ID A0A9P0MLT4_NEZVI Unreviewed; 961 AA.
AC A0A9P0MLT4;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
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=NEZAVI_LOCUS6122 {ECO:0000313|EMBL:CAH1395952.1};
OS Nezara viridula (Southern green stink bug) (Cimex viridulus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Pentatomomorpha; Pentatomoidea; Pentatomidae; Pentatominae; Nezara.
OX NCBI_TaxID=85310 {ECO:0000313|EMBL:CAH1395952.1, ECO:0000313|Proteomes:UP001152798};
RN [1] {ECO:0000313|EMBL:CAH1395952.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; OV725079; CAH1395952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P0MLT4; -.
DR OrthoDB; 629407at2759; -.
DR Proteomes; UP001152798; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000020; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000078; Valine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; NF004349; PRK05729.1; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP001152798}.
FT DOMAIN 43..641
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 697..842
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 905..960
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 961 AA; 110963 MW; 61D28A551430798B CRC64;
MFCGFNTFQP TLKKINVNTL RLFENFPGIS NSFKPNVFED DNYSQWVDKG LFQPRKNGQI
YSILLPPPNV TGTLHIGHAL TISVQDTMAR WNRMCQNEVV WTPGVDHAGI ATQVIVEKFL
MKQGISRFDI GRTKFVEEVW KWKSDKSKVI NLQIKKLGAS VDWEREFFTL DKKHRDAVNF
ALIQLFKKEL IYREESLINW SPHLRSVVSD IEVDYIDIDG PTALSLPGYS KPITFGNLID
FSYRIVGSAD KEIVVSTTRI ETMFGDVAIA VNPNDNRYKP YWGCKFHHPF NGTEIPLVLD
HRVDPTFGTG AVKITPAHDP TDFQISKSHS LPKRSVINEE GVLENCGGFS GMLRFDARES
ICSELANLGL LKHIRPHKMK IPICSRSGDV LEYLIKPQWF IKCKEMAKKA IVAVEERKLI
IKPENYQENW FNWLKNIQDW CISRQLWWGH QLPFYYCEGS NDNVWIAAEN EEEALKKSKY
YVSGPVIAHR DPDVLDTWFS SGILPFACFG WPDKTEQYKK YYPLNTLITG NDILFFWVAR
MVMLGLELTN QLPFKEVFLH GIICDSQGRK MSKSLGNVIA PEDVINGKSL KELHCTIENS
LLSSEEKQKA YTSLRNLYPE GISECGVDAL RFTLLSNNIK SQYINFDLKQ CIRNKHFCNK
IWQACYFANL WLKKMNLTSE FLMLDLCENH QPCTLMEKWI LAKLNYSIYV VNEGIKNGDF
HLSTSSLRNF IHLELCDIYI EYIKPTLQKG SSAESRSALQ TLVYTLVTSL KCMSPFMPFL
TEHLYQSLPI KKNGFIMETS YPSYNENFQK THKELLERVS SILMVINEIR RIKHRIGINH
QQVSVCIVEH SIELQNFKDV IETLAKCKIN FGTPNIEINS WIEENVSGFT TYFQQDVYKS
KVMDRAALSD RRNKLQIKLN KLLDISKNEG YQKNAPLKVK KSHCDQIESL KKEIEKLEVN
N
//
