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Database: UniProt
Entry: A0A172ULM9_9MYCO
LinkDB: A0A172ULM9_9MYCO
Original site: A0A172ULM9_9MYCO 
ID   A0A172ULM9_9MYCO        Unreviewed;       880 AA.
AC   A0A172ULM9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN   ORFNames=A7U43_12270 {ECO:0000313|EMBL:ANE79985.1};
OS   Mycobacterium adipatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE79985.1, ECO:0000313|Proteomes:UP000077143};
RN   [1] {ECO:0000313|EMBL:ANE79985.1, ECO:0000313|Proteomes:UP000077143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE79985.1,
RC   ECO:0000313|Proteomes:UP000077143};
RA   Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT   "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT   sp. YC-RL4.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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_02004}.
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_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
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_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR   EMBL; CP015596; ANE79985.1; -; Genomic_DNA.
DR   RefSeq; WP_067995320.1; NZ_CP015596.1.
DR   AlphaFoldDB; A0A172ULM9; -.
DR   STRING; 1682113.A7U43_12270; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000077143; 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   CDD; cd00817; ValRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   NCBIfam; TIGR00422; valS; 1.
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   Pfam; PF10458; Val_tRNA-synt_C; 1.
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; SSF46589; tRNA-binding arm; 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_02004};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02004};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000077143}.
FT   DOMAIN          25..435
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          445..573
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          616..758
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          815..879
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          813..840
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           535..539
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         538
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   880 AA;  97460 MW;  EE0ED4CC51A1BBB4 CRC64;
     MTDSPRDRAD ALPKSWEPGA VESELYQGWV DAGYFTADPA SDKPAYSIVL PPPNVTGSLH
     MGHALDHTLM DALTRRRRMQ GYEVLWLPGM DHAGIATQSV VEKQLAVDGK SKEDFGRELF
     IDKVWDWKRE SGGTIGAQMR RLGDGVDWSR DRFTMDDGLS RAVRTIFKRL YDAGLIYQAE
     RLVNWSPVLQ TAISDLEVKY SDVEGELVSF RYGSMNDDEP HLVVATTRLE TMLGDTAIAV
     HPDDDRYRAL VGQTLAHPFL DRQIIVVADQ HVDPEFGTGA VKVTPAHDPN DFEIGIRHNL
     PMPSILDKAG AITGTGTRFD GMDRFEARVA VREALAAEGR IVAEKRPYLH SVGHSERSGE
     PIEPRLSLQW WVNVESMAKA AGDAVRNGDT VIHPASLEPR WFAWVDNMHD WCISRQLWWG
     HRIPIWHGPD GQQVCLGPDE TAPEGWEQDP DVLDTWFSSA LWPFSTMGWP DRTPDLEKFY
     PTSVLVTGYD ILFFWVARMM MFGTFVAGDD VIPEGAVPFE NVFLHGLIRD EFGRKMSKSK
     GNGIDPLDWV EKFGADALRF TLARGASPGG DLSIGEDHAR ASRNFATKIF NATKFALMNG
     AQLAPLPALA ELTDADRWIL GRLEEVRAEA DSAMESYEFS RACEAIYHFA WDEFCDWYLE
     LAKVQFGQSE HAAHTAVVLA TVLDNLLKLL HPVMPFVTET LWTTLTGAES LVIADWPSPS
     GIPVDSVANQ RITDMQKLIT EVRRFRSDQG LNDRQRVPAK VVGIDAAGLD AQLPAIAALA
     WLTEPADGFT PSAAVEVRLT GGTVLVELDT SGTVDVAAER KRLEKDLAAA QKELAQTTGK
     LGNEAFLAKA PEAVVDKIKA RQQLAAEEVE RITARLGGLS
//
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