ID   A0A318Z108_9EURO        Unreviewed;       941 AA.
AC   A0A318Z108;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:PYH40965.1};
GN   ORFNames=BP01DRAFT_408710 {ECO:0000313|EMBL:PYH40965.1};
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:PYH40965.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH40965.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH40965.1,
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; KZ821272; PYH40965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318Z108; -.
DR   STRING; 1450539.A0A318Z108; -.
DR   OrthoDB; 3149897at2759; -.
DR   Proteomes; UP000248349; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR24096:SF428; DIDEMETHYLASTERRIQUINONE D SYNTHETASE TDIA-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        63..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          564..643
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   941 AA;  104735 MW;  878F03213A65015F CRC64;
     MSFRNLQHLL ETVAAREGSG NVISYPLGSL HEPRVLSYNQ LFMLALKASQ VLRSREDFQR
     GRVVLLHFNA HLDIIIWFWA VLFVGCLPAL SIPFSNHPSH RTAHLEHLSK MLSSPICLTR
     ASLLPEFGGQ EAIDPIAVES FDVENASPME SSDICRDSSS DDNAILMLTS GSTGYSKAVC
     LSHGQILAAI TGKYWVIELP EMTSFMNWVG LDHVAAMIEI HLQAMYGCKD QIHVQAPDVL
     SNPMAFIDLI HKHRVSRTFA PNFFLGKIRA TVKSQGEFVQ REWDLSCLRY IASGGEAVVT
     RTCEEVSKLL EQYGAPPNAI VPGFGMTETC AGAIFNTNFP CYDVRRSAEF ASVGSCMPGI
     SMRISDGENK PLPAGEIGSL EVSGPVVFQE YFNNPSATAE AFTPDNWFRT GDRGVIDEAG
     NLTLVGRAKE TMIVNGVNYY PHAIESALDE ANIPGLTRSF NCCFSSFPPG GDTEEIVVVY
     LPDYAPEDMI ARVQTTDAMS KVVMMSTGCR PKLLPLDRSM LQKSAIGKLS RAKIKTAYEK
     GDYQNYLEIN EEMVKLYRRV TRKDPKDALE QQLLSIFTNS LDLPAGEFDV QTPIFDMGIT
     SIELIKLKKN IEEHLDLTQE LPMITLMTNS TVRDLASALH DLQQKQQEYN PVVKLQGQGS
     KKPLWLVHPG VGEVLVFLNL AKFLVDRPVY ALRARGFNDG ETPFETIEEV VATYHAAIKR
     EQPEGPYALA GYSYGSMLAF EVGKVLESHG DDVRFLGSFN LPPHIKARMR QLDWKECLLH
     LSYFLDLITE ARSRELSQEF LMAEGGTTRE EALARVMAEA DQARLNELAL SEAALVKWAS
     LAFSLQSMAV DYDPSGSIAG MDVFYCIPLA VVASSKKQWR EEQLSKWEDF TRSAPRFHDV
     GGAHYTMLSP EHVFGFQKTL RAALDARDTW IIFPVILAQT K
//