SYC_ALIB4
ID SYC_ALIB4 Reviewed; 467 AA.
AC A8ERE6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Abu_0245;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV66520.1; -; Genomic_DNA.
DR RefSeq; WP_012012109.1; NC_009850.1.
DR AlphaFoldDB; A8ERE6; -.
DR SMR; A8ERE6; -.
DR STRING; 367737.Abu_0245; -.
DR EnsemblBacteria; ABV66520; ABV66520; Abu_0245.
DR KEGG; abu:Abu_0245; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_7; -.
DR OMA; AKYWMHN; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000001136; 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 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; Zinc.
FT CHAIN 1..467
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000332786"
FT MOTIF 32..42
FT /note="'HIGH' region"
FT MOTIF 271..275
FT /note="'KMSKS' region"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 467 AA; 53425 MW; 38087A0920A24301 CRC64;
MNTLHIFDSV KKEKVEFKPI QEGKVKIYVC GPTVYDDSHL GHARSAIAFD LLHRVLKVND
YEVTMTKNFT DIDDKIIKKM YETNKTLENI TNQYINAYKA DMKALNILDN TIEPKATENL
EVMKEMISNL ISKDVAYKTS DSVYFDTSKD NLYGTLSHKS NDENSQARVE ENQEKRNSAD
FALWKFEKAN DVSFDAPFGK GRPGWHIECS AMIEKHLAYK DSPYQIDIHA GGADLLFPHH
ENEAAQTRCS SGQNLAKYWM HNGFVNINGE KMSKSLGNSF FLKDVLKSYS GEVIRFYLMS
THYRADLSFN EEDLIASKKR LDKIYRLKKR VYGIEDSSVN KKFKEDILNA LNDDINTSIA
LSVIDEMINS ANDKLDSNPK DKNLKKELIS NINFIEEVLG IGGNDAYAYF QFGINESTKE
KIESLILKRN EAKKTKDFQT ADKLRDELSS MDISLMDTVN GTVWEKL
