ID   M7T611_9EURY            Unreviewed;       346 AA.
AC   M7T611;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   05-DEC-2018, entry version 30.
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
CC       two-step reaction: tyrosine is first activated by ATP to form Tyr-
CC       AMP and then transferred to the acceptor end of tRNA(Tyr).
CC       {ECO:0000256|HAMAP-Rule:MF_02009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) +
CC         L-tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536,
CC         Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707; EC=6.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02009,
CC         ECO:0000256|SAAS:SAAS00342899};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02009}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. TyrS type 4 subfamily. {ECO:0000256|HAMAP-Rule:MF_02009}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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|HAMAP-Rule:MF_02009,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00011234,
KW   ECO:0000313|EMBL:EMR74284.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02009,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00011243};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053781};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02009};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02009,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00011245,
KW   ECO:0000313|EMBL:EMR74284.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02009,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00011248};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02009,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00011244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053781}.
FT   COILED      132    152       {ECO:0000256|SAM:Coils}.
FT   MOTIF       222    226       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02009}.
FT   BINDING      32     32       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02009}.
FT   BINDING     158    158       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02009}.
FT   BINDING     162    162       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02009}.
FT   BINDING     165    165       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02009}.
FT   BINDING     180    180       Tyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02009}.
FT   BINDING     225    225       ATP. {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
//