ID A0A370B4B6_9ACTN Unreviewed; 1376 AA.
AC A0A370B4B6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:RDG35229.1};
GN ORFNames=DVH02_26435 {ECO:0000313|EMBL:RDG35229.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG35229.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG35229.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG35229.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-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:RDG35229.1}.
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DR EMBL; QQNA01000242; RDG35229.1; -; Genomic_DNA.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000253741; 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; cd17646; A_NRPS_AB3403-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
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; 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:UP000253741}.
FT DOMAIN 1037..1112
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 148062 MW; C71C26C837D18422 CRC64;
MSVLLTENTG DAGDAGGTES SGDLGAAGNT VDTGNTGRAD RRPGSGSGSD TDTVLPLTAA
QSGMWFAQAL DPLSPAQNTA ECLRIEGPLD PDLFATALRR VTAETDALRV RVVDTPGGPR
QHLAATVELP LTVHDPGDAD YTDHTDVTDV TDDTDDTDDP DHTDNTDGAD GAEARADAWM
RADLAEPCDL AKGPLFRHAL FRVGQDRWLW YQRIHHLVMD GYGYSLLVRR TAEIYTALVR
GEEPPPRTFG SLADLVAQDD AYRSSAAFEA DRAHWAHWAA ECGDRPEASR LAGRGALPAR
TFRRRTAYPE PGTKERLRAV ADRTRSTWPD VLIAAQALYT ARATDRSEVV LGLPLMGRMG
SAALRVPGMV MNVLPLRLDL SPAATFDELV RQVVLRVREL RRHQRYRYED IRRDLGLLGE
SRGLVGPLVN VMPFDYGVDF AGAPARARNL SAGPVEDLTV NVYDRADGRG LHVDHDGNPA
LYDDAELAAH QERFLHLLHR IAGSGADAPL SSYTIATPAE HELVVDEFNR TGRALPPTTL
VGPIESRAAL TPEATALVYG DTSLTYAGLN ERANRLARHL RTLGAGPGAV VAVSVPRSVE
LVVSLLAVVK AGAAYLPLDP DYPAGRLTYM LQDAAPVCAV VDRAGRLPAD AGTPLVVLDG
LDVSGYPRID PARPLTRDHP AYLIYTSGST GRPKGVVVPH AAIDNRLRWM QDTYRLTAGD
RVLQKTPSSF DVSVWEFFWP LRVGATLVVA EPGGHKDPGY LARLIHEQAV TVCHFVPSML
QVFLSEADAG SCGSLRLVFA SGEALPRETV NAFGSALPGA RLHNLYGPTE AAVDVTYHAC
VPGAPGPVPI GGPVWNTRLY VLDAALQPCP PGVAGELYLA GRQLADGYLN RPELTACRFV
ADPFGPPGGR MYRTGDLARW TGRGEVEYLG RTDHQVKLRG QRIELGEIET ALAALDGVDG
ACAVVREDRP GEQRLVGYVT GRADPAALRA ALAPVLPEHM VPSAVVALDA FPLGPSGKLE
RRELPAPVFT GGGGARRPSG PREEALTRLF AQVLEAERVG PDDAFFDLGG TSLLAVRLVA
RVREEFGTEL TIGSLFEAPT PAALAARLDS TGPAASDALG VVLPLRAGGE RPALFAIHPA
GGIAWCYAGL AARLGRDQPV YGVQARGLTG DEALPRTLHE EAADYVRQIR AVRPHGPYRL
LGWSVGGVLA HTVAVLLQEA GEKVELLALL DAFPAEQWRE RPAPEEGDAL TAVLRMAGFD
RTDENTPDDV VATLRRAGSP LAGLGDRTLA RIVDIVPNHA RMMREHRHRR YEGDLLFFTA
AAPRAEDWLD RESWRPHVSG RIVNLDLDCT HPQLLRGPHL DDIAAVLTAR TRELDA
//
