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Database: UniProt
Entry: K9V8P2_9CYAN
LinkDB: K9V8P2_9CYAN
Original site: K9V8P2_9CYAN 
ID   K9V8P2_9CYAN            Unreviewed;       861 AA.
AC   K9V8P2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   ORFNames=Cal6303_4910 {ECO:0000313|EMBL:AFZ03807.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03807.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ03807.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03807.1,
RC   ECO:0000313|Proteomes:UP000010477};
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) 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, ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; CP003610; AFZ03807.1; -; Genomic_DNA.
DR   RefSeq; WP_015200420.1; NC_019751.1.
DR   AlphaFoldDB; K9V8P2; -.
DR   STRING; 1170562.Cal6303_4910; -.
DR   KEGG; calt:Cal6303_4910; -.
DR   PATRIC; fig|1170562.3.peg.5379; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000010477; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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-RELATED; 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   Pfam; PF09334; tRNA-synt_1g; 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|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000010477}.
FT   DOMAIN          40..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          222..405
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          419..603
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          625..664
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          702..822
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          288..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   COMPBIAS        288..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  97092 MW;  0B97BEA5ACD14F06 CRC64;
     MDSRYNPADI EEKWQKTWAE LGLDKTSSDS SKPKFYALSM FPYPSGSLHM GHVRNYTITD
     AIARLKRMQG YRVLHPMGWD AFGLPAENAA IDRNVPPSQW TYQNIQHMRS QLQKLGLFID
     WDNELATCSP DYYRWTQWIF LQFFQAGLAY QKEAAVNWDP IDQTVIANEQ VIDGRSWRSG
     AIVERKLLRQ WFLKITAYAE ELLQDLDKLP GWPEKVRKLQ ANWIGKSTGA YLEFPVVGMD
     EKIGVYTTRP DTVYGVSYVV LAPEHPLTTK VTTASQADAV AEFAKEVGNQ SELERTAEDK
     PKRGIPTGGM AINPFTGEEI PILIADYVLY EYGTGAVMGV PAHDVRDFKF AKNYNLPIKF
     VIVPNDNKEA HNQDAAYTDA GILVNSQQFD DMDSIEAKKA IVKYAESQGF GKERVQFRLR
     DWLISRQRYW GAPIPIIHCP ECGAVPVPDA DLPVQLPDNI ELTGRGGSPL ANLESWVNVP
     CPSCGTPAKR ETDTMDTFID SSWYYLRFTD ANNSEEIFTK EKVNSWMPVD QYVGGVEHAI
     LHLLYSRFFT KVLRDHACAP NGERGLLQFD EPFKQLLTQG MVQGLTYMNP KKSDKDKWVP
     TNLVNAADPR DPQTGDPLQL VYATMSKSKG NGVAPEDIIA KYGVDTARMF ILFKAPPEKD
     LEWDEADVEG QFRFLNRVWR LVTEYIAVDS KSNKLQESKA EKDLRRAIHI AIKEISEDVN
     EGYQLNTAIS ELMKLSNALT DADCKTSPIY SEGIRTLLLL LAPFAPHIAE ELWHLLGNKE
     SVHTQAWLNH DPEALIADEI TLVVQVNGKK RADIPVPAKA DKAELEKYAL ASEAVQRHLE
     GKEIKKVIVV PGKLVNFVVA G
//
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