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Database: UniProt
Entry: C1E3K3_MICCC
LinkDB: C1E3K3_MICCC
Original site: C1E3K3_MICCC 
ID   C1E3K3_MICCC            Unreviewed;      1060 AA.
AC   C1E3K3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=MICPUN_96323 {ECO:0000313|EMBL:ACO62953.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO62953.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO62953.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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   EMBL; CP001325; ACO62953.1; -; Genomic_DNA.
DR   RefSeq; XP_002501695.1; XM_002501649.1.
DR   AlphaFoldDB; C1E3K3; -.
DR   STRING; 296587.C1E3K3; -.
DR   GeneID; 8242980; -.
DR   KEGG; mis:MICPUN_96323; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   InParanoid; C1E3K3; -.
DR   OMA; LDTWMDS; -.
DR   OrthoDB; 5473263at2759; -.
DR   Proteomes; UP000002009; Chromosome 4.
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: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; 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; 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; 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:UP000002009}.
FT   DOMAIN          108..733
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          781..930
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          994..1048
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  117895 MW;  8FF39817C380B105 CRC64;
     MKVAEEDPEA AAKKAAKKAA KAAEAAAKKA KLEAKKAKLA EMEAAKKAKE AAGGGDGGKK
     KKEKKGGVDE EDLAALKAAQ AVPKGEYKDP AVVPMAKAYD PKNVEAAWYD WWEKEGYFKP
     TMGTSKPKFV IVIPPPNVTG ALHIGHALTN SIQDTIVRWR RMSGYEALWV PGTDHAGIAT
     QTVVEKKLQR EEGITRHDLG REKFLERVFE WKEQYGGKIF NQLKRLGSSL DWSRERFTMD
     EMLSKAVKEA FVRMHADGLV YRDNRLVNWC CRLKTAISDI EVDYVDLDGS KEMSVPGQDG
     KVEFGSIWSF AYPIEGGGEI VVATTRPETM LGDTAVAVHP DDARYKDVQG KHVIHPFNGR
     KIPIICDAEL VDMSFGTGAV KITPAHDPND FQTGKRHNLE FINMLTEEGM INDEGGDRFK
     GMKRFTARPA VIAALDELGL YRGKADNPMR LGLCSRSKDV IEPMLKPQWW VACDKMAAEA
     CDAARSKELE ILPNFMEPTW FRWLENIRDW CISRQLWWGH RIPAYYVKFE GEAEEECGMP
     GGSSEKLDRW VIGREEDEAR AEAEKKFPGK AFTLEQDEDV LDTWFSSGLF PFSVFGWPDE
     TPDLAEFYPT ALLETGHDIL FFWVARMVMM GMKLTGKVPF KQVYLHAMVR DAHGRKMSKS
     LGNVIDPLHV IEGISLKDLN ETLTGGNLDE KEVKKAQQGQ AQDYPEGIPE CGTDAMRFAL
     VAYTAQGRDI NLDVLRVVGY RHWCNKLWNA IRFAIMNLGD DYKPPEEPLT VNTPGLPPAS
     KWALHRLNSA VKTTVDAMEV YDFSNATTGV YAFWQYDVCD VFIELMKPVM NGADEAAKKA
     TRDTLWTCLD GGLRLLHPFM PFVTEELWQR LPRRAAETAP SIMVADYPAF TDARVDAAVE
     ESMAVAQEIV KATRSLRAAY NLQPKAKAEL FVVTRGDVAT VAAKQFAEGI ATLAGCARVD
     VIGPDDEVPP GCGVTVINES VSVYLMLKGV VDPAAEIAKL EKKSSQTMKS IAALQKQMEM
     PGYEEKVPEN VRADNAEKLS KLGAEVASTA AAMEDFKKLI
//
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