ID D5X7B7_THEPJ Unreviewed; 328 AA.
AC D5X7B7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN OrderedLocusNames=TherJR_1638 {ECO:0000313|EMBL:ADG82487.1};
OS Thermincola potens (strain JR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC Thermincola.
OX NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG82487.1, ECO:0000313|Proteomes:UP000002377};
RN [1] {ECO:0000313|EMBL:ADG82487.1, ECO:0000313|Proteomes:UP000002377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR {ECO:0000313|EMBL:ADG82487.1,
RC ECO:0000313|Proteomes:UP000002377};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT "Complete sequence of Thermincola sp. JR.";
RL Submitted (MAY-2010) 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}.
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DR EMBL; CP002028; ADG82487.1; -; Genomic_DNA.
DR RefSeq; WP_013120501.1; NC_014152.1.
DR AlphaFoldDB; D5X7B7; -.
DR STRING; 635013.TherJR_1638; -.
DR KEGG; tjr:TherJR_1638; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_0_0_9; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000002377; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002377}.
SQ SEQUENCE 328 AA; 36987 MW; EC28F963C3D16B7C CRC64;
MSKGRILSGM RSTGRLHIGH LSVLENWVKL QDEYECFFMV ADWHALTSNY ADTHDMQQNI
RDLVIDWMAA GLDPSKSTIF VQSHVKEHAE LHLLFSMITP LSWLERVPTY KDQIAQLGKQ
GKDLNTYGFL GYPLLQAADI LVYKANAVPV GEDQLPHLEF TREVARRFNF MYKAEIFPEP
QPIIGQVALL PGIDGRKMSK SYNNFINISS ESKDLAAKVN AMITDPARIK KTDPGHPEIC
TVHTYHTIYS AAELEDIRTK CRAGEIGCVA CKKMLGAKLD ELLNPIREKR AALEKNPDYV
NKVLAEGAEK ARSVASEVLK EVRKVMNM
//
