(data stored in ACNUC7421 zone)

SWISSPROT: SYV_ALCBS

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   11-DEC-2019, entry version 89.
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=ABO_0492;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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}.
DR   EMBL; AM286690; CAL15940.1; -; Genomic_DNA.
DR   STRING; 393595.ABO_0492; -.
DR   PRIDE; Q0VSA8; -.
DR   EnsemblBacteria; CAL15940; CAL15940; ABO_0492.
DR   KEGG; abo:ABO_0492; -.
DR   eggNOG; ENOG4105CA4; Bacteria.
DR   eggNOG; COG0525; LUCA.
DR   HOGENOM; HOG000020094; -.
DR   KO; K01873; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000008871; 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   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;
DR   PRODOM; Q0VSA8.
DR   SWISS-2DPAGE; Q0VSA8.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..931
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022162"
FT   COILED          859..931
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           523..527
FT                   /note="'KMSKS' region"
FT   BINDING         526
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
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
//

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