ID W7J591_9PSEU Unreviewed; 1465 AA.
AC W7J591;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:EWC64202.1};
GN ORFNames=UO65_0528 {ECO:0000313|EMBL:EWC64202.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC64202.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC64202.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC64202.1,
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 -!- 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:EWC64202.1}.
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DR EMBL; AYXG01000020; EWC64202.1; -; Genomic_DNA.
DR STRING; 909613.UO65_0528; -.
DR PATRIC; fig|909613.9.peg.543; -.
DR eggNOG; COG1020; Bacteria.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd01097; Tetrahydromethanopterin_reductase; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.20.20.30; Luciferase-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; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020459; AMP-binding.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR024011; Biosynth_lucif-like_mOase_dom.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR04020; seco_metab_LLM; 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; PF00296; Bac_luciferase; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 4.
DR PRINTS; PR00154; AMPBINDING.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 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 1356..1431
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1426..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1465 AA; 158280 MW; EDF117CC1E877E60 CRC64;
MEAEERRALL AELLRRRSEQ DSAVPLSYAQ RRLWFLDQLQ PGSAVYNVPL GYDITGPVHV
GALERALTEV VRRQEVLRTA FRSTGGTPHQ VVLPPEPVTV PVVDLTAPGR SADEVARLAD
EEAGAPFDLV AGRTIRARLL RLAEQRHRLL ITVHHLACDA FSVGVLGEEL AVQYRAALTG
LPPGEPDLPM QYADFAEWQD SALAGPELDR LLAYWKNRLA GMPTRHLPTD HPRPPVQSYR
GAAHTFELPA DAVQRLEELS RAEGVTLFSV LLAAFAVLLR AHVGEDEVVV GTPVSGRERP
ELAGLIGFFT NTLVLRCDLA AGPTFRQLVQ RLWTEVRGAL AHQDLPFEKL VEELHPDRDL
AQNPLFQVLF SYRYEEEGAG LSLDGCGVRQ VLGDTGTARF DLTLSLARTP AGVTGRVEYS
TDLFEAATAE RIAARYARVV TAAAQDPDRP VDRLAALPED ELATLSAWQV GPRAEVAEVL
VHRVLERRAA ATPDAVAVVA ADATLTYREL DERAELLARQ LRHLGVAADE PVGVHLGRGS
LLVVALLGIL KAGAAYLPLD PGYPRDRLAF MVGDAGVRLV VADERWAAAA GRLGADRVVV
PDPTGVPDVE PVAVTAENLA YVIYTSGSTG RPKGVMVTHR NAVNLFAGMT EAFGADEPGT
WLAVTSVSFD ISVVELLWAL AHGHRVVLRG EPPRASAAPA AGSAATDAAR TRPIDFSLFY
FGNDSEANSG DRYRLLLEGA KFADRNGFTA VWTPERHFHR FGGLYPNPSV VAAAVAAITE
RVQVRGGSVV MPLHDPLRVA EEWSVVDNLS AGRVGISLAS GWNANDFALA PDRFDKRKQL
MMDGLAEVRQ LWRGETVSRR NGVDAEVEVG VFPRPVQQAL PVWLTSAKHP ETFRMAGEAG
TGVLTHLLGH DLEELAEKIE LYRRTWREHG HGPGDGHVAV MVHTFVGTDV DEVRELVREP
LSRYLESSFD LIASFGATTA SAQDFKSLAP RELRELVDRA FDRFFATASL LGTPQVCADM
VDRMKAVGVD EVACLVDFGV DEQAALDALT HLTTVREITD ERRAAALAEA DEQPIAGQLR
DHGVTHLQCT PSLARLLLTD RDARAELPRL RRLLVGGEAL PADLARVLDD AVGGTVHNMY
GPTEATVWAT TARVEPGGPV SIGRPLANAR AYVVDRGMRL CPVGVPGELL LGGGGVARGY
LDRAGTTAER FQPDPFDPTP GARVYRTGDL ARWAPDGGLE FLGRLDDQVK LHGHRIELGE
VETALAEHPD VRSAVAVIRG AGAEQRIACH FVPAAGRTPT GPELRAFLTT RLPAYMVPGA
FHPIDAVPLT PNGKVDRRAL PEAPGARPQS ASAYAPPTTA TERLVADVWQ DVLGVDEVGV
DDSFFDLGGN SLLVVVARAR LLEHRDGGLS LVDMFRYPSV RALAEAMDRE PDERSDEAAG
AGAARGAARR AAGRGAARRS TRTGE
//
