ID H3ALQ2_LATCH Unreviewed; 676 AA.
AC H3ALQ2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=TARS1 {ECO:0000313|Ensembl:ENSLACP00000010573.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000010573.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000010573.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01101791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01101800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3ALQ2; -.
DR Ensembl; ENSLACT00000010652.1; ENSLACP00000010573.1; ENSLACG00000009316.1.
DR GeneTree; ENSGT00940000154969; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009316; Expressed in pelvic fin and 6 other cell types or tissues.
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; 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; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF36; THREONINE--TRNA LIGASE 1, CYTOPLASMIC; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 71..133
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 339..612
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 78324 MW; BF3F99BBD53D755C CRC64;
LKNMKVERKG NVGVEQHKEG GKKKTKEETA GGGRAELNPW PAYINERLDL YLKLKAEHDA
IIAERAVKES KPIKITLPDG KQIDGESWKT TPYQIACGIS QGLADNTVVT KVNKIVWDLD
RPLEEDCSLE LLKFDDEDAQ AVYWHSSAHI LGEAMERVYG GCLCYGPPIE NGFYYDMFLE
NEGVSSNDFP ALENLCKKIM KEKQPFERLE VKKETLLEMF KYNTFKCRIL NEKVNTPTTT
VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD MESLQRIYGI SFPDPKLLKE
WEKFQEEAKN RDHRKLGREQ ELFFFHDLSP GSCFFLPRGA YIYNTLIEFI RREYRVRGFQ
EVVTPNVFNS KLWQTSGHWQ HYGENMFSFE VEKEIFALKP MNCPGHCLMF DHRPRSWREL
PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAMK QIEEEIKGCL EFLRAVYTVF
GFTFKLNLST RPEKFLGDVE VWNQAEKQLE NSLKEFGEKW ELNPGDGAFY GPKIDIQIKD
AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIIH RAILGSVERM IAILTENYGG
KCFIVQKILK RPFWLSPRQV MIVPVGPTCD EYAQKMRQQF HNARLMTDVD LDAGCTLNKK
IRNAQLAQYN FILGKK
//
