ID   SYV_SYNY3               Reviewed;         910 AA.
AC   Q55522;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=slr0557;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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_02004}.
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_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; BA000022; BAA10881.1; -; Genomic_DNA.
DR   PIR; S76034; S76034.
DR   AlphaFoldDB; Q55522; -.
DR   SMR; Q55522; -.
DR   IntAct; Q55522; 2.
DR   STRING; 1148.1001391; -.
DR   PaxDb; Q55522; -.
DR   EnsemblBacteria; BAA10881; BAA10881; BAA10881.
DR   KEGG; syn:slr0557; -.
DR   eggNOG; COG0525; Bacteria.
DR   InParanoid; Q55522; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; Q55522; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR11946; PTHR11946; 1.
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; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..910
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106237"
FT   COILED          845..909
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           539..543
FT                   /note="'KMSKS' region"
FT   BINDING         542
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   910 AA;  102737 MW;  4D909BCD889BF42E CRC64;
     MTTSLPPQYE PTVTEAKWQT AWEESHAFKA DPDRPGEPYC VVIPPPNVTG SLHMGHAFES
     SLIDTLVRYH RMRGDNTLWL PGTDHASIAV QTILERQLKA EGKTRDDLGR EKFLERAWQW
     KAESGSTIVN QLRRLGVSVD WTRERFTMDE GLSQAVKTAF IKLYEEGLIY RGNYLVNWCP
     ASQSAVSDLE VENQEVDGHL WYFRYPLTDG SGELVVATTR PETMLGDTGV AVNPHDERYA
     AMVGKTITLP LVNREIPIVA DELVDPEFGT GCVKVTPAHD PNDFVMGQRH NLPFINLLNK
     DGSLNENGGD FAGQDRFEAR KNVVQALEAQ GFLVKIEPYR HSVPYGDRGK VPVEPLLSTQ
     WFVKIESLAQ NALACLDEDN SPNFVPERWG KVYRDWLVKL KDWCISRQLW WGHQIPAWYV
     ISETNGAITD HTPFIVAYDE AEALAKAKAE YGPTVQLQQD PDVLDTWFSS GLWPFSTMGW
     PEQTDDLAKY YPTSTLVTGF DIIFFWVARM TMMAGHFTGQ IPFKDVYIHG LVRDENGKKM
     SKSANNGIDP LLLINKYGTD ALRYTLIREV AGAGQDISLQ YDRQKDESES VEASRNFANK
     LWNAARFVMM NLDGQTPQQL GLAPGEDLEL ADRWILSRLN QVIQQTREQI EDYGLGEAAK
     GLYEFIWGDF CDWYIELAKP RLWNKEGGDV GTQRQLVARQ VLAHTLDSII KLLHPFMPHI
     TEELWQTLHQ AEGQFLALQA YPTVNQSLVD PALETQFALL IETLRTIRNL RAEAGIKPGA
     MVTVILQSEN DQERQTLQLG ETYIRDIGKV ENLQVVSQLP PEQTQAIAGV VDTIQVLIPL
     SGLVDLDILR NKIQKTLDKV TKEYESIEKR LSNPGFVNKA PEEVIAGAKE SLNAAAVQRQ
     MLQERLKMLG