SYY_NEIG2
ID SYY_NEIG2 Reviewed; 431 AA.
AC B4RP13;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=NGK_0091;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
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_02006}.
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_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
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DR EMBL; CP001050; ACF28790.1; -; Genomic_DNA.
DR RefSeq; WP_003687313.1; NC_011035.1.
DR PDB; 6OTJ; X-ray; 2.85 A; A/B=1-431.
DR PDBsum; 6OTJ; -.
DR AlphaFoldDB; B4RP13; -.
DR SMR; B4RP13; -.
DR EnsemblBacteria; ACF28790; ACF28790; NGK_0091.
DR KEGG; ngk:NGK_0091; -.
DR HOGENOM; CLU_024003_0_3_4; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 402899at2; -.
DR Proteomes; UP000002564; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; cd00165; S4; 1.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 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; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT CHAIN 1..431
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_1000189311"
FT DOMAIN 353..422
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 39..48
FT /note="'HIGH' region"
FT MOTIF 231..235
FT /note="'KMSKS' region"
FT BINDING 34
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 171
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 175
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6OTJ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 368..376
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6OTJ"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6OTJ"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:6OTJ"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:6OTJ"
SQ SEQUENCE 431 AA; 47182 MW; 952804AFCB48CBEC CRC64;
MSVIQDLQSR GLIAQTTDIE ALDALLNEQK IALYCGFDPT ADSLHIGHLL PVLALRRFQQ
AGHTPIALVG GATGMIGDPS FKAAERSLNS AETVAGWVGS IRSQLTPFLS FEGGNAAIMA
NNADWFGSMN CLDFLRDIGK HFSVNAMLNK ESVKQRIDRD GAGISFTEFA YSLLQGYDFA
ELNKRHGAVL EIGGSDQWGN ITAGIDLTRR LNQKQVFGLT LPLVTKSDGT KFGKTEGGAV
WLNAKKTSPY QFYQFWLKVA DADVYKFLKY FTFLSIEEIG VVEAKDKASG SKPEAQRILA
EEMTRLIHGE EALAAAQRIS ESLFAEDQSR LTESDFEQLA LDGLPAFEVS DGINAVEALV
KTGLAASNKE ARGFVNAKAV LLNGKPAEAN NPNHAAERPD DAYLLIGEYK RFGKYTILRR
GKRNHALLVW K
