AC   MF_00041;
DC   Protein; auto
TR   HAMAP; MF_00041; -; 1; level=0
XX
Names: Cys_tRNA_synth
XX
ID   SYC
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
GN   Name=cysS;
XX
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;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
end case
case <OC:Bacteria>
CC   -!- SUBUNIT: Monomer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF01406; tRNA-synt_1e; 1; trigger=no
DR   PRINTS; PR00983; TRNASYNTHCYS; 1; trigger=no
DR   NCBIfam; TIGR00435; CysS; 1; trigger=no
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
case <FT:8>
KW   Phosphoprotein
end case
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004817; F:cysteine-tRNA ligase activity
GO   GO:0006423; P:cysteinyl-tRNA aminoacylation
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYC_ECOLI (P21888)
FT   MOTIF           30..40
FT                   /note="'HIGH' region"
FT   Condition: x-T-x(5)-H-[LIVFA]-G-[HN]
FT   MOTIF           266..270
FT                   /note="'KMSKS' region"
FT   Condition: [KR]-M-[GSA]-[KS]-S
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: E
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [KS]
FT   From: SYC_BACSU (Q06752)
case <OC:Bacillaceae>
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT   Condition: S
end case
XX
Size: 404-546;
Related: None;
Template: P21888;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BURL3, PHOPR, TROW8, TROWT
Plasmid: None
Comments: Atypical sequence in STRCO that contains a weird additional N-terminal
 domain constituted of multiple repeats; not taken into account in size range
 For archeal missing cysS see:
 MEDLINE=99412295; PubMed=10482537;
 Hamann C.S., Sowers K.R., Lipman R.S., Hou Y.M.;
 "An archaeal aminoacyl-tRNA synthetase missing from genomic analysis.";
 J. Bacteriol. 181:5880-5884(1999).
 MEDLINE=20086427; PubMed=10622715;
 Li T., Graham D.E., Stathopoulos C., Haney P.J., Kim H.S.,
 Vothknecht U., Kitabatake M., Hong K.W., Eggertsson G., Curnow A.W.,
 Lin W., Celic I., Whitman W., Soll D.;
 "Cysteinyl-tRNA formation: the last puzzle of aminoacyl-tRNA
 synthesis.";
 FEBS Lett. 462:302-306(1999).
XX
# Revision 1.40 2023/06/01
//