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SYV_MYCLE
ID   SYV_MYCLE               Reviewed;         886 AA.
AC   Q9CBY7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=ML1472;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; AL583922; CAC30422.1; -; Genomic_DNA.
DR   PIR; A87093; A87093.
DR   RefSeq; NP_302037.1; NC_002677.1.
DR   RefSeq; WP_010908358.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBY7; -.
DR   SMR; Q9CBY7; -.
DR   STRING; 272631.ML1472; -.
DR   PRIDE; Q9CBY7; -.
DR   EnsemblBacteria; CAC30422; CAC30422; CAC30422.
DR   KEGG; mle:ML1472; -.
DR   PATRIC; fig|272631.5.peg.2748; -.
DR   Leproma; ML1472; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..886
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224505"
FT   COILED          820..851
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           540..544
FT                   /note="'KMSKS' region"
FT   BINDING         543
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   886 AA;  98915 MW;  D219EA2B657CC6C4 CRC64;
     MTTSPSSSAD LLPKSWDPGA MESVIYQKWL NSGYFAADPA STKPGYSIVL PPPNVTGSLH
     MGHALEHTMM DALTRRKRMQ GYEVLWQPGM DHAGIATQSV VEKQLAINGK IKEDFGRELF
     VDKVWDWKRE SGGAIAGQMR RLGDGVDWSR DRFTMDDGLS RAVRMIFKRL YDAGLIYRAE
     RLVNWSPVLR TALSDIEVIY DEIEGELISF RYGSLDDDEP HIVVATTRVE TMLGDTGIAV
     HPDDKRYQHL VGTTLPHPFI DRELVIVADE HVDPEFGTGA VKVTPAHDPN DFEIGLRHNL
     PMPNVMDVKA VIVDTGTEFD GMDRFEARIA VREALAVQGR IVEEKRPYRH SVGHSERSGE
     VIEPRLSLQW WVRVESLAKA AGDAVRNGDT VIHPASMESR WFAWVDDMRD WCISRQLWWG
     HRIPIWYGPN GEQVCVGPDE TPPEGWQQDP DVLDTWFSSA LWPFSTLGWP QMTPELEKFY
     PTSILVTGYD ILFFWVARMM MLGTFVGGDD AITLGGCRGP QVPFTDVFLH GLIRDEFGRK
     MSKSRGNVID PLAWMDMFGA DALRFTLARG SSPGGDLAIG EDHVRASRNF GTKLFNATRY
     ALLNGAALVP LPALTALTDA DRWILGRLEQ VRAEVDSAFD GYEFSRACEA LYHFAWDEFC
     DWYLELAKAQ LADGLTHTTA VLAAALDTLL RLLHPVMPFI TETLWQALTQ LESLVIATWP
     EPSGISLDLV AAQRISDMQK LVTEIRRFRS DQGLVDRQKV PARLSGVEDS DLATQVGFVT
     SLALLTAASN DFRPSALLEV RLGPNKDRAV VVELDTSGTI DVAAERRRME KDLAAAQKEL
     ASTAAKLANA DFLAKAPEAV VVKIRDRQRM AKEETDRIIA RLAGLQ
 
 
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