ID A0A024GMT2_9STRA Unreviewed; 1089 AA.
AC A0A024GMT2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=BN9_090620 {ECO:0000313|EMBL:CCI48019.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI48019.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI48019.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI48019.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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}.
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:CCI48019.1}.
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 EMBL; CAIX01000199; CCI48019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GMT2; -.
DR STRING; 65357.A0A024GMT2; -.
DR InParanoid; A0A024GMT2; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000053237; 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:UP000053237}.
FT DOMAIN 38..115
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 201..768
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 806..931
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 124545 MW; 48AA0934C5DF3D94 CRC64;
MDKVEAQTQE LNLEDNNPKT TKTFSRRDHL IDIERIIAAK WEKERVFEAE PDTTKPKYMA
SFPFPYMNGY LHVGHLFSMS KAEFSARYHR LLGENVLFPF GFHCTGMPIQ AAANKLRNEL
DQYGCPPDFS IDEVKTDGNE VSNSDALLNK SKGKRSKLAA KTSGIVRQYD IMQLSDIVEE
EIPNFREPLY WLRFFPPRAV DDLKRYGMNI DWRRSFITTD VNPFYDAFVR WQLNILKKNG
RISRGKRPSV FSVMDQQSCA DHDRASGEGV GPQEYTIVKL LVKKPLPSKL GSLTEYKVYL
APATLRPETM YGQTNCFVLP DGKYGAYLMN DRDVFIMSRR AARNLAHQEY ARKWGQEECI
LELSGWDLLG LGLHAPNAKF ETIYTLPLLT ISMGKGTGIV TSVPSDSPDD YAALRDLKQK
KALREKYNIT DEMVLPFDAV PIIHIEGYGD TAAVKVCNDL KIVSQNDTAK LAKAKELVYL
KGFYEGVMLL GPFKGKKVCD AKPLARQELL KRGDAISYWE PESLVMSRSG DECVVAHLDQ
WYLTYGAEDW KNRVLEHVSD PKRFNTYNPI ALGEFKATLG WLKEWAPCRQ SGLGTKLPWD
PQFVVESLSD STIYMAYYTI AHHLHVDLYG AEFGSHGLRP EQMTEQVFDY IFLRGPLPSD
SDIPRHVLDL LRGEFEYWYP LDLRASGKDL IRNHLTMSLY HHSEIWRNDP SKWPRSFFTN
GHVLVDSEKM SKSKGNFLTI RNCAEEFGAD ATRFACADAG DSMDDANFSR DTCNMAILRL
TTEEEWIKKM KEENSSLRHG EYSFNDRMFL NQMNDLILKT KNFFDRLQWR EGLHTGYFEF
QLARDAYRDL CTRGEIAMHS KVLDRYVNAQ TIMLSPICPH FCEHIWSIMG NSGFVSTTSW
PIVDSVDHSL LRAGDFLGKT IRHFRDIQAK SSGNNRSKSS TKGSEAVPTK RSHAHIYLAT
EFPLWQQKLL QIMSTQFDST ANAFPSDLMS TLKAAIDEDE ILKKMTKYVM QFAAFVRSEA
EVRGKDAMEL STPYDQKEVL EANRLYLTRS LELEHVDFFY VSQALPENAD AKKVEAALPG
KPSLFLYSA
//
