ID N1JJC7_BLUG1 Unreviewed; 1101 AA.
AC N1JJC7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=BGHDH14_bgh05345 {ECO:0000313|EMBL:CCU79005.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU79005.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU79005.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU79005.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU79005.1}.
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; CAUH01004177; CCU79005.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JJC7; -.
DR STRING; 546991.N1JJC7; -.
DR EnsemblFungi; BLGH_03379-mRNA-1; BLGH_03379-mRNA-1; BLGH_03379.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; N1JJC7; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
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:EnsemblFungi.
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; 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 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:UP000015441}.
FT DOMAIN 152..774
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 819..962
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 125371 MW; 36EFBBFD05A62616 CRC64;
MADNYDPIEK DTIQVPNANQ PFENEAKTLL ASATNSGVTE SQVNGLVSST GPPALPPFSV
KTKVKSEKEL EKERKKAEKQ AKFDQKKNKA VTSITATTSK SKEKKATAQK KSEDENLPHY
IEDTPHGEKK IIKSFENPYF KAYNPIAVES AWYAWWEKEG FFKPEFTTDG EVKEKGSFVI
VEPPPNVTGN LHMGHALGTA LQDVLIRWNR MHGKTTLWLP GCDHAGISTQ SVVENMLWRR
KQQTRHDLGR SKFIETTWEW KNEYHQRINN VLKRMGGSFD WTREAFTMNE NFSAAVQETF
VSLHEEGIIY RANRLVNWCT KLNTALSNLE VVNKELVGRT LLEVPGYEKK IEFGVIIHFQ
YPIEGMDEMI EVATTRIETM LGDTAIAVHP DDPRYQHLVG KMAIHPFITG RKMPIIADTY
VERDFGSGAV KITPAHDPND YAMGERHKLE FVNILTDDGR MNENAGPYAG KKRFDVRYLI
QDDLKKLGLY IDKKDNPMSV PLCDKSKDII EPLMKPQWWM KMKDMAAAAL SAVKNNDIKI
QPESAEKAYI RWMENVNDWC LSRQLWWGHQ VPMYFAQVEN GSNDESDNNL WFSGRTLEEA
EAKAKKAFPN QELTLRRDED VLDTWFSSGL WPFATLGWPK KTHDLDKLFP TSLLETGWDI
LFFWVARMIM FSLKMTGKVP FSEVYCHSLI RDSEGRKMSK SLGNVIDPQD VIEGILLENL
HKKLSQGNLA PGEVEKATNY QKTAFPDGIP QCGTDALRFA LVSYTTGGGD IAFDIKVIHG
YRKFCNKIYQ ATKYVCGRLG SEFIPPKTSK PTREESLAER WILHKMNIAA QEINQALQDR
EFMKSTTIIY QYWYNNLCDV FIENSKTIFQ EGTAEEKLSA LNTLYTVLDC ALTMIHPYMP
FLTEELWQRL PRRPGDKTPS IVLAQYPTYD EQFDDPLAET AYELILGISK GIRSLMSGYS
IKDEGLVFIQ TFDTISSTTA SEQLASIKSL SGKGIDKISL LSATDSRPLG CVAFTVSSTA
VVYLHVKGRV DIESEILKTT VKLAKTTQGI ERQKKILGDK NYQAKVSEEL QDFERKKLRD
LEVEKNTFEV TIKQFESIKC E
//
