SYV_PHOPR
ID SYV_PHOPR Reviewed; 953 AA.
AC Q6LUW1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
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=PBPRA0483;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG18914.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR378664; CAG18914.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041393870.1; NC_006370.1.
DR AlphaFoldDB; Q6LUW1; -.
DR SMR; Q6LUW1; -.
DR STRING; 298386.PBPRA0483; -.
DR EnsemblBacteria; CAG18914; CAG18914; PBPRA0483.
DR KEGG; ppr:PBPRA0483; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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; -; 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..953
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224527"
FT COILED 884..953
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 953 AA; 108244 MW; 2AC58F6B9D199594 CRC64;
MEKTYNPQSI EQALYQRWEE AGYFKPHGDT SKDAYSIMIP PPNVTGSLHM GHAFQDTIMD
TLIRAERMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKAE
SGGTITKQLR RLGASVDWDR ERFTMDDGLS AATQEVFVRL FEEDLIYRGK RLVNWDPKLH
TAISDLEVES KDKKGFMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
RYKDLIGKQI KLPIVGRLIP IVGDEHADMD KGTGCVKITP AHDFNDYEVG KRHSLPMINI
LTFNADIRDA AEVFDTNGEA NDAYNSELPA KYHGMERFAA RKAIVAEFDE LGLLEEVKDH
DLTVPYGDRG GVAIEPMLTD QWYVRTAPLA APAVKAVEDG QIQFVPKQYE NMYFAWMRDV
QDWCISRQLW WGHRIPAWYD NYGKVYVGRT EDEVREKNNL ASVVVLRQDD DVLDTWFSSA
LWTFGTQGWP ENTDALKTFH PSEVLVSGFD IIFFWVARMI MMTMHFVKDE EGNAQVPFKT
VYMTGLIRDE NGDKMSKSKG NVLDPIDMID GIGLEELVEK RCGNMMQPKL AAKIEKQTRK
AFEGGIEPYG TDALRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVLMNTEEHD
CGMAEGAELE FSLADQWITS QFEVAAKEFN AHLDNYRLDM AANTLYEFIW NQFCDWYLEL
TKPVLWKGTE AQQRATRYTL ITVLEKTLRL AHPILPYITE SIWQSVKPLV DGVEGETIMT
QALPQFNEDN FNADVVADLE WVKAFITSIR NLRAEYDIAP SKGLDVMIKV ADEKDAARIQ
ANEIVLTSLA KLDSIKVLAK NEETQACATS LVGKSELMIP MAGLIDKDAE LARLDKEVAK
TQGEIKRIEG KLNNQGFVAK APEVVITKER EKLEGYQETL VKLEAQKETI AAL
