ID V2XU31_MONRO Unreviewed; 640 AA.
AC V2XU31;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Amp-dependent synthetase and ligase {ECO:0000313|EMBL:ESK96361.1};
GN ORFNames=Moror_7147 {ECO:0000313|EMBL:ESK96361.1};
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:ESK96361.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK96361.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96361.1,
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:ESK96361.1}.
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DR EMBL; AWSO01000050; ESK96361.1; -; Genomic_DNA.
DR RefSeq; XP_007844401.1; XM_007846210.1.
DR AlphaFoldDB; V2XU31; -.
DR STRING; 1381753.V2XU31; -.
DR KEGG; mrr:Moror_7147; -.
DR HOGENOM; CLU_000022_59_7_1; -.
DR OrthoDB; 2596785at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
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 PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF29; ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G08470)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ESK96361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 96..479
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 534..615
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 640 AA; 71308 MW; 130FAF20CCC47538 CRC64;
MVVRRKAVAV SRDARRLLFL RSSSQRRNLT QVPSKGRSYV QGSLQPPLDN RTFTEYFVDE
ILQNHSQRPA LVCRTEKPRA HGGPPSPNLG GSSHLAWDFE EFNRHIDALA RGLLSLGVQK
GDRIGIVMGN NSSYAMLQWA AARIGSILVT INPAYRIDEL AATLRIVGVK HLFVVPRIRT
SSYLDMLMSK FPDLKHSVPG EIQEEALPEL RNLIVVDNKD LHRDELRKLD IRSVIDWRDI
LMWREGTQEK RRVEEISRTI HKDDVVNMQF TSGTTGLPKA VALTHSNLLN NALSIGRCMR
LTHKDIAMSL RSFTALIILG DLAAWVYGAA IVYPSEVFHP PSIIDAVIAE KCTALHGVPT
HFLGVLTEVE KRKKEGDKLD MSSLRTGIAA GSSVPIELMK KLISDLNLRD LTNAYGMTET
SPVSFQTTPD DPIVHRTETV GRVQPHVKAK LIDPDGNIVP IGKPGELCVA GYLLQKGYWG
DEEQTRKVMR KDEEGTLWMH TGDEGVMDHD GYLKIVGRIK DIIIRGGENL FPIQIEDILL
KNPDIHEVAV IAVPDAKYGE VVGAWVVRTP GTNASRNEVR RTVSENMNPQ NAPAWVWFVG
EDGNPDELPK TASGKVMKHV LRKWSKELAE RGVGGVSNGR
//
