ID   R9C808_9BACI            Unreviewed;       881 AA.
AC   R9C808;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   12-APR-2017, entry version 29.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02004,
GN   ECO:0000313|EMBL:EOR25514.1};
GN   ORFNames=A499_05126 {ECO:0000313|EMBL:EOR25514.1};
OS   Bacillus nealsonii AAU1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1202533 {ECO:0000313|EMBL:EOR25514.1, ECO:0000313|Proteomes:UP000014030};
RN   [1] {ECO:0000313|EMBL:EOR25514.1, ECO:0000313|Proteomes:UP000014030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAU1 {ECO:0000313|EMBL:EOR25514.1,
RC   ECO:0000313|Proteomes:UP000014030};
RA   Joshi C.G., Duggirala S.M., Nathani N.M., Bhatt V.D., KaPatel J.A.,
RA   Parnerkar S.P.;
RT   "Whole genome shotgun sequencing of Bacillus nealsonii AAU1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As
CC       ValRS can inadvertently accommodate and process structurally
CC       similar amino acids such as threonine, to avoid such errors, it
CC       has a "posttransfer" editing activity that hydrolyzes mischarged
CC       Thr-tRNA(Val) in a tRNA-dependent manner. {ECO:0000256|HAMAP-
CC       Rule:MF_02004, ECO:0000256|SAAS:SAAS00711212}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val). {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711221}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711188}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711246}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site.
CC       {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711216}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EOR25514.1}.
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DR   EMBL; ASRU01000054; EOR25514.1; -; Genomic_DNA.
DR   RefSeq; WP_016201732.1; NZ_ASRU01000054.1.
DR   EnsemblBacteria; EOR25514; EOR25514; A499_05126.
DR   OrthoDB; POG091H01HY; -.
DR   Proteomes; UP000014030; Unassembled WGS sequence.
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-HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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 {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711227};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711241};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00711237};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014030};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00711219};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711254,
KW   ECO:0000313|EMBL:EOR25514.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711287};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711230}.
FT   DOMAIN       21    566       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      609    755       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      815    880       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      813    840       {ECO:0000256|HAMAP-Rule:MF_02004}.
FT   MOTIF        49     59       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   MOTIF       526    530       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   BINDING     529    529       ATP. {ECO:0000256|HAMAP-Rule:MF_02004}.
SQ   SEQUENCE   881 AA;  101822 MW;  93FC13E07FE4CCFA CRC64;
     MDMKEISMPT KYDPASIEKG RYDWWLEGKF FEANQDEGKQ PYTIVIPPPN VTGKLHLGHA
     WDTTLQDILT RMKRMQGYDV LWLPGMDHAG IATQAKVEEK LRAQNISRYD LGREKFVEET
     WKWKEEYASH IRAQWSKLGL GLDYSRERFT LDEGLSKAVR EVFVSLYNKG LIYRGEYIIN
     WDPATKTALS DIEVIYKDVQ GAFYHMKYPL ADGSGYIEVA TTRPETMLGD SGVAVHPKDE
     RYQHLIGKKV VLPIVGREIP IVADDYVEMD FGSGAVKMTP AHDPNDFEVG NRHNLERILV
     MNEDGTMNER AGKYEGMDRF ECRKQIVKDL QELGVLFKME EHMHSVGHSE RSGAVVEPYL
     STQWFVKMQP LADAAIALQD KEAEKVNFVP NRFENTYMRW MENIRDWCIS RQLWWGHRIP
     AWYHKETGEI YVNDEAPTDI ENWTQDTDVL DTWFSSALWP FSTLNWPDTE AEDYKRYYPT
     AALVTGYDII FFWVSRMIFQ GIEFTGERPF KDVLIHGLVR DEQGRKMSKS LGNGVDPMDV
     IAKYGADSLR YFLSTGSSPG QDLRFSIEKV ESTWNFANKI WNASRFALMN MDGLTYDQID
     LTGEKSVADN WILTRLNETI ETVTRLSDRY EFGEVGRVLY NFIWDDFCDW YIEMAKLPLY
     GDDEAAKLTT RSILAYVLDN TMRLLHPFMP FITEEIWQNL PHAAESITVA KWPEVNPAFT
     DDKAANDMKL LVEIIRSVRN SRAEVNTPMS KKISILLKAK DEEIKTTLIE NKSFIERFCN
     PETLSIDIDI AVPDKAMTAV VTGVEIILPL EGLINMEEEI ARLTKELEKW NKEVERVQKK
     LSNEGFVKKA PEKVINEERA KEQDYLEKRA AVEARINELK G
//