ID A0A241W8J3_9GAMM Unreviewed; 337 AA.
AC A0A241W8J3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=B9T34_07440 {ECO:0000313|EMBL:OTG90336.1};
OS Acinetobacter sp. ANC 3813.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977873 {ECO:0000313|EMBL:OTG90336.1, ECO:0000313|Proteomes:UP000194864};
RN [1] {ECO:0000313|EMBL:OTG90336.1, ECO:0000313|Proteomes:UP000194864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3813 {ECO:0000313|EMBL:OTG90336.1,
RC ECO:0000313|Proteomes:UP000194864};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-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:OTG90336.1}.
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DR EMBL; NEGK01000004; OTG90336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241W8J3; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000194864; 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 337 AA; 37641 MW; 4E142EFEE4DC2E65 CRC64;
MSNLDNRPVI LTGDRPTGQL HLGHFVGSLR SRVGLQDSHH QHILLADAQA LTDNADNFEK
VRRNILEVAT DYLAVGIDPT KTTICVQSCL PALNEMTMLY LNFVTVSRLE RNPTIKSEIQ
MRGFERDIPA GFLCYPVAQA ADITAFKASV VPVGEDQIPM IEQTNEIVRR LNRQIGRDVL
PECKALLSNV GRLPGFDGKA KMSKSLGNTI VLDASDKDIK KAVNSMYTDP NHLRIEDPGQ
VEGNVVFTYL DAFDPDKEAV AELKEHYRRG GLGDGTVKKR LEGVLKELIL PIRERRMELA
KDPDYIMDIL KTGTDKCRDI TQQTLDEIKS GLGMFHF
//
