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SYV_MYCTU
ID   SYV_MYCTU               Reviewed;         886 AA.
AC   P9WFS9; L0T9U7; O53175; P67599;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 2.
DT   03-AUG-2022, entry version 58.
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=Rv2448c;
GN   ORFNames=MTV008.04c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-14, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP45241.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP45241.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70863; G70863.
DR   RefSeq; NP_216964.1; NC_000962.3.
DR   RefSeq; WP_003412604.1; NZ_KK339370.1.
DR   AlphaFoldDB; P9WFS9; -.
DR   SMR; P9WFS9; -.
DR   STRING; 83332.Rv2448c; -.
DR   PaxDb; P9WFS9; -.
DR   GeneID; 885892; -.
DR   KEGG; mtu:Rv2448c; -.
DR   PATRIC; fig|83332.12.peg.2744; -.
DR   TubercuList; Rv2448c; -.
DR   eggNOG; COG0525; Bacteria.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm;
KW   Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:34915127"
FT   CHAIN           2..886
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106232"
FT   COILED          819..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;  98800 MW;  A6C88C98C9077AA6 CRC64;
     MTASPHPAAD MLPKSWDPAA MESAIYQKWL DAGYFTADPT STKPAYSIVL PPPNVTGSLH
     MGHALEHTMM DALTRRKRMQ GYEVLWQPGT DHAGIATQSV VEQQLAVDGK TKEDLGRELF
     VDKVWDWKRE SGGAIGGQMR RLGDGVDWSR DRFTMDEGLS RAVRTIFKRL YDAGLIYRAE
     RLVNWSPVLQ TAISDLEVNY RDVEGELVSF RYGSLDDSQP HIVVATTRVE TMLGDTAIAV
     HPDDERYRHL VGTSLAHPFV DRELAIVADE HVDPEFGTGA VKVTPAHDPN DFEIGVRHQL
     PMPSILDTKG RIVDTGTRFD GMDRFEARVA VRQALAAQGR VVEEKRPYLH SVGHSERSGE
     PIEPRLSLQW WVRVESLAKA AGDAVRNGDT VIHPASMEPR WFSWVDDMHD WCISRQLWWG
     HRIPIWYGPD GEQVCVGPDE TPPQGWEQDP DVLDTWFSSA LWPFSTLGWP DKTAELEKFY
     PTSVLVTGYD ILFFWVARMM MFGTFVGDDA AITLDGRRGP QVPFTDVFLH GLIRDESGRK
     MSKSKGNVID PLDWVEMFGA DALRFTLARG ASPGGDLAVS EDAVRASRNF GTKLFNATRY
     ALLNGAAPAP LPSPNELTDA DRWILGRLEE VRAEVDSAFD GYEFSRACES LYHFAWDEFC
     DWYLELAKTQ LAQGLTHTTA VLAAGLDTLL RLLHPVIPFL TEALWLALTG RESLVSADWP
     EPSGISVDLV AAQRINDMQK LVTEVRRFRS DQGLADRQKV PARMHGVRDS DLSNQVAAVT
     SLAWLTEPGP DFEPSVSLEV RLGPEMNRTV VVELDTSGTI DVAAERRRLE KELAGAQKEL
     ASTAAKLANA DFLAKAPDAV IAKIRDRQRV AQQETERITT RLAALQ
 
 
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