ID A0A068NEW0_9ACTO Unreviewed; 880 AA. AC A0A068NEW0; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 13-NOV-2019, entry version 34. 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}. 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; 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 REGION 494 516 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 860 880 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. 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 //