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Database: UniProt
Entry: A0A1C6LFR5_9NEIS
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ID   A0A1C6LFR5_9NEIS        Unreviewed;       633 AA.
AC   A0A1C6LFR5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=PSELUDRAFT_0112 {ECO:0000313|EMBL:SCK05427.1};
OS   Vogesella sp. LIG4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK05427.1, ECO:0000313|Proteomes:UP000198213};
RN   [1] {ECO:0000313|EMBL:SCK05427.1, ECO:0000313|Proteomes:UP000198213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00184}.
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DR   EMBL; LT607802; SCK05427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6LFR5; -.
DR   OrthoDB; 9802304at2; -.
DR   Proteomes; UP000198213; Chromosome i.
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:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000198213};
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..61
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          242..533
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          242..533
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
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         510
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   633 AA;  71752 MW;  7DCA7A728795CB0F CRC64;
     MPDIRLPDGS VRSFDKPVTV HEVAASIGTG LARAALAGRV DGKLVDTSHL IDANADLAII
     TDKDADGLSI IRHSTAHLLA YAVKELFPEA QVTIGPEIEN GFYYDFAYKR PFTPEDLVAI
     EKKMSELAKK DIPVERYELP RDEAIAYFKS IGEAYKAEII ASIPQGEVLS LYREGEFTDL
     CRGPHVPSTG KLKVFKLMKV AGAYWRGDSN NEMLQRVYGT AWAKKEDLEQ YLHMLEEAEK
     RDHRKLGKQL DLFHLQDEAP GMVFWHPKGW QLWQSIEQYM RKTLAAAGYQ EIRTPMVMDR
     VMWEKSGHWE NYRDAMFTTE SEKRDYAVKP MNCPGHVQVF NSGLRSYREL PMRLAEFGAC
     HRNEPSGALH GIMRVRGFVQ DDAHIFCTDD QIIAEAKAFN ELTMAVYKRF GFEQVSVKLS
     LRPEKYAGTL ETWDRAEEGL REALRACGIE WEELPGEGAF YGPKIEYHIK DALGRSWQCG
     TLQLDYVLPE RLDAEYVADD NSRKRPVMLH RAVLGSLERF IGILIENHAG AFPLWLAPVQ
     MVVMNITSAQ AEYAQQVADK LRSQGFRVDL DLRNEKIGYK IREHSLQKLP YQVVIGDKEM
     EGGLVAVRAR GEDLGQMSVD AFVQQLTAAL AQN
//
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