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Database: UniProt/TrEMBL
Entry: C5CUE9_VARPS
LinkDB: C5CUE9_VARPS
Original site: C5CUE9_VARPS 
ID   C5CUE9_VARPS            Unreviewed;      1776 AA.
AC   C5CUE9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ACS20362.1};
GN   OrderedLocusNames=Vapar_3746 {ECO:0000313|EMBL:ACS20362.1};
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS20362.1};
RN   [1] {ECO:0000313|EMBL:ACS20362.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S110 {ECO:0000313|EMBL:ACS20362.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA   Leadbetter J.R., Spain J.C., Han J.I.;
RT   "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001635; ACS20362.1; -; Genomic_DNA.
DR   STRING; 543728.Vapar_3746; -.
DR   KEGG; vap:Vapar_3746; -.
DR   eggNOG; COG0318; Bacteria.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_0_9_4; -.
DR   OrthoDB; 6297021at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          600..675
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1666..1741
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1776 AA;  192109 MW;  5A270523377B60B1 CRC64;
     MEKNTQAQQA PISPRPTNFV AHLRALADAR RDDIWLTVVS AVDGTERAEP ISYGTFERRV
     RALAARLQQQ FAKKGERALV MLDNGDHYAV SMLACFYAGV IAVPVFPPES ARPQHLARLT
     GIAADSQARC VLTSEAMARA MNAASAGLRQ FGDAHIVAVD TVDISLADAW TPFEPADGDV
     AFLQYTSGST SAPKGVIVTH GNLMANEEAI QRSMGVGPGD SFVSWAPLYH DMGLIGGLLQ
     PLYSGIPLVL TSPGYFLERP VRWLELISRH RATLSGGPDF AYRLCLERVK DAQLAPLDLS
     SWRVAYTGAE PVRADTEIEF ISRFASAGFD AAAVYPCYGL AEATLFVTGG RRGGGLVAPT
     FSATGLASGV GAPADEGAAL VGCGNVAPGH RIEIVDAESL SAAAPGKIGE IWTCGPSIGH
     GYWGKERETR ETFVERNGQR WLRTGDLGFM HEGQLYVTGR IKDLIIVRGH NIYPQDIERL
     IEAEVDAVRK GRVAVFATQG PGGEGIGVAA EVSRSMQKLV PAAVLVDALG AAVSEVFGET
     LSVVLLLNPG GMPKTTSGKL QRSACRAGWL DGSADAYAVY QHGAFVRGGL GEAVAEAPLD
     EVEQAVAAIW REVCKHGDDR PLGRDAHFFN RGGSSLTATQ AAARIGARWQ IDFPARRLFE
     QPRLRDCASA IRELQLQGVR PQPAPIAVLS AERRLLPLPL SHAQERQWFL WQIDPESAAY
     HVSGALRLAG ALRVDALQAA FDGLVARHES LRTVFSAGAD GSVEQWIRPG GSVPLALVDL
     RGAEAEADAR LDEATRRLKA QPFDLTQDPL LRAALIRTAD EVHVLAVVMH HIVSDGASMQ
     LLIDELAAGY AAHLKGDTVR LAAPRIQYAD HALWQREWLA AGEGERQLAW WRTQLGDTHT
     VLELRTDHPR KPQAGYGAAS HAFELPASLL ARLRKAADGG GATLFMVLLA GFQALLHRYT
     GQEDIRIGAP FANRNRVEAE GVVGLFVNTL VLRNPIHGRL GASRVLAQAR DAVLGAQAHQ
     DVPFEQLVQM LQPERSLSRT PLFQVMFNHL FEDYRSLGQL PGIAAQDHAL PDLAAQFELT
     LEARERPGGQ LSLALIYAAE LFEPGTMARM ASHYVAVLQA LVERPHQPIG DIELLGAPEQ
     AQLAQWGVNG HREPQPEPVH RMIERQARMQ PDATALLFAD ESLGFAELNR RANRLAHRLI
     ALGVKPEVLV GIAMERSVEM VVAILGVLKA GGAYVPLDPE YPAERLAYMV QDSGIGLLLT
     QRSVAYCVAN CVPDRRALTV LEVDAADLGA EPESDPQVGL HIENLAYVIY TSGSTGKPKG
     AAIRHSALHS CMAWMQGIYK LTRADTVLHK APFGFDVSVW ELFWPMTSGA RLVVANPGDH
     RDPARLVELI QRHQVTTLNF VPSMLQAFLA HKGIEASTRL RHIICGGEAM PAETQKETLE
     RLHGAGLQNL YGPTETTIHV THWACRNDGQ SQVPIGKPIS HTSAHVLDAE LNLVPQGVAG
     ELYLGGISLA RGYLKRAGLS AERFVADPFD SAGGGRLYRT GDLVRWNGEG QLEYLGRIDH
     QVKIRGFRIE LGEIEAELLA QPAVREAVVV ARDGPAGARL VGYLAPHAGE AIDTAALKER
     LAQVLPDYMV PRAFEVLDAL PLNANGKVDR KALPEPALAS GQAYEAPQGH VAQTVAAVWS
     EVLQVAQVGL HDNFFDLGGH SLLLIRAHRL LEDRLHTAIP VVNLFKYPTV QSLVQWLEQA
     PARAAASASA AAASDDRALR QRAAMLQRRK AAERVN
//
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