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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.
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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
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