ID   A0A0L0LYX3_9BURK        Unreviewed;       891 AA.
AC   A0A0L0LYX3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   07-SEP-2016, entry version 10.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004, ECO:0000256|SAAS:SAAS00026840};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004, ECO:0000256|SAAS:SAAS00105779};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN   ORFNames=BPUN_2238 {ECO:0000313|EMBL:KND55597.1};
OS   Candidatus Paraburkholderia kirkii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=198822 {ECO:0000313|EMBL:KND55597.1, ECO:0000313|Proteomes:UP000053677};
RN   [1] {ECO:0000313|Proteomes:UP000053677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot2 {ECO:0000313|Proteomes:UP000053677};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) 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:SAAS00351456}.
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:SAAS00105829}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00026902}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00578901}.
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:SAAS00545212}.
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:KND55597.1}.
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DR   EMBL; LFKV01000015; KND55597.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND55597; KND55597; BPUN_2238.
DR   Proteomes; UP000053677; 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; -; 3.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
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   PANTHER; PTHR11946:SF5; PTHR11946:SF5; 4.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00470524, ECO:0000313|EMBL:KND55597.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00470577};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00429251};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053677};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00470431};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00470540, ECO:0000313|EMBL:KND55597.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00470586};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00470559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053677}.
FT   DOMAIN        1    556       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      611    765       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      825    889       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      823    885       {ECO:0000256|HAMAP-Rule:MF_02004}.
FT   MOTIF       479    483       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   BINDING     482    482       ATP. {ECO:0000256|HAMAP-Rule:MF_02004}.
SQ   SEQUENCE   891 AA;  100457 MW;  DDB51F6901D6F615 CRC64;
     MDSLTRYHRM LGENTLWVPG TDHAGIATQI VVERQLDAQG ISRHDLGREE FLKRVWAWKQ
     QSGSTITNQV RRLDASIDWS REYFTMDDRM SAAVRDVFVT LYKQGLIYRG KRLVNWDPVL
     GTAVSDLEVV SEEENGHLWH IRYPLPDGSG HLTVATTRPE TMLGDVAVMV HPDDERYQHL
     IGKTVLLPLC DREIPVIADE YVDREFGTGV VKVTPAHDFN DYAVGQRHKL PQIEILTLDA
     KINDNAPEKY RGMDRFDARK QVVQDLEALG LLKSVKPHKL MVPRGDRTHV VIEPMLTDQW
     FVAVTKPAPE GTFNPGKSIT ETSLDVVRSG KIRFVPENWT TTYYQWLENI QDWCISRQLW
     WGHQIPAWYG ENGEIFVAKT EEEARAEAEA QGYKGPLKRD EDVLDTWFSS ALVPFSSLGW
     PNETKELKAF LPSSVLVTGF DIIFFWVARM VMMTTHFTGK VPFDTVYVHG LVRDAEGQKM
     SKSKGNTLDP IDIVDGIDLE SLVTKRTTGL MNPKAAAQIE KKTRREFPEG IPSFGTDALR
     FTMASMATLG RNVNFDLARC EGYRNFCNKL WNATRFVLMN CEGHDCGFAN AGACKPGDCG
     PGSYTDFSQA DRWIVSLLQH TEAEVEKGFA DYRFDNVASA IYEFVWDEYC DWYLELAKVQ
     IQTGTPEQQT ATRRTLLRVL EAVLRLAHPI IPFITEALWQ KVAPLTDAFP AGAREDEVSI
     MTQPYPRAEQ KKIDESAEQW ASELKTVIDA CRNLRGEMNL SPAVKVPLLA HGDAARLSAF
     APYVAALARL SEVKIIEDEA ALDQQAYSAP VAIVGSKLVL KVEIDVAAER ERLTKEVDRL
     NTEIAKCNAK LGNESFVSKA PAAVVEQERK RLAEYGTTIE KLQAQLLRLP V
//