SYW_PYRHO
ID SYW_PYRHO Reviewed; 386 AA.
AC O59584;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140};
DE Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140};
GN Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=PH1921;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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=BAA31046.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000001; BAA31046.1; ALT_INIT; Genomic_DNA.
DR PIR; G71206; G71206.
DR RefSeq; WP_010885986.1; NC_000961.1.
DR PDB; 3JXE; X-ray; 3.00 A; A/B=1-386.
DR PDBsum; 3JXE; -.
DR AlphaFoldDB; O59584; -.
DR SMR; O59584; -.
DR STRING; 70601.3258363; -.
DR EnsemblBacteria; BAA31046; BAA31046; BAA31046.
DR GeneID; 1442768; -.
DR KEGG; pho:PH1921; -.
DR eggNOG; arCOG01887; Archaea.
DR OMA; SIYHRFM; -.
DR OrthoDB; 33997at2157; -.
DR BRENDA; 6.1.1.2; 5244.
DR EvolutionaryTrace; O59584; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00140_A; Trp_tRNA_synth_A; 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 InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..386
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136730"
FT MOTIF 82..90
FT /note="'HIGH' region"
FT MOTIF 253..257
FT /note="'KMSKS' region"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3JXE"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3JXE"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 332..357
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:3JXE"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:3JXE"
SQ SEQUENCE 386 AA; 45305 MW; 9E3C392F4028B2DD CRC64;
MVEEFKVTPW EVEGVVDYDK LIKHFGTSPL TEDLLEKTAE LTKSELPIFF RRKFFFSHRD
YDLILKDYEE GRGFFLYTGR GPSGPMHIGH IIPFFATKWL QEKFGVNLYI QITDDEKFLF
KENLTFDDTK RWAYDNILDI IAVGFDPDKT FIFQNSEFTK IYEMAIPIAK KINFSMAKAV
FGFTEQSKIG MIFFPAIQIA PTFFERKRCL IPAAIDQDPY WRLQRDFAES LGYYKTAALH
SKFVPSLTSL SGKMSASKPE TAIYLTDSPE DVEKKVWKFT LTGGRPTLKE QREKGGEPEK
CVVFKWLEIF FEEDDKKLKE RYYACKNGEL TCGECKRYLI SKIQEFLKEH QRRRKKAEKL
VEKFKYTGKL AQEMWNEAIP EPLKRS