GenomeNet

Database: UniProt
Entry: A0A2P7EGR1_9SYNE
LinkDB: A0A2P7EGR1_9SYNE
Original site: A0A2P7EGR1_9SYNE 
ID   A0A2P7EGR1_9SYNE        Unreviewed;       400 AA.
AC   A0A2P7EGR1;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007};
DE            EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007};
DE            Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007};
GN   Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007};
GN   ORFNames=C7K08_02665 {ECO:0000313|EMBL:PSI02413.1};
OS   Synechococcus lacustris str. Tous.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1910958 {ECO:0000313|EMBL:PSI02413.1, ECO:0000313|Proteomes:UP000240206};
RN   [1] {ECO:0000313|Proteomes:UP000240206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tous {ECO:0000313|Proteomes:UP000240206};
RA   Cabello-Yeves P.J., Picazo A., Camacho A., Callieri C., Rosselli R.,
RA   Roda-Garcia J., Coutinho F.H., Rodriguez-Valera F.;
RT   "Ecological and genomic features of two cosmopolitan and abundant
RT   freshwater picocyanobacteria.";
RL   Submitted (MAR-2018) 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_02007}.
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_02007};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSI02413.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PXVC01000006; PSI02413.1; -; Genomic_DNA.
DR   STRING; 1910958.BTM30_03950; -.
DR   OrthoDB; 9804243at2; -.
DR   Proteomes; UP000240206; 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: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_02007; Tyr_tRNA_synth_type2; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01479; S4; 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_02007,
KW   ECO:0000256|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02007};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02007, ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240206};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          341..375
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|Pfam:PF01479"
FT   MOTIF           40..49
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT   MOTIF           234..238
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT   BINDING         237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   400 AA;  43349 MW;  DCE2D8BD1FEBEB9A CRC64;
     MLSLNKNLDW FXRGVADLFP DNVETALTNK PLRIKLGIDP TGSEIHLGHS ILFRKLRAFQ
     DAGHTAVLII GDFTARIGDP SGKSATRVQL SSDEVEANAT TYLEQLGQGQ DPSLSLLDFH
     TPNRLEVRRN SEWLTDLNLP KVIELLALST VGQMLAKEEF ANRYAGGTAI SLHEFLYPLL
     QGYDSVAIKA DLELGGTDQK FNVAMGRDLQ RHFGXXPQFG LLMPILPGLD GVQKMSKSLG
     NTVGLKEDPL SMYSKLEKVP DGLVDQYITL LTNLELGALP SNPRERQMAM ALEVTRLRHG
     DRAAAAAQAD AANLVAGAAA SAEVPEVSLG AVNFPAKAFY LLSAAGICSS SEAKRQIQGG
     GVKLDGEKLS DPNQEFQTAT ELEGKVLQLG KKIFRRLKAL
//
DBGET integrated database retrieval system