(data stored in ACNUC7421 zone)

SWISSPROT: SYC_THEFY

ID   SYC_THEFY               Reviewed;         466 AA.
AC   Q47TG4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000255|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000255|HAMAP-Rule:MF_00041};
GN   OrderedLocusNames=Tfu_0212;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00041};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00041}.
DR   EMBL; CP000088; AAZ54250.1; -; Genomic_DNA.
DR   RefSeq; WP_011290659.1; NC_007333.1.
DR   SMR; Q47TG4; -.
DR   STRING; 269800.Tfu_0212; -.
DR   EnsemblBacteria; AAZ54250; AAZ54250; Tfu_0212.
DR   KEGG; tfu:Tfu_0212; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; TFUS269800:G1G4Q-216-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
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: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; 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; 1.
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.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TG4.
DR   SWISS-2DPAGE; Q47TG4.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN         1    466       Cysteine--tRNA ligase.
FT                                /FTId=PRO_0000240969.
FT   MOTIF        31     41       "HIGH" region.
FT   MOTIF       267    271       "KMSKS" region.
FT   METAL        29     29       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   METAL       211    211       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   METAL       236    236       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   METAL       240    240       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00041}.
SQ   SEQUENCE   466 AA;  52130 MW;  35B2E0734A511648 CRC64;
     MSLRFYDTRT RQVRDFVPLR EGCVSLYLCG ATVQAPPHIG HIRSGVSFDI LRRWLMYRGY
     RVIFCRNVTD IDDKILNVAA SEGVQWWEVS ERNYRAFAEA YDTLGCLPPT VEPRATGHIP
     EMIELMRRLI DRGHAYVAED GSGDVYFDVT SYAEYGSLSN QRLEEMRAAE DGDARAKRDP
     RDFALWKGAR PGEPSWPTPW GPGRPGWHLE CSAMATKYLG PTFDIHGGGV DLVFPHHENE
     SAQSRAAGDG FARYWLHNGL LTTGGEKMSK SLGNSLLIPE ITRRVRPVEL RYYLGQAHYR
     SNLDYSEESL REAASAYQRL ENFLVRVNEI AGPIPDDVPV PEEFAAALDD DLGVPQALAV
     AHNHVREGNS ALAEGAKERA AQIGARLRAM LAVLGLDPLS PQWAGSDDSG LHDVVDSLVS
     VVLEQRQEAR KRKDYATADR IRDQLAEMGI AVEDTPQGPR WELKRS
//

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