ID A0A3Q7RH50_VULVU Unreviewed; 903 AA.
AC A0A3Q7RH50;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_025845047.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025845047.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025845047.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025845047.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025845047.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025845047.1; XM_025989262.1.
DR AlphaFoldDB; A0A3Q7RH50; -.
DR STRING; 9627.ENSVVUP00000009384; -.
DR Ensembl; ENSVVUT00000012325; ENSVVUP00000009360; ENSVVUG00000006969.
DR Ensembl; ENSVVUT00000012352; ENSVVUP00000009384; ENSVVUG00000006969.
DR KEGG; vvp:112912591; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000286640; Unplaced.
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:Ensembl.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT DOMAIN 61..257
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 271..332
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 443..600
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 638..678
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 728..849
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 903 AA; 101630 MW; 880210BDC215E84B CRC64;
MASACRRLGF YISFLKNQLD GGPAIISVGR RVIPGCARGI YSATGEWTKE YTLQTRKDVE
KWWHQRIKEQ ASKISEADKS KPKFYVLSMF PYPSGKLHMG HVRVYTISDT IARFQKMRGM
QVINPMGWDA FGLPAENAAI ERNLHPESWT QSNIEHMRKQ LDRLGLCFSW DREITTCLPD
YYKWTQYLFI KLYEAGLAYQ KEALVNWDPV DQTVLANEQV DEHGCSWRSG AKVEQKYLQQ
WFIKTTAYAK AMQDALADLP EWYGIKGMQA HWIGDCVGCH LDFTLKVDGQ VTGEKLTAYT
ATPEAIYGTS HVAISPSHRL LHGHSSLKET LRKALVPGKD CLTPVMAVNM LTQQEAPVVI
LAKADFEGSL DSKIGIPSTS PEDTTLAQTL GLPYSEVIET LPDGTERMSS SAEFTGMNRQ
DAFLALTQKA RKKRVGGDVT SNKLKDWLIS RQRYWGTPIP MVHCPACGPV PVPLQDLPVT
LPHITSFTGK GGSPLAAASE WVNCSCPRCK GAARRETDTM DTFVDSAWYY FRYTDPQNTH
SPFNTALADY WMPVDLYIGG KEHAVMHLFY ARFFSHFCHD QKMVRHREPF HKLLAQGLIK
GQTFRLPSGQ YLQREEVDLT GSVPVHSETK EQLEVTWEKM SKSKHNGVDP EEVVGQFGID
TIRLYILFAA PPEKDILWDV KTDALPGVLR WQQRLWTLVT RFIEARASGM VPRPELLSNE
ERAESKKLWE YKNAVISEVT GHFTEDFSLN SAIAQLMGLS SNLLQASQRV VLHSPEFEDA
LCALVVMAAP MAPHITSELW AGLAQVPRKL CAHYAWDAGV LLQAWPTVDP KFLQQPDVVE
MAVLINNKAC GKIPVPQGVA QDQDKVHELV LQSELGVKLL QGRSIKKAFL SPRTALINFL
VQD
//
