ID U6L0U3_EIMTE Unreviewed; 1693 AA.
AC U6L0U3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=ETH_00014365 {ECO:0000313|EMBL:CDJ42209.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ42209.1};
RN [1] {ECO:0000313|EMBL:CDJ42209.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42209.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ42209.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42209.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG675701; CDJ42209.1; -; Genomic_DNA.
DR RefSeq; XP_013232959.1; XM_013377505.1.
DR EnsemblProtists; CDJ42209; CDJ42209; ETH_00014365.
DR GeneID; 25252030; -.
DR VEuPathDB; ToxoDB:ETH2_0515700; -.
DR VEuPathDB; ToxoDB:ETH_00014365; -.
DR OrthoDB; 213912at2759; -.
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 Gene3D; 3.40.50.620; HUPs; 3.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:CDJ42209.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1693
FT /note="valine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004673472"
FT DOMAIN 192..282
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 878..920
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 1171..1255
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT REGION 82..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1649..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1693 AA; 186770 MW; 987B40755D23E2D3 CRC64;
MTCPSFNLLL LLPPLLALNS FTVSRASSTL PRGFNQRAAW ICCPLEGLLG ATSDPTRQQE
RPRSAAEGTI AALPTALFKR QRTHHNGQPR LREPIAAASS NTGQPRETSL DSSRSDIDTT
GTGMSAAATA RAALQAHPIF PFTEMESTLL QWWESESLFE PMKLTEETAP EKAQAAEPPR
AATEECAGGV KVFCMAPPNL TGSLHAGHFM SLTIEDVLFR FQRQREASTH PPLGQQQKQQ
KQQQKQLQQR QSEERQQKKG EEPWDGTPQE WMRKQQQKQQ SEKLQQHVLR SFWVPGVDHA
GMGLQLLLER HLSKRRKKGL YVPRCCSHCL RSIVSNAFLE GRGLQLYGQQ LCMREPQQTR
ELSLRGLGSN SLMQECRGSS SNDSGRCSCS TRECEQQLGL LQRWLRICWT HIQRQQRSLG
LGCWWASACC TVSAAAVSLT RQAFVLLHES GLLRRQLHPL QALRGKEHRH FTVVVPNELL
EVKETHLTDQ QQRQQQQQKS EGGEECQEKL LTSLLQAAKW DGGLFVELPI SNGSSATNSS
SSSGGNGSDD DASIITRSSC SKASSSSSNS RRSGSSNSKG CDATEELQRL LVPVGSLQDF
LQVCAAVTDD SSIFYQLKGK QVCVPLLQRS VPVLLQERGD RKHPHVAAAS HHISYCTCSS
STSSNASTST NCHSTNGCSS SSIQPNNDRR DLLPAFAALQ WEAVPGRAQL AACVAAALRH
AVGTSLQQQQ QQQAAREKAL LAILLLTEGA QVHLSRQQPG EFVSTLNGQA TVTRAKPQWF
FATDRVAPRV VQLLCSPQNK TLQSHEQQVQ QDAYFTSSTW LQGVGTALPL PLPLTSASNK
EIESSSSRGA SSTNNGSSSA TYTDANGLDV IPGRYFPELL QQLQSDRTWC ISRQGWWGVP
VPAYLVRFKN QQQHQHLQQQ QEQEVPLCQR IVAAARVLDR CHSQAALGTS KGKRGSSCSQ
IRANLFEAYS AALHELQQRQ EQEQLQQQSG LQKTEGLDAA SASRASLPQL GPCCCSQNAG
PGPGAAGDAS TGKEFAVAAL DEATARRKAV AFIRQQQRQQ QKQHMQQHVQ HATEFEILED
TDVLDTWFSS ALWPLTSLFH AEETFSKRYG AATSGKQTQE QQQQPLKQQQ REYPKAQESG
RVSHADSALF DYQKQQQRLQ EGLENSSSFL FPRLYPYSCL VTGHDILPFW VARQLLLSVA
LCGVLPLSRV VLHPLLTDMR GHKLSKSKGN APKTQMDQWI TQYGADALRM SLLACCGARR
LSSIDACKVQ RASRGLTKIW NGARLLQLLR ERLQACESCA AEASQGLGCT STYSARLSLP
QRSALSSTSR MCDDVYSHLQ GGHVAAAAAR FWEFWEDLSD WILPAAQTEM KLADTLCKSH
HGSSEQQQRQ RIQQQHPQEE EDRLRARGRL WPAVLGRIYH DTVRALHPFA PFISEAIYLA
LFSIVPKSEA DGRGSGKKSG SYDNNGQSFA PASAFQPLLC SAWPVAGAYR DLQAETAVQV
VRTAVASVRR AMQEANKRPQ KQQPSEQQQP HHAGDASCAA GAMLNKDAGE TGNRGGCSVS
VRCTDEIMLT SLKEAVPLMA GLCDLPSKSF SISVLEHQQL HQNKQVEKKE DDLMPFRRRS
FLSRVVMLPG SRSNSRGDRA LELEVAASFG EGGGSSRAPS ARRTQKAAEG NCRHRLSLQR
KLQDLERRVT APE
//
