ID   SYC2_TROW8              Reviewed;         450 AA.
AC   Q83HQ8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=TW456;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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   -!- 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; BX251411; CAD67124.1; -; Genomic_DNA.
DR   RefSeq; WP_011096404.1; NC_004551.1.
DR   AlphaFoldDB; Q83HQ8; -.
DR   SMR; Q83HQ8; -.
DR   GeneID; 67388232; -.
DR   KEGG; tws:TW456; -.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OMA; HAWPASE; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 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; PTHR10890; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..450
FT                   /note="Putative cysteine--tRNA ligase 2"
FT                   /id="PRO_0000159513"
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