ID A0A0G4KR70_9PEZI Unreviewed; 611 AA.
AC A0A0G4KR70;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=BN1708_002373 {ECO:0000313|EMBL:CRK11940.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK11940.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK11940.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK11940.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CVQH01003335; CRK11940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4KR70; -.
DR STRING; 100787.A0A0G4KR70; -.
DR OrthoDB; 166496at2759; -.
DR Proteomes; UP000044602; 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; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; 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:UP000044602}.
FT DOMAIN 67..433
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT REGION 17..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 68003 MW; F8F1ED8BA5B9BD54 CRC64;
MRPIRLAARL PLRRPSQTTR SGWVCPSCHH GQIRRSSSGS SSGSSSGSSA SDRSASSSSS
AHTKPFYVTS PIFYVNASPH VGHMYTMILA DSLKRWQTLR GRNALYCTGT DEHGMKVQRA
AAKQGIPPKA FCDSNADKFR QLAAACGIDN DFFVRTTDAD HVEAVQHFWH LLRAGGHIYE
STHSGWYCVS DECFYAEDEV ERAVVPQTGR TIMASIATGS EVEWTEEKNY HFRMKAMRDR
LLQFYDDNPD WIVPRARMNE VVSWVRHNLE DLSISRPVSR LDWGIRVPDD PSQTIYVWVD
ALINYLTKAG FPAWAPGDEH RGGWPADVHV IGKDIVRFHG VYWPALLLAV GLPPPKQLLS
HAHWTLGKKK MSKSVGNVVN PFQAIERWDL DTMRYVMLRD GGLENDADYE NRFISARYEK
DLQWTLGNAL SRITRSTKWH VADAVRWARD QQAARGAGTQ ASTEASADAP QAPLRRLAAL
VDETPRLMAA AMETDLNPST AIKAAMTLLV EANRFIADSA PWDKTKVPSD AARNEIVFHA
AEALRVAGLV LQPFMPGKMG EMLDILGVQP ARRTFAYATF GGDVEYGARK EAAPLPRGKW
TGLFPPAVAT E
//
