SYC_MYCPN
ID SYC_MYCPN Reviewed; 437 AA.
AC P75423;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=cysS; OrderedLocusNames=MPN_356; ORFNames=MP480;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; U00089; AAB96128.1; -; Genomic_DNA.
DR PIR; S73806; S73806.
DR RefSeq; NP_110044.1; NC_000912.1.
DR RefSeq; WP_010874712.1; NC_000912.1.
DR AlphaFoldDB; P75423; -.
DR SMR; P75423; -.
DR STRING; 272634.MPN_356; -.
DR EnsemblBacteria; AAB96128; AAB96128; MPN_356.
DR KEGG; mpn:MPN_356; -.
DR PATRIC; fig|272634.6.peg.383; -.
DR HOGENOM; CLU_013528_0_0_14; -.
DR OMA; GWHAECA; -.
DR BioCyc; MPNE272634:G1GJ3-559-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..437
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159433"
FT MOTIF 33..43
FT /note="'HIGH' region"
FT MOTIF 262..266
FT /note="'KMSKS' region"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 50665 MW; A94BE766B9A948BD CRC64;
MNQFEPKFTL IDTVSNQSVV LEQKQINIYL CGPTVYNDLH LGNTRPLIVF DVLQRVLQAA
QYKVQFVQNI TDIDDKIIKI AQQQEISEAQ LCKQQITAYK SLLKKLNILP IKHLQVTDKI
DKMPGYIARL VKKGFAYVSP LGNTYFSVSQ LPQYGILANR VVETIEDEAT DKRNKLDFVL
WKQTTAGVKW NSPWGWGRPG WHVECAFLID YSFKDQLTIH GGGVDLKFPH HENENAMHMA
LYDKPLTQHW MHIGHLMFEN QKMSKSLQNF LLAVDFLTIH DFRILRWLFY QKHYYHPLDL
SQSLIEQACS DIKRIQKAVN VCRTWFVYSE QSAIPAPKQF EPVFKALLNN LNFANAITHI
WKLVKQINHD VSKQNLSGLK EHLSHLEWAL NILGIGFKSI HTKLNVQLIK KWASLRKNGQ
LDKADEVRQK LIKKGLL