SYC_BORBU
ID SYC_BORBU Reviewed; 480 AA.
AC O51545;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=cysS; OrderedLocusNames=BB_0599;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000783; AAC66952.1; -; Genomic_DNA.
DR PIR; F70174; F70174.
DR RefSeq; NP_212733.1; NC_001318.1.
DR RefSeq; WP_002662611.1; NC_001318.1.
DR PDB; 3SP1; X-ray; 2.55 A; A/B=1-480.
DR PDBsum; 3SP1; -.
DR AlphaFoldDB; O51545; -.
DR SMR; O51545; -.
DR STRING; 224326.BB_0599; -.
DR PRIDE; O51545; -.
DR EnsemblBacteria; AAC66952; AAC66952; BB_0599.
DR KEGG; bbu:BB_0599; -.
DR PATRIC; fig|224326.49.peg.990; -.
DR HOGENOM; CLU_013528_0_1_12; -.
DR OMA; AKYWMHN; -.
DR Proteomes; UP000001807; 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; 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; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..480
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159359"
FT MOTIF 29..39
FT /note="'HIGH' region"
FT MOTIF 278..282
FT /note="'KMSKS' region"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3SP1"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 37..56
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3SP1"
FT TURN 158..164
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:3SP1"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3SP1"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 319..341
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:3SP1"
FT HELIX 451..463
FT /evidence="ECO:0007829|PDB:3SP1"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:3SP1"
SQ SEQUENCE 480 AA; 56022 MW; 8C689854C8AFA60F CRC64;
MILKLYNTRT KDFSELTNFE NVKVYACGPT VYNYAHIGNF RTYIFGDLLI KTLRFLGYKV
NYAMNITDIG HLTGDLDDGE DKVAKTAREK GLTVYEISEF FTEAFFNDCR KLNIVYPDKV
LVASKHIPIM IEVVKILEEK KITYFSNGNV YFDTSCFKSY GEMAGIDLID KDMTLPRVDV
DKFKRNKTDF VLWFTNSKFK DQEMKWDSPW GFGYPSWHLE CAAMNLEYFK DALDIHLGGV
DHIGVHHINE IAIAECFLNK KWCDVFVHGE FLIMDYNKMS KSRGNFITVK DLEDQNFSPL
DFRYLCLTSH YRNQLKFSLD NLQASKIARE NLINKLSYFY ESLDPVDLNT LNKDLKNFGF
SVEKEYYDSF VEKISFDLNV AQGLALLWEI IKSDNLSFVS KLRLAFIFDE IMSLNLREEI
LKNLQNHDVV IDENMKALIE ERRIAKCEKN FKRADEIRDF FAKKGFVLVD TKEGTKVKRG
