SYY_PYRHO
ID SYY_PYRHO Reviewed; 375 AA.
AC O58739;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02009};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02009};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02009};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02009};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02009}; OrderedLocusNames=PH1011;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH TYROSINE, AND
RP SUBUNIT.
RX PubMed=16325203; DOI=10.1016/j.jmb.2005.10.073;
RA Kuratani M., Sakai H., Takahashi M., Yanagisawa T., Kobayashi T.,
RA Murayama K., Chen L., Liu Z.-J., Wang B.-C., Kuroishi C., Kuramitsu S.,
RA Terada T., Bessho Y., Shirouzu M., Sekine S., Yokoyama S.;
RT "Crystal structures of tyrosyl-tRNA synthetases from Archaea.";
RL J. Mol. Biol. 355:395-408(2006).
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_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:0000255|HAMAP-Rule:MF_02009};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02009,
CC ECO:0000269|PubMed:16325203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02009}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_02009}.
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DR EMBL; BA000001; BAA30108.1; -; Genomic_DNA.
DR PIR; F71093; F71093.
DR RefSeq; WP_010885097.1; NC_000961.1.
DR PDB; 2CYC; X-ray; 2.20 A; A/B=1-375.
DR PDBsum; 2CYC; -.
DR AlphaFoldDB; O58739; -.
DR SMR; O58739; -.
DR STRING; 70601.3257425; -.
DR EnsemblBacteria; BAA30108; BAA30108; BAA30108.
DR GeneID; 1443332; -.
DR KEGG; pho:PH1011; -.
DR eggNOG; arCOG01886; Archaea.
DR OMA; YIGFEIS; -.
DR OrthoDB; 59062at2157; -.
DR BRENDA; 6.1.1.1; 5244.
DR EvolutionaryTrace; O58739; -.
DR Proteomes; UP000000752; Chromosome.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..375
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240269"
FT MOTIF 251..255
FT /note="'KMSKS' region"
FT BINDING 37
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009,
FT ECO:0000269|PubMed:16325203"
FT BINDING 168
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009,
FT ECO:0000269|PubMed:16325203"
FT BINDING 172
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009,
FT ECO:0000269|PubMed:16325203"
FT BINDING 175
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009,
FT ECO:0000269|PubMed:16325203"
FT BINDING 190
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009,
FT ECO:0000269|PubMed:16325203"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:2CYC"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2CYC"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 352..360
FT /evidence="ECO:0007829|PDB:2CYC"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:2CYC"
SQ SEQUENCE 375 AA; 43276 MW; 8A4BC945037A9F1B CRC64;
MDIEERINLV LKKPTEEVLT VENLRHLFEI GAPLQHYIGF EISGYIHLGT GLMAGAKIAD
FQKAGIKTRV FLADWHSWIN DKLGGDLEVI QEVALKYFKV GMEKSIEVMG GDPKKVEFVL
ASEILEKGDY WQTVIDISKN VTLSRVMRSI TIMGRQMGEA IDFAKLIYPM MQVADIFYQG
VTIAHAGMDQ RKAHVIAIEV AQKLRYHPIV HEGEKLKPVA VHHHLLLGLQ EPPKWPIESE
EEFKEIKAQM KMSKSKPYSA VFIHDSPEEI RQKLRKAFCP AREVRYNPVL DWVEYIIFRE
EPTEFTVHRP AKFGGDVTYT TFEELKRDFA EGKLHPLDLK NAVAEYLINL LEPIRRYFEK
HPEPLELMRS VKITR
