ID A0A1S3LES7_SALSA Unreviewed; 1021 AA.
AC A0A1S3LES7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Name=mars {ECO:0000313|RefSeq:XP_013989462.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013989462.1};
RN [1] {ECO:0000313|RefSeq:XP_013989462.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_013989462.1; XM_014133987.1.
DR AlphaFoldDB; A0A1S3LES7; -.
DR STRING; 8030.ENSSSAP00000044732; -.
DR KEGG; sasa:106566135; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
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; 2.
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; 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; IPR004045; Glutathione_S-Trfase_N.
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; PF18485; GST_N_5; 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 SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 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:UP000087266}.
FT DOMAIN 1..75
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 72..201
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 877..933
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 961..1017
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT REGION 203..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 113521 MW; 9D708630C170C74C CRC64;
MKLFVSDGNP HCVKVLAVLE FTGVKCDVKH VNHEERVVPY LSRPALPALL LPSGTYLFSP
NSICQYLIEV NGQESSDIVN QWLEWEATEL QPAVMQALHM VVLQGKGAQT TRVLQGPLSY
LDQSLSKRTT LFLTAEMVSV ADVVLWAALY PILSDSSLVS GNQTELQHWF ERVGMLAACG
SAAQTALHGK GLKAESLKTY LQRQPSTHHG QGQVQGRGSQ PCNSPEGDDD GDCVLSEEEI
QSFAVTWGKG LADLPMVPER QHPILPVEGK RNVLVTSALP YVNNVPHLGN IIGCVLSADV
FARYGRLRGW NVLYVCGTDE YGTATENKAR EEGLTAQQIC DKYHAVHASI YQWFQVDFDF
FGRTTTKKQT EIAQNIFWRL HERGFLLEDI VEQLRCEACQ RFLADRFVEG TCPYCSYPEA
RGDQCDKCGK LINAVELREP TCKVCSQTPV VQSSKHLFLD LPKLEAELEQ WLEKSTGSGD
WTANAKQITR SWVRDGLKPR CITRDLKWGT PVPHPDFSDK VFYVWFDAPI GYLSITANYT
DQWEMWWKNP QQVELYNFMA KDNVPFHSVV FPCSLLGAQD NYTLVNHLVA TEYLNYEDTK
FSKSRGVGVF GDMAKDTGIP SDVWRFYLLY LRPEGQDSAF SWVDMATKNN SELLNNLGNF
INRAGMFVSK FFESYVPAMD LQQEDKRLLA QVGWELKQYM NLMDRVKIRD ALKCILNISR
HGNQYIQVNE PWKKIKGDET DRQRSGTVTG VSVNVACLLS VMLQPYMPTV SQTICQQLNA
PPTVTGTMLQ GTGNFVCSLP AGHHIGTVSP LFQKLEAEQI ESLKKRFGGQ QPEEEEEEAK
PKKPKTAAQT DVNAQPAPSP ASHPAAQTAV NGADAERARE LTLAVAEQGE KVRTLKGQKA
EKAVIGAEVT KLLELKKQLS LAEGKHPEPV LIKGKKNAQP APSPASHPAA QTAVNGADAE
RARELTLAVA EQGEKVRTLK GQKAEKAVIG AEVTKLLELK KQLSLAEGKH PEPVLIKGKK
K
//
