ID   SYV_ALCBS               Reviewed;         931 AA.
AC   Q0VSA8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Valyl-tRNA synthetase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valine--tRNA ligase;
DE            Short=ValRS;
GN   Name=valS; OrderedLocusNames=ABO_0492;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 (By
CC       similarity).
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM286690; CAL15940.1; -; Genomic_DNA.
DR   RefSeq; YP_692212.1; -.
DR   GeneID; 4211958; -.
DR   GenomeReviews; AM286690_GR; ABO_0492.
DR   KEGG; abo:ABO_0492; -.
DR   NMPDR; fig|393595.12.peg.489; -.
DR   HOGENOM; Q0VSA8; -.
DR   OMA; Q0VSA8; TDQWYVS.
DR   BioCyc; ABOR393595:ABO_0492-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02004; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR002303; Val-tRNA_synth_Ia.
DR   InterPro; IPR011321; Val-tRNA_synth_Ia_C.
DR   InterPro; IPR019754; Val-tRNA_synth_Ia_N.
DR   InterPro; IPR019499; Val-tRNA_synth_Ia_tRNA-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.287.380; Val-tRNA_synth_Ia_C; 1.
DR   PANTHER; PTHR11946:SF5; tRNA-synt_val; 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   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.
FT   CHAIN         1    931       Valyl-tRNA synthetase.
FT                                /FTId=PRO_1000022162.
FT   COILED      859    931       Potential.
FT   MOTIF        42     52       "HIGH" region.
FT   MOTIF       523    527       "KMSKS" region.
FT   BINDING     526    526       ATP (By similarity).
SQ   SEQUENCE   931 AA;  105906 MW;  D41D1B42071748B5 CRC64;
     MIMDKTYQPD RIEQSWYENW EQAGHFKPSG QGDPFCIMIP PPNVTGSLHM GHAFQDTIMD
     TLVRYRRMQG RNTLWQVGTD HAGIATQMVV ERKLAGEGTN RHELGREKFL DKVWEWKRES
     GGTITRQLRR MGASVDWTRE RFTMDDGLSN AVREVFVRLH KEGLIYRGKR LVNWDPALHT
     AISDLEVENV EEQGHMWHFR YPLSDGSGHL VVATTRPETM LGDTAVAVHP QDPRYKDMIG
     KSIRLPLADR NIPIIADDYV DPDFGSGCVK ITPAHDFNDY EVGKRHDLPM INILTIDAAL
     NDEVPEGYRG LDRVEARKKV VDDLDALGLL EKVDDHTLQV PRGDRSGVVI EPYLTDQWFV
     AVEELAKPAI AAVENGDIQF VPKNYENMYF SWMRDLQDWC ISRQLWWGHR IPAWYDADGN
     VYVGRDEEEV RAENNLGDTP LSQDDDVLDT WFSSALWTFS TLGWPDDTDA LRTFHPTDVL
     VTGFDIIFFW VARMIMMTLK FTDQVPFKKV YVHGLVRDND GQKMSKSKGN VLDPLDMIDG
     ITLDALIDKR TKGLMQPQKE KQITKRTNKD FPDGINPYGT DALRFTFLSL ASTGRDIKWD
     MGRIEGYRNF CNKIWNAARY VMMNTEGEDC GIDTDSEVEL SLADRWIISA LQRAELEVSE
     ALDSFRFDVA SHAAYEFIWN EYCDWYLELS KPVLWGDEYS DAQKRGTRRT LVTVLEAILR
     MAHPFMPFIT EEIWQKVGPL AGKASAAGKG EKTDTIMLQP FPASEPAKID TNAETGAEWV
     KAVISAVRNI RGEMGIPLGK ALPIYLHNGK DSDKALLDAN RVFLCKLAKL ESITWLTAED
     SAPASATALV GDMEILVPMA GLIDKEAEIE RLSKEIEKLR KEVGRAEGKL KNPKFVDKAP
     QAVVDKEKAK LDDYRSQLAK LEEQLEKIKY L
//