SYV_PSYA2
ID SYV_PSYA2 Reviewed; 984 AA.
AC Q4FQL0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Psyc_1850;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19698.1; -; Genomic_DNA.
DR RefSeq; WP_011281108.1; NC_007204.1.
DR AlphaFoldDB; Q4FQL0; -.
DR SMR; Q4FQL0; -.
DR STRING; 259536.Psyc_1850; -.
DR PRIDE; Q4FQL0; -.
DR EnsemblBacteria; AAZ19698; AAZ19698; Psyc_1850.
DR KEGG; par:Psyc_1850; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000546; 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; -; 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..984
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224541"
FT COILED 954..984
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 65..75
FT /note="'HIGH' region"
FT MOTIF 579..583
FT /note="'KMSKS' region"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 984 AA; 111720 MW; 2FDC2329FA41E267 CRC64;
MSNPNNIESS KTNLTTSIQA ALSQLENAYN PSEVEAGMYQ GWEDSGYFQP TFDKDESFSI
ALPPPNVTGS LHMGHGFNNA IMDALTRYHR MDGDNTLWQP GTDHAGIATQ MVVERRLEAE
GIKRRDMSRE DFIDKVWEWK EESGGNITRQ IRRLGSSVDW SRERFTMDDG LSNAVKEVFV
RLFDDGLIYR GKRLVNWDPK FQTALSDLEV ENVDEKGSLW HFRYHFTDTD ITTQDGKNYL
VVATTRPETS LGDTAVAVNP KDERYAHLIG KTITLPITGR IVPIVADDYV DIEFGTGCVK
ITPAHDFNDY ELGRRHELPL INILDAHAHI LPAMEVYPDL QTREPTLETT PADYAGLERF
AARKLLVEQA GEQGWLEKIE DYALKAPRAE RGGAIVEPWL TDQWYVAVKE LAQPAIAAVE
DGQIEFVPAQ YKNMYMAWMN GIQDWCISRQ LWWGHRIPAW YDEEGSIYVA RDEAEVRSKY
NLAADVKLRQ DDDVLDTWFS SGLWTFSTLD WADVNADPRV METFHPTSVL VTGFDIIFFW
VARMIMMTMH FVKNEDGTPQ IPFKTVYVHG LVRDGNGQKM SKSKGNVLDP IDIIDGIELE
ALVEKRTSNM MNPKDAAKIE KQTRKEFPEG IPAFGTDALR FTFTSLASTG RDINFDLKRV
EGYRNFCNKI WNASRFVLMN CVDKEGNAQA IDQTANADVW ELPEKWIMSR LNSTITNIHQ
HFDQYRLDMV SHDIYEFIWN EYCDWYVELA KASLNDDSVS DERKAQIRYV LLHVLETALR
FSHPIMPYLT EQIWQTIAPL LNRKETDSIV IAAYPQTDNS QISEQTEADM AWLQELIASV
RNIRGEMKLG NAVRLPVLLQ NISAAEDTRL SRIANQFKAL AKVESLTILK EGDEVPLSSS
SMVGQLRVLV PMKGLIDPTA ELARLGKSYD KLKGQSEGIA RKLGNEGFVS KAPVEVVDAE
KAKLAELEGQ LTAMTAQMEE LKNL
