ID   A0A239KGQ3_9ACTN        Unreviewed;      1759 AA.
AC   A0A239KGQ3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Non-ribosomal peptide synthase domain TIGR01720/amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SNT17527.1};
DE   Flags: Fragment;
GN   ORFNames=SAMN06264365_1512 {ECO:0000313|EMBL:SNT17527.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNT17527.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNT17527.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNT17527.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; FZNR01000051; SNT17527.1; -; Genomic_DNA.
DR   OrthoDB; 5476914at2; -.
DR   Proteomes; UP000198415; Unassembled WGS sequence.
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:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19540; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01720; NRPS-para261; 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; 2.
DR   Pfam; PF00668; Condensation; 2.
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; 4.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198415}.
FT   DOMAIN          148..223
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1180..1254
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1640..1666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:SNT17527.1"
SQ   SEQUENCE   1759 AA;  187577 MW;  2DE6BD0F7A50151A CRC64;
     YVGRPGLTAQ RFVADPFGGG RLYRTGDRVK WAASGELVFA GRADEQVKVR GFRVEPGEVE
     AVLAGHEAVA QAAVIVREDR PGDKRLVGYL VAAGDELDVA AVREFAAERL PDYMLPILTV
     LDSLPVTVNG KLDRAALPAP DLPTAGRAAA TAAEEILCGL FAEILGVESV PADVSFFELG
     GDSLSAMRLI ARIRSVFESE VSVRGLFTAP TVAGVAEQIA AAAGTARRAL TAGERPAVLP
     LSYGQQRMWF LNRIEDAGQS VAYNMPMALR ISGDLDVAAL EAALGDVADR HEVLRTIYPE
     VNGVACQQIL EGAAGRPSLL VSEVAESDVS SVVAAFFGRG FDLSVELPWR TRLLAVAPGE
     FVLAIVAHHI ALDGWSMGVL TRDLRAAYTA RRQGQAPAWS SLDVQYADYA LWQREVLGDL
     DDESSLIAGQ LRHWREALSG APQELALPFD RQRPAIPSMR GAAVDLSVDA GTHARLVELA
     QRSGSTMFMV AHAALAVLLS RVGAGFDIPL GTSVAGRGDA ALDDLVGFFV NTLVLRTDLS
     GDPTFTELLA RVRETDLAAY ANQEVPFERL VDELSPVRSL AHNPLFQVMF VVQNLPQGSG
     GGWDLPDVLV QPAAQDAEQH AAKFDLTVTF EERRDEGGRP AGINGGILYA TDLFDESTAR
     SLADRLVAVL TQVAADPQLT LSQVDVLTGA ERDLVTREWN DTAVPVAAVS VPELIQRWVT
     ETPDAVAVRD GGGRSLTYGQ LDEWSQGVAS GLRSAGVNRG DRVGLCLPRS VEMVAAMLGV
     WRVGAAFVPL DPQLPAARRE FMTVDGGTSL VLSDWDRSWE SGADVQAAQL DGRDLAYVIY
     TSGSTGTPKG VAVAHAGVAS LAQVMAPVLD VSAGTAALQF ASFSFDASVL DVVTVLGAGG
     SLVIADGEQR QDMAALSRLV RDANVQVASV VPSLLAALDP AQVAGIRRWV LGAEFLSADL
     ASRWSAGSQV WNTYGPTEAT VITTAAPVTL PVAGAGPSMG RPIGNARVLV LDEFLQPVPV
     GVVGEVYIGG LGLARGYVNR PDLTAHRFVA DPSGVGGRLY RSGDLARWDS EGLLHFAGRS
     DEQVKIRGFR IEPAEVQAVL QQHPEVAQAA VVARDNQLIG YLVAASNELD VAAVREFAAG
     RLPEYMLPTL LVLDTLPLNA NGKLDQAALP APDLPTTGRA AATATEEILC ELFAEILGIE
     SVPADASFFE LGGDSIMSML LVSRARRAGL TITARNIFEH RTPAALATVA TTEDHATTGE
     PGTGDIPLTP VMHELLHRAG DHLDQVYQST VVVTPAGLDL DTLTASLQAL VDHHDMLRAT
     LHTDRLTVPE PGIVNAGEWT ERVDAAGIDG EEFDDLIDRH LREAAERLDP RNGVMAQFVW
     FDRGPDVQGR LQLVVHHLVM DAVSWRFLVP DLAEAYTTLA AGREVALQPV PTSFRHWSRA
     LTAQAGSPER RAELPHWLET LRDPDPAITV QPVDPARDTG ATMRQMSLRL PTDVTTSLLT
     TVPTAFHAGV EDILLTGFAA AIGEWRRTQG RKSRGVLVDL EGHGRVPLGD GVELSRTAGW
     FTNSYPVRLD PGATDFAGLR AGRPVAGQAV KRVKEQLRAT PDDGLGYGML RHLNAETSTE
     LDGLRSAQIG FNYLGRFSDN ADGPDGRQRD WQPTAGGRGG GGTGNDIPVM HPLEAMGVVR
     DLSEGPHLSL VLSWAADLME EPTIRELLDL WASALTGLVI HTADTGNGGY TPSDFPLVDL
     SQDELDDFEA AAKQIEEGA
//