ID A0A2V5JIC9_9EURO Unreviewed; 1058 AA.
AC A0A2V5JIC9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=NRPS-like enzyme {ECO:0000313|EMBL:PYI36626.1};
GN ORFNames=BP00DRAFT_469446 {ECO:0000313|EMBL:PYI36626.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI36626.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI36626.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI36626.1,
RC ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ825464; PYI36626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5JIC9; -.
DR Proteomes; UP000248817; 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 Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 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.
PE 4: Predicted;
FT DOMAIN 46..355
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 571..641
FT /note="Carrier"
FT /evidence="ECO:0000259|Pfam:PF00550"
FT DOMAIN 692..934
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 1058 AA; 117767 MW; 2A7F4CC7AC999FD0 CRC64;
MVGVVNSAPE GFNAPRRLLV TQVDTIAKHS PNRRFGLIPN GTEVDQGFRE VTFRDLSQAV
NAMSWWIDDT LGKPQSGEKI AYLGNNDVRY IIFMLACHKT GYTIFLPSTR LSDEAYNRVL
MDTKCTHLLF SREKSPIASR LRTLDWKMQF QEVPSVADIL GNGSGTSHFE FSKTYDEVVD
QIAFIIHSSG TTGMPKPVPL THGFLGTIDF AALIPMPPGR SSAFFNDLAS DDPKPNDLVL
SSTPYFHLMG LTSFFESIFH NIPFVASPER LLSVGFLIDL IRHTKPTVTI LPPSILEDMS
YSDEALRCLS TLKFVCYGGA PLAPEVGEKL ARYTQLRSAI GSSEMGIICS MVPEGENTWG
YFEWNPLYQV DMQLIGDGLY ELVIPRVEYS LVMHGIFHTF PELKEYRSKD LYTRHPTNPK
LWKYHGRYDD VIVLSNGEKL NPISLEKIVE GHPSVHRALL IGQRRFQTCL LIEPDFDKVA
TPVDEKGLIS MIWPVVQAAN KTVPDYGQIA KTMIRLSSRE KPFRLTAKGT TQRHAVNKDY
AEEIEEIYAA QDRELAMDLP SAITPDTVCG YLQNVICKLT GRQSINPSDD LYSRGLDSLQ
AIQLSKILKN SVSSYNPELN TENLNVQQIY AHPTAEGLAN LLLGILDEPS SPIATVSRSD
KIAQLISKYT NDLHIRESDV LPQLPALSTV ILTGSTGSLG SYILDDLLRK PQVAKVYCFN
RSEDSLTRQR EGFQEKGLQT SPLDNPNKVE FLHVQFGETH FGLSDRQYTE LLDTVDVIIH
NAWKVNFNHP VSSFEDPHLK GVREFVRFSQ DSRYRAHLAF VSSVSTIGAW KPSDGVPAIP
EVPMETADAT LEQGYGESKY IGESICVEAS KKAGVPTSIL RVGQIAGPDT RLGAWNPHEW
LPSLIKTSKA TGKVPSDLGG YPIDWVSVDT LARIVNELVL GRRASLGETR NAVFHLVNPS
RTTWAALIPA IQERYPVQPV PLVDWVADLE TIQDPSDCDV QEKPALKLLA FFHGLADNAD
VLSADISVER TRKGSETMAS LGPVSPAQMA NWLNQWNF
//