ID A0A1F6IAE0_9BACT Unreviewed; 325 AA.
AC A0A1F6IAE0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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 ORFNames=A2868_04205 {ECO:0000313|EMBL:OGH19632.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_01_FULL_40_15b.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798594 {ECO:0000313|EMBL:OGH19632.1, ECO:0000313|Proteomes:UP000176941};
RN [1] {ECO:0000313|EMBL:OGH19632.1, ECO:0000313|Proteomes:UP000176941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGH19632.1}.
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DR EMBL; MFNR01000002; OGH19632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6IAE0; -.
DR Proteomes; UP000176941; Unassembled WGS sequence.
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; 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.
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 325 AA; 36925 MW; 93A8DB29C2313A55 CRC64;
MKKRVLSGIR ATGRLHLGNY LGAVKGMLEL QNDPEYETFY MVADVHTITT PYNVEELRRA
RREVIIDYLA AGLDPEKSVI FQQSEIPEHF ELAFLLSSIT TIAKMQHLPT FKEKVKQYPQ
HSTMALLNYP VLMAADILIY KAEAVPVGID QEPHLEVARE IARRMNQDYG TDFPEPKRFA
TNGEYVPSLT GEGKMSKTVE GSYINLTDSL EEIKSKVAKI PTDSGQGSEI SGGVKTLMEF
VELFEGKEKR NEFENQYRDK GLRYGEIKSE LSEAIFKELE PIQKRRVELE KDTKYIDKVI
AEGAEKARKV AQETVLEVRQ KMGLA
//
