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Entry: A0A5C6S361_9BACT
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ID   A0A5C6S361_9BACT        Unreviewed;       904 AA.
AC   A0A5C6S361;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 20.
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=FRY97_02220 {ECO:0000313|EMBL:TXB68905.1};
OS   Phaeodactylibacter luteus.
OC   Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
OC   Haliscomenobacteraceae; Phaeodactylibacter.
OX   NCBI_TaxID=1564516 {ECO:0000313|EMBL:TXB68905.1, ECO:0000313|Proteomes:UP000321580};
RN   [1] {ECO:0000313|EMBL:TXB68905.1, ECO:0000313|Proteomes:UP000321580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42180 {ECO:0000313|EMBL:TXB68905.1,
RC   ECO:0000313|Proteomes:UP000321580};
RA   Bowman J.P.;
RT   "Genome of Phaeodactylibacter luteus.";
RL   Submitted (AUG-2019) 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=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC         diphosphate; 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:ARBA00047552, ECO:0000256|HAMAP-
CC         Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC       Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       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|ARBA:ARBA00060830,
CC       ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TXB68905.1}.
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DR   EMBL; VOOR01000003; TXB68905.1; -; Genomic_DNA.
DR   RefSeq; WP_147165792.1; NZ_VOOR01000003.1.
DR   AlphaFoldDB; A0A5C6S361; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000321580; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   FunFam; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000032; Valine--tRNA ligase; 1.
DR   FunFam; 3.90.740.10:FF:000010; Valine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; NF004349; PRK05729.1; 1.
DR   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   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}; Reference proteome {ECO:0000313|Proteomes:UP000321580}.
FT   DOMAIN          16..581
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          636..777
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          837..901
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          877..904
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           543..547
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         546
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   904 AA;  103413 MW;  43DF8624B0059E7C CRC64;
     MTELSTRYNP QETEEKWYGH WMDKRYFHSE PDDREPYSIV IPPPNVTGVL HMGHMLNNTI
     QDILVRKARL EGKNACWVPG TDHASIATEA KVVKQLREKG IKKSDLSREE FLAHAFEWKD
     KYGGIILDQL KKLGASCDWE RTRFTMEPKL SDAVIKVFVD LYNKGKVYRG LRMTNWDPEA
     LTVLSNEEVL YKEENSRLYY LRYAIEGETD SWITIATVRP ETILGDAAIA VNPDDERFAH
     LVGKRAIVPL INRPVPIIAD RYVDTEFGTG ALKITPAHDM NDYEIGERHG LEVIDVLNDD
     GTMSEAAQLF VGEDRFTARK LIVKALEAAG HLAKTEDYRN KVGRSERTNA IVEPRLTLQW
     FVKMKAFGQQ ALRAVKSGEV KFFPEHFYNM YHSWLNEDNI RDWCISRQLW WGQRIPAWYY
     EDQIFVAETA EAALEKAREA TGKNLSLTDL KQDEDVLDTW FSSQLWPISV FDGFENPEAL
     RYYYPTNVLV TGWDIIFFWV ARMVIMGYEY APELLGEAKA AEGVQPFREV YFTGMVRDKE
     RRKMSKSLGN SPDALALIDR YGADGVRFGM LSSASAGNDI IFDAPFDKET KEVLNESKLC
     EQGRNFCNKM WNALRLIKGW ELADDEPDAV SQLAAQWMEH KLLQTTEKLE QLFAQYRLSE
     ALMTTYKLIW DDFCSWYLEM VKPDYGAPVS AQTVEATVRI FEQLMTLLHP FMPFVTEEIW
     HQLRSRAEGE DCVVSRYPVS APYNAAMIGQ VEQAKTIVAS VREARNAKGI KMKDELNLFA
     QNDESSQDLL SLNGLKAMIV KMANLAKLEV TGEDVPNSVS FLSGQSKFFL ELNQEVDTAE
     ECERLTKELA YQEGFVAQVM KKLGNERFVN NAPEQVVARE RQKLADGEAK IKNLKEELAA
     MGCA
//
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