SYC_RHOBA
ID SYC_RHOBA Reviewed; 537 AA.
AC Q7US70;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=RB4675;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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; 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-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 family.
CC {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- CAUTION: The Arg residue that is thought to bind ATP in this protein is
CC missing; it probably binds ATP elsewhere. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD73927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294140; CAD73927.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_866241.1; NC_005027.1.
DR AlphaFoldDB; Q7US70; -.
DR SMR; Q7US70; -.
DR STRING; 243090.RB4675; -.
DR EnsemblBacteria; CAD73927; CAD73927; RB4675.
DR KEGG; rba:RB4675; -.
DR PATRIC; fig|243090.15.peg.2196; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_0; -.
DR InParanoid; Q7US70; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
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;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..537
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159466"
FT REGION 171..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 537 AA; 58486 MW; 8487F55CF6BFEA8C CRC64;
MTAADPTASV ASPSSAQPAI RVYNTLSKTK EPFLPLRAPR VGMYLCGPTV YAESHIGHMV
GPVIFDTIKR YLTYSGYEVT WVVNITDVDD KLIGKSKERG IPMSQIAVEM TADYLANLRE
LGVNQIDHLP RATDHMPQII AFIGSLESKG FAYAIDGDVF FDVTKDPGYG QLSNRSVEDQ
QGEGGGAAAK KRNPGDFALW KSARPGEPFW DSPWGEGRPG WHIECSAMSH EILGETFDIH
GGGLDLMFPH HENERAQSTC CHGAPMVKYW MHNGLMRAGE KGKVGGKSDR ENAAAEAASV
EEQASGKISR SKGAGGLADL IRSQTGERIR FFLLRTQYRS TIVYNEETLA EAGTSLEAFY
RYFDRFAEIT GDSFYDLSAA TRRADGGFDP AGDALLTEIH AIREKFLAAM DDDFNTGAAI
SVLFDALRTL NRHIDANQLA AGADAKSPAV ESLVKATSVI AELSRVLGLF AKPPATSGGD
EADAELLDSV VHLLINLRKE ARERKDYATG DAIRDRLADL GVALLDKKEG TSWERKS
