ID I0JZL6_METFB Unreviewed; 468 AA.
AC I0JZL6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:CCG92685.1};
GN ORFNames=MFUM_720052 {ECO:0000313|EMBL:CCG92685.1};
OS Methylacidiphilum fumariolicum (strain SolV).
OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX NCBI_TaxID=1156937 {ECO:0000313|EMBL:CCG92685.1, ECO:0000313|Proteomes:UP000004837};
RN [1] {ECO:0000313|EMBL:CCG92685.1, ECO:0000313|Proteomes:UP000004837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolV {ECO:0000313|EMBL:CCG92685.1,
RC ECO:0000313|Proteomes:UP000004837};
RX PubMed=22740660; DOI=10.1128/JB.00501-12;
RA Khadem A.F., Wieczorek A.S., Pol A., Vuilleumier S., Harhangi H.R.,
RA Dunfield P.F., Kalyuzhnaya M.G., Murrell J.C., Francoijs K.-J.,
RA Stunnenberg H.G., Stein L.Y., DiSpirito A.A., Semrau J.D., Lajus A.,
RA Medigue C., Klotz M.G., Jetten M.S.M., Op den Camp H.J.M.;
RT "Draft Genome Sequence of the Volcano-Inhabiting Thermoacidophilic
RT Methanotroph Methylacidiphilum fumariolicum Strain SolV.";
RL J. Bacteriol. 194:3729-3730(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; 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:CCG92685.1}.
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DR EMBL; CAHT01000080; CCG92685.1; -; Genomic_DNA.
DR RefSeq; WP_009060681.1; NZ_CAHT01000080.1.
DR AlphaFoldDB; I0JZL6; -.
DR STRING; 1156937.GCA_000953475_01793; -.
DR eggNOG; COG0215; Bacteria.
DR InParanoid; I0JZL6; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000004837; 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 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:UP000004837};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT DOMAIN 24..325
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT DOMAIN 362..393
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|Pfam:PF09190"
FT MOTIF 38..48
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT MOTIF 277..281
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ SEQUENCE 468 AA; 54494 MW; 64AC8BA7F4580AD4 CRC64;
MKFSFPLPPF RLYNTISRKL EPIEPINPPH VTMYACGPTV YNLAHIGNFR TFLCVDLLRR
ALELFGYKVI HTMNYTDIDD KTIAASRAAG LSLAEYTQKY IDAFEQDMQT LNMLKPHFQP
KATEHIEKMI EFIRQLIDKN HAYIGEDGSV YFRIASFPDY GKLSHLEKDK LKPGSHILAD
EYIKEHYGDF ALWKAKKPED GDVGWISPWE IGRPGWHIEC STMSICYLGN EIDIHCGGVD
LIFPHHENEI AQSESVTGQN FVRHWFHVAH VLVEGEKMSK SLGNIYTIRD ILERGFNERT
LRYHLLTASH YRQTLNFTWQ GMEASREAVK RIDQWLSRIQ SLPKSQFQLQ EYEEETRFLR
CFVEALADDL NITEAIGHLF DWIRHTNRMM DKGEPLPPLQ RSWHLVDSIL GIGEFSVEIP
PEIQTLLQMR SEARKNKDWA TSDRIRQQLQ QMGWIVQDTP EGQKAWKA
//
