ID K2HYH4_ENTNP Unreviewed; 1049 AA.
AC K2HYH4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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};
GN ORFNames=ENU1_055880 {ECO:0000313|EMBL:EKE41450.1};
OS Entamoeba nuttalli (strain P19) (Amoeba).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=1076696 {ECO:0000313|EMBL:EKE41450.1, ECO:0000313|Proteomes:UP000006769};
RN [1] {ECO:0000313|EMBL:EKE41450.1, ECO:0000313|Proteomes:UP000006769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P19 {ECO:0000313|EMBL:EKE41450.1,
RC ECO:0000313|Proteomes:UP000006769};
RA Hannick L., Karamycheva S., Lorenzi H., Caler E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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 EMBL; JH926030; EKE41450.1; -; Genomic_DNA.
DR RefSeq; XP_008856220.1; XM_008857998.1.
DR AlphaFoldDB; K2HYH4; -.
DR EnsemblProtists; EKE41450; EKE41450; ENU1_055880.
DR GeneID; 20072396; -.
DR VEuPathDB; AmoebaDB:ENU1_055880; -.
DR OMA; LDTWMDS; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000006769; 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: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 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
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 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}.
FT DOMAIN 103..729
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 774..914
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 22..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 979..1013
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 22..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 122196 MW; 454419E281AAE61E CRC64;
MSTPQAKEVK VVKELTAEEI EKKKRREEMK KAKNAAKNEK FKKKQEAQQQ QQKNNLGKAK
KENKKQTKEK EEIKFNKTIK GEKKRVIEPM PNTYSPKYVE EGWYEWWEKE GFFKPEYSKR
SGKKFVMVIP PPNVTGKLHL GHALTNSIQD TIVRYHRMKG DETLWVPGVD HAGIATQVVV
EKKLMREQGV TRHDIGREKF LEEVWKWKDE YGKGICNQLR RLGSSLDWSR EVFTMDEKRG
EAVKEAFCRF YEKGLLYREQ KLVNWCCTLK TAISDIEVEY IDVSKPTAIN VPGYDKPIIF
GNLHEFAYPL VNPATGKDEG EILIDTTRIE TMLGDVCVCI HSKDERYKKY HGWSVRHPFN
GKILPIIEDD ELVDMEFGTG CVKVTPAHDP NDYNVAIRHK LKIINILNDD GTMNQECGEF
AGMKRFECRE AVIEKLKEKG LYKGVKASAM RVPICSRSHD IIEPRIKPQW WVNCKNMARR
AVEAVRKGEL KMYPSEMENV WYRWLENIHD WCISRQLWWG HRIPAYLIKS KKEKEADEFD
MKNWVVARSE EEARKKAAEI KGVSIEDIEL KQDPDVLDTW FSSGLFPFSV MGWPEQTKDL
EKYFPGELLE TGNDIIFFWV ARMVMMSLEL MDCLPFKEVL FHSIVRDAQG RKMSKSLGNI
IDPIDVIEGI SLKGLNDKLY TYNLPEKECV IAAEGQKKDF PNGIEECGTD AMRFALLAYM
TQGHDINLDI NRVVGYRNFC NKIWNAFKFS TMNFRKDFKA QETIEIKKTN SRLDQWILHR
LNVMITSVQQ WFKSYEFGNA TQAIYSFWLY DFCDVYLEAS KGIFKGPDNE RRRASEEVLY
NVIEIGLRVL HPFMPFITEE LWQRLPRRND KEISIMVTSY PEPIEEFNNP ALDEEIKYIY
TIIKGIRSLN GIYSQAIITS KQKPKCTIVT ERDLEGYEVI ISSLAGIGEV NIVKEGIYKG
SPMHVVDNST RIYSHLAGII DYKQEAQRLA GKKEQMEKNL KDLELKINDV HFDKTPEEVK
KTILEKKQSL IEEIKLIQQA ENECLEMLH
//
