ID   SYC_AZOBR               Reviewed;         448 AA.
AC   O07045;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
GN   Name=cysS;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=9608743; DOI=10.1007/s002849900317;
RA   Zimmer W., Wesche M., Timmermans L.;
RT   "Identification and isolation of the indole-3-pyruvate decarboxylase gene
RT   from Azospirillum brasilense Sp7: sequencing and functional analysis of the
RT   gene locus.";
RL   Curr. Microbiol. 36:327-331(1998).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA   Bairoch A.;
RL   Unpublished observations (APR-1998).
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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; X99587; CAA67901.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; O07045; -.
DR   SMR; O07045; -.
DR   PRIDE; O07045; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..448
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159341"
FT   REGION          79..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           31..41
FT                   /note="'HIGH' region"
FT   MOTIF           265..269
FT                   /note="'KMSKS' region"
FT   COMPBIAS        79..95
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:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        246..276
FT                   /note="EPLARYWVHQRLRDRRGARRMSKSLGNLLHR -> SRWPATGSTNGFVTVEG
FT                   REGCPSRWATFFTG (in Ref. 1; CAA67901)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  49574 MW;  45203E2255D5E1D1 CRC64;
     MPLDLYNTLT RRKERFEPMT PDRVGMYVCG PTVYDTAHIG NARPVVFDLL FRLLRRLYPA
     VTYVRNITAS DDKIIDRRAT TGADRGADQA HRGPLPRRHG PLNAAPTIEP RATHHISHMV
     ALIGLLIEPA TPTPRKGTCC SPCRRWRSTG QLSRRSLDEM IAGARVEVAP YKRDSSDFVL
     WKPSTDGQPG WDSPWGRGRP GWHIECSAMA KEHLGVTFDI HGGGLDLILP DHENEIAQSR
     CAHAGEPLAR YWVHQRLRDR RGARRMSKSL GNLLHRGTSC WTEFPGGGHP LGVRPYRSRG
     LPEAEESKAT LDRWYQALRG DPAPAQAELP FDVLAALEDD LNSPLAISHL HELASAVNKA
     TGEAEKAAAK GRCRSAERWA APETRSVVPL GAEGAAALSD ADIQQRIEDR SAARKAKNYA
     EADRIRKELA DLGIVLEDGP QGTTWKRA