ID A0A372GEB5_9ACTN Unreviewed; 339 AA.
AC A0A372GEB5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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 Name=trpS {ECO:0000313|EMBL:RFS83707.1};
GN ORFNames=D0T12_22095 {ECO:0000313|EMBL:RFS83707.1};
OS Actinomadura spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS83707.1, ECO:0000313|Proteomes:UP000262882};
RN [1] {ECO:0000313|EMBL:RFS83707.1, ECO:0000313|Proteomes:UP000262882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52907 {ECO:0000313|EMBL:RFS83707.1,
RC ECO:0000313|Proteomes:UP000262882};
RA Li L., Lin H.W.;
RT "Actinomadura spongicola sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-2018) 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:RFS83707.1}.
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DR EMBL; QVNQ01000006; RFS83707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372GEB5; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000262882; 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:UP000262882}.
SQ SEQUENCE 339 AA; 36546 MW; E0489B8A4A1A23A7 CRC64;
MQTTATDLEG RIAAAPGSFR ILTGDRPTGP LHLGHYFGTL ANRVRLQRAG VELFVLVADY
QVLTDRDVAD RLTEHVEGLV ADYLATGIDP STATIFQHSA VPALNQLMLP FLSLVSVAEL
SRNPTVKDEI AASRQASVSG LMFTYPVHQA ADILFCKANL VPVGRDQLPH QEITRTVARR
FNERYGPVFP VPDALLSAAP SLLGTDGQKM SKSRGNAIAL SAGPDETARL IKGAVTDTDR
HITFAPDTRP QVSNLVLLAA LCQGRDPHAV AAEIGAGGAA ALKKVVTDSV NEFLRPIRAR
RAELAADRTY LRRVLDEGNE RARAIADRTL TEVRTAMTS
//
