Entry sw: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   02-NOV-2016, entry version 74.
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};
GN   OrderedLocusNames=Psyc_1850;
OS   Psychrobacter arcticus (strain DSM 17307 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / 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.,
RA   Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M.,
RA   Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F.,
RA   Richardson P., 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
RT   low-temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As
CC       ValRS can inadvertently accommodate and process structurally
CC       similar amino acids such as threonine, to avoid such errors, it
CC       has a "posttransfer" editing activity that hydrolyzes mischarged
CC       Thr-tRNA(Val) in a tRNA-dependent manner. {ECO:0000255|HAMAP-
CC       Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val). {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
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site.
CC       {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
DR   EMBL; CP000082; AAZ19698.1; -; Genomic_DNA.
DR   RefSeq; WP_011281108.1; NC_007204.1.
DR   ProteinModelPortal; Q4FQL0; -.
DR   STRING; 259536.Psyc_1850; -.
DR   EnsemblBacteria; AAZ19698; AAZ19698; Psyc_1850.
DR   KEGG; par:Psyc_1850; -.
DR   PATRIC; 23058561; VBIPsyArc98534_2186.
DR   eggNOG; ENOG4105CA4; Bacteria.
DR   eggNOG; COG0525; LUCA.
DR   HOGENOM; HOG000020094; -.
DR   KO; K01873; -.
DR   OMA; SQYRFDL; -.
DR   OrthoDB; POG091H01HY; -.
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-HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 3.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946:SF5; PTHR11946:SF5; 4.
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;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN         1    984       Valine--tRNA ligase.
FT                                /FTId=PRO_0000224541.
FT   COILED      954    984       {ECO:0000255|HAMAP-Rule:MF_02004}.
FT   MOTIF        65     75       "HIGH" region.
FT   MOTIF       579    583       "KMSKS" region.
FT   BINDING     582    582       ATP. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        25    982       ihamap:Val_tRNA_synth_type1 [T]
FT   MYHIT        38    656       ipfam:tRNA-synt_1 [T]
FT   MYHIT       917    982       ipfam:Val_tRNA-synt_C [T]
FT   MYHIT        65     76       ipat:AA_TRNA_LIGASE_I [T]
FT   MYHIT       704    856       ipfam:Anticodon_1 [T]
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
//