ID   A0A068NEW0_9ACTO        Unreviewed;       880 AA.
AC   A0A068NEW0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-MAY-2019, entry version 31.
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;
OC   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.,
RA   Soby K.M., Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG
RT   27420.";
RL   Genome Announc. 2:e00880-14(2014).
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_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,
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_02005, ECO:0000256|SAAS:SAAS01116702};
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
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_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. 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   EnsemblBacteria; AIE81987; AIE81987; FB03_00410.
DR   KEGG; asg:FB03_00410; -.
DR   KO; K01873; -.
DR   OrthoDB; 32262at2; -.
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; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711227};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711241};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035032};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711254,
KW   ECO:0000313|EMBL:AIE81987.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711287};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711230}.
FT   DOMAIN       30    114       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      141    638       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      682    827       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        58     68       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02005}.
FT   MOTIF       600    604       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02005}.
FT   BINDING     603    603       ATP. {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
//