SYV_SALAI
ID SYV_SALAI Reviewed; 862 AA.
AC A8LVI6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=Sare_0019;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) 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:0000255|HAMAP-Rule:MF_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; CP000850; ABV95955.1; -; Genomic_DNA.
DR RefSeq; WP_012180268.1; NC_009953.1.
DR AlphaFoldDB; A8LVI6; -.
DR SMR; A8LVI6; -.
DR STRING; 391037.Sare_0019; -.
DR EnsemblBacteria; ABV95955; ABV95955; Sare_0019.
DR GeneID; 5707365; -.
DR KEGG; saq:Sare_0019; -.
DR PATRIC; fig|391037.6.peg.19; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
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; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..862
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000088570"
FT REGION 459..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 574..578
FT /note="'KMSKS' region"
FT BINDING 577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 862 AA; 96426 MW; 93E8545378045A97 CRC64;
MPAKASLEGI EQVWSRVWEQ NGTYRFDRSV TRDEVYSIDT PPPTVSGALH VGHVFSYTHA
DAIARFQRMR GKMVFYPMGW DDNGLPTERR VQNYYGVQCD PSLPYDPGYT PPTEPPGRPQ
PISRRNFVEL CRNLTKIDEQ AFEALWRHLG LSVDWSLTYA TIDDRSRAIS QRAFLRNLAR
GEAYLADAPT LWDVSFRTAV AQAELEDRER QGHYYRLSFT SAAGDTIHVE TTRPELLPAC
VALVAHPDDK RYQHLFGSTA VTPVFRVPVP IKAHPLAQPD KGSGIAMICT FGDLTDVLWW
RELALPTRPV MGRDGRLLPE PPPGITNAEA VAAYRTLAGL TAFSAKAKMV ELLRASGDLA
GDPQPTAQAV KFYEKGDKPL EIVTTRQWYV RNGGRNAQLR AALIRRGREL SWSPRFMRSR
YENWVEGLAG DWIISRQRFF GVPIPVWYPL DDSGEPDYER PILPDDAALP VDPSSDTPTG
YHDSQRHQPG GFMADPDVMD TWATSSLTPE IAGGWTVDDD LFGRVFPMDL RPQAHEIIRT
WLFATMLRSH QEFDRLPWRT ALLSGWILDP DRKKMSKSKG NSVVTPMSLL AEYGSDAVRY
WAVSGRPGTD TAFDTGQMKI GRRLAIKILN ATKFVLRFES PTLRAPHVAH VTEPLDRSML
ARLADVVAAA TTGFTQYDYT RSLECTEHFF WSFCDDYLEL VKERAYGNPD DPAVRSAHAA
LALALRTLLR LFAPMLPFVT EEAWSWWQEG SVHRASWPAR QELVGDADGV DRANRIDETN
GSDEAVEDLL GLASGVLAAI RRAKSEAKQS MRASVARLTL RGRASDLAAF ALVSRDVRAA
GVVRDVDTAE ADVPLTPEIT LG
