ID F0VPH1_NEOCL Unreviewed; 781 AA.
AC F0VPH1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=threonine--tRNA ligase {ECO:0000256|ARBA:ARBA00013163};
DE EC=6.1.1.3 {ECO:0000256|ARBA:ARBA00013163};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031900};
GN ORFNames=BN1204_060420 {ECO:0000313|EMBL:CEL70359.1}, NCLIV_060420
GN {ECO:0000313|EMBL:CBZ55617.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ55617.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|EMBL:CBZ55617.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ55617.1};
RA Aslett M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBZ55617.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ55617.1};
RA Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA Wastling J.M., Pain A.;
RT "Comparative genomics and transcriptomics of Neospora caninum and
RT Toxoplasma gondii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
RN [4] {ECO:0000313|EMBL:CEL70359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CEL70359.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000070};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; FR823393; CBZ55617.1; -; Genomic_DNA.
DR EMBL; LN714487; CEL70359.1; -; Genomic_DNA.
DR RefSeq; XP_003885645.1; XM_003885596.1.
DR AlphaFoldDB; F0VPH1; -.
DR GeneID; 13441048; -.
DR VEuPathDB; ToxoDB:NCLIV_060420; -.
DR eggNOG; KOG1637; Eukaryota.
DR InParanoid; F0VPH1; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000007494; Chromosome XII.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd01667; TGS_ThrRS; 1.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF46; THREONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:CEL70359.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 59..153
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 321..664
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 594..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88455 MW; B0E41C72F0123C54 CRC64;
MASGRRAEKG TVAALATAEK IGDPNFQVTE NPGFLQRRLQ VFDALYEKQN QRLKEKPRQE
ISIELPDGSK KSGTAYETSP YDIALEISKS LADASLVAKV LYEPGVGTEA ITAADDEEEE
CACGEHEESQ DDKWILFDMR RPLEGSCKLQ LLKFDSDEAK HVFWHSSAHI LGQAIEATFG
AQLTVGPALT NGFYYDAYMG NATVTEESYG RLEAAAANVI KADQPFCRLV CSKAEALELF
ADNPFKVQLI SSKIPEGGST TVYRCGALVD LCRGPHVPST GKVKAFQVTK HSATYWLGRQ
NLDSLQRVYG VSFPDKKLLK EYLKLVEEAK KRDHRMLGQN LHLFFFDTNV SPGSCFWLPD
GAKVYNKLCA FMREEYRFRG FQEVISPNIF SCDLWKMSGH YQNYKENMYL FDVEGKEWGL
KPMNCPGHCI MFKHLAPSYR QLPLRLADFG VLHRNELSGS LTGLTRVRRF QQDDAHIFCR
MDQVKQEVAD ALNFLFFVYD QFGFSFELFL STRPKKALGD RSLWDAAEGA LKEALEETGR
PWQLNPGDGA FYGPKIDIRL WDALKRPHQC GTIQLDFQLP IRFNLQYRTQ DEAVAASREK
AKDEKSEKRT ENGDEPEATK EEEFGVEQPL RPGMARPVII HRAILGSIER MCAVVIEHTG
GKLPFWLSPR QCIVLPISDK VNDYATSVRD VLHSCGYEVG LDVSNNTVNK KIREAQLQQW
NYLLVVGEKE RADKTVTVRD RADPEHQHVL SMEDLLQLFE KQGMPNSKKT LTLDAWKTSQ
Q
//
