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Database: UniProt
Entry: S6AGF5_PSERE
LinkDB: S6AGF5_PSERE
Original site: S6AGF5_PSERE 
ID   S6AGF5_PSERE            Unreviewed;       640 AA.
AC   S6AGF5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
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:BAN49372.1};
GN   ORFNames=PCA10_36400 {ECO:0000313|EMBL:BAN49372.1};
OS   Pseudomonas resinovorans NBRC 106553.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN49372.1, ECO:0000313|Proteomes:UP000015503};
RN   [1] {ECO:0000313|EMBL:BAN49372.1, ECO:0000313|Proteomes:UP000015503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN49372.1,
RC   ECO:0000313|Proteomes:UP000015503};
RX   PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA   Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA   Fujita N., Nojiri H.;
RT   "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT   resinovorans Strain CA10 (NBRC 106553).";
RL   Genome Announc. 1:e00488-13(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|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00184}.
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DR   EMBL; AP013068; BAN49372.1; -; Genomic_DNA.
DR   RefSeq; WP_016493511.1; NC_021499.1.
DR   AlphaFoldDB; S6AGF5; -.
DR   STRING; 1245471.PCA10_36400; -.
DR   KEGG; pre:PCA10_36400; -.
DR   PATRIC; fig|1245471.3.peg.3674; -.
DR   eggNOG; COG0441; Bacteria.
DR   HOGENOM; CLU_008554_0_1_6; -.
DR   OrthoDB; 9802304at2; -.
DR   Proteomes; UP000015503; 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:UP000015503};
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   640 AA;  73093 MW;  1D089FE46C521CC7 CRC64;
     MPIITLPDGS QRTFDKPVSV LEVAQSIGAG LAKATLAGKV NGRLVDACDL IEDDASLQIV
     TPKDDDGLEI IRHSCAHLVG HAVKQLYPTA KMVIGPVIEE GFYYDIAFER PFTPEDMAAI
     EKRMAELIEK DYDVIKKMTP RAEVIELFKA RGEEYKLRLV DDMPDEKAMG LYFHEEYVDM
     CRGPHVPNTR FLKAFKLTKI SGAYWRGDSK NEQLQRVYGT AWADKKQLAA YIQRIEEAEK
     RDHRRIGKQL DLFHLQEEAP GMVFWHPDGW TVYQVLEQYM RKVQRDHGYV EVRTPQVVDR
     ILWERSGHWS NYAENMFTTS SESRDYAVKP MNCPCHVQIF NQGLKSYRDL PLRLAEFGAC
     HRNEPSGALH GIMRVRGFTQ DDAHIFCTED QVKKEAADFI KLTLQVYADF GFSDISMKLS
     TRPVKRVGSD ELWDRAEGAL ADALNESGLS WEYQPGEGAF YGPKIEFTLK DCLGRNWQCG
     TLQYDPNLPE RLDASYIAED NNRKRPVMLH RAILGSFERF IGMLIEHYAG AFPAWLAPTQ
     AVIMNITDKQ ADFALEVEKT LNESGFRAKS DLRNEKIGFK IREHTLLKVP YLLVIGDREV
     ETRSVAVRTR EGVDLGSMPF ESFSELLAQT VSRRGRQELE
//
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