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Database: UniProt
Entry: B8DWV2_BIFA0
LinkDB: B8DWV2_BIFA0
Original site: B8DWV2_BIFA0 
ID   B8DWV2_BIFA0            Unreviewed;       930 AA.
AC   B8DWV2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE            Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02005,
GN   ECO:0000313|EMBL:ACL28953.1};
GN   OrderedLocusNames=BLA_0660 {ECO:0000313|EMBL:ACL28953.1};
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL28953.1, ECO:0000313|Proteomes:UP000002456};
RN   [1] {ECO:0000313|EMBL:ACL28953.1, ECO:0000313|Proteomes:UP000002456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011 {ECO:0000313|EMBL:ACL28953.1,
RC   ECO:0000313|Proteomes:UP000002456};
RX   PubMed=19011029; DOI=10.1128/JB.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(2009).
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_02005}.
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_02005};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005}.
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_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR   EMBL; CP001213; ACL28953.1; -; Genomic_DNA.
DR   RefSeq; WP_004219130.1; NC_011835.1.
DR   AlphaFoldDB; B8DWV2; -.
DR   STRING; 442563.BLA_0660; -.
DR   GeneID; 66533793; -.
DR   KEGG; bla:BLA_0660; -.
DR   PATRIC; fig|442563.4.peg.688; -.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000002456; 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; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   InterPro; IPR048044; Valyl-tRNA_ligase_actino.
DR   NCBIfam; NF000540; alt_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; 2.
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; 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_02005};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02005};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02005};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02005};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02005}; Reference proteome {ECO:0000313|Proteomes:UP000002456}.
FT   DOMAIN          29..114
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          138..636
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          691..847
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          889..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   MOTIF           601..605
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   BINDING         604
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   930 AA;  104812 MW;  460D56B35490B424 CRC64;
     MTDSEDYSIN ANLTALPDRV GVDGLEAKWR KVWDEDGTYT FHDPGERKAV YSIDTPPPTV
     SGHLHVGHVF SYTHTDIIAR FKRMNGYEVL YPMGWDDNGL PTERRVQNYY GVRVDTSLKY
     DPDFVPPFEG TEGKKIQAKD QVPISRKNFI ELCEKLTAQD EKQFEELWRQ LGLSIDWKQT
     YHTIGEYPQR VAQKAFLRNL ERGEAYQKDA PGLWDVTFQT AVAQAELESR EYPGFYHRIA
     FRFEETGEPI YIETTRPELL PACVALIAHP DDERYKPYFG KMVTSPLFNV KVPVLAHPAA
     EKDKGAGIAM CCTFGDMTDV EWWRDLHLPT RSIIQRNGRI VMDTPDWIHD EKGRQYFAGL
     AGKTTFSARK QIVEDLQETG DMDGEPKPTM RMTNFYEKGD KPLEIVTSRQ WYLENGGTNK
     ALNTELIERG KELNFHPDFM RVRYENWVHG LNGDWLISRQ RFFGVPFPLW YPLDANGEPD
     YSNPLTPSED RLPIDPTIDV PEGYGEDQRD QPNGFMAEPD IMDTWATSSL TPQIVTKWAE
     PGEENERFFK STFPMDLRPQ GQDIIRTWLF STIDRADLEN HCLPWANATL SGWILDPDHK
     KMSKSKGNVV VPNKPIEQFG ADAVRYWAAS ARLGLDATYD EGQMKIGRRL AIKLLNATKF
     ALAIGREDEN HHVGEGATAS WDPKDVTEPL DRAAMAKMAK VVYDATESLN NYEHSKALET
     IEDFFWQFCD DYIELVKNRA YGTAESTGVE PSPQAVKSAR TTLGLGLDAF ARLLAPFLPY
     TTEEVWSWMH AGEGSVHHAP WPKPITYATA AFKASPELLT QAGAALTALR GIKSKAKVSM
     KTPILSVMLN VNDELHDALA PALGDIAEAA RVTGRISLQK ASDLMAKFAR PKGEGTAAPG
     PASDETDVEE ITVVESELGE PPVKKPKAAQ
//
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