SYY_PYRAB
ID SYY_PYRAB Reviewed; 375 AA.
AC Q9V027; G8ZID6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=PYRAB09710;
GN ORFNames=PAB1728;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB49879.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70377.1; -; Genomic_DNA.
DR PIR; B75072; B75072.
DR RefSeq; WP_010868088.1; NC_000868.1.
DR AlphaFoldDB; Q9V027; -.
DR SMR; Q9V027; -.
DR STRING; 272844.PAB1728; -.
DR EnsemblBacteria; CAB49879; CAB49879; PAB1728.
DR GeneID; 1496321; -.
DR KEGG; pab:PAB1728; -.
DR PATRIC; fig|272844.11.peg.1023; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_1_1_2; -.
DR OMA; YIGFEIS; -.
DR OrthoDB; 59062at2157; -.
DR PhylomeDB; Q9V027; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..375
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240265"
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 168
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 175
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 190
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"
SQ SEQUENCE 375 AA; 43054 MW; 1437665DBF82113C CRC64;
MDIEERINLV LKKPTEEVLT VENLRHLFEV GAPLQHYIGF EISGYIHLGT GLMAGAKIAD
FQKAGIKTRI FLADWHSWIN DKLGGDLEVI QEVALKYFKV GMEKSIEVMG GDPKKVEFVL
ASEILENGDY WQTVIDISKN VTLSRVMRSI TIMGRQMGES IDFAKLIYPM MQVADIFYQG
VTIAHAGMDQ RKAHVIAIEV AQKLKYHPIV HNGEKLKPVA VHHHLLLGLQ EPPVWPITSE
EQFKEIKAQM KMSKSKPYSA VFIHDSPEEI KQKLRKAFCP AREVNYNPVL DWAEHIIFRE
EPTEFTIHRP AKFGGDVTYT TFEELKKDFA EGKLHPLDLK NAVAEYLIEL LKPIREYFER
HPEPLELMRS VKITR
