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Database: UniProt
Entry: W6KJQ4_9TRYP
LinkDB: W6KJQ4_9TRYP
Original site: W6KJQ4_9TRYP 
ID   W6KJQ4_9TRYP            Unreviewed;       709 AA.
AC   W6KJQ4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE            EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563, ECO:0000256|RuleBase:RU003748};
GN   ORFNames=GSEM1_T00006676001 {ECO:0000313|EMBL:CCW61774.1};
OS   Phytomonas sp. EM1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW61774.1, ECO:0000313|Proteomes:UP000027080};
RN   [1] {ECO:0000313|EMBL:CCW61774.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW61774.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW61774.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW61774.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC         tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC         COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000204,
CC         ECO:0000256|RuleBase:RU003748};
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DR   EMBL; HF955065; CCW61774.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6KJQ4; -.
DR   EnsemblProtists; CCW61774; CCW61774; GSEM1_T00006676001.
DR   OrthoDB; 168081at2759; -.
DR   Proteomes; UP000027080; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF1; LYSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000027080}.
FT   DOMAIN          288..606
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          49..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   709 AA;  80057 MW;  D59F88CE806E2D9A CRC64;
     MRQVLFVATA SVMPVLSSLT YRHFHGVSPQ ATWNHERSRD MLFRQSPTFT TGLESPQERV
     PSSNANPTSS SSSTTSSLSD SLQGNGRDYS PCKGKKAKGE NGTKLRNHAS AKAPSLPRTG
     FDIPTSYTSF RHATHLKDFL QRYDHVAVGH KVVGVSERVG GRVVSLRDMG RILFLTIHGD
     GHSLQVVRQV DEDFDKEDLK RLKTTLRVGD IIGAVGIAGR TEKGELSLYA KELVILAPYV
     CTDQSICPNL KGFLPITDNE IKYRYRFLDM MTNPNVRQNL CKRHEAIRAL RGYLDDRGFV
     EVETPVLHEV PSGANAKPFI TYHNDNNDSL FLRVAPELHL KQCVVGGMER VYEIGRVFRN
     EDADRSHNPE FTSCELYAAY HSYEDLMGMT EAILQHMARA ANGTTKLTVT SCVDRQLVTL
     DLMPPFHRVS VYDEIQRVAE VELPPPLELN TSRGLAYMSA IMLRHNIPLP PVRTAAQMFD
     KLIDFFIVSR VVQPTFLVDH PLFMSPLAKE HDSRPGLSER FELFINGMEI CNAYSELNNP
     HEQYHRFQQQ LLDRQQGDEE AMALDAVFLK ALQVGLPPTA GWGMGIDRVM MLLNGSSSIR
     DEVIFPLLRK DADSRDAKQR RKTASYFGFN SHLTLFCLGA LEDEMIKCKV PRDFSEKVRQ
     LRKCIHSMSA VARRDAVDSV EAMTQYSMNG WRYEAAMKIL KIVCGHNNW
//
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