SYW2_DEIRA
ID SYW2_DEIRA Reviewed; 351 AA.
AC Q9RVD6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Tryptophan--tRNA ligase 2;
DE EC=6.1.1.2;
DE AltName: Full=Tryptophanyl-tRNA synthetase 2;
DE Short=TrpRS 2;
DE AltName: Full=Tryptophanyl-tRNA synthetase II;
DE Short=TrpRS II;
GN Name=trpS2; Synonyms=trpSII; OrderedLocusNames=DR_1093;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, AND INTERACTION WITH NOS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15520379; DOI=10.1073/pnas.0405483101;
RA Buddha M.R., Keery K.M., Crane B.R.;
RT "An unusual tryptophanyl tRNA synthetase interacts with nitric oxide
RT synthase in Deinococcus radiodurans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15881-15886(2004).
RN [3]
RP ACTIVITY OF THE COMPLEX WITH NOS.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15466862; DOI=10.1074/jbc.c400418200;
RA Buddha M.R., Tao T., Parry R.J., Crane B.R.;
RT "Regioselective nitration of tryptophan by a complex between bacterial
RT nitric-oxide synthase and tryptophanyl-tRNA synthetase.";
RL J. Biol. Chem. 279:49567-49570(2004).
CC -!- FUNCTION: Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but
CC with 5-fold less activity than TrpRS. Increases the solubility of the
CC nitric oxide synthase oxygenase (nos), as well as its affinity for
CC substrate L-arginine and its nitric-oxide synthase activity. The
CC complex between trpS2 and nos catalyzes the regioselective nitration of
CC tryptophan at the 4-position. {ECO:0000269|PubMed:15520379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC -!- SUBUNIT: Homodimer. Forms a complex with nos; one homodimer of trpS2
CC binds one homodimer of nos.
CC -!- INDUCTION: The level of expression increases 2.2-fold, 5 hours after
CC exposure to radiation, and returns to near a base line 5 hours later.
CC -!- MISCELLANEOUS: This protein may not be involved in protein
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF10665.1; -; Genomic_DNA.
DR PIR; E75438; E75438.
DR RefSeq; NP_294817.2; NC_001263.1.
DR PDB; 1YI8; X-ray; 2.10 A; A/B/C=1-351.
DR PDB; 1YIA; X-ray; 3.70 A; A/B/C=1-351.
DR PDB; 1YID; X-ray; 2.40 A; A/B/C=1-351.
DR PDB; 2A4M; X-ray; 2.30 A; A/B/C=21-351.
DR PDBsum; 1YI8; -.
DR PDBsum; 1YIA; -.
DR PDBsum; 1YID; -.
DR PDBsum; 2A4M; -.
DR AlphaFoldDB; Q9RVD6; -.
DR SMR; Q9RVD6; -.
DR STRING; 243230.DR_1093; -.
DR DrugBank; DB02959; Oxitriptan.
DR PRIDE; Q9RVD6; -.
DR EnsemblBacteria; AAF10665; AAF10665; DR_1093.
DR KEGG; dra:DR_1093; -.
DR PATRIC; fig|243230.17.peg.1289; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_0_1_0; -.
DR InParanoid; Q9RVD6; -.
DR OMA; LGHYFGT; -.
DR OrthoDB; 951354at2; -.
DR BRENDA; 6.1.1.2; 1856.
DR EvolutionaryTrace; Q9RVD6; -.
DR PRO; PR:Q9RVD6; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..351
FT /note="Tryptophan--tRNA ligase 2"
FT /id="PRO_0000136717"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..39
FT /note="'HIGH' region"
FT MOTIF 215..219
FT /note="'KMSKS' region"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1YI8"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:1YI8"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1YI8"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:1YI8"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 173..189
FT /evidence="ECO:0007829|PDB:1YI8"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1YI8"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1YI8"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 288..314
FT /evidence="ECO:0007829|PDB:1YI8"
FT HELIX 317..345
FT /evidence="ECO:0007829|PDB:1YI8"
SQ SEQUENCE 351 AA; 38180 MW; 7CBE69160F6CB9C5 CRC64;
MPFVDLEVPT MTTPTPAATP ARPRVLTGDR PTGALHLGHL AGSLQNRVRL QDEAELFVLL
ADVQALTDHF DRPEQVRENV LAVALDYLAA GLDPQKTTCV VQSAVPELAE LTVYFLNLVT
VSHLRQNPTV KAEIAQKGYG ERVPAGFFVY PVSQAADIAA FGATLVPVGD DQLPMLEQTR
EIVRRFNALY APVLAEPQAQ LSRVPRLPGL DGQAKMSKSL GNAIALGDSA DEVARKVMGM
YTDPGHLRAS DPGRVEGNPV FTFLDAFDPD PARVQALKDQ YRAGGLGDVK VKKHLIDVLN
GVLAPIRTRR AEYERDPDAV LRFVTEGTAR GREVAAQTLG QVRRAMRLFG H
