ID D7FED3_HELP3 Unreviewed; 402 AA.
AC D7FED3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 01-MAY-2013, entry version 25.
DE RecName: Full=Tyrosine--tRNA ligase;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
GN Name=tyrS; OrderedLocusNames=HPB8_983;
OS Helicobacter pylori (strain B8).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=693745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8;
RX PubMed=20507619; DOI=10.1186/1471-2164-11-335;
RA Farnbacher M., Jahns T., Willrodt D., Daniel R., Haas R., Goesmann A.,
RA Kurtz S., Rieder G.;
RT "Sequencing, annotation, and comparative genome analysis of the
RT gerbil-adapted Helicobacter pylori strain B8.";
RL BMC Genomics 11:335-335(2010).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
CC two-step reaction: tyrosine is first activated by ATP to form Tyr-
CC AMP and then transferred to the acceptor end of tRNA(Tyr) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
CC diphosphate + L-tyrosyl-tRNA(Tyr).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. TyrS type 2 subfamily.
CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR EMBL; FN598874; CBI66540.1; -; Genomic_DNA.
DR RefSeq; YP_003729004.1; NC_014256.1.
DR EnsemblBacteria; CBI66540; CBI66540; HPB8_983.
DR GeneID; 9349444; -.
DR KEGG; hpl:HPB8_983; -.
DR PATRIC; 38176283; VBIHelPyl164240_0949.
DR HOGENOM; HOG000242791; -.
DR KO; K01866; -.
DR OMA; GGNDQKF; -.
DR BioCyc; HPYL693745:GJAE-1005-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 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; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT DOMAIN 341 401 S4 RNA-binding (By similarity).
FT MOTIF 47 56 "HIGH" region (By similarity).
FT MOTIF 232 236 "KMSKS" region (By similarity).
FT BINDING 235 235 ATP (By similarity).
SQ SEQUENCE 402 AA; 45694 MW; C7AEBEA27DB07F20 CRC64;
MEQKIAIALK EIKRGANEII GLEYIEKLVR KYYETNERFI VKAGFDPTAP DLHLGHTVLI
QKLALLQQYG ARVKFLIGDF TAMIGDPTGK NETRKPLNRE QVLENAKTYE EQIYKILDEK
HTEVCFNSTW LDALGAKGMI ELCAKFSVAR MLERDDFAKR HKENRPISIV EFLYPLLQGY
DSVAMDADIE LGGNDQKFNL LVGRFLQRAY GLNKEQSVIT MPLLEGLDGV QKMSKSLGNY
VGITEEPNAM FGKIMSVSDD LMWRYYTLLS TKTLEEIEDL KHGILNQTLH PKAVKEKLAG
EIVARYYDND QAIKAKEQFS KVFSANLLPE ILSESDFDEG VGILDVLKQI GFCPSTSQAR
RDIQGGGVKI NQEVIKDESY RFVKGNYVIQ LGKKRFMKLN IN
//
