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Database: UniProt
Entry: A0A1I0WK00_9FIRM
LinkDB: A0A1I0WK00_9FIRM
Original site: A0A1I0WK00_9FIRM 
ID   A0A1I0WK00_9FIRM        Unreviewed;       360 AA.
AC   A0A1I0WK00;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE            EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN   ORFNames=SAMN05216249_104105 {ECO:0000313|EMBL:SFA88558.1};
OS   Acetitomaculum ruminis DSM 5522.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Acetitomaculum.
OX   NCBI_TaxID=1120918 {ECO:0000313|EMBL:SFA88558.1, ECO:0000313|Proteomes:UP000198838};
RN   [1] {ECO:0000313|EMBL:SFA88558.1, ECO:0000313|Proteomes:UP000198838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5522 {ECO:0000313|EMBL:SFA88558.1,
RC   ECO:0000313|Proteomes:UP000198838};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOJY01000004; SFA88558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0WK00; -.
DR   STRING; 1120918.SAMN05216249_104105; -.
DR   OrthoDB; 9801042at2; -.
DR   Proteomes; UP000198838; 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:UP000198838}.
SQ   SEQUENCE   360 AA;  41132 MW;  CA196AA6C2EE54B5 CRC64;
     MGKIILTGDR PTGKLHVGHY VGSLRRRVEL QNSGEFEKIY IMIADTQALT DNAENPEKIR
     QNIIEVALDY LSAGLDPEKS ILFIQSQVPQ LTELTMFYMN LVTVSRLQRN PTVKSEIQMR
     NFETSIPVGF YCYPISQASD ITAFKATTVP AGEDQEPMVE QTREIVRKFN SVYGETLVEP
     EILLPDNDAC LRLPGTDGKA KMSKSLGNCI YLSETADEVK KKVMSMYTDP DHLRVEDPGK
     VEGNTVFTYL DAFCKDEYFE EFLPDYANLD ELKAHYRRGG LGDVKVKKFL IKVLNAELEP
     IRKRRAEYEK DIAYVYEILK KGSETAREVA QKTLDDVKAA MKINYFEDEE LIAYHIKKYQ
//
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