ID A0A482XS09_LAOST Unreviewed; 1031 AA.
AC A0A482XS09;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018335};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=LSTR_LSTR006215 {ECO:0000313|EMBL:RZF48248.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF48248.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF48248.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF48248.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF48248.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
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:RZF48248.1}.
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DR EMBL; QKKF02002619; RZF48248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482XS09; -.
DR STRING; 195883.A0A482XS09; -.
DR InParanoid; A0A482XS09; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
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 CDD; cd00939; MetRS_RNA; 3.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 3.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR041598; MARS_N.
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 InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
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; PF00043; GST_C; 1.
DR Pfam; PF18485; GST_N_5; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 3.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 3.
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 SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 3.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 3.
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:UP000291343}.
FT DOMAIN 53..181
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 857..913
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 916..972
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 982..1031
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT REGION 201..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 114528 MW; 8EF18B471D9442AE CRC64;
MKLFTNTGNS ASLKILISSS FAKVDIPIEV ISASEAGFQN PKRLPILQID DVSIFSSNAA
AQYLYSPSDG HLSAVQRWLD WEAVLLQPVL VKSSKLENCP NVSEHLSKLN STLGKQQYLI
KDVLTVSDIV VWSTLFPIFT DEQLEPIFSA KYESIGNWFK HLANLPEFKS AVEKFSHPGG
IACIQNVGAA GYFPAVNTTT TATPASDPCK KAKPSKPRKD LLPSESSESS EALPKEPPIT
DVELQAAHNA WKSGPTIKPK PSVTPVLPIA GERNVLITSA LPYVNNVPHL GNIIGCVLSA
DVFARYSRLK NWNTLFVCGT DEYGTATETK AIEEGLTPEQ ICNKYFEIHK EIYSWFNISF
DKFGRTTTKQ QTEVVHEMFR KVHSNGFTSV SAMEQLLCEK CDKYLADRFV EGTCPKCSYE
DARGDQCDGC GNLINAVELI KPRCKLCQTR PVVRLSDQLF LELPKVEKRV AEWLESASDG
WSNNAKVISK AWLKDGLKPR CITRDLKWGI PVPLPGFEKK VFYVWFDAPI GYMSITKTYT
EKWRSWWEKD KSGNVKVTLY QFMAKDNVPF HSIMFPSTLF AAGGNFNLVS HLMATEYLNY
EDGKFSKSRG VGVFGTDAKE TGIPSDIFRF YLLYVRPEGQ DSSFSWADLV TKNNSELLNN
LGNFINRALV FVEKFFDYLI PEMNLTEDDY TYVVYINRLL SEYSAALENG SFRFGLRHIL
GISRYGNLYF QTNQPWALMK GSAEDKKRAG SVIGLSCNIA CLLAILLKPY MPQTCDVIAK
QLNAPDSVFV LPSHLALLLS PGHKIGKPAP LFTKIEPSTV EELKKRFGGK QQPATNGPAS
NNKKKPTTAT LSSHTASIKA MEDAVAKQGN LVREMKASGV PKTEWQPQVT VLLDMKKQLA
ELQKHASVDN VTGNGDVEGL RKKVAEQGDL VRKVKSSGVP KSEWQPHVDV LLSLKKQLAE
AEKQSQSTNS ITDSSVVGPA ESVKDLEEKI TKQGDLVRKM KGSGASRSEW QPQVNILLDL
KKQLAAAQKT C
//
