ID U4KN10_9MOLU Unreviewed; 640 AA.
AC U4KN10;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000256|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000256|HAMAP-Rule:MF_00184,
GN ECO:0000313|EMBL:CCV65667.1};
GN ORFNames=BN85306460 {ECO:0000313|EMBL:CCV65667.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV65667.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV65667.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
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, ECO:0000256|HAMAP-
CC Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00184}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00184}.
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DR EMBL; FO681348; CCV65667.1; -; Genomic_DNA.
DR RefSeq; WP_030004527.1; NC_022549.1.
DR AlphaFoldDB; U4KN10; -.
DR STRING; 61635.BN85306460; -.
DR KEGG; abra:BN85306460; -.
DR HOGENOM; CLU_008554_3_2_14; -.
DR OrthoDB; 9802304at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 3.30.54.20; -; 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; IPR012676; TGS-like.
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:SF56; THREONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 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; SSF81271; TGS-like; 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:0000256|HAMAP-Rule:MF_00184};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00184}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00184};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00184}; Reference proteome {ECO:0000313|Proteomes:UP000032737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00184}.
FT DOMAIN 1..60
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 270..538
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
SQ SEQUENCE 640 AA; 73672 MW; 542CD66DE30A179C CRC64;
MKLFLPDGKF LEVANNSTAF DVAKGISMSL AKKAVAAIYE GQVIELNKPI KADGHFKIIT
KEDPEAFAVL NHSSAHLLAQ AIKSIYPNAC FGVGPAIDEG FYYDVDLGDI KFTDELLPAI
EKKMVELSKQ GFDIVGKEVS YEEAKQIFSN DVYKLELIEG LKDDVITVYQ QGDFIDLCRG
GHVANTKEIK HFKLLNIAGA YWRGNSSNKQ LTRVYGVSFY SKEDLDKHLV MLEERKARDH
RKIGKEMGIF MITNEAGAGL PFWLKNGATI RRIIERYITD KEISLGYEHV YTPILANADL
YKTSGHWDHY QDSMFPPMDM GDGEKLVLRP MNCPHHMLIF KDTLHSYKEL PIRIAELGMM
HRYEKSGALS GLQRVREMTL NDAHIFVRPD QIKEEFTRTL NLLLEVYKDF KITDYKFRLS
YRDPENTEKY FKDDQMWEEA QKMLKEAMDE LNLNYFEAIG EAAFYGPKLD VQVKTALGND
ETLSTIQLDF LLPRRFELTY VGEDGKNDNT PVVIHRGIVS TMERFVAYLI EEYKGAFPLW
LAPVQLKVIP VNLNFHEDFA VELSEMFKKR GIRVELDLRN EKLGYKIREA QTKKIPYQLV
IGDKEVDNRS VTYRRYGKID QTSVALDEFI ELIENEINQK
//
