UniProt: A0A2D0RQZ5

Database: UniProt
Entry: A0A2D0RQZ5_ICTPU

LinkDB:  A0A2D0RQZ5_ICTPU 
Original site:  A0A2D0RQZ5_ICTPU

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (12)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
All databases (19)   

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ID   A0A2D0RQZ5_ICTPU        Unreviewed;       809 AA.
AC   A0A2D0RQZ5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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   Name=lars2 {ECO:0000313|RefSeq:XP_017332933.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017332933.1};
RN   [1] {ECO:0000313|RefSeq:XP_017332933.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017332933.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); 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:ARBA00001372};
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   RefSeq; XP_017332933.1; XM_017477444.3.
DR   AlphaFoldDB; A0A2D0RQZ5; -.
DR   GeneID; 108270607; -.
DR   CTD; 23395; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000221080; Chromosome 1.
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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
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; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF3; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
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}.
FT   DOMAIN          68..259
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          272..431
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          444..602
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          640..680
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          728..802
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   809 AA;  91925 MW;  C32C44FD0CF74E01 CRC64;
     MMHKTCQFAV YSVGLLKQVG CLHPWFVQAT PAIRSGIRSV FSESGVWERD YRADTRRRVE
     TWWHPRIQEQ WHKDMKEQCT QKKKFYVLSM FPYPSGRLHM GHVRVYTISD TIAQFQRMRG
     HKVLNPMGWD AFGLPAENAA IERGLDPEHW TKSNIQSMRE QLNSLGLCFN WDREVTTCLP
     DYYKWTQYLF VKLYEAGLAY QKEALVNWDP VDQTVLADEQ VDENGCSWRS GARVEQKLLR
     QWFIKTTNYA KPLLDALADL PEWYGVKAMQ ANWIGECSGC YFDHVLRLDD KETGEVLSAY
     TSSPEAVFGA AFISILPSHR LLHGSSPVGP ALHKALQPGR NSLSEVTALN VFTGREVPVV
     ISAKTEFPGH LDTVIGIPDS SEEDACVAQE LGVSWESVVK SEEDGSYTLI NSSEFTGQSR
     EEAFNSITQK ARKRNVGGYL TSSKLRDWLI SRQRYWGTPI PIVHCSSCGP VSVAVEELPV
     MLPKVTSLTG KGARPLQSAQ EWVNCSCPRC KGPAQRETDT MDTFVDSAWY YFRYTDPHNS
     ERPFDRSLAD QWMPVDVYIG GKEHAVMHLY YARFLSHFCK DQGLVSHKEP FKKLLVQGLI
     KGQTFRVAES GQYLKKEHID FTASEPVQRE SGKQLQVSWE KMSKSKHNGI DPEEVVQQYG
     IDTVRLYILY ASPPEQDILW DVKTDALPGV LRWQSRLWGL VTKLREAREG SDTPNPSILN
     KKERLEARKI WENKNQAIVQ VTTHLTEDFL LNAAISRLMG LTNTLSQASP RVVLHSVEFE
     QALVSLCVMA APMAPHLTSE LWAVPFSTA
//

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