ID E5A9A7_LEPMJ Unreviewed; 529 AA.
AC E5A9A7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Similar to cysteine synthase B {ECO:0000313|EMBL:CBY00248.1};
GN ORFNames=LEMA_P013780.1 {ECO:0000313|EMBL:CBY00248.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929138; CBY00248.1; -; Genomic_DNA.
DR RefSeq; XP_003843727.1; XM_003843679.1.
DR AlphaFoldDB; E5A9A7; -.
DR STRING; 985895.E5A9A7; -.
DR EnsemblFungi; CBY00248; CBY00248; LEMA_P013780.1.
DR GeneID; 13290367; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_039949_1_0_1; -.
DR InParanoid; E5A9A7; -.
DR OMA; MPALNML; -.
DR OrthoDB; 2643608at2759; -.
DR Proteomes; UP000002668; Genome.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF253; CYSTEINE SYNTHASE 1; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 372..486
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 529 AA; 58157 MW; 30E6748224AAF971 CRC64;
MASQNLLNTY SGPDALRKYF DPDCQPLLPL VELPASLNPF YQDGVRIHAK LMSMHPANNV
KIMPAMNMLN KGVSPENTKS VVEYSSGSTV ISLALASRIN HNVQDVRAYL SNKTSRSKLR
LMQFFGLDIT LFGGPSQPDP RDERGGIQQA RALAQDNSTI LNPNQYENDA NWQAHVKWTG
PQIHKQLPSI NVLCVGMGTS GTMTGLGQYF KNNKPSVTRL GVCTAAGDRV PGPRSLALLG
PVEFPWRDSV DFIEEVGSKD AFNLSLQLCR EGLICGPSSG FNLQGLLSFL QKRKDAGTLK
YLAGSTGLID CAFICCDLPY QYVDEYFDKL GDKAFHPIHN QNLTTVDLYR YDEAWELNPT
QALESFTNDT TTPPAITLVD LRKPDDFALD HIPGSHNLPL QTANASTPSP FFAAHVLEAQ
WKELETTFTN ERIDAHELSG KNVCVICYNG DTARVATSIL RAKGVAANSI KGGIQALRQD
LPHLLQSTRG RRTVQSGYKH AANVAVQEVR ADSLSPRAWG RTDLDQVVV
//
