(data stored in SCRATCH zone)

SWISSPROT: C6WGI2_ACTMD

ID   C6WGI2_ACTMD            Unreviewed;       503 AA.
AC   C6WGI2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 64.
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   OrderedLocusNames=Amir_0329 {ECO:0000313|EMBL:ACU34298.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34298.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34298.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU34298.1; -; Genomic_DNA.
DR   RefSeq; WP_012782961.1; NC_013093.1.
DR   STRING; 446462.Amir_0329; -.
DR   EnsemblBacteria; ACU34298; ACU34298; Amir_0329.
DR   KEGG; ami:Amir_0329; -.
DR   eggNOG; ENOG4105CRK; Bacteria.
DR   eggNOG; COG1190; LUCA.
DR   HOGENOM; HOG000236578; -.
DR   KO; K04567; -.
DR   OMA; EDPYPHK; -.
DR   OrthoDB; POG091H0098; -.
DR   Proteomes; UP000002213; Chromosome.
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   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; C6WGI2.
DR   SWISS-2DPAGE; C6WGI2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675073, ECO:0000313|EMBL:ACU34298.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675072};
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:UP000002213}.
FT   DOMAIN      187    502       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       415    415       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       422    422       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       422    422       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
SQ   SEQUENCE   503 AA;  55948 MW;  4AE4A970637EA54C CRC64;
     MSEQPQTGSP TSDDDLPEQL RVRREKRARL LERGVDPYPV EVARTHSLRE VREAHTGLDP
     DTGTGEVVGV TGRVMFIRNT GKLAFATLRE GDGTELQAML SLNKVGEQAL ADWKSDVDLG
     DHVFVRGEVI TSRRGELSVM ADEWAITAKA LRPLPVAHKE LAEETRIRQR YVDLILREQA
     RDTVRNRAKL VRSLRESFHR RGFTEVETPM LQTLQGGAAA RPFVTRSNAL DIDLFLRIAP
     ELYLKRCVVG GIEKVFEINR NFRNEGIDSS HSPEFSMLEY YEAYATYDTN AVMTRELIQE
     AAMAVAGSHV VTLVDGTEYD LGGEWTTLTM YGSLSEAAGV EVTPGTSVDD LRALADKLGL
     ETDPKLGHGK LVEELWEHLV GDHLHAPTFV RDFPVETSPL TRQHRSTPGV AEKWDLYVRG
     FELATGYSEL VDPVVERERL EAQARLGASG DVEAMPVDED FLRSLEYGMP PSGGVGMGID
     RLLMAITGLG IRETILFPLV RPE
//

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