SYY_IDILO
ID SYY_IDILO Reviewed; 401 AA.
AC Q5QVP5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02007};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02007};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02007}; OrderedLocusNames=IL2236;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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:0000255|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:0000255|HAMAP-Rule:MF_02007};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}.
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DR EMBL; AE017340; AAV83068.1; -; Genomic_DNA.
DR RefSeq; WP_011235463.1; NC_006512.1.
DR AlphaFoldDB; Q5QVP5; -.
DR SMR; Q5QVP5; -.
DR STRING; 283942.IL2236; -.
DR PRIDE; Q5QVP5; -.
DR EnsemblBacteria; AAV83068; AAV83068; IL2236.
DR KEGG; ilo:IL2236; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_5_0_6; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 402899at2; -.
DR Proteomes; UP000001171; 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; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 PANTHER; PTHR11766; PTHR11766; 1.
DR PANTHER; PTHR11766:SF1; PTHR11766:SF1; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..401
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000236727"
FT DOMAIN 338..399
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 43..52
FT /note="'HIGH' region"
FT MOTIF 227..231
FT /note="'KMSKS' region"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ SEQUENCE 401 AA; 44993 MW; C1C3D39AAFFC835E CRC64;
MKTEVAEAIA EITRGAEEVL LEQELAEKLA SGKPLTVKAG FDPTAPDLHL GHTVLINKLR
VFQDFGHKVV FLIGDFTGMI GDPTGKNVTR KPLTTEQVIA NAETYKEQVF KILDPAKTEI
RFNSEWMSKM GAADMIKLAA RQTVARMLER DDFKKRYQNN QSIAIHEFLY PLVQGWDSVE
LKADVELGGT DQRFNLLMGR ELQKEEGQRP QTVIMTPLLE GLDGVQKMSK SLNNYIGITE
PANDMFGKIM SVSDELMWRY FQLLSFRSIT EIDELKAAVA DGKNPRDVKV LLAKEIIARF
HSEDDAEKAE QDFIQRFQKN ALPDDIPEKT VQVGAEGMAI GNVLKEAGLV ESTSEALRMI
KQNAVKVDGE KFSDSRYLCT EKDSGVYQVG KRRFAKINLT A