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Database: UniProt
Entry: A0A1L9V564_ASPGL
LinkDB: A0A1L9V564_ASPGL
Original site: A0A1L9V564_ASPGL 
ID   A0A1L9V564_ASPGL        Unreviewed;       696 AA.
AC   A0A1L9V564;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=AMP-dependent synthetase/ligase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPGLDRAFT_137753 {ECO:0000313|EMBL:OJJ79041.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ79041.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV878923; OJJ79041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9V564; -.
DR   STRING; 1160497.A0A1L9V564; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_137753; -.
DR   OrthoDB; 45466at2759; -.
DR   Proteomes; UP000184300; Unassembled WGS sequence.
DR   GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd05943; AACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR005914; Acac_CoA_synth.
DR   InterPro; IPR032387; ACAS_N.
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   NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR   PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184300}.
FT   DOMAIN          45..102
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          113..501
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  76650 MW;  C1C1E919656F75DC CRC64;
     MPSIDGLNNH DGPRELWRHS SPQDTKMYDF MKRASQKHGV SLGGYHDLWQ WSVSEPAKFW
     EDVWHYTAVK AHKPYETVLE SDQQLFPRPA FFAGSRLNYA ENLLYPASSP DENAVAVISA
     TELDREYVSW KELRDRVRQC ANALKEAGLQ SGDRVAGFLG NHVNTVVAML ATTSIGAFWT
     GVSPDTGVHA VLERLGQIEP KVLFADNASL YNGKVHSAQA KVQQIVSDLP LLERLVVFET
     IKSHQSNLAE LQPQQGKAYS YDEFLSTASN QSASLEFASL EPDHPVYILY SSGTTGAPKP
     IVHGALGTLL QHKKEHVLHC DIRPGDRLFY FTTVTWMMWH WLIGALASGA TIVTYDGSPF
     RPFDAEGGNG EMAMPRLIDE LQITQFGTSA KYLSILEQAS LNPREHPHRP VTLQTLRAIF
     STGSPLAPST FEYVYSSIHP DTMLGSITGG TDILSLFCGS CPILPVRKGE IQCRCLGMAV
     YAFDYAGKDI SASSEPGDLV CTTPFPAQPV MFWPPGPVGA EKYRKSYFDL FGPSIWHHGD
     FVRLNPVTYG VTMLGRSDGV LKPAGVRFGS AEIYNVLLKH FTEEIEDSLC IGRRREGIDT
     DETVVLFVKL ASNNDTNPII PAELAAHIQG TIRKELSARH VPAVVAACPE IPVTSNGKKV
     ENAVKQILCG LNIKIGASVA NASCLDWYCA WALQNP
//
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