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Database: UniProt
Entry: A0A1Y1Y2D9_9FUNG
LinkDB: A0A1Y1Y2D9_9FUNG
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ID   A0A1Y1Y2D9_9FUNG        Unreviewed;       638 AA.
AC   A0A1Y1Y2D9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 25.
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=K493DRAFT_286264 {ECO:0000313|EMBL:ORX91886.1};
OS   Basidiobolus meristosporus CBS 931.73.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC   Basidiobolus.
OX   NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX91886.1, ECO:0000313|Proteomes:UP000193498};
RN   [1] {ECO:0000313|EMBL:ORX91886.1, ECO:0000313|Proteomes:UP000193498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX91886.1,
RC   ECO:0000313|Proteomes:UP000193498};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORX91886.1}.
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DR   EMBL; MCFE01000301; ORX91886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1Y2D9; -.
DR   STRING; 1314790.A0A1Y1Y2D9; -.
DR   InParanoid; A0A1Y1Y2D9; -.
DR   OrthoDB; 1341752at2759; -.
DR   Proteomes; UP000193498; 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   HAMAP; MF_00098; Met_tRNA_synth_type1; 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:UP000193498}.
FT   DOMAIN          42..433
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          447..593
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   REGION          589..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   638 AA;  72483 MW;  C18EF7354E9746AE CRC64;
     MTDTTEKIVR PVADESNRKV REGIALNLNK DVKLPVKGER NILITSALPY VNNVPHLGNI
     IGAVLSADVF ARFTRSRGYN VLYVCGTDEY GTATETKALE EGVSCQELCD KYNALHAQVY
     EWFGVDFDYF GRTTTNQQTE IGQDIFLKLH KNGYLIEDTM TQLFCEKCQR FLADRYVEGT
     CPKCGYVDAR GDQCDQCQQL LNATELISPR CKLDGNAPIT RDSTHMFLDL PKLQQKCEEF
     VEESSQKGSW ANNGKIITQS WLKEGLKARC ITRDLKWGTP VPLEHMKDKV FYVWFDAPIG
     YPSITANYTS EWEKWWKNPE DVKLYQFMGK DNIPFHTVIF PCSLIGTEDP WTMLHHISTT
     EYLNYENGKF SKSRNVGVFG NNVMDTGIPV AVWRYYLLSN RPETNDSVFT WKDFITRNNS
     ELLANVGNFC NRVIKFVDSA KYNGTLPAFS LEGENEKQLI EDVNKLLDAY IDALENVKLR
     SGLEIAMKIS QRGNQYLQES KLDNTLYNNE RAQCDTVVTV AINLIYLLSA VFYPYMPTTS
     ESICRQLNAP LPRIPETFQM NILEGHVIGK PEYLFKRIDG KMEEVYKQKY GGGAKEEPAK
     KKKSKKSKKP AEPKPQADGE KAEEAAPPAE DAKTGESA
//
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