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Database: UniProt
Entry: A0A182K006_9DIPT
LinkDB: A0A182K006_9DIPT
Original site: A0A182K006_9DIPT 
ID   A0A182K006_9DIPT        Unreviewed;      1031 AA.
AC   A0A182K006;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|ARBA:ARBA00024407};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
OS   Anopheles christyi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR004088-PA, ECO:0000313|Proteomes:UP000075881};
RN   [1] {ECO:0000313|Proteomes:UP000075881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACHR004088-PA}
RP   IDENTIFICATION.
RC   STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR004088-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   AlphaFoldDB; A0A182K006; -.
DR   STRING; 43041.A0A182K006; -.
DR   EnsemblMetazoa; ACHR004088-RA; ACHR004088-PA; ACHR004088.
DR   VEuPathDB; VectorBase:ACHR004088; -.
DR   OrthoDB; 5473263at2759; -.
DR   Proteomes; UP000075881; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
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   Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 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}.
FT   DOMAIN          98..710
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          755..906
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          965..1028
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          962..1031
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1031 AA;  116984 MW;  F76D4A8875441140 CRC64;
     MTNPAHPQDN DAAAAPVKTE KQLKKEAEKA AKLAKLQEKL NKKQQQEQQA AIKPKLEKKV
     KETKEVAVYS GTTKEGEKKD LSGPFPDAYS PQYVEAAWYS WWEKEGFFKP EYGQRKLNSS
     KGQFVMVIPP PNVTGSLHLG HALTNAIEDA ITRWHRMKGR TTLWVPGCDH AGIATQVVVE
     KKLWREHKQT RHDLGREKFI EKIWQWRNEK GDRIYHQLKK LGSSFDWDRA CFTMDPKLCK
     AVTEAFVRMH EMGMIYRSSR LVNWSCTLRS AISDIEVDKV EVSGRTQLSI PGYVDKVEFG
     VLVSFAYKVI GSESDEIVVA TTRVETMLGD TAVAVHPKDA RYQHLHGKFV QHPFCDRKLP
     IVCDEFVEMA FGTGAVKITP AHDPNDYDVG KRHNLPFITI FSDDGIIVGD YGSFAGMKRF
     DARKAILSAL QEKGLYRDTK DNPMVVPVCS RSKDIVEPLI KPQWYVKCSE MATKATEAVR
     TGELAITPDV TQKNLLWWGH RIPAYQVVFK DPAKAPKNLS DENLWFVGRS EAEALSKAAT
     TLKVDKTLIS MKQDEDVLDT WFSSGLFPFS VFGWPDNTDD LKQFYPTTLL ETGHDILFFW
     VARMVFFGQT LLGKLPFKEV FLHPMVRDAH GRKMSKSLGN VIDPMDVITG ISLEGLHKQL
     YDSNLDPREI EKAKAGQKQD YPNGIPECGT DALRFALCAY MTQARDINLD IQRVQGYRFF
     CNKLWNATKF ALMYFPGDEK YENITSLDGL ESNLDRWILS RLAGCIESSN RGFEKYEFAL
     ATNACYNFWL YDLCDVYLEC LKTVFQTNNE SAKASARRTL YTCLNLGLKL LSPFMPFITE
     ELYQRLPRGD LAIVASICVA SYPELSSSPW KDESIEKGFE FVQKTARDIR SARSDYNIPN
     KTKTDAYFIC SDEGVRSALE RFTLELETMA FSQVHFGTVP PAGCAILTIS GQCVVHLMLK
     GLIEVEKEIE KMTKKQEALQ QTIAKLQQAM AVPNYTNKVP EDVRKANVEK LDQSKVEIER
     LSAAIDTLKL M
//
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