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Database: UniProt
Entry: I1C8D4_RHIO9
LinkDB: I1C8D4_RHIO9
Original site: I1C8D4_RHIO9 
ID   I1C8D4_RHIO9            Unreviewed;      1036 AA.
AC   I1C8D4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=RO3G_09424 {ECO:0000313|EMBL:EIE84714.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE84714.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE84714.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(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; CH476738; EIE84714.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C8D4; -.
DR   STRING; 246409.I1C8D4; -.
DR   VEuPathDB; FungiDB:RO3G_09424; -.
DR   eggNOG; KOG0437; Eukaryota.
DR   InParanoid; I1C8D4; -.
DR   OMA; KFIEWQF; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000009138; 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   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; 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; 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   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:UP000009138}.
FT   DOMAIN          46..115
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          188..754
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
SQ   SEQUENCE   1036 AA;  117755 MW;  052577BEA75C8C48 CRC64;
     MSTEAPKTAK RDALREFEGK ARALWDNEKA FEINAPTIEE HPNYEDLHKT HPKYMACMPY
     PYMNGRLHLG HAFTFSKVEF CIGYERMKGR RALLPQGFHC TGMPIKACAD KLAREIEMFG
     KNFEKYDEAK EAEKKTEVNK NVKSKVAAKT GNVTYQFQIM LSLGIPITEI HKFSDPYYWT
     EFFPPQTISD MNAFGAKVDW RRAFITTDAN PYYDSFVRWQ MRKLREMQKI KFGERYTIYS
     IIDKQPCMDH DRASGEGVGP QEYTGIKMEV LEWSDAAKEA LVASNDNLKG KKIYLVAATL
     RPETMYGQTN CFVGTDIKYG VYKVNENEAF VVTERAARNM AYQKIFAKEG SIEKLAEIDG
     KSIVGTKIHA PLSQYSAVYV LPMDNVLSTK GTGVVTSVPS DSPDDYATLC DLKKKPDYYN
     IKAEWVAFDP VPLIETPSYG NLTAPKLCEI KKINSQKDRV QLAEAKELAY KEAFYQGVMC
     IGEFSGMAVQ EAKNKVKDIL INSKEAFVYN EPEGLVMSRS GDECVVALLD QWYIDYGEEE
     WKAKTKKCLS QMNTYTVETR HQFEQVLDWL NKWACARSFG LGTKLPWDEQ FLVESLSDST
     IYMAYYTVAH LLHNDLKGSS VGSAGITAEQ MTDSVWNYIF RLGEYPVDCG VPQATLDRLR
     REYEYFYPLD LRASGKDLVP NHLTFFLYNH TAIFPEDKWP QGVRSNGHLL LDSKKMSKST
     GNFMTMSDAV IKYGADATRF ALADAGDSVE DANFEDATAN AAILRLYTLL EWSEEQVAKA
     DTLRTGEFTF FDKIFVNEMN KLINLTEAAY DATCYREVLK YGVYEFQAAK DAYQVACTEA
     VLKKEGLVVS APFPKPSAPV DESLEAATRY IRRTTKAIRD AELNLIKKKK KGKAAESEYK
     PSEPKSLKIF VATKFPEWQE ASLNVMKVHY NNGEFDDVKI RQELGAQGML KDKKVMPFIQ
     EQKKLIAKEG PVAFNRTLIF NEVETLEKAV DELKRALGFH TISIFGHDQW PEEYIKTAES
     AVPGVPSFSF KNESKE
//
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