ID A7F2N9_SCLS1 Unreviewed; 579 AA.
AC A7F2N9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=SS1G_12187 {ECO:0000313|EMBL:EDN95981.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN95981.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR EMBL; CH476639; EDN95981.1; -; Genomic_DNA.
DR RefSeq; XP_001587157.1; XM_001587107.1.
DR AlphaFoldDB; A7F2N9; -.
DR STRING; 665079.A7F2N9; -.
DR EnsemblFungi; EDN95981; EDN95981; SS1G_12187.
DR GeneID; 5483154; -.
DR KEGG; ssl:SS1G_12187; -.
DR VEuPathDB; FungiDB:sscle_05g041620; -.
DR eggNOG; KOG0436; Eukaryota.
DR HOGENOM; CLU_009710_9_0_1; -.
DR InParanoid; A7F2N9; -.
DR OMA; MDTQAFC; -.
DR OrthoDB; 166496at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 49..415
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 476..537
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 579 AA; 65939 MW; 4FB3B5DCDCE36295 CRC64;
MYGLNPSLRG SLQSKTRSLW RTGWVCSSCR ARAIPKVRYS TDTTPKKPYY VTTPIFYVNA
APHVGHLYTM VLADVFKRWQ VLKGETAILC TGTDEHGMKI QRAAAQAGTL PKEFCDNGAE
TFKKLAQRAG LSNDHFVRTT DQDHKETVEY VWYMLKEREY IYESKHEGWY CVSDETFYPE
SVIEKRLDPF TGRTFIASQE TGKEVEWTSE KNYHFRLSAF KDQLLEFYER NPDFVVPLTR
MKDVVNQVSK GLEDLSISRP SDRLSWGIRV PDDDSQTIYV WLDALVNYIT KASYPWAPGN
EAAGGWPADV QVIGKDIVRF HCIYWPAFLL ALNLQPPKRI LTHAHWTMDN QKMSKSVGNV
VNPFFAMDRF GVDVMRYYLI HDGGIKEDSS YGNEYIVERY KKGLQKGLGN LVSRLTRPKV
WNVRSCVEAA HSEGLHNSDI STNQQIALLN NVRPKANDKM QELNPAAALH VIMDTVFETN
KYLQEEAPWS LAKSEEPNAK EKLISAVYHS AEAIRIVGIL LQPYMPEKAS LLLDMIGVIP
ERRTYEYATL GADPSYGDAQ VPLGKCAWDA LFPPLAIET
//
