ID   A0A068NEW0_9ACTO        Unreviewed;       880 AA.
AC   A0A068NEW0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-FEB-2023, entry version 45.
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:AIE81987.1};
GN   ORFNames=FB03_00410 {ECO:0000313|EMBL:AIE81987.1};
OS   Actinotignum schaalii.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinotignum.
OX   NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE81987.1, ECO:0000313|Proteomes:UP000035032};
RN   [1] {ECO:0000313|EMBL:AIE81987.1, ECO:0000313|Proteomes:UP000035032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE81987.1,
RC   ECO:0000313|Proteomes:UP000035032};
RX   PubMed=25189588;
RA   Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA   Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA   Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL   Genome Announc. 2:e00880-14(2014).
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|HAMAP-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; CP008802; AIE81987.1; -; Genomic_DNA.
DR   RefSeq; WP_026428500.1; NZ_CP008802.1.
DR   AlphaFoldDB; A0A068NEW0; -.
DR   EnsemblBacteria; AIE81987; AIE81987; FB03_00410.
DR   KEGG; asg:FB03_00410; -.
DR   Proteomes; UP000035032; 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   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}.
FT   DOMAIN          30..114
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          141..638
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          682..827
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          494..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..880
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           600..604
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   BINDING         603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   880 AA;  98663 MW;  B185192063A820B6 CRC64;
     MTSFNQESEL LDHTEVPDRA TLDGLETTWG KRWEEEGTYA FDRTATRSEV FSVDTPPPTV
     SGSLHIGHVF SYTHTDTVAR YQRMRGKSVF YPMGWDDNGL PTERRVQNYY GVRGDASLPY
     DPNFVPPHQG GAKSIKYADQ VPISRRNFIE LCWKLSEEDE KQFEALWRYL GLSVDWKQNY
     QTIGEKAQKV AQTAFLRNLA RGEAYQAQAP GLWDITFQTA VAQAELEARD YPGAYHALAF
     HGASGDVVIE TTRPELLPAC VALIAHPEDT RYQHLFGTTV RVPIFDMEVP VLAHPKAEMD
     KGAGIAMCCT FGDVTDVEWW RELQLPLHNV LGKDGRLVRD TPEWITSEAG RAMYAEMAGK
     TTFSARKALV EKLKETGEMI GDEKPTMRKT NFFEKGDKPL EIVTSRQWYI RNGGRSHVES
     NGKELRDNLI EAGNQLAFHP DFMHVRYDNW VKGLNSDWLI SRQRFFGVPI PVWYEISENG
     EVKYDAVITP EESRLPVDPS SDVPAGYTED QRGKPGGFAG ETDILDTWAT SSLSPQIAGG
     WLTDEDLFER VYPMDVRPQG QDIIRTWLFS TVVRAHLEFG ELPWKHATIS GWILDPDHKK
     MSKSKGNVVT PMDLLVRHGA DAVRYWAASA RLGVDAAFDE KQMKVGRRLA MKVLNASKFA
     LGMGGEGSPV CLDASRVTEP IDRALLADLA RVVEEATSAF EAFDHTRALE AAETAFWTFC
     DDYLELVKDR AYSDTPEAES ARVTLAIAVD TFLRLLAPFI PYATAEVWSW YRTGSVHRAA
     WPEAAPLREA AGSGNAELLE VAGQALTVLR GVKSAAKVSQ RTSFARVELR GHTALLEEVR
     GDLVRAAHVR GELRFTPDTE ASEQITIGDY ELDEPEPKRK
//