ID A0A1X4NA49_9RHOB Unreviewed; 1047 AA.
AC A0A1X4NA49;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=MGEO_19815 {ECO:0000313|EMBL:OSQ43222.1};
OS Marivita geojedonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Marivita.
OX NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ43222.1, ECO:0000313|Proteomes:UP000193926};
RN [1] {ECO:0000313|EMBL:OSQ43222.1, ECO:0000313|Proteomes:UP000193926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ43222.1,
RC ECO:0000313|Proteomes:UP000193926};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL Submitted (MAR-2014) 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:OSQ43222.1}.
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DR EMBL; JFKC01000037; OSQ43222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4NA49; -.
DR STRING; 1123756.MGEO_19815; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000193926; 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:UP000193926}.
FT DOMAIN 16..510
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 610..726
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 776..916
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 979..1043
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 977..1046
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 692..696
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 695
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1047 AA; 116464 MW; 0423E5CEA886F2F4 CRC64;
MAMEKTFDAS EAEARLYKAW EDSGAFKAGA NASREDTFCV MIPPPNVTGS LHMGHAFNNT
LQDILVRWHR MRGFDTLWQP GTDHAGIATQ MVTEREMAAN GEPSRREMGR EAFLDRVWQQ
KVKSRGTIIG QLKRLGASAD WSREAFTMGG AAGDPDCGNG PNFHDAVIKV FVDMYIKGLI
YRGKRLVNWD PHFETAISDL EVENIENPGH MWHFKYPLAG GATYTYIEKD EDGNVVLEEE
RDYISIATTR PETMLGDGAV AVHPSDERYA PIVGKLCEIP VGPKEHRRLI PIITDEYPDP
TFGSGAVKIT GAHDFNDYGV AKRGNIPCYR LMDTKAHMRD DGAPYEEAAA VAGAVARGEQ
TLTEAETDAL NLVPDHLRGL DRFEARKRVI KEITAEGLAV MTRADNPVLG RKLGEDDDLA
ELVPLVEAKP IMQPFGDRSK VVIEPMLTDQ WFVDAEKIVG PALEAVRSGE VKIVPESGER
TYYHWLENIE PWCISRQLWW GHQIPVWYGF DLSGAGFTDD EGDGDLDLVE MGRLLNAQSL
LRGDERHHSA ASFEDVAAQF GDVLGTLPTP LNHARVVEVE NRDAAAHLLA ASLAEYEAHD
QDPTKLVYPV WRDPDVLDTW FSSGLWPIGT LGWPEQTPEL QKYFPTSVLV TGQDILFFWV
ARMMMMQLAV VDQIPFKDVY LHGLVRDAKG KKMSKSLGNV VDPLEIIDEY GADALRFTNA
AMASLGGVLK LDMQRIAGYR NFGTKLWNAT RFAEMNGVFE NRTPSADIPK ATATVNQWII
GETARVRGEV DAALAAYRFD DAAAALYRFV WGKVCDWYVE FSKPLLLDDG PQTAETKATM
AWVIDQCLIL LHPIMPFITE ELWAVTGDRS KMLVHADWPS YGDDLIDAEA DREMNWVIGL
IEGIRSARQQ MHVPVGLYLP LVVKDMGDAA KAAWDRNEVL IKRLARIDEL TVVDAFPKGC
ATVPMEGATF GLPLADIIDV AEEKARLEKT LQKLAKEIGG MKGRLSNPKF VESAPEEVVE
ETRANLAARE EEAAQLQEAV DRLAELG
//
