ID A0A1G2P8U4_9BACT Unreviewed; 271 AA.
AC A0A1G2P8U4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE Flags: Fragment;
GN ORFNames=A3G03_00855 {ECO:0000313|EMBL:OHA43991.1};
OS Candidatus Taylorbacteria bacterium RIFCSPLOWO2_12_FULL_44_15c.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802333 {ECO:0000313|EMBL:OHA43991.1, ECO:0000313|Proteomes:UP000176355};
RN [1] {ECO:0000313|EMBL:OHA43991.1, ECO:0000313|Proteomes:UP000176355}
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:OHA43991.1}.
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DR EMBL; MHSL01000012; OHA43991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2P8U4; -.
DR STRING; 1802333.A3G03_00855; -.
DR Proteomes; UP000176355; 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}.
FT NON_TER 271
FT /evidence="ECO:0000313|EMBL:OHA43991.1"
SQ SEQUENCE 271 AA; 30248 MW; 9D1F59304BBBA691 CRC64;
MTTKVFSGIR PSGKLHLGNY LGAIKNWIEL QDKADQAIFA VVDYHGITTP YDPKTYQQQI
MDTVLDYLAA GINPDKALLI RQSKVPQHTE LAWLFNTITS VGWLDRLPTY KEQLEKTGVN
NMGLLDYPVL MAADILAEKS NLVPVGEDQL AHIDVTNEIA KRFNSMFGQT FEPVKAHLAE
GARIMSLQDP TKKMSKTGDE GIALSDDPDT IRAKIKKAVT DSGKEVKYDE KSKPAISNLL
TIYHLLSGKE IKTLEKEYDG KSYVDFKNDL A
//
