ID A0A423WH88_9PEZI Unreviewed; 678 AA.
AC A0A423WH88;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=VSDG_01932 {ECO:0000313|EMBL:ROW02693.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW02693.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW02693.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW02693.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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:ROW02693.1}.
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DR EMBL; LJZO01000004; ROW02693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WH88; -.
DR STRING; 252740.A0A423WH88; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 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; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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:UP000284375}.
FT DOMAIN 15..439
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 463..602
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT REGION 613..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76188 MW; 2975D61D14DFAE93 CRC64;
MTANPVLPVE GKRNVLITSA LPYVNNVPHL GNVIGSVLSA DVFSRWSRAR GFQTLFVCGS
DEYGTATETK ALEEGVSPEE LCKKYHALHK DIYDWFLIDF DIFGRTPTEH QTRITQDIFR
KLWDNGFILE REEFQPFCSH EAHNTFLADR FVEGECSICG DNGARGDQCD KCGNLLDPFQ
PESEIGASDD AAAKGTGWLV NPRCKVDGTT PERRKTKHLY LRLDALGDEI KEWFLKASKK
GSWSSNCIQI TDSWIQKGLL PRAITRDLKW GTAIPKGLKG LNDEEYANKV FYVWFDACIG
YCSITANYTD GQNADGKLWE KWWKSKDVDL IQFMGKDNVP FHTIVFPGSQ IGTRDDWTKV
HKLSTTEYLN YEESKFSKSK GVGVFGNNAK DTGIEPNVWR YYLLSRRPET ADSEFKWTEF
VDANNNDLLK NVGNLNQRVV KFCQAKYDSI VPDYTKYTSE GLDAHVKEVN ALLKEYNTHM
DATKLRAGLQ AILAISALGN KLLQDNRIDN RLLTEEPDRC AAVIGLALNH ISLLASILAP
YMPGTAVNIF EQLGLEPQPS IPDTWASDSI KPGHKLGTPK LLFTQIPAAK IEEWREAYGG
EEVRKAKELA AKKAEEKRLA KEKEKEKKRL KKLAAAQAKE NAQPDTKASV ESTEKKEMAD
PAIEQVTEAI AKTDVHTS
//
