ID A0A026WYY4_OOCBI Unreviewed; 957 AA.
AC A0A026WYY4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 08-NOV-2023, entry version 43.
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=X777_13443 {ECO:0000313|EMBL:EZA60354.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA60354.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA60354.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107078; EZA60354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WYY4; -.
DR STRING; 2015173.A0A026WYY4; -.
DR OMA; DWYGRVK; -.
DR Proteomes; UP000053097; 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; 2.
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; 2.
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; 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; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 2.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 2.
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; 2.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 2.
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:UP000053097}.
FT DOMAIN 46..169
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 814..869
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 896..951
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
SQ SEQUENCE 957 AA; 108458 MW; 7DBEEF33E9580052 CRC64;
MQQQWEKALE RNRKNAFLGR LPTLKASAEL SLFSVSSALR FLLSVPKESE ILNDRWLEWE
ITQLQPAILS HANMRTPKNL QKSDLWSLLK DLNSELKDKQ YLIKEHSHLS PADICIWVSL
WSTMLLEDVK DNVAKNLPNL YNWLANIEKQ SIIQESIKEF NLERGAKAVA SIEAASWFPV
NAVSNSRVSE SVSSDVNPKE KDAEAISEEE LRNVAHSWTT GQYLEVKESS YPILPKKSER
NVLITSALPY VNNVPHLGNI IGCVLSADIF ARYCRQRNYN TLYISGTDEY GTATEAKALQ
EKTTPQAICD KFFDIHNDVY RWFGIGFDYF GRTSTPEQTE IVQAFFLKIK SRGYVRSETV
EQLHCELCDR FLADRFVEGT CPGCKYEDAR GDQCDGCGHL VNAIELINPR CKMCNSTPVV
KHSVQFFLDL PKIEEKLKAY NATVEKGWSS VARVVSKSWL RDGLKPRCIT RDLKWGIPVP
VEGFENKVFY VWFDAPFGYI SITKRYTKEY QKWWQPPQDV KVDLCQFMAK DNVPFHTVMF
PACLLAVNQN YTLMKYLMAT EYLNYEDKKF SKSRGIGVFG TDARDTGISA DVWRFYLAYI
RPETQDSNFN WVDLATKNNS ELLNNLGNFV NRALVFAEKF FNSSIPPIEL AEEADWSVLA
LAQRELSSYI NAMEHAKLRD GLKHILAISK HGNQYMQFQQ PWVKIKGTED DKKRAGTVVA
VCCNLACLLS ALLAPFMPTT SKQLRSQLGL SNKSYGYIPE TITNILPTWH KIGKPSPLFT
KIEDQSVEVL RKKYAGQQEV NGEVSTTNKA PDDGIASLET AITKQGTLVR ELKAKHDKSV
WQPQVAILLD LKKKLADLKG NVNVPEKKLP AKKTPAKNKK AEPTQVLEQN GDALTDVAAL
ESAIAKQGNL VRELKAKEEA SVWKPQVEIL LKLKQRLMGL TGTTTPNATD KKSKKKK
//
