ID A0A2Z3YMG9_9CORY Unreviewed; 360 AA.
AC A0A2Z3YMG9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-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 Name=trpS2 {ECO:0000313|EMBL:AWT25246.1};
GN ORFNames=Csp1_04250 {ECO:0000313|EMBL:AWT25246.1};
OS Corynebacterium provencense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1737425 {ECO:0000313|EMBL:AWT25246.1, ECO:0000313|Proteomes:UP000247696};
RN [1] {ECO:0000313|Proteomes:UP000247696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17KM38 {ECO:0000313|Proteomes:UP000247696};
RA Kittl S., Brodard I., Rychener L., Jores J., Roosje P., Gobeli Brawand S.;
RT "Otitis media/interna in a cat caused by the recently described species
RT Corynebacterium provencense.";
RL Submitted (NOV-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}.
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DR EMBL; CP024988; AWT25246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3YMG9; -.
DR STRING; 1737425.GCA_900049755_02203; -.
DR KEGG; cpre:Csp1_04250; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000247696; 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 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:UP000247696}.
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 39097 MW; 7403E395FD2105EA CRC64;
MTNNASLTAA RRRSDRLRQL IDSTAPADAP ARGRLRVLTG DRPTGALHIG HYLGTVRSRV
ELQDKGIDTF LLIADYQVIT DRDSLGDLQG NVRGVLADYL AAGIDPARTT IFAHSAVPAA
NQLMLPFLSL VTEAELHRNP TVKDELAATD GRAMSGLLLT YPVHQACDIL FCHGNVVPVG
QDQLPHIEQA RVIARRFNER YAGGEQVFTE PEALLTDAPM ITGTDGRKMS KSRGNTVPLG
ATADETAKIL RRAVTDAERR ITFEPERRPE VANLLTVAAG FTGGDPRDIA EEIGDAGAGE
LKRVVTEAVN DHLAGHRARR AELLADPGYL MSVLREGNER ANEVADATLT RVREVMGMLY
//
