ID K2JST4_9RHOB Unreviewed; 1039 AA.
AC K2JST4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ECO:0000313|EMBL:EKE73464.1};
GN ORFNames=B30_05357 {ECO:0000313|EMBL:EKE73464.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE73464.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE73464.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE73464.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) 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:EKE73464.1}.
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DR EMBL; AMRK01000002; EKE73464.1; -; Genomic_DNA.
DR AlphaFoldDB; K2JST4; -.
DR STRING; 1208323.B30_05357; -.
DR PATRIC; fig|1208323.3.peg.1107; -.
DR eggNOG; COG0525; Bacteria.
DR Proteomes; UP000006762; 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 Gene3D; 3.40.50.620; HUPs; 3.
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 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:UP000006762}.
FT DOMAIN 14..503
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 603..718
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 768..912
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 971..1035
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 685..689
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 688
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1039 AA; 116027 MW; 5A5668A58FAEFEB5 CRC64;
MEKTFDARDA EARIYEAWDK AGAFKAGANK SRDETFTIMI PPPNVTGALH VGHAFNNTIQ
DILIRWHRMR GFDTLWQPGQ DHAGIATQLM VEKELAKSGK KRTDFTRPEF LEKVWEWKGQ
YGATIINQLK RLGSTCDWSR NAFTMSGAPG APAGEEGNFH DAVIKVFVDM YDKGLIYRGK
RLVNWDPHFE TAISDLEVEN VETPGHMWHF KYPLAGGETY TYVEKDEDGT VTFTEERDYI
SIATTRPETM LGDGAVAVHP DDARYAPIVG KLCEIPVGPK EHRRLIPIIT DDYPDMNFGS
GAVKITGAHD FNDYQVAKRG GLPMYRLMDT RGAMRDDGLS YTDSALLAAE ILAGKTFTEA
EVDAVNLVPD HLRGLDRFEA RKAVVAEINA EGLAVMTRVT RKVKDDEGVE SEITETVPYV
EDKPIMQPFG DRSKVVIEPM LTDQWYVDAE KIVGPALDAV RDGRTKIMPE SGEKVYFHWL
ENIEPWCISR QLWWGHQIPV WYGLDLSAPN FKDDEGDGAL DEVELFRLLT EGGMLHLGDV
HHCAAEFDGV IAAFEGELAD VPTPINHARI VEVDSRQAAI EAFAESLAAY NVSQDPTKLV
YPVWRDPDVL DTWFSSGLWP IGTLGWPEWD ESTSKYFPTD VLVTGQDILF FWVARMMMMQ
LAVVDEVPFH TIYLHQLVRD EKGKKMSKTT GNVIDPLEII DEYGADALRF TNASMASIGG
VLKLSVDRIK GYRNFGTKIW NAARFAEMNE VFENYDPAVI PTPSATVNKW IIGETAKVLK
EVDTAFAEYR FNDGANALYA FVWGKFCDWY VELAKPLFYD GDAATLAETR QTMGWVLDQA
LTMLHPIMPF ITEELWGTVK PGRRLLAISD WPELSLDLVD AEADRELNWV IDLIETIRSS
RAEVHVPAGL KIPMIQVELD EAGKTAWANN EALIMKLARL DSLTPGPMPK GAITITVGGG
TFALPLEGVI DIAEEKARLE KVLGKLSKEL GGLRGRLKNP NFVASAPEEV VAEAQENLAA
REEEEGKIKA ALARLAEIG
//
