ID   A0A317WV34_9EURO        Unreviewed;      1025 AA.
AC   A0A317WV34;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NRPS-like enzyme {ECO:0000313|EMBL:PWY90216.1};
GN   ORFNames=BO70DRAFT_415774 {ECO:0000313|EMBL:PWY90216.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY90216.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY90216.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY90216.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family.
CC       {ECO:0000256|ARBA:ARBA00029454}.
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:PWY90216.1}.
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DR   EMBL; MSFL01000003; PWY90216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WV34; -.
DR   STRING; 1448321.A0A317WV34; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_415774; -.
DR   OrthoDB; 2541582at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd05235; SDR_e1; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT   DOMAIN          534..611
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          509..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  113098 MW;  C6FF259BCFCC6721 CRC64;
     MSPFLNTDKA NPDADLGLAE RLHQQAEVCG STVAVEHGRY QLTYAELDRK ALFLGDQINS
     LSQGESAPVG IIAPRSLDHV VSQVAVIYSG RACVPLDNRL PDEMLTRMLQ KLGTSLVVTD
     VRQQHRLPSL RHLVVDHRMI PDPESVLSPS RNGPRARSFV FHTSGTTGEP KAVEGFAEGV
     ISLCLDPRQV IRKGQRVGHA CNIIFDVCVL DIWGSLLNGA TMVVIPMDVV LDPTALGSFI
     TEKELNLLQL PTSILAIMAH ACPGALSTLD VLVTGGEAIN CRSIQSIFDA GAPGRIINAY
     GPTEASVYMM YHEVSEEDAR KGEIPVGRPF DYVDVFLVDD NLSPVQPGEA GELLISGVCV
     AGGYIGEPEK TAQSFVKVPQ LGRKTPMYRT GDLMRVDEAG LYHFLGRKDN QIKVRGQRVE
     LEALESTLLK TSLVSAAVVV KIKPEEFDRG EFLLAYCVPS SPDISAGVIL KSYMEQAPHL
     MVPRLELIDV LPLQPTGKAD RKTLEQRYRE RLKRSQPKGD QADEAPPFQG NGADEPGDVA
     SRLERIWITA FGLPVDHLKA KDDFVAMGGT SLMAATMIPR IHEAFGVSLR SQQLYENTSF
     DQLTHLVTDL QANGDDRAIQ EEQQAWLQDS TLGQHLRPIE GTVPNWPDEG RIFLTGATGF
     VGIFLLAALA RRSDVEKVAC LVRAEDEPSA RRRLEEALHK YSLSADMAKV IALPGHLDQA
     QLGLSPEEYD AYAEWSSVVF HLGAKVSYVA PYASHRQPNV LGTVHILDFC THRRPKALHY
     SSTITSYGPT GYVTGAKLLP EDERPAAHVA ALPYDMGYSQ SQYVAEGLVW AAIDQGLPIA
     IYRPGFVLGE SGICNPDDFI SRLFMTCMDM GLYPILPGQR KEFVPVDFVV DAMLHISTKL
     SSLGHAYNLV HPHLDDAIST NGSFELLNEL SPYQMRAIPY DQWVDALSGR VGDSMQPLTP
     MLRERVFDQK TRWEVWEHMP EYGRDNMRRA LQDAPEVLNC RAIETVFQRS LQSWMPCCGR
     KSVPN
//