ID G0VFB7_NAUCC Unreviewed; 1021 AA.
AC G0VFB7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=NCAS0E01130 {ECO:0000313|EMBL:CCC70183.1};
GN OrderedLocusNames=NCAS_0E01130 {ECO:0000313|EMBL:CCC70183.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70183.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC70183.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE576756; CCC70183.1; -; Genomic_DNA.
DR RefSeq; XP_003676543.1; XM_003676495.1.
DR AlphaFoldDB; G0VFB7; -.
DR STRING; 1064592.G0VFB7; -.
DR GeneID; 11530258; -.
DR KEGG; ncs:NCAS_0E01130; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; G0VFB7; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000001640; Chromosome 5.
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; 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; 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:UP000001640}.
FT DOMAIN 65..694
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 739..883
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 947..974
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1021 AA; 117845 MW; 73943F500B3CFCB0 CRC64;
MLSIQLRHMG LATRSPRGSL ISALTITRPT RRLLTTSHPI VKKVLPPLNS IELKAYDPEY
VEKNWYEWWD QIGAFKPEFT KDGKIKAEGL FCIPAPPPNV TGALHLGHAL TIAIQDSLIR
YYRMKGKTVL FLPGFDHAGI ATQSVVEKQL WKQEKKTRYD YGRDGFIKKA WEWKEKYHKR
IKNQLKRLGA SYDWSREAFT LDPKLSTAVK EAFVRLHDAG IIYRASRLVN WSVKLKTTIS
NLEVDNKIIN GRTLLTVPDY KDKIEFGVLI YIAYPVIDSN TNERIIVATT RPETLFGDVA
IAIHPEDSRY KHLHGKFVQH PLIPKKIPII LDATAVDMTF GTGAVKITPA HDQNDYNVGK
RHSLQFVNIF TDDGLLNENC GSSWEGLKRF DARQLVIDEL KRKGFFMKQE DNPMIIPLCS
RSGDVIEPLL KPQWWVSQKS MAKTAIDIVE KGEIRFSSSN TKNDYFRWLE NIQDWCISRQ
LWWGHRCPVY FINVEGSEDS AAINRNDGKY WVAGRNLEEA VHKAAKKFPN KKFSLEQDQD
VLDTWFSSAL WPFSTLGWPN KTNDMNLFYP FSMLETGWDI LFFWVTRMIM LGVKLTGSIP
FKEVYCHSLV RDFEGRKMSK SLGNVIDPLD IINGCTLKEL HEKLQQGNLD PKKIDKMKIE
QKKMYPRGIP QCGSDALRFA LCAYTTGGRD INLDISRVEG YRKFCNKIYQ ATKFSIQRLG
DDYQPPSSTH TPASKSLVEK WILYQMNNTI AIVNDSFEKR DFLTCTSKIY ELWYMICDVY
IENFKWLAND TIMEKAAKDT LHTLIENGLK MIHPFMPYLS EELWQRLPDG IGKDESSSIM
KTLYPTPSED FNYGKEAKQY DEILKIIKSM RSLLSEYNIT ANARFFFEIL DDELFDIVRA
EKDAILSVMK GVENISFLAV APDRQPIKND CVSCSISSQV NVYLLVKGQY KDISKELSKQ
LKQLEKLNNI YAATQRMLTN KDFIKKASEE IREMNEKKLI NIHNKILGMQ NTVNNLKRFQ
E
//
