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Database: UniProt
Entry: F6HK37_VITVI
LinkDB: F6HK37_VITVI
Original site: F6HK37_VITVI 
ID   F6HK37_VITVI            Unreviewed;      1085 AA.
AC   F6HK37;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN   OrderedLocusNames=VIT_12s0035g01160 {ECO:0000313|EMBL:CCB55040.1};
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:CCB55040.1, 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   -!- 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; FN595990; CCB55040.1; -; Genomic_DNA.
DR   RefSeq; XP_002264666.1; XM_002264630.3.
DR   AlphaFoldDB; F6HK37; -.
DR   STRING; 29760.F6HK37; -.
DR   PaxDb; 29760-VIT_12s0035g01160-t01; -.
DR   EnsemblPlants; Vitvi12g02058_t001; Vitvi12g02058_P001; Vitvi12g02058.
DR   GeneID; 100248927; -.
DR   Gramene; Vitvi12g02058_t001; Vitvi12g02058_P001; Vitvi12g02058.
DR   KEGG; vvi:100248927; -.
DR   eggNOG; KOG0437; Eukaryota.
DR   HOGENOM; CLU_004174_1_1_1; -.
DR   InParanoid; F6HK37; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000009183; Chromosome 12.
DR   ExpressionAtlas; F6HK37; baseline and differential.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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   NCBIfam; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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:UP000009183}.
FT   DOMAIN          21..105
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          193..754
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          794..924
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          114..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1085 AA;  122695 MW;  40A4EACE401F7D41 CRC64;
     MEGSKSFARR DRLLEIEVKV RNWWEEKDVF RAEAGEKPPE PGEKFFGNFP YPYMNGFLHL
     GHAFSLSKLE FAAAFHRLRG ANVLLPFGFH CTGMPIKASA DKLAWEIQQF GDPPVFPTEV
     EEQPGEEPEP EDPNGGAPAL PDKFKGKKSK AASKSSGQMY QWEIMRSFGL SDSEISKFQN
     PYNWLSFFPP LAMEDLKAFG LGCDWRRSFI TTDMNPYYDN FIKWQMRKLK AIGKIVKDVR
     YTIYSPLDGQ PCADHDRASG EGVQPQEYTL IKMEVVSPYP PKLSSLEGKK VYLAAATLRP
     ETMYGQTNAW VLPDGKYGAF EINDDEVFII TQRAALNLAY QNFSKVPEKP TCLVELTGYD
     LIGLPLKSPL SFNEIIYSLP MLSILTDKGT GIVTSVPSDA PDDYMALHDL KSKPAFRAKY
     GVKDEWIMPF EIIPIIDIPE YGDRSAEKVC NDLKIKSQNE KEKLAEAKRL TYLRGFTEGT
     MLVGEFAGRK VQEAKPLIRS KLIEIGQAIV YSEPEKRVMS RSGDECVVAL TDQWYIIYGE
     PEWKKLAEDC LSNMNLYSDE TRHGFEHTLS WLNQWACSRS FGLGTRFPWD EEFLVESLSD
     STIYMAYYTV AHILQNGDLY GSGTSSVKPE QMTDEVWDFL FSGGPYPTSS DIPSSILNKM
     KQEFEYWYPF DLRVSGKDLI QNHLTFCIYN HTAIMSKNHW PRGFRCNGHI MLNSEKMSKS
     TGNFRTLRQA IEEFSADATR FSLADAGDGV DDANFVFETA NAAILRLTKE LSWMEEVLEA
     EASLRTGALS TYADQVFANE INIAVTLTEQ HYRNCMFREA LKTGFYDLQA ARDEYRFSCG
     AGGMNHDLVW RFMDVQTCLI TPICPHYAEY VRREILKKDG FAVHAGWPTA DSPDLTLKAA
     NKYLQDSIVL MRKLLQKQIL GSKKANKKGA PVTSLTESNL KGLIYVNEQY DGWKEECLRI
     LQSKFDSRNR TFAADKEILE ALQRSSVGQA TNSKQVQKLC MPFLRFKKDE AVALGPQALD
     LRLPFGEIEV LRGNLDLIKR QLGLEQVEIL SGTDPDALAK AGNLVSLLNQ NPPSPGNPTA
     IFLTI
//
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