ID A0A1F6R9D6_9BACT Unreviewed; 841 AA.
AC A0A1F6R9D6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE Flags: Fragment;
GN ORFNames=A3J63_00215 {ECO:0000313|EMBL:OGI17224.1};
OS Candidatus Moranbacteria bacterium RIFCSPHIGHO2_02_FULL_40_12b.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1801639 {ECO:0000313|EMBL:OGI17224.1, ECO:0000313|Proteomes:UP000176579};
RN [1] {ECO:0000313|EMBL:OGI17224.1, ECO:0000313|Proteomes:UP000176579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:OGI17224.1}.
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; MFRX01000021; OGI17224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6R9D6; -.
DR STRING; 1801639.A3J63_00215; -.
DR Proteomes; UP000176579; 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 CDD; cd02883; Nudix_Hydrolase; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
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}.
FT DOMAIN 356..543
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT NON_TER 841
FT /evidence="ECO:0000313|EMBL:OGI17224.1"
SQ SEQUENCE 841 AA; 97329 MW; BF64CF4ED2BED5FE CRC64;
MEKYNPRKIE QKWQKIWQKS GIYKAKDSVK GKNNFYHLVM FPYPSGDLHI GHWYNFAPAD
VFARFKKMQG FNVMSPIGFD SFGLPAENAA IKRKIHPRDW TYKNIQTMKK QLQSMGNMHD
WSREIITSDP GYYKWTQWMF LQLYKNGLAC KKKAPANWCP KCHTVLANEQ VINGKCERCE
TEVVQRDIEQ WLFRITKYAD KLLEGLDKLD WPEKTKIMQR NWIGRSEGAT IKFQIVIPSE
DEESNRLDSS TPLRSAQNDN NFLEVFTTRL DTIYGCTYCV VAPEHPFVAS LLKIKNQKSK
IKNFEEVEEY MVKAQNKTEL ERMEMKEKTG VEIKGIKAVN PFNNEEMPIF VADYVLGHYG
TGAVMAVPAH DERDWEFAKK YNLPIKKVIE PCFYQHTEPG KIKDNEPFVE RDAIAALVKH
WEKDEYIGLK WKKVAWQTLI TGGVEKGQTD EEAAGNEITE ETGYKNLKLI KKLPMVHSKF
YHIPKKENRF AHFNVFYFEL ENGEQEKISN VENDIHEVVW VPKEKMTQFF TAESHNYIWQ
TLDKPAAAYT DEGVLNNSGE YNYLDSREAR EKMTQWLEKN KLGRKKINYK LRDWLVSRQR
YWGAPIPIIY CSKCWENFSK TRPANQGSTF PFPDLSGNSS GLNLNVAVIG GKKHAVIPVP
EKDLPVKLPN ISDYLPTEEG SSPLARSKSF VNAKCPRCKG KAVRETDTLD TFVCSSWYYL
RYADPRNRKK FADGKKLKTW LPVNMYIGGA EHTVLHLLYS RFFAKALKDF GYLDFDEPFS
ALRHQGTILG NDSQKMSKSK GNIIDPDKIV ENFGSDAVKM YLCFMGEYSQ GGPWNPSGIM
G
//
