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Database: UniProt
Entry: A0A2Y9AT66_9MICO
LinkDB: A0A2Y9AT66_9MICO
Original site: A0A2Y9AT66_9MICO 
ID   A0A2Y9AT66_9MICO        Unreviewed;       374 AA.
AC   A0A2Y9AT66;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE            EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN   ORFNames=SAMN05216184_11360 {ECO:0000313|EMBL:SSA45459.1};
OS   Georgenia satyanarayanai.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC   Georgenia.
OX   NCBI_TaxID=860221 {ECO:0000313|EMBL:SSA45459.1, ECO:0000313|Proteomes:UP000250222};
RN   [1] {ECO:0000313|EMBL:SSA45459.1, ECO:0000313|Proteomes:UP000250222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10826 {ECO:0000313|EMBL:SSA45459.1,
RC   ECO:0000313|Proteomes:UP000250222};
RA   Cai Z.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; UETB01000013; SSA45459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Y9AT66; -.
DR   OrthoDB; 9801042at2; -.
DR   Proteomes; UP000250222; 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:UP000250222}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  40530 MW;  BE0E95051FC42844 CRC64;
     MSTEQNADAP VSDALAESTS DASLDRTRAR SQAIEAEIDA NPSRFRVLTG DRPTGNLHLG
     HYFGTLANRV ALQDRGVQTW VLVADYQVIT DRDAVGEIQD RVLSLVADYL AIGIDPARST
     IFTHSTVPAL NQLMLPFLSL VTDSELRRNP TVKSEFEATG GRPMSGLLLT YPVHQAADIL
     FCKANLVPVG KDQLPHLEQT RIIARRFDER YGRAEADRPV FPQPEALLSA ATNLLGTDGQ
     KMSKSKGNTI ELGMDADTTA KRLKKAVTDA DRHITYDPAG RPEVSNLVLL AALASGRDPH
     EVAAEIGDGG GGTLKRVVTE AVNEHFAPIR ARRAELVADP GYLRQVLDEG NERANAVAEA
     TLAEVRTAMG MIYT
//
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