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Database: UniProt
Entry: A0A091IP25_EGRGA
LinkDB: A0A091IP25_EGRGA
Original site: A0A091IP25_EGRGA 
ID   A0A091IP25_EGRGA        Unreviewed;      1175 AA.
AC   A0A091IP25;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
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};
DE   Flags: Fragment;
GN   ORFNames=Z169_00051 {ECO:0000313|EMBL:KFP10102.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP10102.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP10102.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP10102.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; KK500767; KFP10102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091IP25; -.
DR   STRING; 188379.A0A091IP25; -.
DR   Proteomes; UP000053119; 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   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:UP000053119}.
FT   DOMAIN          18..101
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          185..754
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          793..907
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP10102.1"
FT   NON_TER         1175
FT                   /evidence="ECO:0000313|EMBL:KFP10102.1"
SQ   SEQUENCE   1175 AA;  134548 MW;  3C2DCD8B44844CF7 CRC64;
     ERKGTAKVDF LKKIEKEIQQ KWDDERVFEI DASDRQNQKS KGKYFVTFPY PYMNGRLHLG
     HTFSLSKCEF AIGYQRLKGK NCLFPFGLHC TGMPIKACAD KLKREMELYG CPPEFPDEEE
     EEEENSAKKE EEIVIKDKTK GKKSKAAAKT GSSKYQWGIM KSLGLSDEEV VNFSEAEHWL
     DYFPPLAVQD LKSMGLKVDW RRSFITTDVN PYYDSFVRWQ FLTLKERNKI KFGKRYTIYS
     PKDGQPCMDH DRQTGEGVGP QEYTLIKMKV LDPYPAKLSG LRGKNIFLVA ATLRPETMFG
     QTNCWVRPDM KYIGFETVNG DIFICTQRAA RNMSYQGFTK DNGVVPVVKE LMGEEILGAA
     LSAPLTAYKV IYALPMLTIK EDKGTGVVTS VPSDSPDDIA ALRDLKKKQA LRVKYGIKDE
     MVLPFEPVPI IEIPGYGNLC APSVCDELKI QSQNDREKLA EAKERVYLKG FYEGVMLVDG
     FKGQKVQDVK KLIQKMMVDN DEAMIYMEPE KQVMSRSADE CVVALCDQWY LDYGEVNWKK
     QASECLQHLE TFCEETRRNF EATLGWLQEH ACSRTYGLGT RLPWDEQWLI ESLSDSTIYM
     AYYTVAHLLQ GGNLRGQGES PLGIRAHQMS KEVWDYIFFK AAPFPKTEIP KEKLDKLKEE
     FEFWYPVDLR VSGKDLVPNH LSYYLYNHVA MWSDQREKWP VAVRANGHLL LNSEKMSKST
     GNFLTLTQAV DKFSADGMRL ALADAGDTVE DANFVEAMAD AGILRLYTWV EWVKEMIANR
     DSLRSGPANT FNDRVFASEM SAGILKTDQN YEKMMFKEAL KTGFFEFQSA KDKYRELAIE
     GMHRELVFQF IEVQTLLLAP ICPHLCEHIW SLLGKSDSIM RASWPTAGPV DEVLIRSSQY
     LMEVAHDLRL RLKNYMAPAK GKKSTKEPSQ KPSHCTIYVA KNYPPWQHTT LSVLRKHYQV
     SGGQLPDNKV IASELNTLPE LKKYMKKVMP FVAMIKENLE KNGSRVLDLE LEFDECAVLM
     ENLVYLTNSL ELDHIEVKFA SEAEDKIKED CCPGKPFSIF RTEPSVSVFL VNPQPSNGHF
     STKIEIRQGD NRETVIRRLM KMDRGIKDLS KVKLMRFDDP VLGPRRVPVL GKEEAEKTPI
     LDQAIFHIDL DEKRVRVTEN GLTRDIGDTI VYLVH
//
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