ID I1P6S8_ORYGL Unreviewed; 1027 AA.
AC I1P6S8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA03G0007400.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA03G0007400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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 STRING; 4538.I1P6S8; -.
DR EnsemblPlants; ORGLA03G0007400.1; ORGLA03G0007400.1; ORGLA03G0007400.
DR Gramene; ORGLA03G0007400.1; ORGLA03G0007400.1; ORGLA03G0007400.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_2_1; -.
DR OMA; RQWYIRN; -.
DR Proteomes; UP000007306; Chromosome 3.
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 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; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
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}.
FT DOMAIN 116..726
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 771..911
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 117049 MW; C6F041B52654584D CRC64;
PPAGFRWSKC KRERGKKAQG KGKGKGGSXA PGTSSFRWSX KKXEEAKEES CXGXESXGFH
XSRHSSWAEE ISCISNGQAV XPSCCXEIMV CLVGIVRIFW GRSCGSYFEV CTRYYVLPPP
NVTGALHIGH ALTVAIEDAI IRWRRMSGYN ALWVPGVDHA GIATQVVVEK KLMREKKLTR
HDIGREEFVS EVLKWKDEYG GTILNQLRRL GASLDWSREC FTMDKPRSKA VTEAFVRLYK
QGLIYSFFPL LWMICFYTLE GLSPRELGLH SSNSNFXRRG XLSRYXRRNH VKGSWLXYNC
TIRRVDLFCI STXGRIGXDH CRNNKNRNNA WXYSNFCSPX GXXIQASAWR YAIHPFNGRK
LKIICDAELV DPTFGTGAVK ITPAHDPNDF EVGKRRSLEF INIFTDDGKI NNYGGAQFEG
MPRFTARVAV IEALKAKGLY KETKKNEMCL GVCSRTNDVV EPMIKPQWFV NCNTMAKAGI
DAVRSKRIEI IPQQYEQDWY RWLANIHDWC VSRQLWWGHR VPAWYVVLED DQENILGSDN
DRWVVARNES EANLEAHQKY PGKKFELHQD PDVLDTWFSS GLFPLTVLGW PDDTADVEAF
YPGSVLETGH DILFFWVARM VMMGMQLGGD VPFQKVYLHP MIRDAHGRKM SKSLGNVIDP
VDVINGIPLE GLLKRLEEGY LDPNELNIAS DGKKKDFPDG IAECGTDALR FALVSYTSQS
DKINLDIKRV VGYRQWCNKL WNAIRFAMGK LGNHYTPPAT ISVTTMPPIC KWILSVLNKA
IGKTVTSLEA YKSFDATSAI YSWWQYQLCD VFIEAIKPYF FNDSQELESA RAASRDALRV
CLDTGLRLLH PFMPYVTEEL WQRLPQPKDS CRKDSIMVSE YPSLVKEWAD DKLENQIDIA
LDTVNKLRSL KPPTDTNERR PAFALCXGQE IAAIVQCYQS LVVTLSSISS LKILTESDET
PPDCATAVVN KVYLYTSNSK ELSMQKLSLK SXGKREKKFK SCNMPYHRKW KLPVIKRRLH
IMSRRRT
//
