SYY_HALMA
ID SYY_HALMA Reviewed; 346 AA.
AC Q5V4J1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=rrnAC0543;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02008}.
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; AY596297; AAV45561.1; -; Genomic_DNA.
DR RefSeq; WP_011223081.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V4J1; -.
DR SMR; Q5V4J1; -.
DR STRING; 272569.rrnAC0543; -.
DR EnsemblBacteria; AAV45561; AAV45561; rrnAC0543.
DR GeneID; 40151600; -.
DR KEGG; hma:rrnAC0543; -.
DR PATRIC; fig|272569.17.peg.1309; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_0_1_2; -.
DR OMA; YIGFEIS; -.
DR Proteomes; UP000001169; Chromosome I.
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; -; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..346
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240252"
FT MOTIF 40..48
FT /note="'HIGH' region"
FT BINDING 35
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 162
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 166
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 169
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 184
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
SQ SEQUENCE 346 AA; 38095 MW; 887555EC6AC93F7F CRC64;
MDTAERLDLV TRHTTEVVTE DELRTLFEES DPSAYIGYAP TGEMHIGHFT TMRKLADFLR
AGVDVTVLIA DLHAHLDDNK SPFDLLDARS AYYETAIEGM IEAAGADPED VTFVRGTDFQ
LDEEYTLEMY RMAAETTISR TQRAASEVVR ESESPNLGGL IYPLMQTLDV KALDADIAYG
GVDQRGIYML SREILPDHGG ESPICLFAPL LSGLSGGKMS ASDEASKVNL TDSPDEVDEK
INQAYCPAGE VEENGVLEYL QHLVFPVLDV RGDSFVVERP EEYGGDLTYE SYDEVESDFV
SGELHPADLK PSAASAISDV IDPVRERLAD KDELLAEAYP EKYGAE