SYC_PHOV8
ID SYC_PHOV8 Reviewed; 493 AA.
AC A6KZ38;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BVU_1009;
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(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-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}.
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DR EMBL; CP000139; ABR38702.1; -; Genomic_DNA.
DR RefSeq; WP_011965001.1; NC_009614.1.
DR AlphaFoldDB; A6KZ38; -.
DR SMR; A6KZ38; -.
DR STRING; 435590.BVU_1009; -.
DR EnsemblBacteria; ABR38702; ABR38702; BVU_1009.
DR KEGG; bvu:BVU_1009; -.
DR PATRIC; fig|435590.9.peg.1042; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_10; -.
DR OMA; AKYWMHN; -.
DR OrthoDB; 952207at2; -.
DR BioCyc; BVUL435590:G1G59-1054-MON; -.
DR Proteomes; UP000002861; 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;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..493
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000332791"
FT MOTIF 33..43
FT /note="'HIGH' region"
FT MOTIF 283..287
FT /note="'KMSKS' region"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 493 AA; 56316 MW; C25A66D9B79A8B09 CRC64;
MENKLTIYNT LSRQKELFVP LHAPHVGMYV CGPTVYGDAH LGHARPAITF DILFRYLTHL
GYKVRYVRNI TDVGHLEHDA DEGEDKIAKK ARLEQLEPME VVQYYLNRYH KAMEALNVLP
PSIEPHASGH IIEQIELVEE ILKNGYAYES EGSVYFDVAK YNKDHHYGKL SGRNLDDVLN
TTRELDGQSE KRNPADFALW KCAQPEHIMR WPSPWSNGFP GWHCECTAMG KKYLGEHFDI
HGGGMDLIFP HHECEIAQSV ASQGDDMVHY WMHNNMITIN GQKMGKSYGN FINLDEFFHG
THKLLTQAYS PMTIRFFILQ AHYRSTVDFS NEALQAAEKG LERLTEAVKG LERITPATQT
TGIEGVKDLR EKCYTAMNDD LNSPIVIAHL FDGARMINTV LDKKATISAE DLEELKSMFH
LFMYEILGLK EEAANNEAHE EAYGKVVDML LEQRMKAKAN KDWATSDKIR DELAALGFEV
KDTKDGFTWK LNK
