ID   M7T611_9EURY            Unreviewed;       346 AA.
AC   M7T611;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   12-AUG-2020, entry version 35.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02009};
DE            EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02009};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02009};
DE            Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02009};
GN   Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02009};
GN   ORFNames=MBGDN05_00758 {ECO:0000313|EMBL:EMR74284.1};
OS   Thermoplasmatales archaeon SCGC AB-539-N05.
OC   Archaea; Euryarchaeota; Diaforarchaea group; Thermoplasmata;
OC   Thermoplasmatales.
OX   NCBI_TaxID=1198116 {ECO:0000313|EMBL:EMR74284.1, ECO:0000313|Proteomes:UP000053781};
RN   [1] {ECO:0000313|EMBL:EMR74284.1, ECO:0000313|Proteomes:UP000053781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AB-539-N05 {ECO:0000313|EMBL:EMR74284.1};
RX   PubMed=23535597; DOI=10.1038/nature12033;
RA   Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A.,
RA   Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S.,
RA   Schramm A., Jorgensen B.B.;
RT   "Predominant archaea in marine sediments degrade detrital proteins.";
RL   Nature 496:215-218(2013).
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_02009}.
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_02009};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_02009}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 4 subfamily. {ECO:0000256|HAMAP-Rule:MF_02009}.
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:EMR74284.1}.
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DR   EMBL; ALXL01000015; EMR74284.1; -; Genomic_DNA.
DR   EnsemblBacteria; EMR74284; EMR74284; MBGDN05_00758.
DR   PATRIC; fig|1198116.5.peg.117; -.
DR   Proteomes; UP000053781; 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:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02009; Tyr_tRNA_synth_type4; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR023678; Tyr-tRNA-ligase_4.
DR   InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02009, ECO:0000256|RuleBase:RU363036,
KW   ECO:0000313|EMBL:EMR74284.1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02009, ECO:0000256|RuleBase:RU363036};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02009};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02009,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000313|EMBL:EMR74284.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02009, ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02009, ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053781}.
FT   COILED          132..152
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           222..226
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
FT   BINDING         32
FT                   /note="Tyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
FT   BINDING         158
FT                   /note="Tyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
FT   BINDING         162
FT                   /note="Tyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
FT   BINDING         165
FT                   /note="Tyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
FT   BINDING         180
FT                   /note="Tyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
FT   BINDING         225
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02009"
SQ   SEQUENCE   346 AA;  39036 MW;  3DAC4C8042DDE8BF CRC64;
     MNKVDQIMAN TEEIVTVEEL KVVLGKSKPK AYIGFEPSGT VHLGWKICTN KIKDFIECGF
     DFTVLLADWH AYINDKLGGD IDKIKLCGKY MEDCFAAMGV DTSQVRFVYA SDYVSDSAYW
     ELVLRTAKSM SVARVKRAMD IMGRDAEEAE KDLSKLFYPA MQVSDIFYLD LDAAYGGMDQ
     RRAHMLAREV SKKLGKKAPV AIHTPLLTGL QAGGRMDPVE AKMSKSKPGS MISIHDDPAS
     VKKKMNKAFC PERQVEGNPV LEICRYVVFP ELKDEVFLIE RPEKFGGNLK FANYKELEQA
     FVDGLHPLDL KNATAKYVNM ILEPVHTYFE KQPENYNKMK KAGIIQ
//