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Database: UniProt
Entry: H0J0M0_9GAMM
LinkDB: H0J0M0_9GAMM
Original site: H0J0M0_9GAMM 
ID   H0J0M0_9GAMM            Unreviewed;       482 AA.
AC   H0J0M0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   ORFNames=MOY_05876 {ECO:0000313|EMBL:EHK61552.1};
OS   Halomonas sp. GFAJ-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK61552.1, ECO:0000313|Proteomes:UP000004512};
RN   [1] {ECO:0000313|EMBL:EHK61552.1, ECO:0000313|Proteomes:UP000004512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61552.1,
RC   ECO:0000313|Proteomes:UP000004512};
RX   PubMed=22408239; DOI=10.1128/JB.06664-11;
RA   Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT   "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL   J. Bacteriol. 194:1835-1836(2012).
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         Evidence={ECO:0000256|ARBA:ARBA00001080, 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|ARBA:ARBA00004496,
CC       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:EHK61552.1}.
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DR   EMBL; AHBC01000022; EHK61552.1; -; Genomic_DNA.
DR   RefSeq; WP_009097575.1; NZ_CP016490.1.
DR   AlphaFoldDB; H0J0M0; -.
DR   STRING; 1118153.MOY_05876; -.
DR   KEGG; hag:BB497_13060; -.
DR   PATRIC; fig|1118153.6.peg.1185; -.
DR   eggNOG; COG0215; Bacteria.
DR   OrthoDB; 9815130at2; -.
DR   Proteomes; UP000004512; 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; cd07963; Anticodon_Ia_Cys; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000004512};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT   DOMAIN          358..419
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|SMART:SM00840"
FT   MOTIF           29..39
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOTIF           265..269
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   482 AA;  53913 MW;  02FAF7DD3C31EEAC CRC64;
     MQIYNTLTRR KEPFTPLVAG KVSMYVCGMT VYDYCHLGHA RVMVAFDVIT RYLRHRGYDV
     TYVRNITDID DKILKRADEN GETISALTER MIDAMHDDEA RLNVLPPSRE PRATGHIGDI
     IAMIETLIDK GFAYPAKNGD VYYRVRKFAN YGKLNNRQLD DMRSGARVDV DVHKEDPLDF
     VLWKAAKPTE AHWPSPWGDG RPGWHIECSA MSTCCLGDTF DIHGGGPDLT FPHHENEIAQ
     SEAATGKTYV NTWMHAGAVR VNQEKMSKSL GNFFTIRDVL AEHDPEVVRY LLVASHYRSA
     INYSVDSLVE ARKSLTRFYT ALEGVEVQES VGEELQQAPT SEVAFIASKE EVAAYSERFT
     TAMDDDFNTP EALAVLFDLA REVNRAKGES PQKALLLALE LKRLASVLGL LQQSPDTFLK
     GAQQHGVALS ETEIEAKIAQ RKEAKASKDF AQADAIRDEL AALGIILKDS REGTTWVIEA
     PQ
//
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