ID A0A1U8AZ09_NELNU Unreviewed; 1063 AA.
AC A0A1U8AZ09;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=LOC104609078 {ECO:0000313|RefSeq:XP_010273593.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010273593.1};
RN [1] {ECO:0000313|RefSeq:XP_010273593.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_010273593.1; XM_010275291.2.
DR AlphaFoldDB; A0A1U8AZ09; -.
DR STRING; 4432.A0A1U8AZ09; -.
DR GeneID; 104609078; -.
DR KEGG; nnu:104609078; -.
DR eggNOG; KOG0432; Eukaryota.
DR InParanoid; A0A1U8AZ09; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000189703; Unplaced.
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:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
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 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 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:UP000189703}.
FT DOMAIN 97..719
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 765..908
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 979..1048
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 121613 MW; FC3897E905FE9AA1 CRC64;
MVEPGAEDLE RKKKKEEKAK EKELKKLKAA QKAEAAKLQA QKSSSAPKKS ERRNPKRDTG
EENPEDYFDP ETPIGEKKRL SRQMAKQYSP AAVEKSWYAW WEKSDFFVAD ASSSKPAFVI
VLPPPNVTGA LHIGHALTAA IQDTIIRWRR MSGYNALWVP GMDHAGIATQ VVVEKKIMRE
RNLTRHDIGR ERFVSEVWRW KDEYGGTILN QERRLGASLD WSRECFTMDE KRSKAVTEAF
VRLYREALIY RDHRLVNWDC ILRTAISDIE VDYRDIKERT LLKVPGYEDP VEFGVLTSFA
YPLEGGLGDI VVATTRVETM LGDTAIAIHP EDKRYSHLHG KFAIHPFNGR KLPIICDAIL
VDPEFGTGAV KITPAHDPND FEVGKRHNLE FINIFTDDGK INSNGGSEFE GMPRFKARTA
VIEALQKKGL YRGAQNNEMR LGLCSRSNDV VEPMIKPQWF VNCNSMAKEA LDAVMDDGNR
KVEIIPKQYA AEWRRWLENI RDWCISRQLW WGHRIPAWYV LLDDDQLKEF GAYNDHWVVA
RNEEEALLEA NKIFSGKKFQ MTQDPDVLDT WFSSGLFPLS VLGWPDETED LKTFYPTSVL
ETGHDILFFW VARMVMLGMK LGGDVPFRKV YLHPMIRDAH GRKMSKSLGN VIDPLEVING
ISLKGLHKRL EEGNLDPNEL AIAKEGQEKD FPDGIAECGA DALRFALVSY TAQSDKINLD
IQRVVSYRQW CNKLWNAIRF AMGKLGEDYV PPISLSLESM PFSCKWILSV LNSAISKTVS
SLNSYEFSDA ATAIYSWWQY QLCDVFIETI KPYFSGADTK FDSERIAARY TLWVCLDNGL
RLLHPFMPFV TEELWQRLPQ ATGVTKKESV MISEYPSVVK EWTNERIEQE VDLIVSIVKS
HRSLRSSLPS NQRLGRQPAL VLCLKDEVKE IIEAYKQDII TLANLSSLKV LREHDAMLDE
CAVSIVNENL SVHLPLQGTL NAEVEHEKLK KKREELLKQQ ENLMQMMNSS GYKEKVPVHI
QEDNVAKLKK LMEELDIVEK ADRRLGRENA NGIEENKDSL FSS
//
