ID A0A1G0NNS9_9BACT Unreviewed; 319 AA.
AC A0A1G0NNS9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=A2X66_00720 {ECO:0000313|EMBL:OGU25128.1};
OS Ignavibacteria bacterium GWA2_54_16.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798420 {ECO:0000313|EMBL:OGU25128.1, ECO:0000313|Proteomes:UP000182282};
RN [1] {ECO:0000313|EMBL:OGU25128.1, ECO:0000313|Proteomes:UP000182282}
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:OGU25128.1}.
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DR EMBL; MGZS01000109; OGU25128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0NNS9; -.
DR STRING; 1798420.A2X66_00720; -.
DR Proteomes; UP000182282; 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; 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 319 AA; 35904 MW; 33FF3D53108B2CCD CRC64;
MRPTGKLHLG HLVGALENWV SLQGEYQNYH LIADYHALTT DPVSSQIYDH SIDMLIDWLS
AGLDPKISPM FRQSQIKEHA ELHLIFSMLV TTSRLERNPT LKEQVRDLEM DTIVYGHLGY
PVLQAADILL YKGDVVPVGE DQLPHIEITR EIARRFNVLY CEAAPVFPEP EGKLTKFARL
PGLDGRRMSK SIGNTILLSD GPDEIKKKMK GAVTDPQKVR KGDPGRPDIC LVFSYHNKFN
ATETAEIRSG CESGSLGCVD CKLRCAERIT NALAPHREKR AYYESHLDEV KNILHDGETK
ARTVAQHTMS EVHQAMHMG
//
