ID SYC_ECOLI Reviewed; 461 AA. AC P21888; Q2MBQ3; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 2. DT 16-DEC-2008, entry version 88. DE RecName: Full=Cysteinyl-tRNA synthetase; DE EC=6.1.1.16; DE AltName: Full=Cysteine--tRNA ligase; DE Short=CysRS; GN Name=cysS; OrderedLocusNames=b0526, JW0515; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. RC STRAIN=K12; RX MEDLINE=91195046; PubMed=2014166; DOI=10.1093/nar/19.2.265; RA Eriani G., Dirheimer G., Gangloff J.; RT "Cysteinyl-tRNA synthetase: determination of the last E. coli RT aminoacyl-tRNA synthetase primary structure."; RL Nucleic Acids Res. 19:265-269(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91126117; PubMed=1992490; RA Hou Y.M., Shiba K., Mottes C., Schimmel P.; RT "Sequence determination and modeling of structural motifs for the RT smallest monomeric aminoacyl-tRNA synthetase."; RL Proc. Natl. Acad. Sci. U.S.A. 88:976-980(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=91323511; PubMed=1864365; DOI=10.1016/0014-5793(91)80968-9; RA Avalos J., Corrochano L.M., Brenner S.; RT "Cysteinyl-tRNA synthetase is a direct descendant of the first RT aminoacyl-tRNA synthetase."; RL FEBS Lett. 286:176-180(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP CRYSTALLIZATION. RX MEDLINE=99234356; PubMed=10216301; DOI=10.1107/S0907444999001468; RA Newberry K.J., Kohn J., Hou Y.-M., Perona J.J.; RT "Crystallization and preliminary diffraction analysis of Escherichia RT coli cysteinyl-tRNA synthetase."; RL Acta Crystallogr. D 55:1046-1047(1999). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=22027712; PubMed=12032090; DOI=10.1093/emboj/21.11.2778; RA Newberry K.J., Hou Y.-M., Perona J.J.; RT "Structural origins of amino acid selection without editing by RT cysteinyl-tRNA synthetase."; RL EMBO J. 21:2778-2787(2002). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56234; CAA39691.1; -; Genomic_DNA. DR EMBL; M59381; AAA23658.1; -; Genomic_DNA. DR EMBL; X59293; CAA41983.1; -; Genomic_DNA. DR EMBL; U82664; AAB40279.1; -; Genomic_DNA. DR EMBL; U00096; AAC73628.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76303.1; -; Genomic_DNA. DR PIR; A37868; YYEC. DR RefSeq; AP_001173.1; -. DR RefSeq; NP_415059.1; -. DR PDB; 1LI5; X-ray; 2.30 A; A/B=1-461. DR PDB; 1LI7; X-ray; 2.60 A; A/B=1-461. DR PDB; 1U0B; X-ray; 2.30 A; B=1-461. DR PDBsum; 1LI5; -. DR PDBsum; 1LI7; -. DR PDBsum; 1U0B; -. DR DIP; DIP:9386N; -. DR GeneID; 946969; -. DR GenomeReviews; AP009048_GR; JW0515. DR GenomeReviews; U00096_GR; b0526. DR KEGG; ecj:JW0515; -. DR KEGG; eco:b0526; -. DR EchoBASE; EB0193; -. DR EcoGene; EG10196; cysS. DR HOGENOM; P21888; -. DR BioCyc; EcoCyc:CYSS-MON; -. DR BioCyc; MetaCyc:CYSS-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00041; -; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR015804; Cys-tRNA-synt_Ia_C. DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR. DR InterPro; IPR015803; Cys-tRNA-synt_Ia_N. DR InterPro; IPR002308; Cys-tRNA-synth_1a. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR10890; Cys_tRNA-synt_1a; 1. DR Pfam; PF09190; DALR_2; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR TIGRFAMs; TIGR00435; cysS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; KW Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1 461 Cysteinyl-tRNA synthetase. FT /FTId=PRO_0000159394. FT MOTIF 30 40 "HIGH" region. FT MOTIF 266 270 "KMSKS" region. FT METAL 28 28 Zinc. FT METAL 209 209 Zinc. FT METAL 234 234 Zinc. FT METAL 238 238 Zinc. FT BINDING 269 269 ATP (By similarity). FT CONFLICT 316 316 L -> V (in Ref. 1; CAA39691). FT STRAND 3 5 FT TURN 7 9 FT STRAND 10 14 FT STRAND 22 27 FT STRAND 31 34 FT HELIX 38 57 FT STRAND 60 65 FT HELIX 72 80 FT HELIX 85 102 FT HELIX 114 116 FT HELIX 118 130 FT STRAND 133 136 FT STRAND 142 144 FT HELIX 146 148 FT TURN 150 157 FT STRAND 181 186 FT STRAND 200 203 FT HELIX 207 217 FT STRAND 219 225 FT HELIX 228 230 FT TURN 231 233 FT HELIX 234 245 FT STRAND 246 248 FT STRAND 251 254 FT STRAND 260 262 FT HELIX 269 271 FT HELIX 277 281 FT HELIX 286 294 FT STRAND 302 304 FT HELIX 306 323 FT HELIX 336 347 FT HELIX 352 372 FT HELIX 374 388 FT TURN 389 392 FT HELIX 398 401 FT STRAND 406 408 FT HELIX 413 416 FT HELIX 419 428 FT HELIX 432 444 FT STRAND 447 451 FT STRAND 456 460 SQ SEQUENCE 461 AA; 52202 MW; 2FA77FDBB7C5BA99 CRC64; MLKIFNTLTR QKEEFKPIHA GEVGMYVCGI TVYDLCHIGH GRTFVAFDVV ARYLRFLGYK LKYVRNITDI DDKIIKRANE NGESFVAMVD RMIAEMHKDF DALNILRPDM EPRATHHIAE IIELTEQLIA KGHAYVADNG DVMFDVPTDP TYGVLSRQDL DQLQAGARVD VVDDKRNPMD FVLWKMSKEG EPSWPSPWGA GRPGWHIECS AMNCKQLGNH FDIHGGGSDL MFPHHENEIA QSTCAHDGQY VNYWMHSGMV MVDREKMSKS LGNFFTVRDV LKYYDAETVR YFLMSGHYRS QLNYSEENLK QARAALERLY TALRGTDKTV APAGGEAFEA RFIEAMDDDF NTPEAYSVLF DMAREVNRLK AEDMAAANAM ASHLRKLSAV LGLLEQEPEA FLQSGAQADD SEVAEIEALI QQRLDARKAK DWAAADAARD RLNEMGIVLE DGPQGTTWRR K //