ID A0A0N5CDB4_STREA Unreviewed; 540 AA.
AC A0A0N5CDB4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Methionine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00026124};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Mitochondrial methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030331};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001585900.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001585900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
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DR AlphaFoldDB; A0A0N5CDB4; -.
DR STRING; 174720.A0A0N5CDB4; -.
DR WBParaSite; SPAL_0001585900.1; SPAL_0001585900.1; SPAL_0001585900.
DR Proteomes; UP000046392; Unplaced.
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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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}.
FT DOMAIN 21..383
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 411..499
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 540 AA; 62966 MW; BC2F0FA4497D1F19 CRC64;
MFQVLKNVPS LKILFLRKKT FITSPIYYVN ASPHIGHVYS TVIADAAFRY DKLKNPSTNN
NDFIFITGTD EHGQKVQKAA NNANKSPKEF CDDISKNFRD IFDNLNIKYT HFARTTDKSH
IKCVQNMWEI LYSKGYIYKS KYSGYYSYVD EAFYKEKDVE EVEKNNKITL VSKETKNEVQ
YLEEENYMFK LEDLYPKIKK WIIENDVIRP KHYINQILMY MNEVEDLSIS RDIKRMSWGI
PVPNDPSQTI YVWMDALMNY MSAVGQPNDH LIQWPPSWQI IGKDIMKFHA IYWPAFLLAA
DMELPKKLFV HGHWTIDNVK MSKSLGNVVN PFEISNVLSP DGLRYFLLKQ GVPDSDNNYS
NIKAINLVNS DLVNNIGNLL SRSTVKRLNP EQLYFPENYS SLDPKILDEA QDIVEELKVL
SQKVNEHYEN LIFYKGLEEI MSVCKKVNTF FHNTQPWKKS SGNELSSILY ITYETLRVIG
LLMQPITPNY SSNLLNQLGI PENKRTLNYA NFSLDQFTRT SLSKTQKPLL KRIDIIEKKP
//
