ID A0A2N6UYG5_9ACTO Unreviewed; 366 AA.
AC A0A2N6UYG5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN Name=trpS {ECO:0000313|EMBL:PMC90052.1};
GN ORFNames=CJ184_04870 {ECO:0000313|EMBL:PMC90052.1};
OS Actinotignum urinale.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=190146 {ECO:0000313|EMBL:PMC90052.1};
RN [1] {ECO:0000313|EMBL:PMC90052.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0759 {ECO:0000313|EMBL:PMC90052.1};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMC90052.1}.
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; PNHX01000005; PMC90052.1; -; Genomic_DNA.
DR RefSeq; WP_022866391.1; NZ_CP126967.1.
DR AlphaFoldDB; A0A2N6UYG5; -.
DR STRING; 1120933.GCA_000420445_00909; -.
DR OrthoDB; 9801042at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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 NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036}.
SQ SEQUENCE 366 AA; 40468 MW; 792DDCD998754C19 CRC64;
MNVEESLEQS TSDASLAHAL EVSRKIEEKI AVDPSEFRVL TGDRPTGNLH LGHYFGSLKN
RVDLQKKGVE TWLVIADFQV IADRDGTGPV RERVRSLATD YLAVGLDPEE SVIFPHSAIT
GLNELMLPFL SLVTDSELRR NPTVKAEHEA TEGRPLSGLL LTYPVHQAAD ILFCKANLVP
VGKDQLPHLE QARVIADRFD KRYGRPEGHK TPVFPRPQAL LSEAVSILGL DGAKMSKSRG
NTIDIGMSAD ETAKRVKKAV TDSERFITYD PENRPEVSNL VLLAALAQGR DPRAVAEEIG
NGGSGTLKKM VTESINEMFA PIREKRAELV QDMGYIDGII RKGIERANER ADQTLREVLE
AMHMVY
//
