ID   SYV_ANAMM               Reviewed;         823 AA.
AC   Q5P9M8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=AM1170;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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_02005}.
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_02005};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR   EMBL; CP000030; AAV87002.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5P9M8; -.
DR   SMR; Q5P9M8; -.
DR   KEGG; ama:AM1170; -.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
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; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..823
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224606"
FT   MOTIF           52..62
FT                   /note="'HIGH' region"
FT   MOTIF           549..553
FT                   /note="'KMSKS' region"
FT   BINDING         552
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   823 AA;  94004 MW;  C8F916707C698F84 CRC64;
     MNVRVRHFMQ SLDSRYQHKT VEEECNAAWD EHKIYKWKGN VAQSFVIDTP PPTVSGVLHM
     GHVFSYCHTD FIARYQRMAG KDVFYPIGFD DNGLPTERLV EKIKKLRAVQ LERAEFTKMC
     REVSHEFRTK FRNLFRRLGI SYDWALEYHT VSEEVQRLSQ ASFLDLYAKD KLYRKQQPIL
     WDTVDCTAIA HAEVEELDLH SHLNTISFHT VGGEKIDIAT TRPELIPACV ALFFNPEDDR
     YTHLHGQFAV VPVGGHKVKI LPDDKVRIDK GTGLVMCCTF GDETDVYWWR THNLDTKTIV
     SRTGHIVDLA EDTPDAKIPA AQFDGMHVQK ARKAVCDALE GAGLLVSQEP IVHTVKCAER
     SGAPIEILLS HQWFVRVMEH KHELLEQVQK VQWHPDSMRK RMEIWIENLN WDWCISRQRY
     FGVPFPVWYS KREGEVGKVL LPDVRDLPVD PLRDLPSGYG RDEVEPDVDV MDTWATSSIS
     PQFLTKSVGQ VLRNENLEPL FPTDLRAQSH EIIRSWAFYT MLKSYYHNGE IPWQNIMISG
     WCLAEDKTKM SKSKGNAMDP ESTLDLYGAD SVRYWAAKSR LGADTVFSEE VLKTGRRLTT
     KLWNASKFVA TFFLRDNPPA GTTAAPTDLW ILSKLHKAVA HNTENLKLFE YCAALNRTEE
     FFWKDFCDNY LELVKHRAYN HGSAHGHASA VSTLHHTLKT LLLLFAPFLP YVTEAVYGTL
     FSGCIHAQEW PNADEIPYNA SLEQHGDALI KIVEEVRKAK THAQVSVKYP VELITIGGLA
     TDFPESMLED LKHMCCAEQI KLTAPDSTEL EVAVTLAPTV SSN