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Database: UniProt
Entry: A0A1I4SYV3_9EURY
LinkDB: A0A1I4SYV3_9EURY
Original site: A0A1I4SYV3_9EURY 
ID   A0A1I4SYV3_9EURY        Unreviewed;       530 AA.
AC   A0A1I4SYV3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   ORFNames=SAMN04488696_2083 {ECO:0000313|EMBL:SFM69493.1};
OS   Methanolobus profundi.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=487685 {ECO:0000313|EMBL:SFM69493.1, ECO:0000313|Proteomes:UP000198535};
RN   [1] {ECO:0000313|EMBL:SFM69493.1, ECO:0000313|Proteomes:UP000198535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mob M {ECO:0000313|EMBL:SFM69493.1,
RC   ECO:0000313|Proteomes:UP000198535};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
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DR   EMBL; FOUJ01000004; SFM69493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4SYV3; -.
DR   STRING; 487685.SAMN04488696_2083; -.
DR   OrthoDB; 6838at2157; -.
DR   Proteomes; UP000198535; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00674; LysRS_core_class_I; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.10.770; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 1.
DR   HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
DR   InterPro; IPR042078; Lys-tRNA-ligase_SC_fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00467; lysS_arch; 1.
DR   PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; An anticodon-binding domain 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|HAMAP-Rule:MF_00177};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00177}.
FT   MOTIF           30..38
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   MOTIF           276..280
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   530 AA;  58926 MW;  3A4AA5FA7383283F CRC64;
     MADITHWADV IADEVLAKGK KHLVATGITP SGHIHIGNMR EVVTADVAYR ALIDKGAEAE
     FIYIADTYDP LRKVYPFLDE SYAEHVGKPL SEIPCPCGEH KNYSEHFLEP FLAALEHLGI
     HPKVYRADEL YKEGAYVEAI KQALLKKDEI AAILQKRSGK TPVDTWNPFN PICNECGKVN
     TTIVTGFDID AETVDYECSC GSNDTVPMKG GGKLTWRVDW PARWKALGVT VEPFGKDHAS
     RGGSYDTGVE IAKEIFGYEA PHPIVYEWIM LGQKGAMSSS TGVVVSISDM LKVVPPEVLR
     YLIIRTKPEK HIRFDPALPL LTLVDEFERL HSSDKATDYD KRMIELSHAA GLCHTDIPFK
     HMTTIYQVAA GDLDKILNIV KRAGYDVSNE KCIRELTDNV GNWLEMYAPD NAKFSVQEEL
     PVSTSQLTDL QRVFLSNFSA ILDKSGELNG EDYHNLVYSA KEAGTELNTN IAAALEVAPE
     SLEVNPKELF KAVYVSVLGQ PSGPKAGWFL SSLEKDFLAQ RFKEAAEYRP
//
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