ID I4ANJ5_BERLS Unreviewed; 647 AA.
AC I4ANJ5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Fleli_3198 {ECO:0000313|EMBL:AFM05530.1};
OS Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB
OS 1366 / Fx l1 / Sio-4) (Flexibacter litoralis).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Bernardetiaceae;
OC Bernardetia.
OX NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM05530.1, ECO:0000313|Proteomes:UP000006054};
RN [1] {ECO:0000313|Proteomes:UP000006054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4
RC {ECO:0000313|Proteomes:UP000006054};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Lang E., Kopitz M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Flexibacter litoralis DSM 6794.";
RL Submitted (JUN-2012) 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|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; CP003345; AFM05530.1; -; Genomic_DNA.
DR RefSeq; WP_014798960.1; NC_018018.1.
DR AlphaFoldDB; I4ANJ5; -.
DR STRING; 880071.Fleli_3198; -.
DR KEGG; fli:Fleli_3198; -.
DR PATRIC; fig|880071.3.peg.3200; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_10; -.
DR OrthoDB; 9802304at2; -.
DR Proteomes; UP000006054; Chromosome.
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:UP000006054};
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..63
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 244..555
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
SQ SEQUENCE 647 AA; 74094 MW; D46AD19DE90C479D CRC64;
MSKINVTLPD GSLRTYPQGV TAFDVAKSIS EGLARNVLAA EVNGEVWDST RALPETTALK
LLTWNDENGK MAFWHSSAHL LAEALEALYK NVKFAIGPPI ENGFYYDVDF GEKTFSSDDL
PKIEKKMKEL ARQKNEFVRK EVSKADAIAY FTEKADPYKL EMIDALEDGS ITFYTQGNFT
DLCRGPHIPH TGTVKAVKLL SVAGAYWRGD ENRQQLTRIY GITFPKEKEL KEYLIQVEEA
KKRDHRKLGK ELELFTFSER VGLGLPLWLP KGTMLRERLE QFLRKEQIKR GYDPVVTPHI
GHKNLYVTSG HYEKYGEDAF QPIKTPSEDE EFFLKPMNCP HHCEIYKTKP HSYRDLPLRL
AEFGTVYRYE QSGELHGLTR VRGFTQDDAH IFCTPEQVKD EFKSVIDLVL YVFKVFGFTE
YSAQVSLRDP DNKTKYVGSD ENWNLAERQI KEAAEEKGLN TIIEYGEAAF YGPKLDFMVR
DAIGRKWQLG TIQVDYNLPE RFELEYTGSD NKPHRPVMIH RAPFGSIERF VAILIESTGG
NFPLWLSPDQ LVVLPISERF NDYAKEIVQK LRQNDIRGTI DERNEKIGRK IRDAEVGKTP
YMLLVGEKEV ESNMVSVRKK GEGDLGTMSL EDFTKHFISA VDAELAE
//
