ID A0A177D549_ALTAL Unreviewed; 636 AA.
AC A0A177D549;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=CC77DRAFT_974638 {ECO:0000313|EMBL:OAG14636.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14636.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14636.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14636.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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DR EMBL; KV441498; OAG14636.1; -; Genomic_DNA.
DR RefSeq; XP_018380057.1; XM_018535903.1.
DR AlphaFoldDB; A0A177D549; -.
DR STRING; 5599.A0A177D549; -.
DR GeneID; 29121497; -.
DR KEGG; aalt:CC77DRAFT_974638; -.
DR VEuPathDB; FungiDB:CC77DRAFT_974638; -.
DR OMA; HLNTTEY; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000077248; 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:UP000077248}.
FT DOMAIN 16..407
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 436..571
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT REGION 562..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 72045 MW; 51E6DF5A3312817C CRC64;
MTGSKKILPV EGERNVLITS ALPYVNNVPH LGNIVGSVLS ADVFARFSRA RGYNTLYVCG
TDEYGTATET KAIEEKVTPK ELCDKYYALH SEVYKWFNIS FDHFGRTPTQ QQTDIAQDIF
TKLYKNGFLE EQTTTQPYCE THKSFLADRF VEGTCPLCAY EDARGDQCDK CGHLLDPLEL
KNPRCKLDGA TPVPRETKHV YLCLDKLQPM EEEWFKKASK EGNWSSNGVQ ITSSWLKEGL
RPRGITRDLK WGTAVPLEGY EDKVMYVWFD ACIGYVSITA TYTEDWKKWW HNPEHVKLYQ
FMGKDNVPFH TVVFPCSQIG TKDKWTMLNT ISTTEYLNYE KGKFSKSRNI GVFGNNAKET
GIPSDVWRYY LLSHRPETGD TEFEWDGFIA ANNNELLKNL GNFINRVIKF VNNAKIYDSV
VPDYTKFDDD YFTQHKKKVN DSLKTYIAEL EDVKIRAALA TALHVSSLGN LLLQDNRLDN
KLATEQPDRC AAVVGLALSQ IHLLASLIQP YMPDTTTAIL SQLNAEFLII PDTWEARSLP
VGHKIGTAGY LFSQIKPEKE QEWREQFGGE EARKAKEEKA KKAAAKKAEK ERKKAKKDAE
KAKGVEAAEK GQDGPAAKTA EEEVSRGVEQ VSLQTS
//
