ID A0A3B4V8E3_SERDU Unreviewed; 920 AA.
AC A0A3B4V8E3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000026300.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000026300.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 41447.ENSSDUP00000026326; -.
DR Ensembl; ENSSDUT00000026771.1; ENSSDUP00000026300.1; ENSSDUG00000019070.1.
DR Ensembl; ENSSDUT00000026797.1; ENSSDUP00000026326.1; ENSSDUG00000019070.1.
DR GeneTree; ENSGT00550000075017; -.
DR OMA; HLNTTEY; -.
DR Proteomes; UP000261420; Unplaced.
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; cd00570; GST_N_family; 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; 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; IPR036249; Thioredoxin-like_sf.
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; PF14497; GST_C_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 SUPFAM; SSF52833; Thioredoxin-like; 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 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 72..206
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 860..916
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 103002 MW; 1FB42D90518597D0 CRC64;
MKLFVSEGNP HCLKVLAALE VTGVQCDVQY VNHEETVVPF LSRPALPAMF LPSGLYLFSA
NAICQYLFEV NGQESSELCS QWLEWEATDL QPALLLALHM AVLQGKGSQV SNVLQGPLNY
LDQSLSKGNT PYLTGEAVSV ADVVLWAALY PVLSDSSLAL GERKSVKPWF DRVAAMHSCQ
SAVQKVLRGK GLQGMKSYMQ RQPAPQSSQC RDTQPCNSNP AECEEGERVV SEEEMEAAVL
TWSKDLNGGP LATERQHPIL PQEGKRNILL TSALPYVNNV PHLGNIIGCV LSADVFSRYG
RLRGWNLLFV CGTDEYGTAT ENKAREEGLT PQQICDKYHA IHSSIYKWFQ IDFDFFGRTT
TEKQTEIAQN IFWRLHKHEF LVEDTVEQLR CENCQRFLAD RFVEGICPHC SYPEARGDQC
DKCGRLINAV ELREPQCKVC RQTPVIRSSK HLFLDLPKLE TQLEQWLDKS TSTGDWTVNA
KQITRSWLRD GLKPRCITRD LQWGTPVPHP DFKEKVFYVW FDAPIGYLSI TANYTDKWEK
WWKNPQQVEL YNFMAKDNVP FHSVVFPCSL LGAQDNYTLV NHLVATEYLN YEDTKFSKSR
GVGVFGDMAK DTGIPADVWR FYLLYVRPEG QDSAFSWADM ALKNNSELLN NLGNFINRAG
MFVTKFFEGC VPAMELQQED KKLLALVGWE LQQYIQLMDK VKIRDALKHI LNISRHGNQY
IQVNEPWKKI KGGDTERQRA GTVTGVSVNI ACLLSVMLLP YMPTVSQTIR DQLNAPQSCI
NTMLQGTGTF VCTLRAGHRI GTVSPLFQKL EVDQIEALKK RFGGQQTTAQ SAASAQPAAV
PAPAAPAAEV ATVNGVDPEK AKQLTQAVAE QGDKVRALKA QKAEKAVITA EVAKLLDLKK
QLAVAEGKNP EPAPQKSKKK
//
