SYY_THET2
ID SYY_THET2 Reviewed; 432 AA.
AC P83453;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=TT_C1033;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=12110594; DOI=10.1093/emboj/cdf373;
RA Yaremchuk A., Kriklivyi I., Tukalo M., Cusack S.;
RT "Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA
RT recognition.";
RL EMBO J. 21:3829-3840(2002).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}.
CC -!- MISCELLANEOUS: Although this protein is a class I aminoacyl-tRNA
CC synthetase, it displays a class II mode of tRNA recognition.
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; AE017221; AAS81375.1; -; Genomic_DNA.
DR RefSeq; WP_011173450.1; NC_005835.1.
DR PDB; 1H3E; X-ray; 2.90 A; A=1-432.
DR PDB; 1H3F; X-ray; 2.00 A; A/B=1-432.
DR PDBsum; 1H3E; -.
DR PDBsum; 1H3F; -.
DR AlphaFoldDB; P83453; -.
DR SMR; P83453; -.
DR STRING; 262724.TT_C1033; -.
DR DrugBank; DB03978; Tyrosinal.
DR EnsemblBacteria; AAS81375; AAS81375; TT_C1033.
DR GeneID; 3168499; -.
DR KEGG; tth:TT_C1033; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_5_0_0; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 402899at2; -.
DR EvolutionaryTrace; P83453; -.
DR Proteomes; UP000000592; 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; 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; 2.
DR PANTHER; PTHR11766:SF1; PTHR11766:SF1; 2.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT CHAIN 1..432
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055665"
FT DOMAIN 369..430
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 46..55
FT /note="'HIGH' region"
FT MOTIF 232..236
FT /note="'KMSKS' region"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1H3E"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1H3E"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1H3F"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1H3F"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 285..301
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:1H3F"
FT HELIX 384..392
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:1H3F"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1H3F"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:1H3F"
SQ SEQUENCE 432 AA; 48718 MW; 71B04B8976B8D91B CRC64;
MAGTGHTPEE ALALLKRGAE EIVPEEELLA KLKEGRPLTV KLGADPTRPD LHLGHAVVLR
KMRQFQELGH KVVLIIGDFT GMIGDPSGRS KTRPPLTLEE TRENAKTYVA QAGKILRQEP
HLFELRYNSE WLEGLTFKEV VRLTSLMTVA QMLEREDFKK RYEAGIPISL HELLYPFAQA
YDSVAIRADV EMGGTDQRFN LLVGREVQRA YGQSPQVCFL MPLLVGLDGR EKMSKSLDNY
IGLTEPPEAM FKKLMRVPDP LLPSYFRLLT DLEEEEIEAL LKAGPVPAHR VLARLLTAAY
ALPQIPPRID RAFYESLGYA WEAFGRDKEA GPEEVRRAEA RYDEVAKGGI PEEIPEVTIP
ASELKEGRIW VARLFTLAGL TPSNAEARRL IQNRGLRLDG EVLTDPMLQV DLSRPRILQR
GKDRFVRVRL SD
