ID G4U6E9_NEUT9 Unreviewed; 1082 AA.
AC G4U6E9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=NEUTE2DRAFT_154654 {ECO:0000313|EMBL:EGZ78206.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ78206.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ78206.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL890999; EGZ78206.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U6E9; -.
DR STRING; 510952.G4U6E9; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR Proteomes; UP000008513; 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; 2.170.220.10; -; 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 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; 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 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:UP000008513}.
FT DOMAIN 138..758
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 802..947
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 36..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1053..1080
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 122506 MW; 9AB01DF0BCD86248 CRC64;
MPLSLWRLAI GSSRRHSLLK FTSTRVLPVP RQYSTYNNDK KVTMPGEDQP VAAPAAAPKK
NDKKEKAKAD KAAKFAAKQA AAKAKQPAAQ SAPKEKKEKT PALPPYEDNT PAGEKKVIQS
FEHPHFSAYN PSAVEAAWYQ WWEKAGYFKP ESCRKPSAGK FVIPLPPPNV TGALHCGHAL
ANSLQDTLIR WYRMKGYETL WVPGCDHAGI STQSVVEKML WKKEKKIRQE LGREKFTDLV
WEWKGEYHQR INNAQKLMGG SMDWSREAFT MDKNLTAATM ETFCRLHDEG LIYRSNRLVN
WCTHLNTALS GLEVETKEIT GRTLLDVPGY DKKVEFGVLT HFKYQIDGSE ETIEVATTRP
ETMLGDTGIA VNPEDPRYTH LVGKFARHPF VDRLLPIVTD NYVDKEFGTG AVKLTPAHDF
NDYQLGQRHN LEFINILNEN GTLNDNAGPF KGQKRFDARY TVVEELTKLG LFVKKEPNPM
KIPLCEKSKD VIEPMMTEQW WVRMKEMGEA ALQVVEEGKV KISPESATKS YKRWLSDIQD
WCISRQLWWG HRIPAYRVIF EGEEGQRENE KSEWVVGRTQ EEAQAKAEAK FAGRKFTLEQ
DPDCLDTWFS SGLWPMAILG WPNTENLDFK KFFPTSMLET GWDILFFWVS RMIMLSLKMT
GEVPFTEVYC HSLIRDSEGR KMSKSLGNVI DPLDIIRGIE LEDLHAKLLV GNLKEEEVAR
ATKYQKTAFP GGIPECGADA MRFTLLSYTT GGGDINFDIR VMHAYRRFCN KIWQASKYVL
GKLPQDFVPK GELDTANFSV PEKWILHRMN VAVKGMNEAL EAREFSRATK VAYQFFYDEL
CDVFIENSKG ILSDGTPEEQ QSVQQTLYHA LDVALRLLHP IMPYITEELW QHLPRKQGDG
ETIMLAPYPA FESQLEFATE AEDYELGLKC AGGIRSLAAD YNIKSDGRAF IKATTADSLA
TVSAQLAAIR TLCGKGVKEV NVLGADEELP RGCAVYVINA EITVLLQVGG SISDIDAEIK
KITTKLQKTD LTIKKQQELL SKDGFEKVSE AVQESEKQKL ADAQAAKENY QRTLEEFSKL
KI
//
