ID   SYW1_HALSA              Reviewed;         513 AA.
AC   Q9HN83;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Tryptophan--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00140};
DE            EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE   AltName: Full=Tryptophanyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00140};
DE            Short=TrpRS 1 {ECO:0000255|HAMAP-Rule:MF_00140};
GN   Name=trpS1 {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=VNG_2208G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00140};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG20338.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG20338.1; ALT_INIT; Genomic_DNA.
DR   PIR; F84371; F84371.
DR   RefSeq; WP_010903639.1; NC_002607.1.
DR   AlphaFoldDB; Q9HN83; -.
DR   SMR; Q9HN83; -.
DR   STRING; 64091.VNG_2208G; -.
DR   PaxDb; Q9HN83; -.
DR   EnsemblBacteria; AAG20338; AAG20338; VNG_2208G.
DR   GeneID; 5953293; -.
DR   GeneID; 62885368; -.
DR   KEGG; hal:VNG_2208G; -.
DR   PATRIC; fig|64091.14.peg.1698; -.
DR   HOGENOM; CLU_032621_3_1_2; -.
DR   InParanoid; Q9HN83; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 33997at2157; -.
DR   PhylomeDB; Q9HN83; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00140_A; Trp_tRNA_synth_A; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
DR   Pfam; PF00579; tRNA-synt_1b; 2.
DR   PRINTS; PR01039; TRNASYNTHTRP.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..513
FT                   /note="Tryptophan--tRNA ligase 1"
FT                   /id="PRO_0000136720"
FT   MOTIF           86..94
FT                   /note="'HIGH' region"
FT   MOTIF           393..397
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   513 AA;  56055 MW;  56C06025F3EE502B CRC64;
     MTSDDTDDTA GADDVALDPW GSATISDYRA LFDEFGIEAF EDVLDGVPTP HSLMRRAIIF
     GHRDYRRVAA AMRNDEPFAA LSGFMPTGDP HIGHKMVFDE LIWHQQQGGD AYALIADLEA
     HSARGLDWAE IDEHAEDYLL SLLALGFDAD EGELYRQSTN RELQDLAFEL GIEANTSEFE
     AIYGFGGDTD VSHMQSVVTQ MADILYPQLD APKPTVIPVG PDQDPHVRFA RDLAERTRYF
     KVTEAFASVA FDDDERPLVR AAYDARSQYA ADTDQPRCTE AADWLAAEPA AADGVDAATA
     ESVVQKLENA GMEPLRPRVR FFDRQATDEA FTALIDEIAG EKRVFEGHVD AFELSAETAR
     DLALAVEVDH GGYGFVPPSS VYHRFMTGLT GGKMSSSEPA SHISLLDDPE TGADKVAAAT
     TGGRDTAAEQ RERGGEPDDC PVYELYAYLL AGDDDALAEE VYAECANGDR LCGGCKEQAA
     DLMAQFLETH QENREAARDV LAELDIDLDS ARV