ID   SYV_COLP3               Reviewed;         973 AA.
AC   Q488M6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=CPS_0738;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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_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; CP000083; AAZ27693.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q488M6; -.
DR   SMR; Q488M6; -.
DR   STRING; 167879.CPS_0738; -.
DR   EnsemblBacteria; AAZ27693; AAZ27693; CPS_0738.
DR   KEGG; cps:CPS_0738; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000547; 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; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
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..973
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224464"
FT   COILED          901..970
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           569..573
FT                   /note="'KMSKS' region"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   973 AA;  110937 MW;  F2650EE687C39838 CRC64;
     MLQQNNEQLL NLLPDKMMEK TFNPTDIEQS LYTSWEEQGY FSPTGEGDSY SIAIPPPNVT
     GSLHMGHAFQ QTIMDTLIRY QRMQGKNTLW QTGCDHAGIA TQMVVERKIA AEEDKTRHDY
     GREGFIDKIW EWKEESGGTI GKQMRRLGNS IDWSRERFTM DDGMSEAVQE VFVRLFEDDL
     IYRGKRLVNW DPKFHTAISD LEVENKDKKG HMWHLRYPLA NGAKTAEGLD YLVVATTRPE
     TMLGDTGVAV NPEDPRYKDL IGKQVLLPLV NRLIPIVGDD HADMEKGTGC VKITPGHDFN
     DNEVGKRHAL PQINILDKDA AILATAEVYD TKGEVCNAYD TGLPSEFAGM DRFVARKAIV
     AKFDELGLLV EVKDHDLVAP YGDRSGVIIE PLLTDQWYVR VEKLAGPAVD AVKDGQIEFV
     PKQYENMYFS WMNNIQDWCI SRQLWWGHRI PAWYDENEKV YVGRTEEEVR ANNDIAADMK
     LRQDDDVLDT WFSSALWTFS TLGWPKDTED LKTFHPTDVL VTGFDIIFFW VARMIMMTMH
     FNKDENGKAQ IPFKKIYMTG LIRDENGDKM SKSKGNVVDP LDMIDGISLE DLLQKRTGNM
     MQPKLAKKIE KLTRKEYPEG IEAHGTDALR FTLTSVATTG RDISWDMKRL EGYRNFTNKL
     WNASRYVMMN TEEFDCGQSS PEGKAGDMEL SLADRWIIGQ FEQTVKTVHE AFDTYRFDLA
     SQALYEFTWN QFCDWYLELT KPVLFKENEA QQRGTRHTLV NVLEALLRLM HPIMPFITET
     IWQRVQPLSD FSKNGDSIMV QAFPQFDESK CDQQAIDDLE WVKQFIIAIR NIRGEMDISP
     SKELPVLLKN VNDNDQRRLD ENEQFLSSLA KLESITVLAD DEQGPASASA VVGDLSVLIP
     MAGLIDKEAE LARLDKAIEK LEKEAGRVRG KLGNENFVSK APAAVIEKEQ AKLADAESTL
     AKILEQKIQI AAL