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Database: UniProt
Entry: A0A3B4F332_9CICH
LinkDB: A0A3B4F332_9CICH
Original site: A0A3B4F332_9CICH 
ID   A0A3B4F332_9CICH        Unreviewed;       724 AA.
AC   A0A3B4F332;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   Name=tars {ECO:0000313|RefSeq:XP_005738194.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000004975.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000004975.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005738194.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_005738194.1; XM_005738137.2.
DR   AlphaFoldDB; A0A3B4F332; -.
DR   STRING; 303518.ENSPNYP00000004975; -.
DR   Ensembl; ENSPNYT00000005100.1; ENSPNYP00000004975.1; ENSPNYG00000003864.1.
DR   GeneID; 102204214; -.
DR   CTD; 6897; -.
DR   GeneTree; ENSGT00940000154969; -.
DR   OrthoDB; 1119631at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; Unplaced.
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; 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; THREONINE-TRNA LIGASE; 1.
DR   PANTHER; PTHR11451:SF54; THREONYL-TRNA SYNTHETASE; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|RefSeq:XP_005738194.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000695023}.
FT   DOMAIN          79..143
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          353..614
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  83280 MW;  73B259670A30691F CRC64;
     MAEKTVVDKM SELQVDEGKK EGTGSGKDGG KKKGKNAAED SGGRAELSPQ PQYIEERLTL
     YTKLKAEHDA LMAERAAKDS KPIKVTLPDG KVVEAESWKT TPYKVACGIS QGLADNTVIA
     KVNDSVWDLD RPLEEDCSLQ LLKFDDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE
     NGFYYDMFLE NNEGVSSNDF PCLESLCKKI IKEKQPFERL EIKKETLLEM FKYNTFKCRI
     LNEKVTTPTT TVYRCGPLID LCRGPHVRHT GKIKALKIHK NSSTYWEGKA DMETLQRIYG
     ISFPDPKMLK DWEKFQEEAK NRDHRKLGRE QDLFFFHDLS PGSCFFLPKG AFIYNTLIEF
     IRSEYRKRGF QEVVTPNVYN SKLWQTSGHW QHYSENMFSF EVEKEIFALK PMNCPGHCLM
     FDHRPRSWRE LPFRMADFGV LHRNELSGAL TGLTRVRRFQ QDDAHIFCSM DQIESEIKGC
     LDFLRTVYDV FGFTFKLNLS TRPEKFLGDP EVWDQAEKQL ENSLNEFGEK WVLNPGDGAF
     YGPKIDIQIK DAIGRYHQCA TIQLDFQLPI RFNLTFVSHD GDDKKRPVII HRAILGSVER
     MIAILTENYG GKWPLWLSPR QVMVVPVGPT CEEYAEKIKQ EFHSSGLMTD VDLDPSCTLN
     KKIRNAQLAQ YNFILVVGEK EKTSNTVNVR TRDNKVHGEH SVEECIKRLK QLKTSRCRNA
     EEEF
//
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