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Database: UniProt
Entry: E4ZYM1_LEPMJ
LinkDB: E4ZYM1_LEPMJ
Original site: E4ZYM1_LEPMJ 
ID   E4ZYM1_LEPMJ            Unreviewed;       401 AA.
AC   E4ZYM1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Aminomethyltransferase folate-binding domain-containing protein {ECO:0000259|Pfam:PF01571};
GN   ORFNames=LEMA_P108120.1 {ECO:0000313|EMBL:CBX96547.1};
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).
CC   -!- SIMILARITY: Belongs to the GcvT family. CAF17 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007270}.
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DR   EMBL; FP929129; CBX96547.1; -; Genomic_DNA.
DR   RefSeq; XP_003840026.1; XM_003839978.1.
DR   AlphaFoldDB; E4ZYM1; -.
DR   STRING; 985895.E4ZYM1; -.
DR   EnsemblFungi; CBX96547; CBX96547; LEMA_P108120.1.
DR   GeneID; 13289980; -.
DR   eggNOG; KOG2929; Eukaryota.
DR   HOGENOM; CLU_007884_7_0_1; -.
DR   InParanoid; E4ZYM1; -.
DR   OMA; WEADPRT; -.
DR   OrthoDB; 2874334at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   InterPro; IPR045179; YgfZ/GcvT.
DR   InterPro; IPR017703; YgfZ/GcvT_CS.
DR   NCBIfam; TIGR03317; ygfZ_signature; 1.
DR   PANTHER; PTHR22602:SF0; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22602; UNCHARACTERIZED; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          81..180
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
SQ   SEQUENCE   401 AA;  44568 MW;  7FDA4874F5F48EFA CRC64;
     MVVPMPEDDI QNHNHNHNKI LADSKQHAGT APSCALWQTR SYVDHSHFHV NRTRAVATMP
     IRFYSSTHSP SQPRKSGSAP LAHRSLISLS GPDAAKFLQG LITNNVDASR QAPFYAAFLD
     ARGRVLWDVF IWVWPELVAE KGHWACYIEV DQTEAGALKK HLKRHKLRSK VTIEDAESVG
     IWAAWGDAPA QVPKENAVSD LQDPRAPGLH RYLVAHDRTS LADRSEVLDV SEYHLQRYLL
     GVPEGPVEIP RESALPMECN IDLSSGIDFK KGCYVGQELT IRTKHTGVVR KRMLPIQLEH
     PGASVSPPVS GTDIKQLDDD GRTKRGRAAG KFIAGVGQVG LALCRLEMMT SMKVSAEGGS
     WKPGMQFGVD TDNGVVKVKP VLHDWFLSRE SHLWDKNRTR I
//
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