ID   SYV_CUTAK               Reviewed;         870 AA.
AC   Q6A7F4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=PPA1568;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT83311.1; -; Genomic_DNA.
DR   RefSeq; WP_002531079.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A7F4; -.
DR   SMR; Q6A7F4; -.
DR   STRING; 267747.PPA1568; -.
DR   EnsemblBacteria; AAT83311; AAT83311; PPA1568.
DR   KEGG; pac:PPA1568; -.
DR   PATRIC; fig|267747.3.peg.1613; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000000603; 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; 3.40.50.620; -; 2.
DR   HAMAP; MF_02005; Val_tRNA_synth_type2; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..870
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224612"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           63..73
FT                   /note="'HIGH' region"
FT   MOTIF           595..599
FT                   /note="'KMSKS' region"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   870 AA;  97279 MW;  B5DFC14C31ABB64D CRC64;
     MTSQTFTTSS ATPPTRGVVP DKPALEGLEV KWGKIWEDEQ LYAFDATTVD SREQVFAIDT
     PPPTVSGHLH PGHVFSYTHT DTVARYQRMR GKKVFYPMGW DDNGLPTERR VQNYYGVRCD
     PSLPYDPDFT PPSKPNPKRQ VPISRRNFVE LCVELTAVDE KTFQDLWRAV GLSVDWNQLY
     TTISPESQRI AQLAFLRNYA RGEAYLSDAP TLWDVTFSTA VAQAELEARD YPGAYHRLGF
     HRPNGEDVFI ETTRPELLAA CCALIAHPDD ERYQHLFGTT VTTPLYGVEV PVLAHSAAEM
     DKGAGIAMCC TFGDLTDVAW WRELQLPTRT IIGRDGRILS ETPQWIIDAG SAERYEAIAG
     KTTFTARKLV VEALVESGEM DGEPKPTQRK ANFYEKGDKP LEIIGTRQWY IRNGGRDDDL
     RNALLERGRE LEWVPEHMRH RYENWVEGLN GDWLISRQRF FGVPFPVWYP LGTDGEPDYD
     HPLLPDESAL PVDPASQPPS GYQESQRGVA GGFIGDPDVM DTWATSSLTP QIVTGWERDA
     DLFAKTFPMD FAPEAHDIIR TWVFSRVVRA HLENGMLPWK RAAISGFVTD PDRKKMSKSK
     GNTVVPTEII DQFGADAVRW RAAMARPGMD SPFDKAQMKV GRRLAMKILN ASKFVLGFGE
     GGQVCDITNP ADLSMLAGLR ELIAEATEAF DKFNYTAALE VCEQFFWTFC DDYLELIKER
     AYDSEGADNA GALSARTALR LALDVMLRLF APFLPFVTEE VWSWWKDGSV HTSSWPTADE
     VPATGDVDLM SDVSAALVEL RGVKSTHKVP MRTPILSARI SAPASVIANL KAVESDLTKV
     SKTESLTFLT GGDKLVLEAE LGEPPAKRKK