ID   A0A271JDP7_9BACT        Unreviewed;       342 AA.
AC   A0A271JDP7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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};
GN   ORFNames=B1759_04810 {ECO:0000313|EMBL:PAP80699.1};
OS   Rubrivirga sp. SAORIC476.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC   Rubrivirga.
OX   NCBI_TaxID=1961794 {ECO:0000313|EMBL:PAP80699.1, ECO:0000313|Proteomes:UP000216627};
RN   [1] {ECO:0000313|EMBL:PAP80699.1, ECO:0000313|Proteomes:UP000216627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAORIC476 {ECO:0000313|EMBL:PAP80699.1,
RC   ECO:0000313|Proteomes:UP000216627};
RA   Kumagai Y., Kogure K., Yoshizawa S.;
RT   "Whole genome sequence of Rhodothermus Rubrivirga sp. SAORIC476.";
RL   Submitted (FEB-2017) 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}.
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:PAP80699.1}.
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DR   EMBL; MVOI01000003; PAP80699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A271JDP7; -.
DR   OrthoDB; 9801042at2; -.
DR   Proteomes; UP000216627; 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   342 AA;  37266 MW;  E1EC9E81B14DDFFE CRC64;
     MPDSPSSLPV IVSGIQPSGT LHLGNYLGAI RQNIALANDE AARSEAFLFI VDYHALTTLR
     DPEALRRYTM DVALDYLALG LDPDKASLFV QSDIPQLTEL TWIFLCLTPS SQLEKGVSYK
     DKVAQGLTAN GGLLTYPILQ AADILAYTAP GRGLKVPVGA DQKQNLEISR DTAGRFNQAY
     RPEDAPLFPL PDPHILDEVS VIPGLDGRKM SKSYDNTIGI FDEGKALKKK VMSILSDSTP
     LEAPKDPDAD HTFALIRHFA TDDERAEIAA AYRAGGYGYG HAKKALLGMI DRHFGEARER
     RRALAERPEH VRDILQAGAE AARARASEVM AEVRDAVGFL NA
//