(data stored in SCRATCH zone)

SWISSPROT: Q3ILD7_PSEHT

ID   Q3ILD7_PSEHT            Unreviewed;       511 AA.
AC   Q3ILD7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 103.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252,
GN   ECO:0000313|EMBL:CAI85608.1};
GN   OrderedLocusNames=PSHAa0518 {ECO:0000313|EMBL:CAI85608.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85608.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85608.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys). {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|RuleBase:RU000336, ECO:0000256|SAAS:SAAS00675040}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|SAAS:SAAS00675054}.
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DR   EMBL; CR954246; CAI85608.1; -; Genomic_DNA.
DR   RefSeq; WP_011327221.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILD7; -.
DR   STRING; 326442.PSHAa0518; -.
DR   EnsemblBacteria; CAI85608; CAI85608; PSHAa0518.
DR   GeneID; 32565524; -.
DR   KEGG; pha:PSHAa0518; -.
DR   eggNOG; ENOG4105CRK; Bacteria.
DR   eggNOG; COG1190; LUCA.
DR   HOGENOM; HOG000236578; -.
DR   KO; K04567; -.
DR   OMA; EDPYPHK; -.
DR   OrthoDB; POG091H0098; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00775; LysRS_core; 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; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILD7.
DR   SWISS-2DPAGE; Q3ILD7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675073, ECO:0000313|EMBL:CAI85608.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675072, ECO:0000313|EMBL:CAI85608.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675044};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00684990};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN      173    508       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       420    420       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       427    427       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       427    427       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
SQ   SEQUENCE   511 AA;  58638 MW;  F3D9FC54543E0B01 CRC64;
     MTDQIQDENK LIAERRGKLD AIRQNCPANG HPNQFRREHY TADLQAQFGD KSKEELVELQ
     QVVSIAGRIL AKRGPFFVIQ DMKGRVQSYA SKDVQKDLKE KYGQLDTGDI IGVKGALNKS
     GKGDLYVEMT EYQLLTKSLR PLPEKFHGLS DQETKYRQRY VDLITNEATR ETFRIRSQVV
     EGIRRFLADR DFMEVETPML QVIPGGASAR PFVTHHNALD IDMYLRIAPE LYLKRLVVGG
     FDRVFEINRN FRNEGLSTRH NPEFTMIEFY QAYADYIDLM NITEDMLRTV AENVLGSAVV
     VNTTKDENGE VIDSVEYDFG QPFTRLSMSD AILKYNPEFD AAVFNDPENH FEQLKAYAKQ
     VHVKIPENCV WGPGKFLCEI FEETAEHMLI QPTFITGYPW EVSPLARRND ENSFVTDRFE
     FFVGGRELAN GFSELNDAQD QAERFTRQVE EKDAGDDEAM HYDEDYIRAL EYGLPPTAGE
     GIGIDRLVML FTDSPTIKDV ILFPHMRPQA D
//

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