SYC_MESH7
ID SYC_MESH7 Reviewed; 406 AA.
AC Q4A786;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000255|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000255|HAMAP-Rule:MF_00041};
GN OrderedLocusNames=MHP7448_0641;
OS Mesomycoplasma hyopneumoniae (strain 7448) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=262722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7448;
RX PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00041}.
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DR EMBL; AE017244; AAZ54003.2; -; Genomic_DNA.
DR AlphaFoldDB; Q4A786; -.
DR SMR; Q4A786; -.
DR EnsemblBacteria; AAZ54003; AAZ54003; MHP7448_0641.
DR KEGG; mhp:MHP7448_0641; -.
DR HOGENOM; CLU_013528_0_0_14; -.
DR OMA; GWHAECA; -.
DR Proteomes; UP000000553; 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 Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
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 PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..406
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000332859"
FT MOTIF 18..28
FT /note="'HIGH' region"
FT MOTIF 250..254
FT /note="'KMSKS' region"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 406 AA; 47723 MW; 756DECC5375D5F76 CRC64;
MTMNLINKKN LNIYLCGPTV YSDVHIGNLR TIIIFDAIFE CLKNKGFSIN FLHNITDIDD
KIIEKAQELG ISEAELTEKY TNEYFKILEI FNIKKPTKIV RVTEKIEKII EYIKLLEKKG
FTYYNKNNDL VFDILKIPNY GIISGQKIES LLDKNTKKTK SNNDFVLWKK TQKGLFFKSL
FGLGRPGWHT ECAALIYDYF QKKSLDLHGG GVDLIFPHHE NENAQHFALT GNPIAENWFR
SGFVNLNGKK MAKSLNNVLL AKDFSHKYNP DIIRSIFLSI NPTVPINLTE ELIKNHKKLI
EKYQKICFEW YFDKKNEKTE KVEQVLNLFI EGKFAKANFL IMELIKQKEN STIRKIFLNL
RFNFTKMRLD PESQEKIKNW NKLIMDKNYS EADKIREELW KIFKNS
