ID   D1CIB0_THET1            Unreviewed;       785 AA.
AC   D1CIB0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   10-JUN-2026, entry version 88.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   OrderedLocusNames=Tter_2592 {ECO:0000313|EMBL:ACZ43481.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / CCMEE 7001 / YNP1).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia;
OC   Candidatus Thermobaculales; Candidatus Thermobaculaceae; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ43481.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA   Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Cys) + L-cysteine + ATP = L-cysteinyl-tRNA(Cys) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661, Rhea:RHEA-
CC         COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78517, ChEBI:CHEBI:456215;
CC         EC=6.1.1.16; Evidence={ECO:0000256|ARBA:ARBA00047398,
CC         ECO:0000256|HAMAP-Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC       Rule:MF_00041}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00041}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001826; ACZ43481.1; -; Genomic_DNA.
DR   RefSeq; WP_012876512.1; NC_013526.1.
DR   AlphaFoldDB; D1CIB0; -.
DR   STRING; 525904.Tter_2592; -.
DR   KEGG; ttr:Tter_2592; -.
DR   eggNOG; COG0215; Bacteria.
DR   eggNOG; COG1216; Bacteria.
DR   HOGENOM; CLU_357121_0_0_0; -.
DR   OrthoDB; 135131at2; -.
DR   Proteomes; UP000000323; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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   NCBIfam; TIGR00435; cysS; 1.
DR   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00041};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00041};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00041};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00041};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00041};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00041}; Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT   DOMAIN          355..410
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|SMART:SM00840"
FT   REGION          747..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           29..39
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOTIF           275..279
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   COMPBIAS        776..785
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   785 AA;  90295 MW;  A317A2BF0D277457 CRC64;
     MRLYNTLTRR VEEVVPVEPG RIRMYTCGPT VYRYIHIGNL RSFCTADWIR RALLREGYEV
     IHVKNITDVG HMRQELLDQG EDKLEAEARR VGRTPGEIAE FYTRAFMRDE ARMNILPASV
     FPRATQHVGE MIEIVRELER QGYAYRAGGN VYFDVARLPQ YGQLSGNSLP ELTSSQEDAT
     ADKRSPLDFA LWKEAEPGRL MAWDSPWGRG FPGWHIECTA MAIKYLGTEI DIHTGGVDNI
     FPHHENERAQ SEAYVGHRWV RHWVHTQHLL TDGLKMSKSM SNDYTLDDIV ARGFEPLALR
     YLFTTAHYRT RLNFTFRALA GAQTSLRRLR MAALAARDEA VAPPDEEAMR PWREAFDRSL
     RDDLNLPAAM AVVWDVVRRS GLGPAERAAL LAEFDEVLGL DVFAEPDSGL LLEPRQDVRE
     LLALRAEVRA RGDYALADAL RSDLEARGVE LRDTRQGTRA YRLRINRLPH VFTSSAEVPS
     RVGEPDRYEW SVNLIARNNR EDLERCLRSL ARHLHGRSLE VVVVDSGSTD DTLGLMLELY
     HRGYWEEEGV RVPLKVLFAD HNIGFAASRN ATMRASEGWY VVWLDTSVEL AGDVWTPLEE
     ALADRSVGVA GPFGLVTEDL REFERTPGPD ADAMEGYLFA FRRALLEEVG LLDNEKFRFY
     RLADVYYSFF FKAAGLRVVV VPEVERRIIL HPHREWYSLL PEERQTKSKH NYDLFRARWH
     HGESLLVARD GQVERWLEHD HPRHVDADHF HPPEELPPPG VPHVHPHRHL PDHQHNHPHY
     HFQGD
//