ID F6HP70_VITVI Unreviewed; 1318 AA.
AC F6HP70;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=VIT_16s0100g00370 {ECO:0000313|EMBL:CCB56476.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB56476.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN596000; CCB56476.1; -; Genomic_DNA.
DR STRING; 29760.F6HP70; -.
DR PaxDb; 29760-VIT_16s0100g00370-t01; -.
DR EnsemblPlants; Vitvi00g04527_t001; Vitvi00g04527_P001; Vitvi00g04527.
DR EnsemblPlants; Vitvi16g00938_t001; Vitvi16g00938_P001; Vitvi16g00938.
DR Gramene; Vitvi00g04527_t001; Vitvi00g04527_P001; Vitvi00g04527.
DR Gramene; Vitvi16g00938_t001; Vitvi16g00938_P001; Vitvi16g00938.
DR eggNOG; KOG0017; Eukaryota.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; F6HP70; -.
DR Proteomes; UP000009183; Chromosome 16.
DR ExpressionAtlas; F6HP70; baseline and differential.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
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; IPR001584; Integrase_cat-core.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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 PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50994; INTEGRASE; 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:UP000009183}.
FT DOMAIN 514..680
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1241..1310
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 150592 MW; FD7FAC36F283F684 CRC64;
MDSQVETEAK PDIEDPEKKK KKEEKAKAKE LKKLKALQKA EAAKLQAQQA SSNASKKSER
KIKRDAEGEN AEDYIDPETP FGEKKRLSRQ MAKQYSPSAV ENSWYEWWEK SGFFVADSSS
SKPPFVIVLP PPNVTGALHI GHALTSAIQD TIIRWRRMSG YNALWVPGMD HAGIATQVVV
EKKLMRERKL TRHDIGRENF VSEVWNWKNE YGGVILKQQR RMGASLDWTR ECFTMDEKRS
LAVTEAFVRL YKEGLIYRDL RLVNWDCILR TAISDIEVDY EDIKVRTLLK VPGYEKPVEF
GVLTSFAYPI EGGEEIVVAT TRVETMLGDT AIAVHPDDER YTRFHGKFAI HPFNGRKLPI
ICDAILVDKN FGTGAVKITP AHDPNDFEVG KRHNLEFINI FTDDGKINSN GGPEFAGMPR
FKAREAVVAA LHEKGLYKGA KDNEMRLGLC SRTKDVVEPL IKPQWYVSCS GIANEALDAV
MDDENRKIEI IPKQYAADWK RTGVRGRRLR LNNRAKSPFE LVHTDVWGPC RTASTLGFQY
FVTFIDDYSR CTWLFLMKNR AELFSIFQKF YTEIQTQFNI SIRVLRSDNA REYFSAQFTS
FMSHHGILHQ SSCAHTPQQN GVAERKNRHL VETARTLLLH NHVPFRFWGD AVLTACYLIN
RMPSSPLGDP GRYRRLVGKL NYLTITRPDI SFPVSVVSQF LQSPCDSHWD AVIRILRYIK
STPGQGVLYE NRGHTQVVGY TDADWAGSPT DRRSTSGWLE NIRDWCVSRQ LWWGHRIPAW
YVTLEDDKMK ELGAYTDHWV VARNEEEAQI EASRMFPGKN FQISQDPDVL DTWFSSGLFP
LTVLGWPDDT QDLKAFYPTS VLETGHDILF FWVARMVMLG IKLGGDVPFR KVYLHPMIRD
AHGRKMSKSL GNVIDPLEVI NGISLEGLHK RLEEGNLDPS ELVVAKEGQV KDFPNGIAEC
GADALRFALV TYTAQSDRIN LDIQRVVGYR QWCNKLWNAI RFAMSKLGDD YTPPMEIVPD
VMPFTCQWIL SVLNKAISKT VSSMDSYEFA DAASTVYSWW QFQLCDVFIE VVKPFFSSND
PKFASARRFA QDTLWVCLDN GLRLLHPFMP FVTEELWQRL PPARDCARKE SIVISDYPSV
VQCWTNERVE YEMDLVESTV KSLRSLRSLM PAKERHERRP AYVLCRTDAI AEIINSYELE
ILTLATLSSL KVLNEGDDAP IGCAVSVVNE SLSVYLKLQG ALNAEAEREK LRKKMEEIRK
QQEHLTQIMS ASGYQEKVPA RIHEENVAKL SSLMQELLSF EQASQHLERD IAAEQESH
//
