ID A0A0L7REX3_9HYME Unreviewed; 969 AA.
AC A0A0L7REX3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 08-NOV-2023, entry version 35.
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=WH47_05470 {ECO:0000313|EMBL:KOC69527.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC69527.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC69527.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC69527.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) 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; KQ414606; KOC69527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7REX3; -.
DR STRING; 597456.A0A0L7REX3; -.
DR Proteomes; UP000053825; 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; 1.
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; 1.
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; 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; PF18485; GST_N_5; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 1.
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; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053825}.
FT DOMAIN 66..189
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 909..964
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT COILED 836..863
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 969 AA; 109549 MW; 0D684E0688E77301 CRC64;
MNISTNEGNP NVLKLVIAAK MAQQSFTVKT VQPKVSFLGR LPFIELSSGL VLFSTNAAMQ
LLVSSPEDSK VVTNKWLEWE ASQLQPSIAV YGSTGTYKTA NKSCLWSLLK ELNIALKDKK
YLIEDNNDLS LADACIWVTI WSTILVTDIG NELCKEYVSI KNWLSNIELL PIIQNSLKEY
KFQRGLKAIL SVQAVSWFPA NTAVISRSAP NSKPTPSDVS PTKEKEVETI SQEEIQNITS
NWSSTSYPEM KNSSYPVLPK KGEKNILITS ALPYVNNVPH LGNIIGCVLS ADIFARYCRQ
RNYNTPCYLL NFTITIIYYI SGTDEYGTAT EAKALEEKTT PQAICNKFFD IHNDIYRWFR
IGFDYFGRTT TPEQTEIVQS FFLRIKSQGY ILNETVDQLL CESCDRFLAD RFVEGTCPRC
KYEDARGDQC DGCGHLVNAT DLISPRCKVC SSRPIVKKSV QFFLDLPKAK DKLKEWSPTV
EKGWSSVARV VAKPWLRDGL KPRCITRDLK WGIPVPVEGY ENKVFYVWFD APFGYISITK
RYTQEYEQWW KPKDVQVDLY QFMAKDNVPF HAIMFPACLI AANEGHTLIK HLMATEYLNY
EDTKFSKSRG IGVFGTDARD TGIPADVWRF YLAYVRPETQ DSNFNWVDLA TKNNSELLNN
FGNFVNRALV FAEKYFDSKV PLIELQEDDL VLLVLAQREL SSYVHSMKQA KLRDGLKHVL
AISKHANVYM QFQEPWVKIK GTDNDKKRAG TIIGICCNLA CLLSALLAPF MPNTARELRS
QLGLDNNHYG YISDVITNIL PTGHKIGKPS PLFKKIEDKD VEALRKKYAG KQETENNGEN
SDIKSLESEV AELGNKVKEL VAKHEGQIFS NLKKMFTDII GEKSKSPESK SKKSDLVFVP
EQNGDASMDV ASLEAAIAKQ ANLVRELKAK EEKSVWRPEV EKLLNLKKQL ADLNGTAPAP
TDKKSKKKK
//
