ID A0A316Z9T2_9BASI Unreviewed; 1063 AA.
AC A0A316Z9T2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=FA09DRAFT_299352 {ECO:0000313|EMBL:PWN96953.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN96953.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN96953.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN96953.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819297; PWN96953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316Z9T2; -.
DR STRING; 58919.A0A316Z9T2; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000245946; 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; 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: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:UP000245946}.
FT DOMAIN 109..736
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 782..931
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 119211 MW; 9455A2A102D6D81E CRC64;
MSAPPAAPAP GPGAEALPLG PDGQPMTKSA AKRAAKEAER AAQKAAKQNM KEQKESAAAD
KPAEPKRAKA KKEKKPEIEW VNNTKPGEKK DLSGPMENGY NPDHVEQSWY EWWEASGFYT
PKEPTDADPY DLDRTFVIPA PPPNVTGALH IGHALTISIQ DTLVRWYRMR GWRVLFNPGY
DHASISTQAV VEKRLMKLEG KTRHQYGREE FLRRVYDWSQ EYKKRIGGQT RRLGASYDFT
REAYTMDATR SRAVNEAFCR LHEQGVIYRA SRLVNWCCRL NTTLSTLEVE QKTLPGRTLL
QVPGYDEKER VEFGVIVSFA YPVSGSESDE RLIVATTRVE TMLGDSAVAV HPKDPRYTHL
HGKTLDHPFL PGRKIPIVTD SIAVDMEFGT GAVKITPAHD PNDYEVGKRH SLEFINILND
DGTLNENAGE FKGMKRFHAR RAVIEALKAK GLYVETKDNP MTVPVCSRSG DIVEPLIKPQ
WWVSCKPLAD AAVEAVNSQN MVIVPDSSRR EFFRWMDIIQ DWCISRQLWW GHRCPAYFVN
IEGKEQDEND ATQWVVGRTE EEAHERAAKL AGGAKYTLRQ DEDVLDTWFS SGLWPFSIMG
WPEQTPDLKH FYPNAMLETG WDILFFWVAR MVMLGVHFTG KIPFKEVFCH AMVRDAHGRK
MSKSLGNVID PLDVISGATL EALHEQLRQG NLEEKEVIKA TQGQKKDFPK GIPQCGTDAL
RFALCNFTAA GRDINLEIQR VEGYRKFCNK LWNATKFALM KLEGDFAPAD EEHVSGKECA
AERWILFRLN EAVRTVNEAL EARNFMAATT AAYNFWLYEL CDVYIEAIKP IADPVAEDQA
ARRSAQETLY TCLEAGMRLL HPFMPYVTEE LWQRLPRRKS HTAPSISIAP FPEVLDARNQ
ASAAHDFDNV MAAVRSVRAL ASDYGLATGI QAYLETSDAQ TAELLRSQQL IIVTLIKGCT
SVEVVSASEV PQGCAVASLP SARTNAHVLV KGKVDIDSEL SKLMAKVELN GAALAKIETQ
RSSADWEKTP AEVQQAALER EQNLEAEKQA LLAAKATFES LRG
//
