ID V2WI88_MONRO Unreviewed; 669 AA.
AC V2WI88;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acetoacetyl-synthetase {ECO:0000313|EMBL:ESK86563.1};
GN ORFNames=Moror_9791 {ECO:0000313|EMBL:ESK86563.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK86563.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK86563.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK86563.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK86563.1}.
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DR EMBL; AWSO01000919; ESK86563.1; -; Genomic_DNA.
DR RefSeq; XP_007854133.1; XM_007855942.1.
DR AlphaFoldDB; V2WI88; -.
DR STRING; 1381753.V2WI88; -.
DR KEGG; mrr:Moror_9791; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR OrthoDB; 45466at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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:SF4; ACETOACETYL-COA SYNTHASE (AFU_ORTHOLOGUE AFUA_8G04770); 1.
DR PANTHER; PTHR42921; 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 Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 42..96
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 109..476
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 669 AA; 74407 MW; 18C443FBEB8675EB CRC64;
MSTSYFEHSK LLWKPEYPQY TNVEGFRKMV NRSRGLNLKD WHDIYKYSIE NYDFWVDLWK
YLRIIYSVPP EKIMTPGTIP EVPEWFPGAR LNYAENLLWR NDDGVAITAG GEQGKIEECS
YRELRLKVQE MASAMKANGV GVGDRVAAII TNSIVAVTIA LATTSIGAIF SGTATDMGQD
GILDRYRQIQ PKVIFSETET QYGGKKTNLL PKVSAVIKSL SDIGLRRAVL LPSSITGKIV
TLRDVPNTIT LPEFLATGDN SELKFEQLPF NHPVYILYSS GTSGPPKCIV HSAGGALLQS
KKDTMLSKDL RQEEVHFQYT TTGWLLWTYM LTVLSVGARL VLYDGSPFYP NIKTYLNANF
FGTSPRFMAE VQGQGINPLE VAPFTSLRTV SVTGAVLTPP MFEFTFNAFG RKIFLISTSG
GTDIFCSLVS GAPTLPVYTG ETQYKALGMK VEVFDPDGNN VEEKSEPGEL VVTRPHPSLP
KLWGDTPDGQ KLRETYFSHY PGIYQHGDFL IVNPETKGVM ILGRSDGVLN PSGVRFGSGE
IYSVLEKFTK GGIDDTICIG QRRPQDKHER VLLFVKMRPG HSLTKSLENE IRSAIKNALS
ARHVPEYIFQ VEDIPYTVNG KKIEIAIKQI VSGSTMKPSG TVANPESLQL YYKYKDIENV
VGSSARAKL
//
