SYY_AERPE
ID SYY_AERPE Reviewed; 364 AA.
AC Q9YA64;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=APE_2074.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA81085.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000002; BAA81085.2; ALT_INIT; Genomic_DNA.
DR PIR; E72512; E72512.
DR PDB; 2CYA; X-ray; 2.20 A; A=1-364.
DR PDBsum; 2CYA; -.
DR AlphaFoldDB; Q9YA64; -.
DR SMR; Q9YA64; -.
DR STRING; 272557.APE_2074.1; -.
DR EnsemblBacteria; BAA81085; BAA81085; APE_2074.1.
DR KEGG; ape:APE_2074.1; -.
DR PATRIC; fig|272557.25.peg.1380; -.
DR eggNOG; arCOG01886; Archaea.
DR OMA; YIGFEIS; -.
DR BRENDA; 6.1.1.1; 171.
DR EvolutionaryTrace; Q9YA64; -.
DR Proteomes; UP000002518; 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.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 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..364
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240262"
FT MOTIF 238..242
FT /note="'KMSKS' region"
FT BINDING 39
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 165
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 169
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 172
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 187
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2CYA"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:2CYA"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:2CYA"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 323..346
FT /evidence="ECO:0007829|PDB:2CYA"
FT HELIX 349..360
FT /evidence="ECO:0007829|PDB:2CYA"
SQ SEQUENCE 364 AA; 40765 MW; 3C9ABE0E3BE7EC6B CRC64;
MVRVDVEERF NRIARNTVEI VTEEELKGLL ASGARIKGYI GYEPSGVAHI GWLVWMYKVK
DLVEAGVDFS VLEATWHAYI NDKLGGDMDL IRAAARIVRR VMEAAGVPVE RVRFVDAEEL
ASDKDYWGLV IRVAKRASLA RVRRALTIMG RRAEEAEVDA SKLIYPLMQV SDIFYMDLDI
ALGGMDQRKA HMLARDVAEK LGRKKPVAIH TPIISSLQGP GRMEASQGEI DDVLAEVKMS
KSKPETAVFV VDSDDDIRRK IRKAYCPAKQ VQGNPVLEIA RYILFARDGF TLRVDRPAKY
GGPVEYTSYE ELERDYTDGR LHPLDLKNAV AESLIEVVRP IRGAVLGDPA MKRALEAIEG
KVTR
