(data stored in SCRATCH zone)

SWISSPROT: D3UW85_XENBS

ID   D3UW85_XENBS            Unreviewed;       965 AA.
AC   D3UW85;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02004,
GN   ECO:0000313|EMBL:CBJ79594.1};
GN   OrderedLocusNames=XBJ1_0444 {ECO:0000313|EMBL:CBJ79594.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79594.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79594.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79594.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|HAMAP-
CC       Rule:MF_02004, ECO:0000256|SAAS:SAAS00889227}.
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,
CC         ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537,
CC         ChEBI:CHEBI:456215; EC=6.1.1.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02004, ECO:0000256|SAAS:SAAS01116702};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00889229}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00889155}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00889246}.
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DR   EMBL; FN667741; CBJ79594.1; -; Genomic_DNA.
DR   RefSeq; WP_012987050.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0444; -.
DR   EnsemblBacteria; CBJ79594; CBJ79594; XBJ1_0444.
DR   GeneID; 8830067; -.
DR   KEGG; xbo:XBJ1_0444; -.
DR   PATRIC; fig|406818.4.peg.410; -.
DR   eggNOG; ENOG4105CA4; Bacteria.
DR   eggNOG; COG0525; LUCA.
DR   HOGENOM; HOG000020094; -.
DR   KO; K01873; -.
DR   OMA; FATKLWN; -.
DR   BioCyc; XBOV406818:XBJ1_RS01945-MONOMER; -.
DR   Proteomes; UP000002045; 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; -; 1.
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; D3UW85.
DR   SWISS-2DPAGE; D3UW85.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711227,
KW   ECO:0000313|EMBL:CBJ79594.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711241};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00889220};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00889138};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711254,
KW   ECO:0000313|EMBL:CBJ79594.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711287};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711230};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       28    645       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      688    839       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      900    958       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      896    923       {ECO:0000256|HAMAP-Rule:MF_02004}.
FT   MOTIF        56     66       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   MOTIF       568    572       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   BINDING     571    571       ATP. {ECO:0000256|HAMAP-Rule:MF_02004}.
SQ   SEQUENCE   965 AA;  109987 MW;  542492B058451C4A CRC64;
     MEKTPANQTQ SEPSLDKTYN PTEIEQPLYN HWEKNGYFKP NGDTSRESFC IVIPPPNVTG
     SLHMGHAFQQ TIMDTMVRYQ RMQGKNTLWQ AGTDHAGIAT QMVVERKIAA EEGKTRHDYG
     RDAFIDKIWQ WKAESGGNIT NQMRRLGNSV DWERERFTMD EGLSKAVKEA FVRLYQEDLI
     YRGKRLVNWD PKLRTAISDL EVENREVKGS MWHLRYPLAD GAKTAEGKDY LIVATTRPET
     LLGDTGVAVN PEDPRYKDLI GKEIILPLMN RRIPILGDEH ADMEKGTGCV KITPAHDFND
     YEVGKRHSLP MINILTFDGD IRDEAEIFDT NGESSDVYSA DIPAEYRGME RFAARKAIVA
     EFEKQGLLVE TKPHDLTVPY GDRGGVVIEP MLTDQWYVRT APLAKVALEA VENGDIQFVP
     KQYENMYYSW MRDIQDWCIS RQLWWGHRIP AWYDAQGNVY VGRDEEEVRR ENNLSADITL
     TQDEDVLDTW FSSGLWTFST LGWPEQTEAL KTFHPTNVLV SGFDIIFFWI ARMIMMTMHF
     IKDENGKPQV PFKTVYMTGL IRDDEGQKMS KSKGNVIDPL DMIDGISLEN LLEKRTGNMM
     QPQLAEKIGK RTEKQFPEGI EAHGTDALRF TLAALASTGR DINWDMKRLQ GYRNFCNKLW
     NASRFVLMNT EGQDCGQNGG EMSLSLADRW ILAEFNQTVK TYREALDTYR FDIAANILYE
     FTWNQFCDWY LELSKPAINK GSEAEVRAAR HTLIEVLEGL LRLAHPIIPF ITEIIWQRVK
     VVKGINADTI MLQPFPEFDQ TKVDELALND LEWIKEAIIA VRNIRAEMNI APSKPLEVLL
     RDANADAQRR VAENLNFIQS MGRLTSVTVL AAGEEAPVSV TKLINGTEIL IPMAGLIDKD
     VELARLDKEI EKLDKEINAI EAKLANDGFV SRAPEAVVAK ERERLAINHA AKEKLLAQKE
     TIAAL
//

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