ID A0A093XIG7_9PEZI Unreviewed; 1079 AA.
AC A0A093XIG7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=O988_07255 {ECO:0000313|EMBL:KFX92463.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX92463.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX92463.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX92463.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- 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:KFX92463.1}.
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DR EMBL; JPJR01001682; KFX92463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XIG7; -.
DR STRING; 1391699.A0A093XIG7; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR Proteomes; UP000029329; 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 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:UP000029329}.
FT DOMAIN 130..752
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 797..945
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 121602 MW; B818F8900C2D97E2 CRC64;
MATNSGSTNP IGEQAGPTGP AASGNDAASK AGAPATGAEG TKVKSEKELE RERKKAEKQA
KFDAKKKGAA PAAAQSSKSK EKKAKAAEKA AEETLPEYVE ETPFGEKKIL KSFDDPQYKA
YNPIAVESAW YSWWEKEGFF KPEFTADGEI KPEGKFVIVE PPPNVTGMLH IGHALANALQ
DVMIRWNRMQ GKTTLWLPGC DHAGISTQSV VEKTLYRKEG KTRHDLGREK FVQTVWEWKG
EYHEKINAVL RKMGGSFDWT REAFTMDENL SAAVTETFCQ LHEEGTIYRA NRLVNWCTQL
NTALSNLEVE NKELTGRTLL DVPGYEKKIE FGVIVHFKYP IEGTEETIEV ATTRIETMLG
DTGIAVHPDD ERYKHLVGKN AVHPFIKGRL LPIFADTYVE KDFGTGAVKV TPAHDPNDFN
LGKSHNLEFI NILNDNGTFN ENGGVYEGQK RFDVRYKIQD DLKALGLFVD KKDNAMKVPL
CEKSKDVIEP LLKPQWWMKM DDLAAEAVKV VKNGEIKILP ESAEKSYYRW MESPQDWCLS
RQLWWGHQIP IYYAQIEGES SYDSDDKLWF AGRTEEQALE KARKALPGKT FTLKRDEDVL
DTWFSSGLWP FSTLGWPNAT HDFEKLYPTS MLETGWDILF FWVARMIFLG KKLTGKVPFT
EVYCHSLVRD SEGRKMSKSL GNVIDPQDII HGISLQDLHA KLQTGNLNPN EVEKATKYQK
TSFPDGIPQC GTDALRFALV SYTTGGGDIA FDIKVIFGYR KFCNKIYQAT KYVLGNLPAD
FVPRASAKKT GKESLAEKWV LHKFTNASKD INKALEEREF MRSTNIVYHY WYDSLCDVFI
ENSKAIIQNG TDEEKLSALN TLYTALEGAL TMIHPFMPFL TEELWQRLPR RQEDKTPSIV
KAKYPVYDAE MDDPASEEAY ELVLGVSKGI RSLMSEYSLK DEAEVYIQAF DSTSHSTVTA
QTQSIKSLCG KGVSTVQILG SADSRPAGCV PFSVSAAAVV FLRVTGRVDI DNEISKANKK
LQKTQQGIDK QRKILDDPDY KAKVSEALQE VERKRLADLE AEQRGFEETI KQFEQLKLE
//
