A0A2S6GTC4_9PSEU        Unreviewed;      1692 AA.
AC   A0A2S6GTC4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:PPK68492.1};
GN   ORFNames=CLV40_105221 {ECO:0000313|EMBL:PPK68492.1};
OS   Actinokineospora auranticolor.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=155976 {ECO:0000313|EMBL:PPK68492.1, ECO:0000313|Proteomes:UP000239203};
RN   [1] {ECO:0000313|EMBL:PPK68492.1, ECO:0000313|Proteomes:UP000239203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YU 961-1 {ECO:0000313|EMBL:PPK68492.1,
RC   ECO:0000313|Proteomes:UP000239203};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:PPK68492.1}.
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DR   EMBL; PTIX01000005; PPK68492.1; -; Genomic_DNA.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000239203; 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:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   CDD; cd08952; KR_1_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 6.10.40.10; -; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR036299; Polyketide_synth_docking_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08990; Docking; 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   Pfam; PF00975; Thioesterase; 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; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239203};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PPK68492.1}.
FT   DOMAIN          33..455
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1336..1411
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1692 AA;  179064 MW;  CD65B6BC1DD526FE CRC64;
     MPTEEQLRYY LKRVVGDLDA ATARVRELEE RDTEPIAVVG MACRFPGGVR GPDDLWRLVA
     DGRDAITPFP ADRGWDLEGL YHPDPDHPGT SYAREGGFLH DAADFDAGFF GISPTEARAM
     DPQQRLLLEV SWEAVEHAGI DPTTLRESRT GVFAGLMYHD YAALLAHDEG AQDHAGTGNA
     GSVLSGRVAY ALGLQGPAVT IDTACSSSLV ALHLAARALR AGDATLALAG GVSVMATPGL
     FVSFTKQRGL ARDGRCKPFS DHADGAGFAE GVGVLLLERL SDARRHGHPV HAVVRGSAVN
     SDGASNGISA PNGPAQRRVI AQALADARIA PDTVDLIEAH GTGTTLGDPI EAQAILATYG
     QHRARPARLG SIKSNLGHTQ AAAGVAGVIK AIEAMRHGVL PASRHAEHPT TKVDWTAGSV
     ELLAAAEPWP DTPVRRAAVS SFGISGTNAH VILEQPETAP EPEFSVARAP ILLSGRTPGG
     VRAQAAALRT HVLDRPDLSL SDIGRTLALH RTAFEHRAGF VAAGREELLD RLGAVEETTR
     ARTGSGVLFV FPGQGSQWEG MAGPLRSDPV FARRLDECVE ALGEFVDWPV LDVLLGAPGA
     PSLDRIDVVQ PALWAMMVSL AEVWRAHGVA PDAVVGHSQG EIAAACVVGA LSLRDGARIV
     ARRSGFWQEL AGLGGMHAVS LPADEVARRI EPWGGVIAVA ADNSPYATTV SGEVGALDEL
     AAELTADGVG HRRVRGIGIA AHSPQIDRYR DALRAELAVV APKASEIPLY STVTGDLIDT
     GRMDAAYWWD NTREPVRFHQ AVRKALAGGI HGFVEVSPHP TLLPALAEVA QDTGARVAAA
     GTLRRQDGGP ERVLAALTEA HDQGIAVDWR TVFPGDRVPA ALPPYAFQHR RYWPEIAPPQ
     SPAWRYRVRW RPVPVDRPGR PGRWAIIGTA DHQPIAEALR RLGADVEITA DAERALAEFD
     NALALPGTLL DAVALVRALD TPGSGRLWLA TRHAVSTSDS APTPEAAAIW GLGRVAALEH
     PTRWGGLVDF PEAADERTWD LLARAVNATG EDQIAVRDGL LARRLVPAAP RVGEPTWCPK
     GTALVTGGTS GVGALLARWL VGLGTRDLIL TSRRGTDAPG ADALAADLRA AGATVRVISC
     DIADRDAVAA LLADTDVRTV VHAAGALTSA PTVDIDARHL AETMAAKVDG ARHLHELTTD
     LDAFILVSSG AGVWGGAGQG AYAAANAYLD ALAEQRRAQG LAATSVAWGA WGGDGTLARD
     PAIADALARR GNRMMDPDRA LDALRGALHD GDTTLVVADL DWSLFAPTFT IGRPSPLLAE
     IPRPAAPAVE PVEDVTDIPA LVRGLVASVL GHASPADLDP ARSLPEAGFD SLMSIRLRNA
     IAAATGRQLR ADLAFAHPSV DAITRLLTDA EEPEPATEPD SLYAFFRSSW EQGRIGDGYR
     LLTAAADLRA KFDTDAGAAN RVPPVRLARG KADPVIILFS TYVAIGGVHE YVRLATPFRG
     RREVAVLQPP GFERDHALPR DVDVLLGTQA AAVLDCADGR PFVLAGLSSG GTMAHAIAAH
     LEDRGHHPAG VALLDVYFEP TEIATLFDGD LDEGMFEREH TWTPMTTPRL TATAHYLSLF
     GGWTPPPISA PTLLLRAAEP HSPPLSDKPE DWQASWDLPH TAVDVPGTHF TLVEDHAPTT
     AEALERWIRD LP
//

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