ID F1A3L6_DICPU Unreviewed; 1049 AA.
AC F1A3L6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-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=DICPUDRAFT_159231 {ECO:0000313|EMBL:EGC29212.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29212.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; GL871465; EGC29212.1; -; Genomic_DNA.
DR RefSeq; XP_003294258.1; XM_003294210.1.
DR AlphaFoldDB; F1A3L6; -.
DR STRING; 5786.F1A3L6; -.
DR EnsemblProtists; EGC29212; EGC29212; DICPUDRAFT_159231.
DR GeneID; 10506335; -.
DR KEGG; dpp:DICPUDRAFT_159231; -.
DR eggNOG; KOG0432; Eukaryota.
DR InParanoid; F1A3L6; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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:SF57; VALINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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:UP000001064}.
FT DOMAIN 49..691
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 745..904
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 993..1048
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1049 AA; 120843 MW; 8E1846C53328D64F CRC64;
MNRLLNNNKT LLFNTRNQIS FNRYYIRAPF DESLIKSSFD PKNVELNKYK FWEDHGLFKP
KENKNGEKFS MVLPPPNVTG SLHIGHSLTT TIQDSLVRYN RMLGKEVVWI PGLDHSGIAT
QVAVEKQLLV KEKKTRYDLG REKFLEKVFE WTEIYSKNIN NQLRITGSSL DWSRSVFTLD
QQRNNAVQEA FIRLFNMGLI YRSTRLVNWC PQLQSVISDI EIDHQQIEKP TSIKLKSRVK
SIEVGVIYDV AYQIDNSDSS MEQLKDLIVS TTRPETIFGD TGIAIHPEDE RYKSYHGRFA
VHPFTQKRIP IVLDPILVDK TLGTGVVKIT PGHDFNDYQC GTRHSLEFIN IMNSNGTLNE
NTIPEFNGVD RLDARPLVIK KLEEKGLYHG KKPHPTTLSI CSRSGDLLEP ILKPQWYVDC
KAMASRSVGY VEKDEIKIVP ESFKENWFRW LNNIQDWCIS RQLWWGNPIP AYLIIENNLR
ATDNNDGNNS IINGMSLVNE KWVVAKTEEE AAEIAIKNYN LKKGEFTLEK DQDVLDTWFS
SGLFPISSLG WPNEKESIDF KKYFPLDVME TGSDILFFWV ARMVMLCSTL VPESPIPFNS
ILLHPMIRDS QGRKMSKSLG NVIDPLNVIN GITLKELKDN VLSSNLTDKE KSIATKGLDK
EFPQGIPQCG TDSLRLSLSQ YPINGKDINL DINKIIGIRL FCNKLWNASK LVLSNCNNIE
SIKPITMYYN GNTEPFDYNS ITLIDKWILT RLSKLIESSN SNFNSFNLST ISQSLYSFFQ
YDFCDLYLEC IKVELNRNNE SSKMVLINVL DTYLRLLHPF MPFITEDIWQ RLPRASQMES
LNCEQTISIM VSEYPTTNYK YHKQYLQDEA KIEKEISLFQ SVLHATRAQR SLLTIHDKTK
VNVTLHVDAD SFRDKFNINL LNTFEQLKDS FEKIANASLV ISGQIISQNQ INESNGKITT
IADGLQIQIE FDSNENNQFL NPAQSQQSQQ QSQQALQSKI TKLESFINDL EKTINSQDFK
QRVPLKVQEQ KIDKLNKYKI ELNELLNRK
//
