ID   A0A4Y5WAJ9_9PSED        Unreviewed;       943 AA.
AC   A0A4Y5WAJ9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
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   ORFNames=CCZ28_21925 {ECO:0000313|EMBL:QDD91521.1};
OS   Pseudomonas psychrotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=237610 {ECO:0000313|EMBL:QDD91521.1, ECO:0000313|Proteomes:UP000320313};
RN   [1] {ECO:0000313|EMBL:QDD91521.1, ECO:0000313|Proteomes:UP000320313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS51 {ECO:0000313|EMBL:QDD91521.1,
RC   ECO:0000313|Proteomes:UP000320313};
RA   Asaf S., Kang S.M., Lee I.J.;
RT   "Complete genome sequence of Pseudomonas psychrotolerans CS51.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC         Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR   EMBL; CP021645; QDD91521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y5WAJ9; -.
DR   Proteomes; UP000320313; 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   CDD; cd00817; ValRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02004};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02004};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02004}.
FT   DOMAIN          14..621
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          664..816
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          878..940
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          874..943
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           544..548
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   943 AA;  106504 MW;  2A373FB6B2A7802A CRC64;
     MDKTYQPHAI ETSWYQTWER QGYFAPQGSG EPYTIMIPPP NVTGSLHMGH GFNNAIMDAL
     IRFRRMQGRN TLWQPGTDHA GIATQMLVER RIGAEGLSRH DLGREKFLEK VWEWKNESGG
     NISRQIRRLG SSVDWSRERF TMDDGLSEAV KEAFVRLHEH GLIYRGKRLV NWDTKLHTAI
     SDLEVESHDE KGHLWHLRYP LADGARTAEG VDHLVVATTR PETLLGDAAV AVHPEDPRYK
     DLIGQYVELP LVGRRIPIVA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLINVFDA
     DAAILPGAQV FNLDGSVNGM FDATLPAAYA GLDRFEARKR IVADLDAAGR LEKIEDHALK
     VPKGDRSGTV IEPWLTDQWY VSTKPLADKA IAVVESGEIQ FVPKQYENMY FSWMRDIQDW
     CISRQLWWGH RIPAWYDQAG NVYVGRDEAE VRAKHNLGDI VLRQDDDVLD TWFSSGLWTF
     STLGWPEQTE ALKTFHPTDV LVTGFDIIFF WVARMIMLST HLTGQIPFKT VYVHGLVRDG
     QGQKMSKSKG NVLDPLDIVD GIDLDTLLQK RTSGLMQPKL AEKIAKQTRA EFPDGIASYG
     TDALRFTFCS LATTGRDIKF DMGRVEGYRN FCNKLWNAAN FVMENVEGQD TGVNDEPVEL
     SSVDRWIISQ LQRTEAEVTR QLDAFRFDLA TQALYEFVWD EYCAWYLELV KPVLWDENAS
     LERQRGTRRT LARVLEVVLR LAHPFMPFIT EEIWQRLKAP AGVQGETLML QPWPVANEAR
     IDAAAEGDIE WVKALMLGVR QIRGEMKISM AKRIDIIVAN ASAEDQRRLA DFEPLLNKLA
     KLESVRVLAA GEEAPMSATT LVGEMEVLVP MAGLIDKDAE LARLDKEIGR LEGEVKRVGG
     KLGNEGFVAK APAEVLEKER AKLAEAEQAL AKLVDQQQRI ATL
//