SYW_AERPE
ID SYW_AERPE Reviewed; 372 AA.
AC Q9Y924;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 104.
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=APE_2461.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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}.
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DR EMBL; BA000002; BAA81476.2; -; Genomic_DNA.
DR PIR; D72477; D72477.
DR PDB; 3A04; X-ray; 1.97 A; A=1-372.
DR PDB; 3A05; X-ray; 2.20 A; A=1-372.
DR PDBsum; 3A04; -.
DR PDBsum; 3A05; -.
DR AlphaFoldDB; Q9Y924; -.
DR SMR; Q9Y924; -.
DR STRING; 272557.APE_2461.1; -.
DR EnsemblBacteria; BAA81476; BAA81476; APE_2461.1.
DR KEGG; ape:APE_2461.1; -.
DR PATRIC; fig|272557.25.peg.1635; -.
DR eggNOG; arCOG01887; Archaea.
DR BRENDA; 6.1.1.2; 171.
DR EvolutionaryTrace; Q9Y924; -.
DR Proteomes; UP000002518; 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 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; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..372
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136718"
FT REGION 247..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 79..87
FT /note="'HIGH' region"
FT MOTIF 256..260
FT /note="'KMSKS' region"
FT TURN 12..17
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:3A04"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:3A04"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:3A04"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3A04"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:3A04"
FT HELIX 334..364
FT /evidence="ECO:0007829|PDB:3A04"
SQ SEQUENCE 372 AA; 42154 MW; 90E3D4F2E8121A2B CRC64;
MAAERLDPWG AVEIKDYDRL LRTFGIRPFS EVLPLLRKAG MEPSFLMRRG IIFGHRDFDK
ILEAKARGER VAVLTGFMPS GKFHFGHKLT VDQLIYLQKN GFKVFVAIAD AEAFAVRRIG
REEAVRIAVE EYIANMIALG LDPKDTEFYF QTNRGTPYFR LIQLFSGKVT AAEMEAIYGE
LTPAKMMASL TQAADILHVQ LDEYGGYRHV VVPVGADQDP HLRLTRDLAD RMAGVVELER
PASTYHKLQP GLDGRKMSSS RPDSTIFLTD PPEVARNKLF RALTGGRATA EEQRRLGGVP
EVCSVYHMDL YHLMPDDGEV KHIYTSCRLG KILCGECKQI AWEKLERFLA EHQSRLEKAK
TIAWKLVEPP RF
