ID R1HY03_9PSEU Unreviewed; 435 AA.
AC R1HY03;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041,
GN ECO:0000313|EMBL:EOD63149.1};
GN ORFNames=H480_38605 {ECO:0000313|EMBL:EOD63149.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD63149.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD63149.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD63149.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOD63149.1}.
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DR EMBL; AOUO01000655; EOD63149.1; -; Genomic_DNA.
DR AlphaFoldDB; R1HY03; -.
DR PATRIC; fig|1292037.4.peg.7247; -.
DR eggNOG; COG0215; Bacteria.
DR Proteomes; UP000014139; Unassembled WGS sequence.
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; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00041};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT DOMAIN 310..371
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
FT REGION 130..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..14
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT MOTIF 236..240
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 2
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ SEQUENCE 435 AA; 47921 MW; 8D87A09E976A26FE CRC64;
MCGATVQGVP HIGHVRGALN YDVLRRWLVH NGLDVLLVRN VTDIDDKILT KAAAADRPWW
EWAATHERAF EEAYEQLGCL PPSITPRATG HITQMVELMQ RLIDRGHAYA VDGDVYFSVK
SFDEYGKLSG QGLDDVQQGE TPTRGKQDPR DFTLWKSAKP GEPSWPTPWG DGRPGWHLEC
SAMATTYLGP EFDIHGGGID LRFPHHENER AQSNAAGDPF ARYWLHNAWV TMSGEKMSKS
LGNTVTIPAM LERYRAAELR YYLVQPHYRS NIEYSDAAVS EAAQGYRRIE TFLRRAAQSG
EVTLGTIPAE FAAALDDDLA TPQAFAVVHN TVRDGNAAFD AGDTPKALEL AAAVRAMTDV
LGLDPLSARW SEAGGSDTPT QEALARIVEG LLAERQQARA EKDFARADAA RDRLSQAGIV
VEDTPNGPQW TVKSD
//
