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Database: UniProt
Entry: A0A495ADA8_9BACI
LinkDB: A0A495ADA8_9BACI
Original site: A0A495ADA8_9BACI 
ID   A0A495ADA8_9BACI        Unreviewed;       882 AA.
AC   A0A495ADA8;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
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   ORFNames=D8M06_03725 {ECO:0000313|EMBL:RKQ37918.1};
OS   Oceanobacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ37918.1, ECO:0000313|Proteomes:UP000269301};
RN   [1] {ECO:0000313|EMBL:RKQ37918.1, ECO:0000313|Proteomes:UP000269301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ37918.1,
RC   ECO:0000313|Proteomes:UP000269301};
RX   PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA   Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA   Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT   "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT   bacterium from a hypersaline lake.";
RL   Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC         Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKQ37918.1}.
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DR   EMBL; RBZP01000001; RKQ37918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495ADA8; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000269301; Unassembled WGS sequence.
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   CDD; cd00817; ValRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 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   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02004};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02004};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_02004};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02004};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000269301}.
FT   DOMAIN          22..565
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          609..754
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          815..880
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          813..882
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           526..530
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         529
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   882 AA;  103150 MW;  64E5F131FF3702D6 CRC64;
     MSEKEYSALP PKYNPQEVEK GRYQFWLEGK FFEAKDDPEK EPYSIVIPPP NVTGKLHLGH
     AWDTTMQDTI SRMKRMQGYD VLWLPGMDHA GIATQAKVEA KLKEQGTNRY ELGREKFLEQ
     AWEWKGEYAD FIRSQWEKLG LGLDYSRERF TLDDGLSDAV KEVFVKLYEK ELIYRGEYII
     NWDPTTQTAL SDIEVIYEEV QGKFYHMKYP IKDSDETIEI ATTRPETMLG DTAVAVHPKD
     ERYQHLIGKT VILPIVGREI EIVADEYVDM ELGSGAVKIT PAHDPNDFEI GNRHDLKRIL
     VMNEDGSMNE NAQGYKGLDR FECRKQIVKD LQDMGVLFNI EERVHQVGHS ERSGAVVEPY
     LSTQWFVNMQ PLADAVVEMQ NSDERVNFVP ERFERTYLNW MENIRDWCIS RQLWWGHRIP
     AWYHKETGEV YVGKEAPEDI ENWEQDEDVL DTWFSSALWP FSTMGWPDTE SEDFKRYFPT
     DVLVTGYDII FFWVARMIFQ SKEFTGKRPF KDVLMHGLIR DSEGRKMSKS LGNGVDPMDV
     IDKYGADSLR YFLLTGSTPG QDLRFYWEKV ESTWNFANKV WNASRFSLMN MEGFTYDDID
     LSGEKTLADK WILTRLNETI EQVTKNNDKY EFGEAGRHLY NFIWDELCDW YIEMAKLPLY
     GEDEAKKKTT RSVLAYVLDQ TMRMLHPFMP FITEEIWQKL PHQGDSITVA EWPKVREEFH
     DEKASNEMKR LVSIIKSVRN IRAEVDTPMS KQIKMLVEAE NKAIVEELEK NRVYLENFCN
     PSELSIAQDL DIPEKAMSAV VTGAEIFLPL EGLIDFDKEM KRLEKELEKW NKEVERVQKK
     LSNQGFVSKA PEAVVDEERR KEQDYLDKQA KVKARLAELQ NN
//
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