ID A0A318Z7Q0_9EURO Unreviewed; 2331 AA.
AC A0A318Z7Q0;
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=Amino acid adenylation {ECO:0000313|EMBL:PYH42447.1};
GN ORFNames=BP01DRAFT_425658 {ECO:0000313|EMBL:PYH42447.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH42447.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH42447.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH42447.1,
RC ECO:0000313|Proteomes:UP000248349};
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.
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DR EMBL; KZ821252; PYH42447.1; -; Genomic_DNA.
DR STRING; 1450539.A0A318Z7Q0; -.
DR OrthoDB; 2209130at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 2.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT DOMAIN 765..841
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1828..1907
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2331 AA; 255052 MW; AFBBE46C902C6942 CRC64;
MPSTILDDAD RLRQRWTELV TDVTPSHLPT GIFSKRQTKA PVGKVDVHLD VSLMQACAQE
HDVPALHLVQ AAWAAMLRAY SSSDEITYGG IGLQPHSQKS QWTDAALCRV RLEPDLSVIS
IAEQTLKEGL QEADLLVSVP EALQVFSTLD PKPGNTAIWL RDSTAKAEIS ENEIVAEKTF
DYVLRIDPSL SKLNLIYHKP TVSSAQAEYI ANTFADILHN IGAWNRILPK GSAVCVDRLI
ETAAQRTPNA PAISSWDGQM TYAQFNQTAC HVAQYLESVG VHRGQLVPVC FEKSRWTIII
MVALWKVGAA WVPLDPRHPR QRIETIVESI EATTVITSEA HQALLAGIAP QVITLDQTLI
QVIEQSSDVE FVSQSQPHDV AFVMFTSGST GKPKGVVHEH ASVASSALHH GPAMNINEDT
RALQFGAYTF IISTFEIFTT LIFGGCLCIP SDHDRHTDVR PALRSMNANW AIFTPSFARS
LTTEDAPTLK TLLLAGEAVA QDIIDRWAAV ARLINIYGAS ECSVCMVGPM VTDTPRSCIG
RAVGALSWIV DANDHDRLVP IGAAGELIIE GPTLARGYLA DPERTQAVYI QDPKWAQQKG
ITHRFYKTGD LARYGDDGRI HLIGRKDLQV KIRGQRVELT EIEAHMRAIN NQVKTAVSMV
HPQGKAMLVA FISRQSGFGP EFQHAFHATP ADQVSIAAAA SQMNTELVRR LPPYMIPSAF
IPLAYMPLTA SGKTDRRMIT TFGTGLSLSE LAALAGGAAT TTRTMPSTAD EKQLQQLWSE
ILHCPPEEIG VEDNFFHLGG DSIEAMNLVR RCRAEGYQLQ VSDIMENLVL RDMAKVMVPG
RSSSELPRAR PFELLGEDED SIRSEMLTAS GFQDPDLIQD AYPCTPLQTG LMALSAKIAG
SYIARHTLEL PANLGIDRFK ELWEIVVANN DVLRTRMVET DQYGTVQMVD RGRIQWGRGS
DLEEYLQADE AIPMHVGDAL TRHAIVTAEK TYFVLTIHHA IYDGLSLEML FNDLLDALQG
SVPPARPQFR DFVQHVMEKN HEETTENYWR NDLIEGDLIA FPTLPSATYQ PLANEALIQK
FKISRSGPSD YTTATLIRAA WTLLQARYCD SPDTVFGCTV SGRNASVRGV EDVVGPVIAT
VPIKAHLEPQ QSVTEYLKAV HAHSVAMTPY QNYGLQNIAR VCDNAPSACG FQTLLVIQPA
SSVPEASFIL PFSAPRASFS TVALTLECSL SAEGDILVHV HFDNAVLPRG QVERIVQQLE
HVLQQLAQEP VGTLSELELI SPRDMNDLLQ WNSRIPEATE DCVHNLIAQN TLLNPKAQAV
CAWDGSLTYA ELDNISSRLA AHLMDAGVGP EVFVPLCFEK SMWTIVAMLA TMKAGGAFVP
MDASQPTSRM QLVVKEVSAH VMLCSEEQLG RCPGLVEKAI AVGPGMAQAS LQKMSKTPVS
PSNAAYVIFT SGSTGTPKGS VVEHRAFCTG ALSHKEGLQM GRRVLQFASY TFDASVLEIL
STLVQGGCVC VPSESERRGN IAEAITRMNV DWAVLTPSFV STIDPTSVPT LETLCLAGEA
MTATHVATWT PYVRLVNGYG PSECCVCSSS NRRVVPGTAP NDIGTAVGGA CWVVDRDDHS
KLAPVGCIGE LLVEGHTLAR HYLRNEEKTA AAFISRPSWL PWTRCDRLYK TGDLVKYGPD
GSLLFIGRKD TQVKIRGQRV ELGEIEYHLC LPTEVSQAIV SYPKKGIYAN KLIATLELTA
TSGDGLVPVP STTLQKTGFD LATVSRYMGE TLPVHMVPVI WIVVEKIPSS SSTKIDRKAV
DTWLAQLPAD FQPTMGLQRN EPTVSTLRPD EGKALAISNK IASLVNREGS PLQGKDFNVS
SMGIDSVQVI SLASFIKQTY GVTVDVSRIL DGQMTVRSLA ALIDSELTGS PQVATSSFDA
MKEANALMQA IIKRSPMKKT VFVTGVTGFL GTQILRQLCD RPDVGRVIAH VRASTPSEAF
MRVKDAAVRA QWWSDYYLTK LDVWAGNLAQ PQLGLKPRQW ASLTGESPND GLVHAIIHAG
AAVNWNAGTE ILRAANVDST AELIKAAVSS PARPRLVYVS GGHRWHPNED DREIAAEVAH
ANGYAQTKYL SELLVKQFAA RYSSQFAIVK PGLILGTPEE GVANTDDFVW RLASAVVDAR
CYSRDVGESW MFVTSSTRVA EETIHQAFCP ADAMRTVTFM TDGITEREFW DIFHHELKYP
LRAVDHATYL ETLHQSIQKD AAGHPLWPVM QVFDAIDGRL GGGDVLPDAS VVTPSQRQHV
KATVRRNVQF LVEAGFLASP TGKKMRYMAE KVFQRSGDVW ENVKGMVNGL A
//
