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Database: UniProt
Entry: A0A1U7I5E6_9CYAN
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ID   A0A1U7I5E6_9CYAN        Unreviewed;       629 AA.
AC   A0A1U7I5E6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=NIES2119_28740 {ECO:0000313|EMBL:OKH31463.1};
OS   Phormidium ambiguum IAM M-71.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Phormidium.
OX   NCBI_TaxID=454136 {ECO:0000313|EMBL:OKH31463.1, ECO:0000313|Proteomes:UP000185860};
RN   [1] {ECO:0000313|EMBL:OKH31463.1, ECO:0000313|Proteomes:UP000185860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM M-71 {ECO:0000313|EMBL:OKH31463.1,
RC   ECO:0000313|Proteomes:UP000185860};
RA   Zhu T., Hou S., Lu X., Hess W.R.;
RT   "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT   Habitats.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OKH31463.1}.
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DR   EMBL; MRCE01000050; OKH31463.1; -; Genomic_DNA.
DR   RefSeq; WP_073596916.1; NZ_MRCE01000050.1.
DR   AlphaFoldDB; A0A1U7I5E6; -.
DR   STRING; 454136.NIES2119_28740; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000185860; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
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   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; 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   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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000185860}.
FT   DOMAIN          11..435
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          482..593
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   629 AA;  72615 MW;  FF0910BF0DDE8002 CRC64;
     MYDCRSVEAK WQAVWQQTQI YETDIARAID KTSSERRPFY NLMMFPYPSA EGLHVGNVYA
     FTGADIYGRF MAMNGRDVFE PMGFDAFGIH SENFAIKKGI HPEQLTACNV ERFRQTQLKR
     IGNRFCWNHE VQTTSLAYYK WTQWIFLQLF KAGLAERKKA SVNWCPSCKT VLADEQVIAG
     ECERCSAIAI QRELEQWFFQ ITRYAQRLLD NLEYLDWSER VKTAQRNWIG RSERDGKVHY
     HLRDWLISRQ RYWGVPIPII YCQTCGVVPV PEDQLPVELP QTQDWLPKGT GNSPLADIPE
     FVNTTCPCCN GAARRETDVS DNFLDSAWYF LRYPSSNCSD VPFNPQITAT WLPVDMYIGG
     AEHSVLHLLY SRFITMVLHD LGYIPFEEPF RCFRAHGLLT KDGVKMSKSK GNVVNPDQYI
     EEYGADTLRT YLMFLGPYDQ GGVFCDLGIA GIQRFLNRVW QLVMRYQGSI PSIELDVESQ
     QDLHQTIHKV REDIQALKYN TAIATLMSYL NTLEAKEYVS TAEIKSYLLM LAPFAPHITE
     ELWSRMGESY SIHQQPFPQA NREFLVKAQV TIAVQINGRT RTTLQLAPDA SQEEALALAK
     QSQSLQRYLK EQEVRRVVYV PSRIINLVI
//
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