ID A0A1H6IQX9_9EURY Unreviewed; 569 AA.
AC A0A1H6IQX9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140};
DE Short=TrpRS {ECO:0000256|HAMAP-Rule:MF_00140};
GN Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140};
GN ORFNames=SAMN05192561_10320 {ECO:0000313|EMBL:SEH49016.1};
OS Halopenitus malekzadehii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1267564 {ECO:0000313|EMBL:SEH49016.1, ECO:0000313|Proteomes:UP000199215};
RN [1] {ECO:0000313|EMBL:SEH49016.1, ECO:0000313|Proteomes:UP000199215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10418 {ECO:0000313|EMBL:SEH49016.1,
RC ECO:0000313|Proteomes:UP000199215};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000256|HAMAP-Rule:MF_00140}.
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:0000256|HAMAP-Rule:MF_00140};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00140,
CC ECO:0000256|RuleBase:RU363036}.
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DR EMBL; FNWU01000003; SEH49016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6IQX9; -.
DR STRING; 1267564.SAMN05192561_10320; -.
DR OrthoDB; 371821at2157; -.
DR Proteomes; UP000199215; Unassembled WGS sequence.
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; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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 PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 2.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00140};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00140}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00140};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00140};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00140}; Reference proteome {ECO:0000313|Proteomes:UP000199215}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..124
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT MOTIF 443..447
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 62441 MW; 142CC609D5AE169D CRC64;
MTDDDHTPRE VATAADARDD ADANAAGRGT VTDGGTDTAA GADDVELDPW GSATVDDYRK
LFEEFGIEEF DDVLPDVPHP HYLMRRGVIF GHREYDAVAD AMANDDPFAA LSGFMPTGDP
HIGHKLVFDE LIWHQQQGGD AFGLIADLEA HSARGLSWDE IDEHARSYVL SLIALGFDPE
EGTVYRQSDN REVQDLAFEL GSKANFSELQ ALYGFDGETN VSHMQSTITQ MADILYPQLV
DGPKPTVVPV GPDQDPHLRL ARDLSERMRY FKVTEAFASF ELTDDERQLV RAAYDALAAA
GDGGADGGNV AADADQGTEM EAATADRVRC ADAADWLDTY DPTPDLTDAK GPAIEKLRAA
GKEPLRPRVR FLDRNATDDA FEDLIGRVDG DKRVFEEHID AFDLTHEVAE TLAREVELDH
DGFGFRQPSS IYHRFMSGLT GGKMSSSIPA SHISLLDDPE DGYDKVKAAT TGGRSTAEEQ
RELGGKPDEC PVYELYAYLL ANDDDDLART VYEECEDGDR LCGGCKEQAA ELMREFLADH
QEKREEAAAL LEGMDIDFES DRRGTGGEH
//
