SYY_ARCFU
ID SYY_ARCFU Reviewed; 323 AA.
AC O29482;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02008};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02008};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02008};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02008};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02008}; OrderedLocusNames=AF_0776;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 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_02008}.
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_02008};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02008,
CC ECO:0000269|PubMed:16325203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_02008}.
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DR EMBL; AE000782; AAB90462.1; -; Genomic_DNA.
DR PIR; H69346; H69346.
DR RefSeq; WP_010878279.1; NC_000917.1.
DR PDB; 2CYB; X-ray; 1.80 A; A/B=1-323.
DR PDBsum; 2CYB; -.
DR AlphaFoldDB; O29482; -.
DR SMR; O29482; -.
DR STRING; 224325.AF_0776; -.
DR PRIDE; O29482; -.
DR EnsemblBacteria; AAB90462; AAB90462; AF_0776.
DR GeneID; 24794373; -.
DR KEGG; afu:AF_0776; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_0_1_2; -.
DR OMA; YIGFEIS; -.
DR OrthoDB; 59062at2157; -.
DR PhylomeDB; O29482; -.
DR BRENDA; 6.1.1.1; 414.
DR EvolutionaryTrace; O29482; -.
DR Proteomes; UP000002199; 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_02008; Tyr_tRNA_synth_type3; 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; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023684; Tyr-tRNA-ligase_3.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..323
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055668"
FT MOTIF 41..49
FT /note="'HIGH' region"
FT MOTIF 214..218
FT /note="'KMSKS' region"
FT BINDING 36
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008,
FT ECO:0000269|PubMed:16325203"
FT BINDING 158
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008,
FT ECO:0000269|PubMed:16325203"
FT BINDING 162
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008,
FT ECO:0000269|PubMed:16325203"
FT BINDING 165
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008,
FT ECO:0000269|PubMed:16325203"
FT BINDING 180
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008,
FT ECO:0000269|PubMed:16325203"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:2CYB"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2CYB"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2CYB"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2CYB"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2CYB"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:2CYB"
FT HELIX 297..319
FT /evidence="ECO:0007829|PDB:2CYB"
SQ SEQUENCE 323 AA; 36616 MW; A655AEE4A51166A2 CRC64;
MDITEKLRLI TRNAEEVVTE EELRQLIETK EKPRAYVGYE PSGEIHLGHM MTVQKLMDLQ
EAGFEIIVLL ADIHAYLNEK GTFEEIAEVA DYNKKVFIAL GLDESRAKFV LGSEYQLSRD
YVLDVLKMAR ITTLNRARRS MDEVSRRKED PMVSQMIYPL MQALDIAHLG VDLAVGGIDQ
RKIHMLAREN LPRLGYSSPV CLHTPILVGL DGQKMSSSKG NYISVRDPPE EVERKIRKAY
CPAGVVEENP ILDIAKYHIL PRFGKIVVER DAKFGGDVEY ASFEELAEDF KSGQLHPLDL
KIAVAKYLNM LLEDARKRLG VSV
