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Database: UniProt
Entry: L0KS36_MESAW
LinkDB: L0KS36_MESAW
Original site: L0KS36_MESAW 
ID   L0KS36_MESAW            Unreviewed;       417 AA.
AC   L0KS36;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02006};
DE            EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02006};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006};
DE            Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02006};
GN   Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02006};
GN   OrderedLocusNames=Mesau_04454 {ECO:0000313|EMBL:AGB46789.1};
OS   Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB46789.1, ECO:0000313|Proteomes:UP000010998};
RN   [1] {ECO:0000313|Proteomes:UP000010998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC   {ECO:0000313|Proteomes:UP000010998};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA   O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium australicum WSM2073.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC       step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC       then transferred to the acceptor end of tRNA(Tyr). {ECO:0000256|HAMAP-
CC       Rule:MF_02006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC         Rule:MF_02006};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02006}.
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DR   EMBL; CP003358; AGB46789.1; -; Genomic_DNA.
DR   RefSeq; WP_015318175.1; NC_019973.1.
DR   AlphaFoldDB; L0KS36; -.
DR   STRING; 754035.Mesau_04454; -.
DR   KEGG; mam:Mesau_04454; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_3_5; -.
DR   OMA; YMMAKDS; -.
DR   OrthoDB; 9804243at2; -.
DR   Proteomes; UP000010998; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00165; S4; 1.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02006, ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010998};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   MOTIF           44..53
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   MOTIF           236..240
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         39
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         176
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         180
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   417 AA;  46243 MW;  EA1AE63E35272F75 CRC64;
     MPAFKSDFLR TMSERGFIHQ TSDDAGLDQL FAKETVTAYI GFDATARSLH AGSLIQIMML
     HWLQQTGHRP IALMGGGTSM IGDPSFKDEA RKLLTPQDID GNLAGIRRNF MPYLKFGSGP
     NDAVMVNNAD WLMEINYVNF LRDVGRHFSV NRMLAFDSVK LRLDREQSLS FLEFNYMILQ
     AYDFVELYKR LGCRLQMGGS DQWGNIINGI DLGRRMEDAQ LYALTTPLLT TSSGAKMGKS
     ASGAVWLDPQ MLSPYEFWQY WRNTEDADVA RFLKLYTTLP LDEVARLERL GGSEINEAKK
     ILATEITAHL HGRAAAEQAS ETARKTFEEG ALADTLPAVE ADKAALEAGV GILSLLVSAG
     LASSNGEARR HIQGGAVRLN DQAVSDDRRL VTLQDLSPEN VIKLSLGRKK HILVRPA
//
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