ID W5NBG8_LEPOC Unreviewed; 779 AA.
AC W5NBG8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017977.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017977.1}
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; AHAT01004956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NBG8; -.
DR STRING; 7918.ENSLOCP00000017977; -.
DR Ensembl; ENSLOCT00000018009.1; ENSLOCP00000017977.1; ENSLOCG00000014607.1.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000154969; -.
DR HOGENOM; CLU_008554_0_3_1; -.
DR InParanoid; W5NBG8; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000014607; Expressed in ovary and 13 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; IBA:GO_Central.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; 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:SF51; THREONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 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; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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:UP000018468}.
FT DOMAIN 405..669
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 67..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88475 MW; A9FB2659673F2124 CRC64;
MAETIVARLA AQEEQVRLLT QEVSWLRGGV GGDPAAVAGL CSSPELETLR SENEKLRYRI
LHLRRSLQSE SDPETGAREG EEGKETRAGK SSSREVPGNL TPNLLCLKGS ASCSHGSGYR
RSEDSSLLRQ ARHDHISVWR HRDTVSSGGA EVSSPCEEAA PGLQSLAGDV AWLAVLQFSC
LTTHGWPDTA GCGGVLGTYY WGFSAPESRI MKCRLLILRF DHTKTDCIER SNTLILHLNW
CRSSFVQSSC LTLGVCLSAG QLRLPQCSGD EEREAGELQG RAAIRRVHML ISHVFNTRNE
LFHFLKYNKF KCRILNEKVN TPTTTVYRCG PLIDLCRGPH VRHTGKIKAL KIYKNSSTYW
EGRADMETLQ RLYGISFPDS KMMKEWERFQ EEAKSRDHRK IGKEENPVHF RRGNAVIETQ
LCSWSRGCHN GRIHLRKTWS LSGHWQHYSD NMFSFPVEQD IFALKPMNCP GHCLMFSHRP
RSWRELPLRL ADFGVLHRNE LSGALTGLTR VRRFQQDDAH IFCAMEQIEN EMKGCLEFLR
CVYAVFGFSF QLHLSTRPEK FLGDIQIWDQ AEKQLENSLN EFGEPWKLNP GDGAFYGPKI
DIKIKDAIGR YHQCATIQLD FQLPIRFNLT FVDKEGNDKV RPVIIHRAIL GSVERMIAIL
TENYAGKWPL WLSPRQVMVV PVNPACEPYA QQVCQQFVEA GFMADVDLDS SCLLNKKIRN
AQLAQYNFIL VVGEKEKATG AVNVRTRDNK VHGELALAEA LARLRRLRDS RSRRAEEEF
//
