ID C5P298_COCP7 Unreviewed; 984 AA.
AC C5P298;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=CPC735_037070 {ECO:0000313|EMBL:EER29001.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29001.1};
RN [1] {ECO:0000313|EMBL:EER29001.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 delta SOWgp {ECO:0000313|EMBL:EER29001.1};
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};
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:EER29001.1}.
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DR EMBL; ACFW01000012; EER29001.1; -; Genomic_DNA.
DR RefSeq; XP_003071146.1; XM_003071100.1.
DR AlphaFoldDB; C5P298; -.
DR GeneID; 9696641; -.
DR KEGG; cpw:CPC735_037070; -.
DR VEuPathDB; FungiDB:CPC735_037070; -.
DR HOGENOM; CLU_004427_0_0_1; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000009084; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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 50..258
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 260..454
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 469..571
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 774..909
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 913..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 109332 MW; 9158BEA779F44CAC CRC64;
MRLQLMLGRA ILPHRPTAIS LTAHLRSPRI LLRAASTTPI RKLDLLAIDK KWKGKWEFHK
SRNSSSASAE KAYVLPMFPY PSGTLHMGHV RVYTISDVLA RFKRMKGYDV LHPMGWDAFG
LPAENAAIER GINPASWTKE NIAKMKEQLK GLGTDFDWDR EFMTCSPEFY KHTQRLFLML
HEKGLAYQAK AMVNYDPVDQ TVLANEQVDA NGRSWRSGAV VEKRELKQWF FRITAFKEAL
LKDLDSLASG WPDRILSMQR HWLGKSVGAR LTFKIITPKE RLNVQVFTTR ADTLPGAQYV
ALSLNHPLVT QLAQTDSKLK AFVNSASLLP PDTKVGYRLP SVEAVNPLHA IEENPNIPAE
LPVFVAPYVL GDYGEGAVMG VPGHDSRDFA FWAENMPSTP VISVIEPNLS NGFSNKDDIQ
RAEAFLGEGV LNSTCGKFTG ISSNKAREEI VSSLRDHNNS ADFTESWRLR DWLISRQRYW
GAPIPIIHCG DCGAVPVPVD QLPVELPTID GAGLKGKAGN PLESAEDWLN TPCPNCNKPA
KRETDTMDTF VDSSWYFLRF LDPSNELMPF SPALARPVDT YIGGIEHAIL HLLYSRFVYK
FLAESGLIPG GHRAKPDRAE PFLTLLSQGM VHGKTYTDPA TGRFLRPSEV DLSVPGSPVL
TGTKVKPNIS FEKMSKSKYN GVDPSTCIEK YGADATRAHI LFAAPVSEIL EWDETKIVGI
QRWFSRLWKI ISDSEKSLIS AELGLSRENI RSANNLALPP LDELSDDEAN LLLIAHSTIT
SVSSCMEKNP YALNTVISDL IKFTNAITSS ALSLSPSSPA SKTVLYMLVS SLLKLLAPIA
PAFSSECWEQ LHTSLLSKNE NDQSLSIFSS PWPTPLLTEP QVESLQHRGS KTVAVQVNGK
LRFTATIPRF SSSAVGPVEQ SNGQSKQQGK AERNGPMSEE EQSWIISHIL ETEKGKLWLT
ERNHWEKRKR VVVVGGGKVV NVVF
//
