ID G0WDP1_NAUDC Unreviewed; 1019 AA.
AC G0WDP1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 54.
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 Name=NDAI0G01260 {ECO:0000313|EMBL:CCD25902.2};
GN OrderedLocusNames=NDAI_0G01260 {ECO:0000313|EMBL:CCD25902.2};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD25902.2, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD25902.2, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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; HE580273; CCD25902.2; -; Genomic_DNA.
DR RefSeq; XP_003671145.2; XM_003671097.2.
DR AlphaFoldDB; G0WDP1; -.
DR STRING; 1071378.G0WDP1; -.
DR GeneID; 11497298; -.
DR KEGG; ndi:NDAI_0G01260; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 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:UP000000689}.
FT DOMAIN 60..686
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 732..880
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 948..1012
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 946..973
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1019 AA; 118218 MW; 836A4512787EA66F CRC64;
MLQSYTRIPI RRPVNPSTLI RALNQCYPYS TSNSYNHIIP PPPTLKPFPK AYNPELVEQK
WYDWWLQTRA FEPEFTADGK IKPEGLFCIP APPPNITGAL HIGHALTISI QDSLVRYYRM
KGKTVLFLPG FDHAGIATQS VVEKQIWRQE RKTKYDYGRE EFVKKVWDWK EIYHEKIKNQ
VKQLGASYDW IREAFTLDPK LSSAVVEAFV RLHDEGVIYR ALRLVNWSTK LSTTISNLEV
DNRIIPGRTL IPVPGYEKKI EFGVLTYFAY RVAGSNNGEQ LIVATTRPET IHGDTAVAIH
PDDPRYIHLH GKSVQHPFLD KKLPIILDDK IVDMGFGTGA VKITPGHDFN DYEVSTRHDI
DVVNILTEDG KLNSNCGPKW AGMKRFDARE KIIEDLKELG LFIKQEGHEM TIPICSRSGD
IIEPMLKPQW WVSQKQLAKD AMDVIKKGEI KMWSNRTKSE YLRWLENIHD WCISRQLWWG
HRCPVYFVNI ENKDNSREDG NYWIAGRSHD EALIKAKKKF PSEKFTLEQD EDVLDTWFSS
ALWPFSTLGW PQKTKDMEQF YPFSILETGW DILFFWVTRM ILLGIKLTGS VPFKEVYCHS
LIRDSQGRKM SKSLGNVIDP LDIIHGVTLK ELNAKTVNSN LSEKEVKRVI REQQKIYSRG
IPQCGTDALR FTLCAYTTGA RDINLDLLRV EGYRRFCNKI YQATNFAISR LNNNYIPKLN
NKNLTECHRL VEKWSLYQMN NCAKVMNESF EERNFLTGTT AIYQYWYMIC DVYIEYFKSL
HHTNDAIKMD LAKDVLYELI KNGLKMIHPF MPYISEELWQ RITRNGEFEK CVTITKASYP
IYDPTIANYF ADAQIYDVIL NTTKAIRSLL SEYNIIKNGQ IYISVQDDDE TTSAFVMEKE
ALVSMIKGLS DIAILSNSSE NIVLNDCVMK SVNDKVKIYL LVKGQYEDIR KEIEKNQKKL
KKLEGIKENL KRTLSNSEFL KKATMEVQRI NKEKLTNIQG QILGLQTTVN NLKRFQDDR
//
