UniProt: A0A0F7N228

Database: UniProt
Entry: A0A0F7N228_9ACTN

LinkDB:  A0A0F7N228_9ACTN 
Original site:  A0A0F7N228_9ACTN

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (35)   
   InterPro (18)   
   Pfam (8)   
   PROSITE (4)   
   SMART (5)   
All databases (42)   

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ID   A0A0F7N228_9ACTN        Unreviewed;      1661 AA.
AC   A0A0F7N228;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKH80922.1};
GN   ORFNames=AA958_00665 {ECO:0000313|EMBL:AKH80922.1};
OS   Streptomyces sp. CNQ-509.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH80922.1, ECO:0000313|Proteomes:UP000034283};
RN   [1] {ECO:0000313|EMBL:AKH80922.1, ECO:0000313|Proteomes:UP000034283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH80922.1,
RC   ECO:0000313|Proteomes:UP000034283};
RA   Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA   Kalinowski J., Heide L., Kaysser L.;
RT   "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT   of Meroterpenoid Chemistry.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP011492; AKH80922.1; -; Genomic_DNA.
DR   RefSeq; WP_047014288.1; NZ_CP011492.1.
DR   STRING; 444103.AA958_00665; -.
DR   KEGG; strc:AA958_00665; -.
DR   PATRIC; fig|444103.5.peg.153; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000034283; Chromosome.
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; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR041618; PKS_DE.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR015083; Polyketide_synth_docking.
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: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; PF18369; PKS_DE; 1.
DR   Pfam; PF00550; PP-binding; 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; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 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   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000034283};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          35..461
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1492..1567
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1616..1661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1661 AA;  173255 MW;  A0ECC288D39F956D CRC64;
     MASSNEEKLR DYLKAVTADL RQTRQRLQSL EERDHEPIAV VGMACRYPGG AVSPDALWEL
     VSAGGDAIGE FPADRGWDLE AVFDADPDKA GTSYARRGGF LYDLPEFDAG LFGVSPREAA
     AMDPQQRLLL ELAWEALERA GIAADGLRGS ATGVFAGTSA ADYGPRLHEA TAGAEGYMLT
     GTTPSVASGR IAYTLGLEGP ALTVDTACSS SLVAVHLATR ALRARECTMA LAGGATVMST
     PGMFVEFSRQ RGLASDGRCK SFSDDADGTG WSEGAGMLVL ERLSDARAAG HPVLAVIRGS
     AVNQDGASNG LTAPNGPAQQ RVIAQALADA RLTARQVDAV EAHGTGTSLG DPIEAQALLA
     TYGREHSAEQ PLWLGSVKSN IGHTQTAAGV AGIIKMVQAM RHGRLPRTLH SETPSRHVEW
     AGGGVALLAE EVDWPESDRP RRAAVSAFGI SGTNAHVILE EGPPPAEPAE RSGEGGPRTA
     LWTLSARTGE ALRARAAELA EAVRTEEPPA AGDVGWSLAT TRAAFDERAV VLGGDTAELA
     EGLAALAADR GSPRVVRGSA VSGAARPVFV FSGQGAQWPG MAVGLWDSEP VFAASMERCA
     AALAPYTGYT LREKLTAPAD DAAWERDDVV QPLMWAVMVS LAELWRHHGV TPAAVVGHSQ
     GEFAAAVAAG ALSLEDGARL VAVRSRVVHA LSGHGSMASV SLPVAEVEKR LAETGGDVGV
     AAVNGPSATV VAGVDADVRA FMRDCEEQGV RTRTVPIAYA SHSPLVEPVR EEMLRELAAI
     TPRAGEVPFY STVTGEPMPT ESLDAAYWYR NLRSPVLFAQ TVERLMDAGH TVFLEMGPHP
     VLVPAIEQVL DATETDGRAL GTLRRDEDGE PRFKQALAEA YAAGVVPDWQ VLFPDARTVP
     LPTYPFQRRR YWLADRDDRA PRAAQTRAGG SDEAFWALVE QADTEALRRE LPEVGEDALR
     AVVPALHRWR SRTRTDAALA GQRYEIGWRP AAERRTPGPD GHWLLVTRTG AAGRLADWAD
     AAGAALSARG AGVTVVELDE RADDERAGIA RRLSAALAGE AVDGVLSLLP LDERPHPGHA
     ALPSGVGGLL GLVQALAGLG VAAPVWSLTC AAVKALDDDV LAHPEQAETW GLGRVVALEQ
     PQLWGGLVDL PERPGDEDWL RLCAVLAGGA GDEDQVAIRP GGPRVRRLLP APAPADSPVW
     QPGGTVVVTG GSGSLAPHLA RWLADGGAEH IVLASRRGPD APGHEALAAE LAGRGVGVTA
     LSCDLTDRDS VRALLRRAAE LGGPVRAVVH AATSTRLEPL ADATAAGVAE VLAAKALGAV
     HLAESMDPDG PAELVFFSSI AAVWGSGEHG AYAAANAFLD AYAQQLRGRG RKVTSVAFGA
     WRSEVLPEGL DEAQLERQGL PLLDPELALA GLGREVAGAG GGRPVTLVDV DWETFAPVFA
     SARPRPLLDE IPAVRGALRR SAEAGGTGAA DGGDTGERLR KLAGLPEAAR GREVLDVVTA
     EVAAVLGHSP ADRPAPMRTF KELGFDSLTA VALRNRLRAA TGLSLPVTLV FDHPSPQALA
     RFLTGQLGTA GEQAAPGSVH EELDRLAAAL DAAPVEGAER AAVRDRLQAL AAALAGGGTA
     ASGRGEDDDA DLDDASTDDL LKIIDDEFGP AEPGPTASTT G
//

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