ID F7VSV2_SORMK Unreviewed; 1043 AA.
AC F7VSV2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=SMAC_05409 {ECO:0000313|EMBL:CCC08769.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC08769.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC08769.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC08769.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(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:CCC08769.1}.
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DR EMBL; CABT02000006; CCC08769.1; -; Genomic_DNA.
DR RefSeq; XP_003347110.1; XM_003347062.1.
DR AlphaFoldDB; F7VSV2; -.
DR STRING; 771870.F7VSV2; -.
DR GeneID; 10804523; -.
DR KEGG; smp:SMAC_05409; -.
DR VEuPathDB; FungiDB:SMAC_05409; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_2_1; -.
DR InParanoid; F7VSV2; -.
DR OMA; TIMPPIC; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000001881; 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; 2.170.220.10; -; 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 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:UP000001881}.
FT DOMAIN 99..719
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 763..908
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1014..1041
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 117900 MW; 9D0511A5DBE2ADC6 CRC64;
MAEDQPVAAP AAAPAAPAPK KNDKKEKAKA DKAAKFAAKQ AAAKAKQPAA VSAPKEKKEK
TPALPPYEDN TPAGQKKVIQ SFEHPHFSAY NPSAVEAAWY QWWEKAGYFK PEACRKPSAG
KFVIPLPPPN VTGALHCGHA LANSLQDTLI RWYRMKGYET LWVPGCDHAG ISTQSVVEKM
LWKKEKKIRQ ELGREKFTEL VWEWKGDYHQ RINNAQKLMG GSMDWEREAF TMDKNLTAAT
METFCRLHDE GLIYRSNRLV NWCTHLNTAL SGLEVENKEI TGRTLLDVPG YDKKVEFGVL
THFKYQIDGS EETIEVATTR PETMLGDTGI AVNPEDPRYT HLVGKFARHP FVDRLLPIVT
DSYVDKEFGT GAVKLTPAHD FNDYQLGQRH NLEFINILNE NGTLNDNAGP FKGQKRFDAR
YTVVEELTKL GLFVKKEPNP MKIPLCEKSK DVIEPMMTEQ WWVRMKEMGE AALQVVEEGK
VKISPESANK SYKRWLADIQ DWCISRQLWW GHRIPAYRVI FEGEEGQREH EKSEWIVGRT
QEEAQAKAEA KFAGRKFTLE QDPDCLDTWF SSGLWPMAIL GWPNTENLDF KKFFPTSMLE
TGWDILFFWV ARMIMLSLKM TGEVPFTEVY CHSLIRDSEG RKMSKSLGNV IDPLDIIRGI
ELEDLHAKLL VGNLKEDEVA RATKYQKTAF PGGIPECGAD AMRFTLLSYT TGGGDINFDI
KVMHAYRRFC NKIWQATKYV LGKLPQEFVP KAELDVANLS VPEKWILHRM NVAVKGMNDA
LEAREFSRAT KVAYQFFYDE LCDVFIENSK GILSDGTPEE QQSVQQTLYH TIDVALRLLH
PIMPYITEEL WQRLPRKQGD GETIMLAPYP TFESQLEFAT EAEDYELGLK CAGGIRSLAA
DYNIKSDGSA FIKATTEGSL ATVNAQIAAI RTLCGKGVKE VRVLAADEEL PRGCAVYVIN
AEITVLLQVG GNISDIDAEI KKITTKLQKT DLTIKKQQEL LSKDGFEKVS EAVQESEKQK
LADAQAAKEN YQRTLEEFSK LKI
//
