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Database: UniProt
Entry: A0A3M2LMI5_9ACTN
LinkDB: A0A3M2LMI5_9ACTN
Original site: A0A3M2LMI5_9ACTN 
ID   A0A3M2LMI5_9ACTN        Unreviewed;      1047 AA.
AC   A0A3M2LMI5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:RMI38649.1};
GN   ORFNames=EBN88_16495 {ECO:0000313|EMBL:RMI38649.1};
OS   Streptomyces triticirhizae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2483353 {ECO:0000313|EMBL:RMI38649.1, ECO:0000313|Proteomes:UP000278673};
RN   [1] {ECO:0000313|EMBL:RMI38649.1, ECO:0000313|Proteomes:UP000278673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY642 {ECO:0000313|EMBL:RMI38649.1,
RC   ECO:0000313|Proteomes:UP000278673};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (OCT-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:RMI38649.1}.
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DR   EMBL; RFFJ01000087; RMI38649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2LMI5; -.
DR   Proteomes; UP000278673; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
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   CDD; cd05930; A_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 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; 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   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   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-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}.
FT   DOMAIN          961..1036
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          580..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1047 AA;  111363 MW;  9168781261ED8A45 CRC64;
     MSEDLAMTSP TETHPATRKE EALWLLETMV PGTSANHLSL AFRVEGPLRA DALERALIRL
     TGRHRALRTV YRATDTELRR SVLPPGQFRL PVGDIPAATG DAIRDLEAFV AQPLPLDGTP
     PLRAGVLRGA DGDTFCLVVH HLVFDTASAT ILRDELVTLY EAALAGRDLD AELTEPAAEF
     TEPEPSEAHL AYWHRQLAGF DRQSLELSYG RPDGPTPDLD GEQLTRDLSP EIRAAVRQAQ
     KDLRAPEAVI LLSAFALLLD GHGAGPDLVV GSPVNVRPPA AERAVGYHIN VVPLRLRVDP
     TLTLAELVRA TRDTFLDGLA HSGVPVDDLG DVAPSAATTW RNPLFRHVFN YVPTVGDPRF
     TLAGTPATLL AVENGCSKFD LEFFVMPSDE GIRLRAAYRT ENFDATEVAA LLERYEALLA
     GLLDHAATPV AEIPLLGPTD RAVIDAANAT RAATDPATVP AAIHARALAT PGATAVVDGD
     RAAGYRALWL AAQDVRDALR AAGLAPGEVV AVVAPRGVEL VAAVLGTWLA GGVYMPIDPD
     HPAQRIAYQL ADSAAPVVLA PPERAELAGE GRVLVPLRAP REDRDEPLDA PPTTADAPAY
     LMYTSGSTGR PKGTLVGHAA LANLTAHFAR ELDATPDDAG LWLTTFSFDI SGLELYVPLW
     AGGRVVVAPD AARLDGAVLR ELLERHDVGI VEATPTTWRA VLDAAGPALA GRRVLCGGEP
     LPAPLAERLI ATGCRLHHVY GPTETTIWST SAVLTKVEGG RVPVGRPISN TVVLVRDEAG
     RELPLGVRGE LCVAGDGVAF GYHDRPELTA ERFPTHPVHG RFYRTGDVAF WRRDGALELL
     GRGDRQVKLR GNRIELGEIE SVLSRHPEVK TAAVVLVDAG GPDAALVAFI EGVGGPELTD
     SVWEHARGEL PRAVVPQEFV IADALPTTLN DKVDYPALLR LAEERRAAAA APNATDPADP
     AGGDPLVAQL IGLWAELLER GDITPDTNFF AHGGHSLMGA ILVQRLEPLT GVSLPLAELF
     ADPTPRRLAA RLRAAGAQDS APGAGTE
//
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