ID A0A0B7NXK7_9FUNG Unreviewed; 743 AA.
AC A0A0B7NXK7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
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 Name=PARPA_14464.1 scaffold 50532 {ECO:0000313|EMBL:CEP20143.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP20143.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP20143.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP20143.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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; LN734230; CEP20143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NXK7; -.
DR STRING; 35722.A0A0B7NXK7; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000054107; 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; IPR036282; Glutathione-S-Trfase_C_sf.
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; SSF47616; GST C-terminal domain-like; 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:UP000054107}.
FT DOMAIN 226..617
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 629..731
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 743 AA; 82648 MW; 2CAD7ADF766A339D CRC64;
MSATIKITVP KLSANTKPYA NALKFSIAAE VTGVKLLETP GEVLALCVSN DVSLTDANAA
LKYIFDATAF NALHSLVIEK EEISVSPLVI KRKLDQAFQN AEDIISNHTN AFAKETSHVS
LVDVIYYGTL FETLSSAKDL SKYPALFAWF NIVSENEKFA AGVDHVKEQT NTGAKPKNKA
AFAAKKATKD IPKPVFNEAT QKVNNVAVKG LDHSVKVLPK DNERNILITS ALPYVNNVPH
LGNIVGSTLS ADVYARYCRA RGYNTAFFCG TDEYGTATET KALEEGVSCQ ALCDKYNAIH
TAVYEWFDLS FDLFGRTTTE KQTEIAQDIF LKNYKNGNIL KETMTQLYCE KCSRFLADRY
VEGTCPHCKY EDARGDQCDA CGKLLNATDL VDPRCKLDGN KPITKDSNHL FLDLAKLQPE
IEAAFKKSAA DGKWSANGIN ISQSWLKEGL RPRCITRDLK WGTPVPLEGY EDKVFYVWYD
APIGYPSITA NYTDEWEKWW KNPENVRLYQ FMGKDNVPFH SVIFPGCEIG TGEKWTIVNH
ISTCEYLNYE GGKFSKSRNV GVFGNNAQAT GIPPSVWRYY LMSVRPETSD SMFTWNEFIT
KNNSELLNNL GNFVNRAIRF IFAKYDGVIP KADFSGKLET GLIKDVNDLL KQYVEAMEAV
KLRSGLGIAM NISARGNQYL QDANLSNALF DESRPKCDAV VATAANLIYL LSAILSPYIP
ASSESMCRQL NAPLPCIASE ECF
//
