ID   SYC2_TROWT              Reviewed;         450 AA.
AC   Q83GH3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 116.
DE   RecName: Full=Putative cysteine--tRNA ligase 2;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase 2;
DE            Short=CysRS 2;
GN   Name=cysS2; OrderedLocusNames=TWT_316;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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;
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}.
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DR   EMBL; AE014184; AAO44413.1; -; Genomic_DNA.
DR   RefSeq; WP_011096404.1; NC_004572.3.
DR   AlphaFoldDB; Q83GH3; -.
DR   SMR; Q83GH3; -.
DR   STRING; 203267.TWT_316; -.
DR   GeneID; 67388232; -.
DR   KEGG; twh:TWT_316; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OrthoDB; 9815130at2; -.
DR   Proteomes; UP000002200; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:TreeGrafter.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:TreeGrafter.
DR   Gene3D; 1.20.120.640; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
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   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Putative cysteine--tRNA ligase 2"
FT                   /id="PRO_0000159515"
FT   REGION          372..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           29..39
FT                   /note="'HIGH' region"
FT   MOTIF           270..274
FT                   /note="'KMSKS' region"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  51274 MW;  2754844783A8B17D CRC64;
     MYTFEVFDSR TRSIVKLEDC LLRLYVCGIT PYKSTHLGHA FTYVGFDTLF RLALDSGRDV
     LYIQNISDID EPLFQYAEKV GIHYKDLART QTKRFFEDMH TLECLPPGYV IPVSKVLDGI
     KTGIEGLISR NMAYKLPNGD VYFDSTLTDP GKMFCFDRKT AMSLMLETDT GKNPFDPLLW
     RGRGAEPQWE ASFGAGRPAW HISCAVLSNL QTQYENVLHI YGGGRDLAFP HHEFTNVLSK
     LIRAPKDNKQ QDTVQDVFMH TGLVSYMGDK MSKSKGNLVF ISQLREQCEK IGLHHSVIRL
     ALLQRHYRED WEWQDECLDR AASRFRLWKS ALQEYIGAKG IRSTADQNKG TQGAWERIHG
     GVFDSNFDHR QPIHPKHSPQ MRDYSEHGSA GQNGTDLDLS LYQAIRFHLC NDLDTPKALD
     AVDSYARKGT ITIPEARAVE KLLGIPLTRV
//