ID A0A2T9YC54_9FUNG Unreviewed; 791 AA.
AC A0A2T9YC54;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=BB559_004874 {ECO:0000313|EMBL:PVU89916.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU89916.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU89916.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU89916.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU89916.1}.
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DR EMBL; MBFT01000515; PVU89916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YC54; -.
DR STRING; 61424.A0A2T9YC54; -.
DR Proteomes; UP000245699; 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:UP000245699}.
FT DOMAIN 227..617
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 649..790
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 791 AA; 89326 MW; 55DDDDE9716D0815 CRC64;
MDTTKNSTDF TFFLNGAPPA TGSLSAIGLL KIALAISINN LSIQTKSNKE IKSKLPFWMV
FNDTNRKLID ANSIIRYIYG IRKLDPSNML QQELVLEWEE KILSCMIENK DISAHVSLNI
IENRIKDGKI SSENNGANIV VFANIYDCFQ RLDGKGKAKY PGISNWFSAM LSNEKVASAI
RIYESQTKEI LTRPEPAETN RKVNSNVAFN FDPKKIVEVK EGERNTLITS ALPYVNNIPH
LGNIIGSVLS ADVYARYSRA RGVNTLYICG TDEYGTATET KALEENISCQ ELCDKYHKIH
SDVYKWFNIS FDWFGRTTTP LQTEITQEMF MKVHGNDYTK TESMHQLYCE KHKRFLADRF
VEGTCPKCGY TDARGDQCDK CGTLINAVEL IDPRCKLDGS APIVRESTHL FLDLEKLQVK
CEMFVSNSYA KGRWSSNGLT ITKSWLNEGL KPRCITRDLK WGVPVPLEGF EDKVFYVWFD
ACIGYISLTA NYTKNWETWW KNPNNVNLYQ FMGKDNVPFH TVVFPSTQIA TGDDYTMLHH
ISTTEYLNYE SGKFSKSRGI GVFGNSAKDT GVDVDVWRYF LLSNRPESSD TMFTWSEFIA
RNNNELLANL GNFCSRILKF TDSTSKYAGI LPQPSAEILG YGDSTSDSAQ VTKSFISDIN
SLLSRYNSSL EAVSLRAGLK LAMEISARGN QYLQDSKFDN SLFTNSREAC DTVVYVCVNL
VYLLSAVFSP YLPTVSENIC KMLNAPARLI PDEFTFDLLP GHVIGTPMHL FSQIDDKMAD
VWRGKYGGSQ E
//