ID A0A1Q9JUU0_9FIRM Unreviewed; 353 AA.
AC A0A1Q9JUU0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=BHF70_10245 {ECO:0000313|EMBL:OLR59963.1};
OS Anaerostipes sp. 494a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261636 {ECO:0000313|EMBL:OLR59963.1, ECO:0000313|Proteomes:UP000242190};
RN [1] {ECO:0000313|EMBL:OLR59963.1, ECO:0000313|Proteomes:UP000242190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=494a {ECO:0000313|EMBL:OLR59963.1,
RC ECO:0000313|Proteomes:UP000242190};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(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:OLR59963.1}.
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DR EMBL; MJIF01000001; OLR59963.1; -; Genomic_DNA.
DR RefSeq; WP_075760151.1; NZ_MJIF01000001.1.
DR AlphaFoldDB; A0A1Q9JUU0; -.
DR STRING; 1261636.BHF70_10245; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000242190; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000242190}.
SQ SEQUENCE 353 AA; 40214 MW; 4A1ED18C4484AAC8 CRC64;
MKNVILTGDR PTGRLHVGHY VGSLKERVRL QNSGNFDEIY IMIADAQALT DNAENPEKVR
QNIIQVALDY LASGLDPDKS TIFIQSMVPE LTELSFYYMN LVTVSRVQRN PTVKAEIQQR
NFEASIPVGF FCYPISQAAD ITAFRATAVP VGEDQLPMLE QCKEIVHKFN TVYGETLTDP
EIILPKNQAC LRLPGIDGKA KMSKSLGNCI YLSDEPEDIK KKVMSMFTDP NHLRVQDPGK
VEGNPVFIYL DAFCRPEYFD EFLPDYKNLD ELKAHYSRGG LGDVKVKKFL NNVLQAELEP
IRERRKMWEK RIPDVYDILK QGSEVAQAKA AQTLHDVRSA MKINYFEDVD LWK
//
