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-JUL-2015, entry version 7.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|SAAS:SAAS00105779};
DE            EC=6.1.1.9 {ECO:0000256|SAAS:SAAS00105779};
GN   Name=valS {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};
RN   [1] {ECO:0000313|EMBL:AIE81987.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE81987.1};
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   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val). {ECO:0000256|SAAS:SAAS00105829}.
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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   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-HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_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|SAAS:SAAS00105940};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00105799};
KW   Ligase {ECO:0000256|SAAS:SAAS00105744, ECO:0000313|EMBL:AIE81987.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00105848};
KW   Protein biosynthesis {ECO:0000256|SAAS:SAAS00105732}.
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
//