ID A0A0G1IIM1_9BACT Unreviewed; 325 AA.
AC A0A0G1IIM1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=UW18_C0003G0271 {ECO:0000313|EMBL:KKT31687.1};
OS Microgenomates group bacterium GW2011_GWF1_44_10.
OC Bacteria.
OX NCBI_TaxID=1618537 {ECO:0000313|EMBL:KKT31687.1, ECO:0000313|Proteomes:UP000034538};
RN [1] {ECO:0000313|EMBL:KKT31687.1, ECO:0000313|Proteomes:UP000034538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT31687.1}.
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DR EMBL; LCHI01000003; KKT31687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1IIM1; -.
DR PATRIC; fig|1618537.3.peg.505; -.
DR Proteomes; UP000034538; 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; 36438 MW; 38DAFAB97FCAC276 CRC64;
MKSTVLSGIR ATGKLHLGNY LGAVKGMLEL QDKDDFQTYY MVADLHTVTT PYEKTTLRGS
IRNIIIDYLS AGLDPQKSTL FIQSMVHEHI ELSYYFSTVT TVAKMQHVTT FKDKVKQHPE
HVTMALLNYP VLMSADILLY KASLVPVGID QEPHLEIARE VARRMNQEYG TSFPEPRRFA
TKGEYVPSLS GEGKMSKSVE GSYINLTDSH EEITKKIRSI PTATVAGGEL TGGLRSLFSF
AELFLPDQVE NYRNAFQKGT LKFVELKDAV ADAIYHDLES IQEKHRAVEQ NISFVDDVIA
DGAQRARLIA SKTLQEVKEK MGMPL
//
