ID A0A0V1L918_9BILA Unreviewed; 1179 AA.
AC A0A0V1L918;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=trs-1 {ECO:0000313|EMBL:KRZ56000.1};
GN ORFNames=T02_5710 {ECO:0000313|EMBL:KRZ56000.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ56000.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ56000.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ56000.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ56000.1}.
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DR EMBL; JYDW01000103; KRZ56000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L918; -.
DR STRING; 6335.A0A0V1L918; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR013057; AA_transpt_TM.
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 PANTHER; PTHR11451:SF46; THREONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF01490; Aa_trans; 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|EMBL:KRZ56000.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 797..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 860..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 963..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 993..1018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1038..1060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1144..1172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..149
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 401..574
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ56000.1"
SQ SEQUENCE 1179 AA; 135511 MW; 5029C1BD2739234B CRC64;
LSTTVLLVGS RFRHLFFRRH IFYSSYNLKN IIPMEQEHST LESMMAKMDF GNKLDIEMNP
WPDFIQRRLD LWAKYMKNYN DELAKKQSEP ITVTLPDGKE VEAVSWRTSP LDIMTKLNMG
GRPIISKVDG VLWDLERPLE KSCNLQFLLF DDDEGKQVFW HSTAHVLGEA AERLFGCCLC
YGPPIENGFY YDMFMDDRTV TAEDMDKLEK IMKAAIDGKQ RFERLELKKE ELMEMFKYNP
FKLRILENKV KTPTTTAYRC GPLIDLCRGP HVRHTGLLNS FKITKNSSTF WEGDSSMESL
QRVYGVSFPS SKQLKLWEKM REEAASRDHR KLGRQQELFI FHELSPGSAF FFPRGAYIYN
TLVEFLRKQY RKRGFREVIT PNIYNSRLWE TSGHWQHYAK NMFKNELSGA LSGLTRVRRF
QQDDAHIFCR QDQIASEIEG CLDFLRFVYE TLGFSMKLYL STRPDDFMGD VKTWDEAEAQ
LQCALEKFKL PWTLNAGDGA FYGPKIDIIV LDAMQRQHQC ATIQLDFQLP VRFDLHYVDE
NHVKQRPVII HRAVLGSIER MIAVLTENFA GKWPFWLSPR QAMVIPVHPE FDDYALQVQQ
KIFDAGFECD VDVDASDTMK KKIRNAQLGK WNFILVVGAK EKENSSVNIR TRDNAVLGEY
SLEKLIEKFN FLKENYILKT SRFIIVTMKS VQLLKYSSTL DDDDYDSAES SSLQNKIIEQ
FSLSEVKKSN DNKNCEKLKI DDDNAVQNEE EIFKWLNEQR STFTYGLSDD QALTNLIKST
VGTGVLAVPE AFSNAGLWFG LIFLIFTVII NLCCLRILVR TSQMMCLRSG KAAVDYGTLA
ELSVFHGPKP LRRFKRHAKF LVNISLAFSQ LGMCSVYFVF IAEHIKQTVE VQNTFSLATY
MAFLLPLFLA LCSIRHLKYL AIPSTLANLV YCVAFVITFQ YIFQELPSWR RLPSIQSLDR
LPLAFGSLMF AFSAAGTILP IENKTKFPKS MNAWNGVLNT SCALSTILYI AVGFYGYIRF
GSDVAGSITL NLPKDEPLYK AVKLMVSFVV SISYPMQFYV PMDIVILKLQ QTIDRPGLRL
AAEYAIRYTL VLITFTFAEL VPHLGLFISL VGALTTSALT FIFPPIIEIL CEYRGSVHNR
RWQLLVFGNL LICLFGMVGL LTGTITSIKA ILHSFRVNE
//
