UniProt: A0A1Y0RX57

Database: UniProt
Entry: A0A1Y0RX57_9CYAN

LinkDB:  A0A1Y0RX57_9CYAN 
Original site:  A0A1Y0RX57_9CYAN

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (45)   
   InterPro (23)   
   Pfam (11)   
   PROSITE (4)   
   SMART (7)   
All databases (51)   

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ID   A0A1Y0RX57_9CYAN        Unreviewed;      2209 AA.
AC   A0A1Y0RX57;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ARV63050.1};
GN   ORFNames=BZZ01_15445 {ECO:0000313|EMBL:ARV63050.1};
OS   Nostocales cyanobacterium HT-58-2.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX   NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV63050.1, ECO:0000313|Proteomes:UP000196302};
RN   [1] {ECO:0000313|EMBL:ARV63050.1, ECO:0000313|Proteomes:UP000196302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV63050.1,
RC   ECO:0000313|Proteomes:UP000196302};
RA   Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT   "Genome sequences and microbial community composition of HT-58-2, a
RT   tolyporphin-producing cyanobacterium-microbial holobiont.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP019636; ARV63050.1; -; Genomic_DNA.
DR   KEGG; ncn:BZZ01_15445; -.
DR   OrthoDB; 499075at2; -.
DR   Proteomes; UP000196302; Chromosome.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.10.129.120; -; 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; 3.10.129.10; Hotdog Thioesterase; 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; 3.
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-like_N.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
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; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
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:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF21394; Beta-ketacyl_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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 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   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196302};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          28..455
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2086..2161
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2209 AA;  242627 MW;  22B56A51E4982330 CRC64;
     MNISDSQRLL LALDEAVEKL EAVERAKTEP IAIVGMSCRF PGGANDPEKF WQLLENGTDA
     ITKIPADRWD ADFYYNPDTN VSGKICTRFG GFLEQVDQFD PQFFGISPRE AISLDPQQRL
     LLEVTWEALE NAGFSLSQLH GSKSGVFVGI GQNDYAQLQF YSGDLTKIGT YEGTGNGFSF
     APGRLSYILG LHGPSIAVDT ACSSSLVAIH LACQSLRTGE CNTAIAGGVH LILSPEVTVF
     LSVSQTLSPD GRCKTFDASG NGAGRGEGCG VLILKRLSDA LADGDNILAL IRGSAVNHDG
     ASGGLTVPNV VAQQTLIQDA LNNAKLEPNE VSYVEAHGTG TPLGDPIEVR ALATVLGEGR
     SKEQPLFIGS VKTNIGHLEA AAGVAGLIKV VLSLQHGQIP AHLHFEQPNP HINWNELPIQ
     VPTKPVGWPT GEKNRIAGVS SFGFSGTNAH VILEQAPQEI QSSKFKIQKE EIIERPVHLL
     TLSAKSQQAL KQLAARYQAH LDKNPHLNLA DICFSANTGR EHFSHRVAVV AESVRQLQQK
     LADFTTEQAT SGVVYQQQQR TKRSSVAFLF TGQGSHYLGM GRQLYQTQPS FRQTIDCCDQ
     ILQPLLNKSL VQILYADDAS LLEDTAYAQP ALFALEYALA GLWRSWGIQP DVVMGYSLGE
     YVAATVAGVF SLEQALKLVT ERGRLMQSLT PQAEMVCVLA TAAVVDAAIQ PYAGQIAIAA
     MNTPNNTVIV GEPEAIQAVV ASLTAQGIHT EKLNVSRGFH SQLIKPILEE FRQVLATVNY
     SSPKISFVST VSGEVMTSEI ACPDYWCEHA CVAVNFVAGM KTLAQQGIEV FVEIGSKPSL
     LGMASDCLAP DMGGFFPSLR PGLPDWQVLL ESLAGLYTRG LSVDWSGFDA DYPRSRLPLP
     TYPFQRQRYW VETTKQTRKL LTSSEKEIFL HPLLNQKLQS PLLKETLFTS EISVNNLPYL
     NDHQVYGKIV VAGAFHISLL LGAVELTFGD NSCILEDIFF TRALVISAEE SRTLQLLITP
     EDSSTASFKL ISLEPEAVEQ SHSWNTHING KISIDKKVIA AKRNREKISI QGLQDRCQQE
     MASSEFYQFL QLRHIQLGST FQWIKSIWKG DKEAVCQMQP PQTLDNLEKY QLHPSLIDSC
     FQLLMATVVL EKDETFVPFS IEQLYFYQSP SSCSQLWCHA YSLPMEKSRE EVVGNILLFD
     QEGEIIAEVI GFKGRRANSH SFLGIPQESL ESWLYEVEWR PQTLTKQKSL NGGLQKTISE
     PRSWLILADD DGIGQQITEQ LQAQGEICTL VLSSNQYEQL TETEFKVNPS RLEDFQRLFT
     AIETSQSSLH GVVHLWSLNT AKEELTSTSL ETTLNQVCSS TLHLVQSLVK AKLVSSPSLW
     LVTRGAVSVK SEQNISGLAQ SPLWGIGKVI ALEHPELNCV RIDLHPEAQK NEVQSLFEEI
     WLGAAKEDQV AYRDQVRYVA RLTRSGQAED TTAQDKLEIP QSEFFRLGVS SRGTLENLQL
     QPITRRQPDA GEVEIQICAT GLNFRDVLNV LGLYPGDPGP LGLECSGLIV GIGEGVQNFK
     IGDPVIALIQ GSFSQYVTVK TAMVVHKPEH LSFEQAATVP VTFLTVCCSL QHVNISPGDR
     VLVHAATGGV GIAAIQLLQQ AGAEIFATAS PQKWEFLKSL GIKHIMNSRT LDFADEIMAK
     TDGQGVDVVI NSLNGEFIPK SLSVLREKGC FLEIGKNGVW EVEQAKQVRP DISYFLVDLV
     KECYEQPALI QSMFCELMQQ FQEGKLKPLP QTVFPFADVL NAFRYMQQAK HIGKIVISQK
     PAPATTYQKP VTFREDATYL ITGGLGGLGL LTARWLVEHG TKHLVLVGRR AANPSVNSQL
     KQLEQAGAKV VVISADISQR EQVNYVLAEI EKSLPPLRGI IHAAGLLDDG ILLQQTWERF
     AKVLAPKVLG AWHLHTLTQK LPLDFFVLFS SAAALLGSPG QANHAAANTF LDALAISRRN
     QGLASLSINW GPWSEVGAAA QRHLNQQMSM KGVGSIAPEP GLQILEKLWS NSPAQMGVVP
     INWSQFDQAL TSQFFSDFTQ TLNQDKKQTT SFLKQLETIP VSDRHACLLA HVNSLVAKVL
     RLNPSEQLDP QQGFFQLGMD SLTSVELRNL LRNSLECSLP STVALEYPTL ETLVDYLAQE
     VLPIEFFAPE SAVQSHQDDS TTSLAILEDL SQEEIANLLA QELESVREE
//

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