ID A0A3N6GNA6_9ACTN Unreviewed; 1322 AA.
AC A0A3N6GNA6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tyrocidine synthase 3 {ECO:0000313|EMBL:RPK85454.1};
GN Name=tycC1 {ECO:0000313|EMBL:RPK85454.1};
GN ORFNames=EES45_01660 {ECO:0000313|EMBL:RPK85454.1};
OS Streptomyces sp. ADI97-07.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK85454.1, ECO:0000313|Proteomes:UP000281409};
RN [1] {ECO:0000313|EMBL:RPK85454.1, ECO:0000313|Proteomes:UP000281409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK85454.1,
RC ECO:0000313|Proteomes:UP000281409};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPK85454.1}.
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DR EMBL; RPGY01000005; RPK85454.1; -; Genomic_DNA.
DR Proteomes; UP000281409; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
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; 3.40.50.12780; 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; 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; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
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; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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:UP000281409}.
FT DOMAIN 999..1074
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1322 AA; 144545 MW; CB7F6E1E87FFA109 CRC64;
MTPTESAQDR LLRQLLAGAP SGAVNIRIPR VPPGTRVPLT PAQRRIWFFS QLYATSNEYN
VFDLVHVDRT PDEDRLRAAL RILVERHVSL RLRLFEVHGE PVQEDCGAYD PEVTWYDVSG
YPEDEAEARA TDIANECSRE VLRPEKPPLW RFSVIRLPRG RAAFVLGFHH VIADHWSWTQ
LVEELTGLLA GTGQEAPEGP DFLDYAAWLH DNHDERRAED DLAYWTEKLG GPLPVLGLPA
DRPRPKVSSR AGHSVPVRVS RDVLDEARRV AREHDTTLYV VMLAAYHVFL GRLSGQRDLV
VGGVFAGRDQ PFSERIFGCF VKSVALRTEL AERSTFSAAV RAVHRTVLEA QDHQYVPYDD
IVARLGVPRD LGVDPVFQAQ FSLQDADPLD ADGFETDPSG LAEYGTAKWD MALVLTGTAQ
GLSGLMECSA DLFDKTTVTR FAAMYGLLLG QLVRAPGAAA ASHPLITDGE RDHILYGLNA
YERPTHTYRS LAEPFEEQVR LRPDATALVG DEGTMTYRRL NDEANRLAHH LAARGVGPGT
RVALCTHRGF AMVVALYAVA KSGGTYVPLD PELPDARLRF MLEDTGPSTV LTAGTAGARV
PEGPWSVISL DDSAPWADMP TTDPERALPH QASHLLFTSG STGRPKAVAS DAAGSVADIL
WMQRHYPYRP GDTALLKTSY GFDVSLWEIC WPLYVGARVA VCRPGEHWDV HYLARMIDEY
EVTTAYVIPT QLQVFLDEWA EGQCSSLRWM ISGGEPVTPR LRDACHSRLG AHLVNGYGPT
EAGRVTDMVV PREPGNPVVP LGRPSSNFRL YVLDEDLDVV PVGVPGESFI AAEVGLSQGY
FNRPALTAER FLPDPYGPPG SRMYRSGDVC RYRDDGVLEH LGRIGDQVKI RGMRIEPSEL
EAVLAEQEGV DRCVVLVVTE GEEQQLAAFV VPEGGVELDP AEIGEQAARM LPRYMVPTSI
HVVDAITTNV NGKPDREALL AHRTGRAGSP GGPSDEVPSY VDGVEERMAA IFRRILGVDH
VAAAESFFTL GGHSLLVFRL IAACTEEFGT ELGVAEIFAA PTVRDLAARV RDPRAAAGGS
LVPLAPRAGA PTLVFVHAAS GSVLPFRELA EDLGEDFSVH ALQAPGPDTP GASSVEELAL
RYLDELEPVR GLSPVFLVGW SMGGSIAVEM AREAERRGAP VDVTVMLDSW PPPACCTTPA
EQERTRRAIE DLDIGAAEGV DLGSLDQDLA RVTERNRLAL LAHRPEPYAG RVHLLRADEP
LPVTTVVPTP DEDEGAWRNV VGDLVREKIP GNHLTLLRGD NTAGLARRLR RITSGSLVFD
EI
//
