ID A0A2G9G8H8_9LAMI Unreviewed; 1081 AA.
AC A0A2G9G8H8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=CDL12_25885 {ECO:0000313|EMBL:PIN01603.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN01603.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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:PIN01603.1}.
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DR EMBL; NKXS01006338; PIN01603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9G8H8; -.
DR STRING; 429701.A0A2G9G8H8; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279}.
FT DOMAIN 22..104
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 194..754
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 794..923
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 119..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 122484 MW; B906FA82F8B39F25 CRC64;
MAEETGKSFA RRDRLLEIES QVQKWWLEGD VFRADAKDLP PKAGEKFFGN FPFPYMNGYL
HLGHAFSFSK LEFAAAYHRL RGANVLLPFA FHCTGMPIKA SADKLTREIE MFGNPPVFPV
VKEEESGEPE GESEGNQTQP GGKFKGKKSK AIAKSGGVKY QWEIMQSYGL SDEEIAKFTN
PYHWLTFFPP LAVEDLKAFG LGCDWRRTFI TTDVNPYFDT FVRWQMRKLK EMGKIVKDLR
YAIYSPLDGQ PCADHDRASG EGVIPQEYTL IKMEVISPFP PKMSALEGKK VYLAAATLRP
ETMYGQTNCW VLPDGKYGAF EINDTDVFIL TKRAALNLAY QRLSRVPEKP TCLVELTGQD
LIGLPLKSPL AFNDVIYTLP MLSVLTDKGT GIVTSVPSDS PDDYMALHDL KAKPAFRAKY
GVKDEWVLPF EIIPIIHHPD FGDKSAERIC IEKKIKSQNE REKLDEAKKI IYKGGFYEGT
MLVGDYTGMK VQEAKSLIRN KLLELEQAVV YSEPEKKVIS RSGDECVVAL TDQWYITYGE
DEWKKAAEEC LAGMNLYSEE TRHGFEHTLS WLNQWACSRN FGLGTRIPWD EQFLVESLSD
STLYMAYYTV AHVLQRGDMY GADRSSIKPE QLTDEVWDFL FVNGPYPKSS EIPSSLLHKM
KQEFEYWYPF DLRVSGKDLI QNHLTFCIYN HAAIMPKHHW PGGFRCNGHI MLNSEKMSKS
TGNFRTLRQA IEEFSADATR FSLADAGDGM DDANFVFETA NAAILRLTKE ISWMEEVLAA
ESSLRNTPPT TYADHVFANE MNIAVKTTEK NYSEYMFREA LKTGFYDLQA ARDEYRLSCG
SGGMNRDLLW QFMDVQTRLI APICPHYAEY IWKVLLKKDG YVVNAGWPEG NSPDLTLKKA
NNYLQDTIVS MRKLLQKQIS GSKKSKTNIT NVQNKPTLGL IFVNEQYGGW KKECLKILQK
KFDAATSTFA PDQEILAELQ KSEIGQSSNF KQIQKLCMPF LRFKKDEVKA VGVQALDLKL
PFGEIEVLTE NCELIKRQLG LERLEVLSAI DADAVARAGD HASVLNSNPP SPGNPTAIFL
N
//
