SYY_NANEQ
ID SYY_NANEQ Reviewed; 376 AA.
AC Q74MD3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=NEQ389;
OS Nanoarchaeum equitans (strain Kin4-M).
OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC Nanoarchaeaceae; Nanoarchaeum.
OX NCBI_TaxID=228908;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kin4-M;
RX PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA Stetter K.O., Short J.M., Noorderwier M.;
RT "The genome of Nanoarchaeum equitans: insights into early archaeal
RT evolution and derived parasitism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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 -!- 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; AE017199; AAR39237.1; -; Genomic_DNA.
DR PDB; 7FG6; X-ray; 2.80 A; A=1-376.
DR PDBsum; 7FG6; -.
DR AlphaFoldDB; Q74MD3; -.
DR SMR; Q74MD3; -.
DR STRING; 228908.NEQ389; -.
DR EnsemblBacteria; AAR39237; AAR39237; NEQ389.
DR KEGG; neq:NEQ389; -.
DR PATRIC; fig|228908.8.peg.399; -.
DR HOGENOM; CLU_035267_1_1_2; -.
DR OMA; YIGFEIS; -.
DR Proteomes; UP000000578; 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 Gene3D; 3.40.50.620; -; 2.
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; 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; Reference proteome.
FT CHAIN 1..376
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240263"
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 BINDING 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 174
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 177
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 192
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:7FG6"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:7FG6"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:7FG6"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 335..359
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 363..367
FT /evidence="ECO:0007829|PDB:7FG6"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:7FG6"
SQ SEQUENCE 376 AA; 43178 MW; AE2183260B61B84E CRC64;
MDIEERINLI AQKPTEEILT IDRLKQYLEQ GIDLNHYIGF EISGFVHLGT GIISMLKVRD
FQKAKVKTTL FLADYHSWIN KKLGGDLETI RKVAKGYFAE ALKVSLKTVG GDPDEVKVVL
GSELYEKLGI EYLENIIKIS MNTTLNRIKK GITIMGRKQG ESISFAQLLY VPMQVADIYS
LNVNLAHGGI DQRKAHVIAI EVSDAFGYKP IAVHHHLLLG MHIDENIRQK LLEAKKTNNR
ELFEDSVIDI KMSKSKPETA IFIHDTPEDI RRKIRKAYCP IGEIELNPII ELVEYVIYPI
LKEPIVIENK KTHQTMEFDN VEQLKEAYAK KQIHPLDLKE YVAEKLIEIL EPARKYFLEG
KGNKYLEELK NLQITR
