UniProt: A0A0E0CU00

Database: UniProt
Entry: A0A0E0CU00_9ORYZ

LinkDB:  A0A0E0CU00_9ORYZ 
Original site:  A0A0E0CU00_9ORYZ

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Ontology (7)   
   GO (7)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Protein domain (14)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
All databases (23)   

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ID   A0A0E0CU00_9ORYZ        Unreviewed;      1070 AA.
AC   A0A0E0CU00;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI03G00790.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI03G00790.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI03G00790.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI03G00790.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001372};
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; A0A0E0CU00; -.
DR   STRING; 40149.A0A0E0CU00; -.
DR   EnsemblPlants; OMERI03G00790.1; OMERI03G00790.1; OMERI03G00790.
DR   Gramene; OMERI03G00790.1; OMERI03G00790.1; OMERI03G00790.
DR   Proteomes; UP000008021; 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:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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   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   Pfam; PF09334; tRNA-synt_1g; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008021}.
FT   DOMAIN          216..282
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          315..769
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          820..896
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          993..1023
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        114..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  120815 MW;  493A4D81B6A2A978 CRC64;
     MVKVKAQPTP TAAAKSAVAG GGEVSTETPR RSARPQQAAK KKRSRDDNSF LTHHQPQLPT
     AETHTAIVTQ THATALLHIG VAATAWERHE VKLWIVREGI ASNEALQEIY PPEPPLAKEK
     EEKKLKAKAK AKEAARLQAQ AASDGPKKSE KKQRKKAVED ENPEDFIDPD TPHGQKKFLA
     SQMAKQYSPA AVEKLWYAWW ESSGYFGADP VLPPPNVTGA LHIGHALTVA IEDAIIRWRR
     MSGYNALWVP GVDHAGIATQ VVVEKKLMRE KKLTRHDIGR EEFVYEVLKW KDEYGGTILN
     QLRRLGASLD WSRERDYRLV NWDCTLRTAI SDVEVDYLDI KEETMLKVPG YNTTVQFGVL
     ISFAYPLEEG LGEIIVATTR IETMLGDTAI SVHPEDNRYK HLHGRYAIHP FNGRKLKIIC
     DAELVDPTFG TGAVKITPAH DPNDFEVGKR RSLEFINIFT DDGKINNYGG AQFEGMPRFT
     ARVAVIEALK AKGLYKETKK NEMCLGVCSR TNDVVEPMIK PQWFVNCNTM AKAGIDAVRS
     KRIEIIPQQY EQDWYRWLAN IRDWCVSRQL WWGHRVPAWY VVLEDDQENI LGSDNDRWVV
     ARNESEANLE AHQKYPGKKF ELHQDPDVLG TWFSSGLFPL TVLGWPDDTA DVKAFYPGSV
     LETGHDILFF WVARMVMMGM QLGGDVPFQK VYLHPMIRDA HGRKMSKSLG NVIDPVDVIN
     GIPLEGLLKR LEEGNLDPNE LNIASDGKKK DFPDGIAECG TDALRFALSD KINLDIKRVV
     GYRQWCNKLW NAIRFAMGKL GDHYTPPATI SVTIMPPICK WILSVLNKAI GKTVTSLEAY
     KFSDATSAIY SWWQYQAIKP YFFNDSQELE SARAASRDAL WVCLDTGLRL LHPFMPCEWA
     DDKLENQIDI ALDTVNKLRS LKPPTDTNER RPAFALCRGQ EIAAIVQCYQ SLVVTLSSIS
     SLKILTESDE TPPDCATAVV NKDLSVYLQL QGALNAEVEL EKLRKKREEI QKLQHALSQK
     MEASGYRGKV PQNVQEEDMR KLTSFLEQLE IISEAEKKLD AKTDFWNLTV
//

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