ID B7JBP5_ACIF2 Unreviewed; 403 AA.
AC B7JBP5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN Name=trpS {ECO:0000313|EMBL:ACK78819.1};
GN OrderedLocusNames=AFE_1789 {ECO:0000313|EMBL:ACK78819.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK78819.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK78819.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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; CP001219; ACK78819.1; -; Genomic_DNA.
DR RefSeq; WP_012536759.1; NC_011761.1.
DR AlphaFoldDB; B7JBP5; -.
DR STRING; 243159.AFE_1789; -.
DR PaxDb; 243159-AFE_1789; -.
DR GeneID; 66432571; -.
DR KEGG; afr:AFE_1789; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_0_0_6; -.
DR Proteomes; UP000001362; Chromosome.
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; 2.
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:UP000001362}.
SQ SEQUENCE 403 AA; 45003 MW; D43A2DEB40FFD34B CRC64;
MREIIVSGMR PTGRLHLGHY HGVLKNWLRL QEEAECYFFV ADWHALTTHY ETIQGISVAV
WDLLIEWLAV GVDPDKAVLF IQSHVPEHAE LALLLGMLTP LSWLERVPTF KDQQEKLRER
DLATFGFLGY PLLMTADILV YDAHKVPVGA DQVAHLEISR ELARRFNSFY GRDADAATQV
EKGLQVMGKR AAKTFLSLQQ RFQQDGDALA VSEAVVFLGG QAGLSAEMRE QLLAHLEGKG
REILREPQAL LTAASKMPGL DGQKMSKSYG NTIPLREAPE VVRKKIRTMP TDPARVARTD
PGTPEKCPVW ALHQVYSGPE TQAWVRNGCT TASIGCLDCK QPVIEAVLAE QAPIRERAEY
WAARPQQLTE IAHAGAQRAR QRAAQTLERV RAAMGLAHER HDC
//
