ID A0A1G2HG23_9BACT Unreviewed; 336 AA.
AC A0A1G2HG23;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=A2919_00215 {ECO:0000313|EMBL:OGZ61200.1};
OS Candidatus Spechtbacteria bacterium RIFCSPLOWO2_01_FULL_43_12.
OC Bacteria; Candidatus Spechtbacteria.
OX NCBI_TaxID=1802162 {ECO:0000313|EMBL:OGZ61200.1, ECO:0000313|Proteomes:UP000178835};
RN [1] {ECO:0000313|EMBL:OGZ61200.1, ECO:0000313|Proteomes:UP000178835}
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:OGZ61200.1}.
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DR EMBL; MHOH01000004; OGZ61200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2HG23; -.
DR Proteomes; UP000178835; 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 336 AA; 37928 MW; 8FDA262CD683ADBA CRC64;
MAKQKQIILT GDRPTGPLHL GHYAGSLRAR VELQDKYKTY ILIADLQALT DNAKNPKKVR
ESVVEVALDY LSVGIDPKKS TIMIQSLIPE LSELMMYYLN IVTVARLNRN PTVKEEMKQK
GFGANVPAGF FVYPVSQAAD ITAFGANLVP VGEEQLPMLE QTKEIVRVFN RIYKPVLVEP
EALVPKNKFE RRLPGIDGKA KMSKSLGNAI YLKDTPKEVE KKVMQMYTDP GHIHKEQAGK
VEGNTVFAYL DVFDTDKKAV AELKKQYRKG GLGDVELKRR LINVLEEFLG PIRKRRKEYA
KDPKKVMDIL TNGSKQGKKT ASKTVENVRE AMYLDY
//
