ID A0A2I2GAA1_9EURO Unreviewed; 985 AA.
AC A0A2I2GAA1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:PLB49801.1};
GN ORFNames=P170DRAFT_409405 {ECO:0000313|EMBL:PLB49801.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB49801.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB49801.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB49801.1,
RC ECO:0000313|Proteomes:UP000234275};
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:PLB49801.1}.
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DR EMBL; MSFO01000004; PLB49801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GAA1; -.
DR STRING; 1392250.A0A2I2GAA1; -.
DR VEuPathDB; FungiDB:P170DRAFT_409405; -.
DR OrthoDB; 2327998at2759; -.
DR Proteomes; UP000234275; 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:UP000234275}.
FT DOMAIN 25..349
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 620..854
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 985 AA; 109606 MW; FFAA55D58A825471 CRC64;
MLTKLCCEQE QDEIGHRLLL NYIDKWALIN PEKIAFYQVI LDSPQDKVVP LKYAHLRNLV
DQLAWWIHGL SGNKCTYKER SIAYLAPSDL RHLLLALACN RIGSKALLLS SRNSAYINAH
LIDECGCELL IFDATCSHVA DQISAKSKIT LHGMNDLVDL LKTKNARSKD FPYYETWASA
YNKPALILQT SGSTGLSKRV PISHSAISTI DIQQSVSKQY TDGRKCHLEV LAEAKRPYQS
FPLFHVAGFE LTCLFLFTGR CVVLGPPRRP PGIEVYKKVV ELARPDAAML APQTLNEIAE
DPPLMSAVVP KLEWIMYGGG PITEKTGDAV SSRTRLMNGF GSTECGSMPL YPTDAPYWNC
YHFHPLSGAD LRPIPNSDGL YELFVVRDET SFPYQSIFHN FPDLHEFPVK DIFQRHPDNE
NYWVYQGRTD DILVLSTGEK INPLPVQDAV SAIPGVRSAL VVGNKQPYPG LLIELGFDAI
FPEAKELIMS RLDKTLADTN FQGSRDAHIQ LKDVIWAGPE KPLARNAKGN LRRSAIEKDY
EDEINRLYGN DDSLISELDP SSEQTLFSGL LEMAGQLVSI DDLDIDEDLF DSGLDSRGAQ
ILVNAINRAS PHEEKAHVLL TGSTGFVGSY VLDSLLRCPE VERIACLDRW TEYRAASSDT
NTTNNPVDVQ YLLGSLEREN FNLDPSVLST LLESITVIVH CQWPVNFNQP LSSFEPNIEG
VENLIRFAHG ASYNPPIVFL SSIATVKQWD KSIPVPEKPL SDPKHAQTWY GQSKLLASVL
LEEAGKTLGT RSSICRLGQV AGPVGRVVKQ RMWPRTDWFP SLLETSRAIG CVPDSLGSAG
RVDWLPVDKL AEIIVQLVVL KHSIDANGMA LTDFHHLVNA EPVSYQDILP VIVKRLGEEV
RVVSLSEWVD RLEKSAATTE NGSNPGLGLG LLSFFQGLKA TQEEAPVVLD TQHTQDRLPL
LGEIGAANGS WMEMWLDQWD FNSRN
//
