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Database: UniProt
Entry: W7J5E4_9PSEU
LinkDB: W7J5E4_9PSEU
Original site: W7J5E4_9PSEU 
ID   W7J5E4_9PSEU            Unreviewed;      1681 AA.
AC   W7J5E4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:EWC64201.1};
GN   ORFNames=UO65_0527 {ECO:0000313|EMBL:EWC64201.1};
OS   Actinokineospora spheciospongiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC64201.1, ECO:0000313|Proteomes:UP000019277};
RN   [1] {ECO:0000313|EMBL:EWC64201.1, ECO:0000313|Proteomes:UP000019277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EG49 {ECO:0000313|EMBL:EWC64201.1,
RC   ECO:0000313|Proteomes:UP000019277};
RX   PubMed=24604655;
RA   Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA   Hentschel U.;
RT   "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT   Bacterium Actinokineospora sp. Strain EG49.";
RL   Genome Announc. 2:e00160-14(2014).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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:EWC64201.1}.
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DR   EMBL; AYXG01000020; EWC64201.1; -; Genomic_DNA.
DR   RefSeq; WP_052020540.1; NZ_AYXG01000020.1.
DR   STRING; 909613.UO65_0527; -.
DR   PATRIC; fig|909613.9.peg.542; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 2378856at2; -.
DR   Proteomes; UP000019277; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 2.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 4.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
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; 2.
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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019277}.
FT   DOMAIN          495..570
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1561..1636
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1681 AA;  179036 MW;  1EC1ADAC1711AF0A CRC64;
     MVLDDFHTQV TEAPDALAVQ DGDLLLTYRD LAAHASALAT RLTDRGVGPE SVVAVYANRS
     AELVVAELAT LLAGAAFLPL DPAHPAARIR QLLELSGAAA VLSTEALVSG GAPLGDDVLV
     VDLTGEPGGA AFPAPPTPDA AALAYVIYTS GSTGRPKGVA VTHGGLANLM RWHHRTYGTR
     RTDRSTLLAS PGFDVSIQDI WFTLTAGAAL VIPPAEVRTS PPELATWLAD EQITVTFLPT
     PLAEAVLDET WPAHTALRFL HTGGSAMQRG VPDGLPFTVV NLYGPTEATV KVTACEVLPG
     GPVPPPIGVP VDGVRCHVLD GLDPVPDGEA GEMCLAGDCV ARGYLGDPAA TAAAFVPDVT
     APGQRMYRTG DKVRRGPDGV FEYIGRYDDQ AKIRGFRIEP GEIATVLKGH PAVHDAFVVV
     EHSGRPDARL VAYVVSAVAP AELVEFVAAR LPAYMVPAAT VALPALPLTP NGKVDRHALP
     APDRAAAGLD DAAVSPRTPT EVAVAGIVAE LLGTAEVGVH DDFFALGGNS LLVGRLAVPL
     ATELNAAVSV AELFNARTVA SLAAIVDERV AAAGGGEPVS PLIAPIPPPL RRVPRDRPIP
     LSLPQERVFF FEQLSPGNLA YNFQATVSLR GKVDVGALRS ALDEIVRRHE ILRTAYVAVD
     GVGYQRPVAE AKASLKVLDV PAADADEVVA AHLREPFDLG NPPLARWVLL RHEDDQNTFL
     HVEHHFVHDG WSLSVFLSEL RVLYPAFVAG LPSPLPELPV QYADYAFWQR DWMRGEVLRA
     HVEHWTARLA GAPDTLELPA DRPRPPVISF RGRAPRILFP TELSRALRAF SRQHRVSLFA
     TMYAGFAALL HRYTGQRDML VGTGAANRNV PELEPLLGML VNTLVLRTEV APDQRFSDLL
     EQVRQSVAET LAWSDTPVDA VIDAIEPTRD PSRTPLFQVM FSFHDSAVPD IDFGGLTGRV
     TERSNRSAKS DLNVIVIPRA EQRLGRAASP EDDDLAMIWE HSSDLFDEDT MTRMVTHYLT
     LLADAVARPD TRVGALRLLP DAEADQLDTW SRGPAVAGTE PVVELIARQA RTRPDAVAVS
     WSEGQLTYGD LWRRAGGLAD ELREAGIAAE EPVAVCADRS VELVVGELAV LLAGGCYLPV
     DPSYPAERIT FMLRDAGVRK VLATLQTQLQ LPAPDSSFRV FDLGAPVADG PVDAGDPVAP
     DRLAYLIYTS GSTGRPKGVA LSHRGLANLV GWHVGEYGLG PADRTALFAS PGFDASTWEI
     WPTLAAGATL CVVPPKLRAA PAELVRWIGD ERITTTFLPT PVAAAVLTEP WPADTALRAL
     LTGGDALPAA PPEGLPFRLF NHYGPTENTV VATAGPVPPG PAGPRPPIGR PIAGVDAHVL
     DAEGRRVPTG VRGELHLGGT AVARGYVDDP ELTAARFPAD PSAAHPGARL YRTGDLVRWL
     PDGQLEFLGR ADEQVKIRGF RIEPEEVAAT LREHPQVRDA VVIARAPEAG AETRLIAYAQ
     SGTAAAEDLP GFLRERLPAY MVPDEVVVLP TLPLTEHGKV DHGALAALAP PAPDVPEAEQ
     LPRTATEERV AQLASALLRG RRVGRDDDFF RVGGHSLLAA RLVAQVNDAF GVAVPIALFL
     QRPTVANLAD AVAVATAGPA TGPIRPSSRR AAARLLSELD QLSDERVESL LRDAEGTEVQ
     Q
//
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