ID S4P722_9NEOP Unreviewed; 928 AA.
AC S4P722;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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};
OS Pararge aegeria (speckled wood butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge.
OX NCBI_TaxID=116150 {ECO:0000313|EMBL:JAA87776.1};
RN [1] {ECO:0000313|EMBL:JAA87776.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA87776.1};
RX PubMed=23622113; DOI=10.1186/1471-2164-14-283;
RA Carter J.M., Baker S.C., Pink R., Carter D.R., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RT "Unscrambling butterfly oogenesis.";
RL BMC Genomics 14:283-283(2013).
RN [2] {ECO:0000313|EMBL:JAA87776.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA87776.1};
RA Carter J.-M., Baker S.C., Pink R., Carter D.R.F., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RL Submitted (MAY-2013) 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; GAIX01004784; JAA87776.1; -; Transcribed_RNA.
DR AlphaFoldDB; S4P722; -.
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; 3.40.50.620; 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; 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; 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}.
FT DOMAIN 1..117
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 757..813
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 817..873
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 878..928
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
SQ SEQUENCE 928 AA; 103404 MW; 4FA9C68D95C4C06D CRC64;
MGKCNEILEW EATRLQPVVS TILTSKSVPS DLKQVLNSLL LMLEGLLTKQ KYVVLDKLSA
GDISIWSTLY PIAFNKTLKE TYLNEFTNIA KWLEELASNK AVQDALSQWD GTVEGPFGSN
AALGVPQITN MVSRIGSPEE APELSVTPEE IEAAKQNLIN GVQNLPESMK SEKPPLPIKG
RRNVLITSAL PYVNNVPHLG NIIGCVLSAD IFARYCRLCG YNTLYVCGTD EYGTATETKA
LEEGITPREI CDKYFAIHDA VYRWFNIGFD YFGRTSTAQQ TEIAQRMFLK LMDNGFVSNQ
SVDQLFCENC QRFLADRFVE GTCPHPGCLY DSARGDQCDK CGKLINAIEL IEPRCKVCSL
KPTVRSSDHL FIELGQLEPS IRTWFNNTEG GWSPPARAVT RSWLRDSLRA RALTRDLKWG
VPVPVPGYTN KVFYVWFDAP LGYLSITQCF TKNYEKWWKK DKDYDIKLYQ FMAKDNVPFH
GIMFPATIIG VNEGYALVDH IFATEYLNYE EGKFSKSRGV GVFGTDAQDT GIPADVWRFY
LASIRPETSD SSFSWTELGT RNNSELLNNL GNFCHRSLSF CANTFKGVLP DMKLTEADYE
VVALVNREVI AYVQQIEKGR LREGLRHVLS VSRIGNQHMQ STQPWVLLKG SDDDKVRGAT
AIALCCQLVA LLCTLLAPYV PDTSRRLRAQ LNVHADALRI NPQNPSLVQY LPAGHVIGKP
EPLFTKLESE VLDQLRAKYA GTQSERANKN GDKKQSTSAE LEAAIATQGE KVRKLKSSTK
DKSIWQPEVD KLLALKKELS SLPTQSAPAP SNTSNGTVAD LEKAVAEQGE KVRKLKSTTK
DKSVWQPEVN KLLALKKQLG DAQSQSKTSV PNVAANNSAA NLEKAIAEQG DKVRKLKGST
KDKSVWQPEV NILLDLKKQL AALQVNNK
//
