ID   G2LTK5_9XANT            Unreviewed;       980 AA.
AC   G2LTK5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 48.
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:AEO43700.1};
GN   ORFNames=XACM_3453 {ECO:0000313|EMBL:AEO43700.1};
OS   Xanthomonas axonopodis pv. citrumelo F1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=981368 {ECO:0000313|EMBL:AEO43700.1, ECO:0000313|Proteomes:UP000001276};
RN   [1] {ECO:0000313|EMBL:AEO43700.1, ECO:0000313|Proteomes:UP000001276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:AEO43700.1};
RX   PubMed=21908674; DOI=10.1128/JB.05777-11;
RA   Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H.,
RA   Setubal J.C., Wang N.;
RT   "Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo
RT   F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains
RT   Provides Insights into Virulence and Host Specificity.";
RL   J. Bacteriol. 193:6342-6357(2011).
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:SAAS00870405}.
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:SAAS00870389}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00889155}.
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:SAAS00870396}.
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DR   EMBL; CP002914; AEO43700.1; -; Genomic_DNA.
DR   RefSeq; WP_014091065.1; NC_016010.1.
DR   EnsemblBacteria; AEO43700; AEO43700; XACM_3453.
DR   KEGG; xax:XACM_3453; -.
DR   KO; K01873; -.
DR   OrthoDB; POG091H01HY; -.
DR   Proteomes; UP000001276; 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; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   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; 2.
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   ECO:0000313|EMBL:AEO43700.1};
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:SAAS00870403};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001276};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00889138};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711254};
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       17    663       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      704    856       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      916    979       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      914    941       {ECO:0000256|HAMAP-Rule:MF_02004}.
FT   MOTIF        43     53       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   MOTIF       586    590       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   BINDING     589    589       ATP. {ECO:0000256|HAMAP-Rule:MF_02004}.
SQ   SEQUENCE   980 AA;  110981 MW;  020053D53036EF86 CRC64;
     MTTLASSYDP SSFESRLYAQ WEAAGYFVPS GKGEPYTVLL PPPNVTGTLH MGHAFQQTLM
     DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GQTRDSLGRE GFIAKVWEWK
     AESGDTIERQ MRRLGTSSDW SRSTFTMDPQ PSAAVNEAFV RWYEQGLIYR GQRLVNWDPV
     LKTAISDLEV ENVEEDGFLW SIRYPLADGV SYEHVEHDAD GNETLRETRD YLVVATTRPE
     TMLGDTAVMV HPEDARYLTL HDARIVLPLT GRQVPVITDD YVDRAFGTGV VKVTPAHDFN
     DYQVGERHNL PLVNLFTVDA KIIDPREQYP DDEYPVVDQG IDWRELNQVQ RRRTGQHFAY
     SIPSAYVGLD RYEARKLVLA HLEDEGRLVE TKPHKLQVPR GDRTGQVIEP YLTDQWFVKM
     DALAKRGLEL VESGQIKFVP PNWINTYRHW MENIQDWCIS RQLWWGHRIP AWFDEAGKCY
     VGHDEAQVRA KHGLGAEIAL HQDSDVLETW FSSQLWPFST LGWPDAQAMA ERGFARYLPS
     SVLVTGFDII FFWVARMIMA TDSFTGQVPF RDVYITGLIR DAQGQKMSKS KGNVLDPLDI
     IDGISIEDLV AKRTHGLMQP RMAEKIEKAT RKEFPDGIIA HGADALRFTI AALATHGRDI
     KFDLGRAEGY KNFCNKLWNA TRFVLMNTEG ARFTGVPQPR TEAEKWILAR LDKATAETHA
     HYANYRFDLL AQSLYEFAWN AFCDWFVELA KPALNNQDAD AAASTRHTLL YVLESLLRLL
     HPLTPFVTEE LWQQVAPRLG ITTATISLQS FPQPGDVDTS SYATAEADVE WLKSMVSALR
     RVRSELNVPP SKQVRLLLQA GTADDRPRVA RFASQLSFLL KLERIDWLDA GQDTPPSAAA
     IVGELTLLVP LEGLVDMDAE RTRLDKEIKR VEGEIAKCNG KLGSATFVQN APAAVVEQER
     ARLNDWTTQL TGLREQRAKI
//