SYC_HALSA
ID SYC_HALSA Reviewed; 494 AA.
AC Q9HQL9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; OrderedLocusNames=VNG_1097G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=12810913; DOI=10.1261/rna.5320603;
RA Evilia C., Ming X., DasSarma S., Hou Y.M.;
RT "Aminoacylation of an unusual tRNA(Cys) from an extreme halophile.";
RL RNA 9:794-801(2003).
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, ECO:0000269|PubMed:12810913};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.39 uM for tRNA(Cys) {ECO:0000269|PubMed:12810913};
CC Note=The catalytic activity of the enzyme increases with increasing
CC salt concentrations and has its maximum at 3 M potassium chloride.;
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; AE004437; AAG19494.1; -; Genomic_DNA.
DR PIR; B84266; B84266.
DR RefSeq; WP_010902789.1; NC_002607.1.
DR AlphaFoldDB; Q9HQL9; -.
DR SMR; Q9HQL9; -.
DR STRING; 64091.VNG_1097G; -.
DR PaxDb; Q9HQL9; -.
DR EnsemblBacteria; AAG19494; AAG19494; VNG_1097G.
DR GeneID; 5952831; -.
DR KEGG; hal:VNG_1097G; -.
DR PATRIC; fig|64091.14.peg.840; -.
DR HOGENOM; CLU_013528_0_1_2; -.
DR InParanoid; Q9HQL9; -.
DR OMA; AKYWMHN; -.
DR OrthoDB; 20883at2157; -.
DR PhylomeDB; Q9HQL9; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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; 1.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..494
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159535"
FT REGION 187..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..41
FT /note="'HIGH' region"
FT MOTIF 287..291
FT /note="'KMSKS' region"
FT COMPBIAS 194..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 494 AA; 54035 MW; 2EBEB9461A557D87 CRC64;
MTQYVSNTRS GEQEAFEPDD PENVLVYTCG LTVSDDAHLG HARLWVQSDV MTRWLSHAGY
GVRHVQNVTD VNEKIVARVG ADGLGDTEAA VAAHYTQSVI DDMRALNLAR ADVYPRVSEH
VPEIIDLIGD LVDAGYAYEA GGSVYFDVRR FEEYGALSGQ QVDELDPQGP DAEQAEKRHP
ADFALWKAGG VSPDDANTHR DDELPPLDGE RGQTWASPWG EGRPGWHIEC SAMAMTHLDD
HIDIHVGGQD LVFPHHENEI AQSEAASGER FADHWLHVRL LETDGEKMSS SLGNFFTVSN
AVAERGPNVV RMLLVSTSYT QRQTYSEATV SEATQRWERL QRAHERAADA IDSVAAHAKP
ADDALRTAVA DARGEFAAAM RADFNTRAAV SALLELASAV NRHVDGTDTY DYQGLHDAVD
AFETLGGDVL GLQFDDGAGE DAVSLADDVI DLVLDVREQE RTAGNYERAD DLRDRLEALG
VSVEDTDDGA TVRR
