ID A0A068NEW0_9ACTO Unreviewed; 880 AA. AC A0A068NEW0; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 12-AUG-2020, entry version 36. 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|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}. 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|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_02005, ECO:0000256|RuleBase:RU363035}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02005, ECO:0000256|RuleBase:RU363035}; 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 ECO:0000256|RuleBase:RU363035, ECO:0000313|EMBL:AIE81987.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02005, ECO:0000256|RuleBase:RU363035}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_02005, ECO:0000256|RuleBase:RU363035}. FT DOMAIN 30..114 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 141..638 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 682..827 FT /note="Anticodon_1" 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 /note="ATP" 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 //