ID A6R6H1_AJECN Unreviewed; 1081 AA.
AC A6R6H1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 85.
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=HCAG_05229 {ECO:0000313|EMBL:EDN08730.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08730.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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};
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DR EMBL; CH476659; EDN08730.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R6H1; -.
DR STRING; 339724.A6R6H1; -.
DR VEuPathDB; FungiDB:HCAG_05229; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OMA; KFIEWQF; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000009297; 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; 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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EDN08730.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 60..123
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 210..788
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 826..951
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1081 AA; 121464 MW; 2EB7482F6EA8524B CRC64;
MAAAAVAAAA LDPSNSAKNT LKLENKYQAQ WKANKVFEVN APSISEIPPD SITAAGLREK
FPKFFGTMAY PYMNGTLHAG HSFTASKVEF MAGTARMEGK RALFPLGFHC TGMPIKACAD
KLVDDIKKFG KHFERYTDEG DEPDEAPAPI QGTKEDLTKF SGKKSKAAAK SVKMKYQFQI
MLALGIPLEE VHKFADPAHW LEFFPPLCVR DLDSIGARID WRRQFVTTDA NAYYDAFTRW
QMNRLHEQGK ILYGNRYTIY SPKDGQPCMD HDRTEGEGVG PQEYTALKLK VREWSPAAQE
LVKGKIEPDA NVYFVPATLR PETMYGQTCC FLGPKIPYGI YKVSEKEYYI VTKRAAWNMA
FQGTFFSSDN FPRDQSELQP LVEAPGSTFV GTLVNAPLSV HTEGVRILPM ESVSATKGTG
VVTSVPSDSP DDYATVVDLA KKADYYGIKK EWAELEILPI IETPSYGNLT APTLVKQLKI
NSPKDAVPLA KAKELAYSEG FYKGTMLHGE FKGQPVQEVK EKVRESLIKS GDAFPFADPA
GKVVSRSNDE CVVAYLGQWF LNYGENDPQW QKETLDYVKG PLNTYSQEAR HGFEKNLEWL
NRWACARTYG LGSRLPWDPH FLVESLSDST IYQAYYTIAH LLHADRYGKE PGRLGIKPEQ
MTDEVWDYIF TRRDLGDDLI RSTGIRKEAF LTMRREFEYW YPLDVRVSGK DLIQNHLTFC
LYIHAALFPR EYWPRSIRVN GHLLLNGEKM SKSTGNFLTL KDAVEKYGAD ATRIAFADAG
DAIEDANFDE SVANSNILRL FTLKEWIEEV AKDSSLRTGP ADAFFDKLFG NELNVLAREA
RKHYADTNFK LALKSALYDF TSARDFYRES TTAAGIGMHR DIILRYIELQ ALLLTPITPH
WSEYVWLEVL NKLPLPRKLS KGKTVSFDPR KPKKLTIFAA KKFPSWQEKY IDLVREAFDE
VSLSINDKEL NGKVSKLGEM KKAMPFVQGL KKRLVTAKEL PETVFNRELG FDELSVLGDM
VAGLIRTTGC KVVEVVAVEE GGKAGTTLDG QPREGLPNVA ENAVPGQPTF HFENIPEAGG
V
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