ID   A0A166I5P4_DAUCA        Unreviewed;       902 AA.
AC   A0A166I5P4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-OCT-2016, entry version 3.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZN10778.1};
GN   ORFNames=DCAR_003434 {ECO:0000313|EMBL:KZN10778.1};
OS   Daucus carota subsp. sativus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; campanulids; Apiales; Apiaceae; Apioideae;
OC   Scandiceae; Daucinae; Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN10778.1, ECO:0000313|Proteomes:UP000077755};
RN   [1] {ECO:0000313|EMBL:KZN10778.1, ECO:0000313|Proteomes:UP000077755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KZN10778.1};
RX   PubMed=27158781; DOI=10.1038/ng.3565;
RA   Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA   Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA   Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D.,
RA   Ashrafi H., Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT   "A high-quality carrot genome assembly provides new insights into
RT   carotenoid accumulation and asterid genome evolution.";
RL   Nat. Genet. 48:657-666(2016).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|RuleBase:RU363035}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KZN10778.1}.
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DR   EMBL; LNRQ01000001; KZN10778.1; -; Genomic_DNA.
DR   Proteomes; UP000077755; Chromosome 1.
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:InterPro.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|RuleBase:RU363035};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077755};
KW   Ligase {ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077755}.
FT   DOMAIN       33    171       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      175    562       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      619    762       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      825    889       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      823    850       {ECO:0000256|SAM:Coils}.
FT   COILED      865    892       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   902 AA;  103090 MW;  1FA9B3820F6B0485 CRC64;
     MIFQNAASAS SESDVFTSPE VSKSFDFTNE ERIYNWWESQ GYFKPNFDRE SDPFVVPMPP
     PNVTGSLHMG HAMFVTLEDI MVRYHRMKGK PTLWLPGTDH AGIATQLVVE RMLASEGIKR
     SELGRDEFTK RVWEWKEKYG GTITNQIKRL GASCDWTKER FTLDEQLSRK IVLYTEVEYS
     EEPGFLYYIK YRVAGGSRSD FLTIATTRPE TLFGDTALAV HPEDERYSKY VGMNAIVPQT
     YGRHIPIISD KYVDKEFGTG VLKISPGHDH NDYLLARKLG LPILNVMNKD GTLNDVAGLY
     SGLDRFEVRE KLWKDLEEID LAVEKKPYTL RVPRSQRGGE IIEPLVSKQW FVTMEPLAEK
     ALKAVEKGEL NIMPDRFEKI YNHWLTNIKD WCISRQLWWG HRIPVWYIVG KDCEEEYIVA
     RSSDEAITKA REKYGKNVEI YQDPDVLDTW FSSSLWPFST LGWPDVSAED FKRFYPTSML
     ETGHDILFFW VARMVMMGIE LTGKVPFSNI YLHGLIRDSQ GRKMSKTLGN VVDPIGTMQE
     FGTDALRFTL ALGTAGQDLN LSTERLTSNK AFTNKLWNAG KFVLQNLPKQ NDTSALSTML
     VYEFNKDECL LTLPLPECWV VSKLHILVDT VTTSYDKFFF GDVGREIYDF FWSDFADWYI
     ETSKARLYNS DGGAVSSVAQ AVLLYVFENI LKMLHPFMPY VTEELWQALP NRTEALIVSS
     WPQTSLPRHT NSIKRFENFQ ALTRAIRNAR AEYSVEPAKR ISASIVANSE VTQYISEFVV
     AIILKQGHDV KWYAFPGCPD DANQSVHLVA GEGLEAYLPL ADMVDITAEV QRLSKRINKM
     QKEYDGLVAR LSSPEFIEKA PREIIDGIKE KASEAEEKLT LTKNRLTFLE STTVVAGSIH
     PA
//