ID A0A8X6N1V2_NEPPI Unreviewed; 1172 AA.
AC A0A8X6N1V2;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
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 Name=Lars1 {ECO:0000313|EMBL:GFS89453.1};
GN ORFNames=NPIL_77501 {ECO:0000313|EMBL:GFS89453.1};
OS Nephila pilipes (Giant wood spider) (Nephila maculata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Araneoidea; Nephilidae; Nephila.
OX NCBI_TaxID=299642 {ECO:0000313|EMBL:GFS89453.1, ECO:0000313|Proteomes:UP000887013};
RN [1] {ECO:0000313|EMBL:GFS89453.1}
RP NUCLEOTIDE SEQUENCE.
RA Kono N., Nakamura H., Mori M., Yoshida Y., Ohtoshi R., Malay A.D.,
RA Moran D.A.P., Tomita M., Numata K., Arakawa K.;
RT "Multicomponent nature underlies the extraordinary mechanical properties of
RT spider dragline silk.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00047469};
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:GFS89453.1}.
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DR EMBL; BMAW01053132; GFS89453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8X6N1V2; -.
DR OrthoDB; 10249672at2759; -.
DR Proteomes; UP000887013; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR FunFam; 1.10.730.10:FF:000020; Leucine--tRNA ligase cytoplasmic; 1.
DR FunFam; 3.90.740.10:FF:000001; Leucine--tRNA ligase, cytoplasmic; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; IPR054509; LARS1_ULD.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR055416; RBD_LARS1.
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 NCBIfam; NF008957; PRK12300.1; 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; PF24810; RBD_LARS1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF22947; ULD_3; 1.
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:UP000887013}.
FT DOMAIN 22..103
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 176..757
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 797..934
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 938..1009
FT /note="Leucine--tRNA ligase RagD-binding"
FT /evidence="ECO:0000259|Pfam:PF24810"
FT DOMAIN 1061..1171
FT /note="Leucine--tRNA ligase ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF22947"
SQ SEQUENCE 1172 AA; 134366 MW; 8723092F51981BA6 CRC64;
MAKERKGTFK VNVLLDIERT VQSEWEKKSI FEEDAPLSND TRTEKYFITF PYPYMNGRLH
LGHTFSLSKC EFAVGYQRLK GKKCLFPFGL HATGMPIKAC ADKLKFEIET YGFPPKFPVE
AIQNEMETEE KEIKLPADKA KGKKSKLTAK TGGATYQWQI MKTLGLSDDE IKKFAEVEYW
LKYFPPLAIQ DLKSMGVKVD WRRTFITTDC NPYYDSFVRW QFLRLKERGK IQFGKRYTIF
SPKDNQPCMD HDRSSGEGVG PQEYTLIKMK IVPPLPQKLS SFTGFSVFLV AATLRPETMY
GQTNCWVRPD MKYVAFQLFN GDIYICTHRA ARNMSYQGFT SENGKVSVLM ELEGKDILGL
PLQAPLTCYD IIYTLPMLTI KEDKGTGVVT SVPSDSPDDY AALRDLKKKP DLRKKFDITD
EMVMKYEPVP IIEMPEFGNM CAVTVCEELK VQSQNDRDKL ALAKDKVYLK AFYEGVMLVG
NHKGLKVQDV KKLIQKDMIN KNEAVLYMEP EKKIMSRSGD ECVVALCDQW YLDYGETTWK
NQALLALKGM ELYHVEVRRN FLATFDWLKE HACSRSYGLG TKLPWDENWL IESLSDSTIY
MAYYTVAHLL QGGVKGSIDG MKGSPLAIKP GDLTPEVWDY IFFKDAPYPK TKMEKSVLLK
LKREFEFWYP MDVRCSGKDL VPNHLTYFIY NHCAIWPSQP EKWPRSARAN GHLLLNSEKM
SKSTGNFLTL SEAVEKYSAD GMRMSLADAG DGIEDANFVE SMADAGVLRL YSFLEWVKEM
IAAKDQLRST TEETFNDKVF FNEINHCIVE SERNYEEMLY KEALRTAFFE LQAARDKYRE
LTVKELMSRD LVFKFIEVQV LLLSPICPHI CEHIWKLLGK QESIMKAKWP KVASVDKVLL
KASAYFMDVA HTFRLRQKNL KGKKGVSVAK PTHAVIWVAR TFPPWQSLVL QTLQKLYKEP
EGLPENKAIA SELGKLSDLK KYMKRVMPFA QVMKEKTKNL GISALNLFLD FDEMAILKEN
KEYLTSTLDL EELSFKYTDE TEDKALEDCC PGEPIIIYST ASSVSLKLIN QQPHNGYVEI
QLPIYEGTTA SSLISRIRKA QKIPEVKQVK LYRYNDIILG PRTIPVLGKT EDGKSVLRED
SKFSIELEKA SISLSENGKK FEIGSQVSYV VE
//
