ID A0A317W8K7_9EURO Unreviewed; 1019 AA.
AC A0A317W8K7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:PWY82061.1};
GN ORFNames=BO70DRAFT_429155 {ECO:0000313|EMBL:PWY82061.1};
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:PWY82061.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY82061.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY82061.1,
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 -!- 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:PWY82061.1}.
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DR EMBL; MSFL01000012; PWY82061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317W8K7; -.
DR STRING; 1448321.A0A317W8K7; -.
DR VEuPathDB; FungiDB:BO70DRAFT_429155; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
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; 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 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 SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT DOMAIN 28..337
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 630..867
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT REGION 453..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..476
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 110150 MW; 450956A633547551 CRC64;
MANIDPRGVL FPAYVDQVAE AQPEAIYAEF PNHPLSYDYG FRKITYRDLA NAINGVAKWL
IETLGPGQDE VLAYFGPTDV RYPALVFGAL KAGYVMYLPS PRNSPAAHRH LLQTLNCTKL
LVTTPRPPPV AGIIAAAPLD VFELPGVNDL LGTTHPHIPF TKTYPAAADE RCVIVHTSGS
TGIPKPIIWT HESIMRYYNM AGLAAPEGDF NQCDLTQGKR QFLCLPAFHS GGLASLSFMA
VPSGMTSVCP ISGIPTAAGM VAALKKTPFD VALVPPSVIL ELAAAPDLLD YVSQHMSHLG
YCGGDLPQAV GELVASRIPL INHYGASEMG MLHLIQSPHR DPLTDWGYVQ VHPGLGIEFR
PTTATESELV MVHRPELTSF QMPPTIFPGI EEYHSQDLFV RHPDPAKADL WRWSARLDDI
ITFLNGEKTN PISMEQHIVA SNPDVSVALP SPEPPAARRR HRAAVAQHRG RQRRVPGPRP
HHQDAHPVHQ PGQALPRSGK GTAQRAATLA LYAPELDALY ADADTLTVRD GPSTGPGPVD
DPAAISAFIE TSLLAVTGWT PDALSAESFF HSGLDSLQIL TLSRTLRNGL QLPEIIPNLI
YRHPNCNPNS NPPLLLLLLP SPSQPQTIIL TGSTGTLGSY LLAALLNNPN ISHIHCLNRN
PSACSIQQSQ ALKFHLPALS PSDPRLTFHT TDLTRPDLGL SPSTLQTLRT TTTTLIHNAW
TVNWLLPLQF FKPLLTATLN LLNFCADAPS SPHFFFLSTV GSVTPSTSPS IPEQIVTTTL
PAANAYSNSK YIAEHLIASA TARSPSLRAS IARVGQVAGA VRAPGLWSRT EWFPSLVRSA
AHLRALPDSL GPMSNLDWVP IDLLADVLVE LAVSPVPSAE EEEEEEEGSE GKGNLNVYHP
HNTHKVQWTT LLPTIASALP DPESSSSPME TIPLAEWRAR VAADVAKTAG DAPDNLQIVL
ERNPAAKLAD FWSVLEGVGA EGSVMVFETE RTQRVSGLLG GVEGVKGGWV EKWVGEWFA
//