ID A0A430A8L1_9ENTE Unreviewed; 338 AA.
AC A0A430A8L1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140};
DE Short=TrpRS {ECO:0000256|HAMAP-Rule:MF_00140};
GN Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140};
GN ORFNames=CBF31_06965 {ECO:0000313|EMBL:RSU03446.1};
OS Vagococcus fessus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=120370 {ECO:0000313|EMBL:RSU03446.1, ECO:0000313|Proteomes:UP000287101};
RN [1] {ECO:0000313|EMBL:RSU03446.1, ECO:0000313|Proteomes:UP000287101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 41755 {ECO:0000313|EMBL:RSU03446.1,
RC ECO:0000313|Proteomes:UP000287101};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000256|HAMAP-Rule:MF_00140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000107, ECO:0000256|HAMAP-
CC Rule:MF_00140};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00140}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00140,
CC 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:RSU03446.1}.
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DR EMBL; NGJY01000002; RSU03446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430A8L1; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000287101; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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 InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
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|HAMAP-Rule:MF_00140};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00140}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00140};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00140};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00140}; Reference proteome {ECO:0000313|Proteomes:UP000287101}.
FT MOTIF 10..18
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT MOTIF 198..202
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT BINDING 9..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT BINDING 17..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT BINDING 134
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT BINDING 146..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT BINDING 198..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
SQ SEQUENCE 338 AA; 37386 MW; 49E354937D840B98 CRC64;
METIFSGIQP SGIPTIGNYI GAMQQFVALQ DDYNCYYCIV DEHAITVPQD RLKLRQQTLE
LAALYLAVGL DPEKATIFIQ SEVSAHAEAA WIVQCNTTIG ELERMTQFKD KSQNNGRTGV
SAALLTYPPL MVADIILYNA NLVPVGEDQK QHLELTRDFV ERFNNRYGTA DQPILVKPEV
KIPKHGARIM SLQEPTKKMS KSDTNAKGYI SMLDEPAAIR KKIKSAVTDS SGKIEYDVEN
KPGISNLLTI FSAMTGESIA TLADRYKDAG YGEFKTDLAE AVVAVLEPIQ TRQKELLSSD
ELHEILDTGA EKANKVAKKT LQKMRNGVGL GRKGRMTL
//
