GenomeNet

Database: UniProt
Entry: A0A0R2CZR9_9LACO
LinkDB: A0A0R2CZR9_9LACO
Original site: A0A0R2CZR9_9LACO 
ID   A0A0R2CZR9_9LACO        Unreviewed;       889 AA.
AC   A0A0R2CZR9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=FC19_GL001576 {ECO:0000313|EMBL:KRM97535.1};
OS   Liquorilactobacillus aquaticus DSM 21051.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423725 {ECO:0000313|EMBL:KRM97535.1, ECO:0000313|Proteomes:UP000051015};
RN   [1] {ECO:0000313|EMBL:KRM97535.1, ECO:0000313|Proteomes:UP000051015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21051 {ECO:0000313|EMBL:KRM97535.1,
RC   ECO:0000313|Proteomes:UP000051015};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRM97535.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AYZD01000001; KRM97535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2CZR9; -.
DR   STRING; 1423725.FC19_GL001576; -.
DR   PATRIC; fig|1423725.3.peg.1618; -.
DR   Proteomes; UP000051015; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing 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}.
FT   DOMAIN          23..572
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          615..761
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          821..885
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          819..889
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           532..536
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   889 AA;  102391 MW;  911A9E4DCAD6DB51 CRC64;
     MILMTKDVAM STKYDPKQVE PGRYQEWLDQ GLFKPSGDKK AKPYSIVIPP PNVTGKLHLG
     HAWDTTLQDM IIRQKRMQGF DTLWLPGMDH AGIATQSKVE ARLAEQGVSR YDLGREKFID
     TVWKWKDEYA DIIHKQWAKL GLSLDYDRER FTLDEGLSQA VRKVFVKLYQ KGLIYRGEYI
     INWDPKARTA LSDIEVIHKD VKGAFYHVKY PFADGTTFNG KNYIEIATTR PETMMGDVAV
     AVHPSDERYK DIVGKTLILP LQGRHIPIIA DEYVDPQFGT GMVKITPAHD PNDFGVGNRH
     DLKRINTMNE DASMNANAGK YEGMDRFEAR KAIVKDLEDQ DYMLRIEPIV HSVGHSERTG
     VQVEARLSTQ WFVKMEPLAK AALANQKTDD PVKFVPERFE NTFEQWMNNI HDWVISRQLW
     WGHQIPAWYH KETGEVYVGE EAPKDIENWE QDPDVLDTWF SSALWPFSTM GWPDENAADF
     KRYFPTDTLV TGYDIIFFWV SRMIFQSVEF TERRPFEHVL IHGLIRDEQG RKMSKSLGNG
     IDPMDVIDKY GADALRWFLS NGSAPGQDVR FSYTKMDAAW NFINKIWNAS RFVIMNLDDD
     TRAELPEKAV WKLSDKWIIS RLNHTIAEVT RLFDGFEFGE AGRALYNFIW NDFCDWYIEM
     AKEDLNGDDQ AAKKNTQNIL CFVLDQTVRL LHPIMPFVTE KIWLSMPHTG TSLVTASYPT
     VVADYDDPQA EREMDNLIEL IKAVRNSRAE VNAPLSSAVD ILIKTKDDQT KQVFEANKDY
     IERFCHSKKL EIAATIDAPA LAMTSVITGA EVYLPLADLV DLNEEIKRLQ KDVKKLTSEV
     KRAESKLSNQ RFVTNAPTEI VEQEREKLSG YKEKLTATNE RIKELEKEL
//
DBGET integrated database retrieval system