SYC_STRCO
ID SYC_STRCO Reviewed; 613 AA.
AC Q9L0Q6;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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}; Synonyms=cysS1;
GN OrderedLocusNames=SCO4235; ORFNames=SCD8A.08;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939119; CAB77329.1; -; Genomic_DNA.
DR RefSeq; NP_628409.1; NC_003888.3.
DR RefSeq; WP_011029523.1; NC_003888.3.
DR AlphaFoldDB; Q9L0Q6; -.
DR SMR; Q9L0Q6; -.
DR STRING; 100226.SCO4235; -.
DR GeneID; 1099675; -.
DR KEGG; sco:SCO4235; -.
DR PATRIC; fig|100226.15.peg.4297; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_11; -.
DR InParanoid; Q9L0Q6; -.
DR OMA; AKYWMHN; -.
DR PhylomeDB; Q9L0Q6; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
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; 2.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
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; Repeat; Zinc.
FT CHAIN 1..613
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159490"
FT REPEAT 36..49
FT /note="1"
FT REPEAT 50..63
FT /note="2"
FT REPEAT 64..77
FT /note="3"
FT REPEAT 78..91
FT /note="4"
FT REPEAT 92..105
FT /note="5"
FT REPEAT 106..119
FT /note="6"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..119
FT /note="6 X 14 AA tandem repeats of P-[TA]-R-G-D-K-K-R-A-
FT [RP]-R-[PL]-G-V"
FT REGION 148..613
FT /note="Cysteinyl-tRNA synthetase"
FT MOTIF 178..188
FT /note="'HIGH' region"
FT MOTIF 411..415
FT /note="'KMSKS' region"
FT COMPBIAS 43..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 613 AA; 67539 MW; 2224A3EA33AC6131 CRC64;
MSAGAGTPRR PAVRGSAPHP ARGSAPGPRP MPTHHPTRGD KKRARRPGVP TRGDKKRAPR
LGVPARGDKK RARRPGVPAR EDKKRAPRPG VPTRGDKKRA PRLGVPARGD KKRARRPGVP
TRGGVARSGN DGPRVPLALL GAYYPGHVTI RLYDTSARQI RDFAPLTPGC VSIYLCGATV
QAAPHIGHIR SGLNFDIMRR WFAYRGYDVT FVRNVTDIDD KIIRKAAEQN RPWWSIGYEN
ERAFNDAYAA LGCLPPTYEP RATGHITEMV EMMRGLIERG HAYEADGNVY FDVRSLPGYL
SLSNQDLDEL RQPSEDGETG KRDLRDFAMW KAAKPGEPSW ETPWGRGRPG WHLECSAMAH
KYLGEEFDIH GGGIDLIFPH HENEIAQAKG FGDAFARYWV HNAWVTMSGE KMSKSLGNSV
LVSEMVKKWP PVVLRYYLGT PHYRSTIEYS EESLREAESA YGRIEGFVQR VTELAGHAVE
PAAEVPPAFA EAMDDDLGVP QALAIVHTTV RQGNSALAAD DKDAAVARLA EVRAMLGVLG
LDPLDAQWAG AQAQGEDLRH VVDSLVRLVL DQREGARARK DWATADAIRD QLGQSGLVIE
DSPQGPRWSL GSR
