SYK2_METAC
ID SYK2_METAC Reviewed; 511 AA.
AC Q8TSN5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Lysine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00252};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252};
DE AltName: Full=Lysyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00252};
DE Short=LysRS 2 {ECO:0000255|HAMAP-Rule:MF_00252};
GN Name=lysS2 {ECO:0000255|HAMAP-Rule:MF_00252}; OrderedLocusNames=MA_0760;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00252};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00252};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00252};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00252}.
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DR EMBL; AE010299; AAM04200.1; -; Genomic_DNA.
DR RefSeq; WP_011020805.1; NC_003552.1.
DR AlphaFoldDB; Q8TSN5; -.
DR SMR; Q8TSN5; -.
DR STRING; 188937.MA_0760; -.
DR EnsemblBacteria; AAM04200; AAM04200; MA_0760.
DR GeneID; 1472652; -.
DR KEGG; mac:MA_0760; -.
DR HOGENOM; CLU_008255_6_0_2; -.
DR InParanoid; Q8TSN5; -.
DR OMA; EIFGEKC; -.
DR OrthoDB; 16292at2157; -.
DR PhylomeDB; Q8TSN5; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00775; LysRS_core; 1.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..511
FT /note="Lysine--tRNA ligase 2"
FT /id="PRO_0000152711"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 421
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
SQ SEQUENCE 511 AA; 58811 MW; 2478F0DA2479926F CRC64;
MTMEINNTDP SENMPLPDDV DLSGSRAFDD SKLAKLNGII SQGLDPYPYR FEKNGDICEI
LVKFEDFEKN EGLSVRTAGR LYNIRKHGKM IFADLGDQTG RIQVLIRKGN LPDEEFATFK
NLMDSGDIIG IQGELFRTKR GENSISVSEF SLLSKSLCAL PEKFHGLKDV ETRYRKRYLD
LIVNAEKREI FVMRSKLISE IRRFLADREF LEFETPILQT VYGGANARPF KTFHNCLGQN
LFLRIAPELY LKRLVVGGYE KVFEISKNFR NEDIDTTHNP EFTMIEVYEA YRDYNDMMDL
TEALISELVF RLTGGYEVKM GENTINLRSP WKRISMEGAL KEYAGLDVFS HSLEELKQIA
IQNRIEDYEK AKSHGEFLAL LFEGLVEDKL VNPTFIYDFP VENSPLAKNH REKEGFVERF
ELFLNGWELA NGYSELNDPL EQEKRFEEQD KKRKLGDLEA QTVDYDFINA LGYGLPPTGG
MGLGIDRLTM ILAGLESIKE VILFPQMKRE D
