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Database: UniProt
Entry: A0A1J6IBH2_NICAT
LinkDB: A0A1J6IBH2_NICAT
Original site: A0A1J6IBH2_NICAT 
ID   A0A1J6IBH2_NICAT        Unreviewed;       971 AA.
AC   A0A1J6IBH2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-JAN-2026, entry version 36.
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=A4A49_03325 {ECO:0000313|EMBL:OIT01922.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451 {ECO:0000313|EMBL:OIT01922.1, ECO:0000313|Proteomes:UP000187609};
RN   [1] {ECO:0000313|EMBL:OIT01922.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UT {ECO:0000313|EMBL:OIT01922.1};
RA   Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Baldwin I.T.;
RT   "The genome of Nicotiana attenuata.";
RL   Submitted (NOV-2016) 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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIT01922.1}.
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DR   EMBL; MJEQ01037188; OIT01922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J6IBH2; -.
DR   SMR; A0A1J6IBH2; -.
DR   STRING; 49451.A0A1J6IBH2; -.
DR   Gramene; OIT01922; OIT01922; A4A49_03325.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000187609; Unassembled WGS sequence.
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:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
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; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR   FunFam; 1.10.730.10:FF:000014; Valine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000126; Valine--tRNA ligase chloroplastic/mitochondrial 2; 1.
DR   FunFam; 3.40.50.620:FF:000020; Valine--tRNA ligase, mitochondrial; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; NF004349; PRK05729.1; 1.
DR   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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|ARBA:ARBA00023054, 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:UP000187609}.
FT   DOMAIN          77..635
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          692..833
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          899..963
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          897..966
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   971 AA;  109845 MW;  117C13FFD5D7411D CRC64;
     MALRTSSSFL SSTSSSCSSS LCFRVNPLLF STQRRYTVSL SRSRRFFAMS AAAAESDGIF
     TSPEVAKSFD FSNEERIYKW WESQGYFKPN IDKGGDPFVV PMPPPNVTGS LHMGHAMFVT
     LEDIMIRYNR MKGRPTLWLP GTDHAGIATQ LVVERMLAAE GVKRADLGRD EFTKRVWEWK
     QKYGGTITNQ IKRLGASCDW TRERFTLDEQ LSRAVVEAFI RLHEKGLIYQ GSYMVNWSPN
     LQTAVSDLEV EYSEEPGTLY YIKYRVAGGS KNDYLTIATT RPETLFGDTA VAVNPQDERY
     AKFIGKQAIV PLTFGRHVPI LSDKYVDKDF GTGVLKISPG HDHNDYLLAR KLGLPILNVM
     NKDGTLNEVA GLYAGLDRFE ARKKLWSDLE ESGLAVKKEA HTSRVPRSQR GGEIIEPLVS
     KQWFVSMEPL AERALEAVSK GELTIMPERF EKIYNHWLSN IKDWCISRQL WWGHRIPVWY
     VSGKDCEEEY IVARSHREAL SKAQEKYGKN VEIYQDPDVL DTWFSSSLWP FSTLGWPDES
     AEDFKRFYPT SVLETGHDIL FFWVARMVMM GIEFTGTVPF SNVYLHGLIR DSQGRKMSKT
     LGNVIDPLDT IAEYGTDALR FTLALGTAGQ DLNLSMERLT SNKAFTNKLW NAGKFILRNL
     PHQDDTLAWE ALLAHKFDKV ESVVKLPLPE CWAVSKLHVL VDEVTASYEK LFFGDVGREI
     YDFFWADFAD WYIEVSKARL YHSGDHSVAS VSQAALLYIF GSILKLLHPF MPFVTEELWQ
     ALPSRQEALI VSAWPPTSLP RDIDSIKKFE NLQALTRAIR NVRAEYAVEP AKLISASIVA
     NPDVIQYISG EREVLALLSR LDLGNVNFAE APPGDANQSV HVVASEGLEA YLPLSDMVDI
     SAEVQRLSKR LVKMQAEYDG LMARLSSSSF VEKAPEDIVR GVREKAAKAE EKLTLTKNRL
     NFLKSKVLIA N
//
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