ID A0A0E0GM18_ORYNI Unreviewed; 1000 AA.
AC A0A0E0GM18;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA03G17430.2};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA03G17430.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G17430.2};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA03G17430.2}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G17430.2};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR AlphaFoldDB; A0A0E0GM18; -.
DR EnsemblPlants; ONIVA03G17430.2; ONIVA03G17430.2; ONIVA03G17430.
DR Gramene; ONIVA03G17430.2; ONIVA03G17430.2; ONIVA03G17430.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
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 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; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 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; 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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591}.
FT DOMAIN 110..673
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 729..878
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 114101 MW; 8F2301CC84DE0B19 CRC64;
MEKQPEVHGP EKAPEKQLDE KTLERKLRKN QKAKEKEEKR LKAKQKEAAM LQAQPALDVL
KKVEKKHRGK AVEDENPEDF IDQDTPNGQK KLLAPQMANQ YCPSTVEKSW YAWWESSGYF
RADSASTKPP FVIVMPPPNV TGALHIGHAL TVAIEDAMIR WRRMSGYNAL WVPGVDHAGI
ATQVVVEKKL MRERNLTRHD IGPDNFVCEV LKWKERYGGT ILNQLHRLGA SLDWSREAFT
MDEQRSNAVT EAFVRLHKEG LIYRDNRLVN WDCTLLTSIS EIEVDHIDLK EETMLKIPGY
ATPVQFGVLI SFAYPLEEGL GEIVVATTRI ETMLGDTAIA VHPEDKRYMH LHGRYAVHPF
NGRKLKIICD AEIVDPSFGT GAVKIAPAHD PNDFEVGRRN NLQFINILTD DGKINSNGGA
QFEGMPRFTA RICIIEALKA KGLYKGAKNT KTSLGICSRT NDIVEPMIKS PQWFVNCNTM
AKVALDAVRS KRIEIIPPQY EQDWYRWLEN IRDWCVSRQH WWGHRVPAWY VTLEDDQEKT
LGSDNDRWIV AKSESAASVE AQKSYPGKKF ILNQDPDVLD TWFSSALFPL AVLGWPDDTA
DLRSFYPTSV LETGLDILFC WVARMVMMGT QLGGDVPFQK VYLHPIVCDT HGRKMCKSLG
NVIDPLEVIN GMTLEGLSDR INLDIKRVVG YRQWCNKLWN AIRFAMGKLG VHYSPPATVD
VSIMPPICKW ILSALNKATG KTVTSLEAYK FSDATSAIYS WWQYQLCDVF IEAIKPYFFN
EPQEFESARV ASRDTLWVCL ETGLRLLHPF MPYITEELWQ HLPQPKYSCR QDSIMISEYP
SLVEEWTNDN LENEMDIVLD TVNKIRSLKT RTERKERRPA FALCRSQDVT ATIQCHQSLI
ILTENDETPA DCAIAIVNKD LSVYLKLQGA INAEAEREKL RKKRDGIQKL HHAVTHMMDA
SGYREKAPQS VQEGDMRKHI ALLQELEVVI LHDYSFGINL
//
