ID A0A1B8SFN2_9MYCO Unreviewed; 888 AA.
AC A0A1B8SFN2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ACT18_12095 {ECO:0000313|EMBL:OBY31525.1}, BST28_10800
GN {ECO:0000313|EMBL:ORA79907.1}, GWR20_21555
GN {ECO:0000313|EMBL:NDJ91695.1};
OS Mycolicibacter kumamotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=354243 {ECO:0000313|EMBL:OBY31525.1, ECO:0000313|Proteomes:UP000092668};
RN [1] {ECO:0000313|EMBL:OBY31525.1, ECO:0000313|Proteomes:UP000092668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Roo {ECO:0000313|EMBL:OBY31525.1,
RC ECO:0000313|Proteomes:UP000092668};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium kumamotonense strain Roo.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORA79907.1, ECO:0000313|Proteomes:UP000192713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45093 {ECO:0000313|EMBL:ORA79907.1,
RC ECO:0000313|Proteomes:UP000192713};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NDJ91695.1, ECO:0000313|Proteomes:UP000466523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CST 7247 {ECO:0000313|EMBL:NDJ91695.1,
RC ECO:0000313|Proteomes:UP000466523};
RA Sanchez-Estrada R., Gonzalez-Y-Merchand J.A., Rivera-Gutierrez S.;
RL Submitted (JAN-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBY31525.1}.
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DR EMBL; JAACYR010000114; NDJ91695.1; -; Genomic_DNA.
DR EMBL; LFOE01000015; OBY31525.1; -; Genomic_DNA.
DR EMBL; MVHU01000013; ORA79907.1; -; Genomic_DNA.
DR RefSeq; WP_019737256.1; NZ_MVHU01000013.1.
DR AlphaFoldDB; A0A1B8SFN2; -.
DR STRING; 354243.BST28_10800; -.
DR PATRIC; fig|354243.3.peg.2504; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000092668; Unassembled WGS sequence.
DR Proteomes; UP000192713; Unassembled WGS sequence.
DR Proteomes; UP000466523; Unassembled WGS sequence.
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}.
FT DOMAIN 26..437
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 446..579
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 622..762
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 823..887
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 821..848
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 54..64
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 541..545
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 888 AA; 98751 MW; 2D68E1B5BE4A6D0C CRC64;
MTATPNAANA EHLPKSWEPG AVEDAIYQRW VDAGYFTADP ASTKPGYSIV LPPPNVTGNL
HMGHALDHTL MDALTRRKRM QGFEVLWLPG MDHAGIATQS VVERQLAVDG KTKEDFGREL
FIEKVWDWKR QSGGTIGAQM RRIGDGVDWS RERFTMDEHL SRAVRTIFKR LYDAGLIYQA
ERLVNWSPVL QTAISDLEVK YEDIEGELVS FRYGSLDDAQ PHIVVATTRL ETMLGDTAIA
VHPDDDRYRH LVGTSLDHPF LDRQIAVVAD THVDPEFGTG AVKVTPAHDP NDFEIGLRHQ
LAMPTILDTK GRIAGTGTQF DGMDRFEARV AVREALAAQG RIVAEKRPYL HSVGHSERSG
EVIEPRLSMQ WWVNVSSMAK AAGDAVRNGD TVIHPKSLEP RWFSWVDDMH DWCISRQLWW
GHRIPIWHGP DGQKVCVGPD ETPPEGWEQD PDVLDTWFSS ALWPFSTMGW PDATPELAKF
YPTTVLVTGY DILFFWVARM MMFGTFVGGD DALTAGGTRG AQVPFRNVFL HGLIRDEHGR
KMSKSRGNGI DPLDWVEVFG ADALRFTLAR GASPGGDLSI GEDHARASRN FVTKLFNATR
FALLNGARLA PLPSLDELTD ADRWILGRLE EVRAEVDSAF DGYEFGRACE ALYHFAWDEF
CDWYVELAKT QLGEGLSRTT AVLAAVLDTL LRLLHPVIPF VTETLWQELT GEESLVIAEW
PEPSGIILDQ VAAQRIADMQ KLVTEVRRFR SDQGLRDRQK VPARLTGIDG ADLATQVAAV
TSQAWLTEPG ADFTPSATVE VRLGRGDRGN TVVVELDTSG TVDVAAERRR LEKDLAAAEK
ELVATAAKLD NEAFLAKAPE AVVDKIRARQ QVARDEVDRI TGRLAGLT
//
