ID SYY_ANAVT Reviewed; 398 AA.
AC Q3MEN7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 01-MAY-2013, entry version 50.
DE RecName: Full=Tyrosine--tRNA ligase;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
GN Name=tyrS; OrderedLocusNames=Ava_0925;
OS Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT "Complete sequence of Anabaena variabilis ATCC 29413.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA20549.1; -; Genomic_DNA.
DR RefSeq; YP_321444.1; NC_007413.1.
DR ProteinModelPortal; Q3MEN7; -.
DR STRING; 240292.Ava_0925; -.
DR EnsemblBacteria; ABA20549; ABA20549; Ava_0925.
DR GeneID; 3681299; -.
DR KEGG; ava:Ava_0925; -.
DR PATRIC; 35422298; VBIAnaVar43351_1714.
DR eggNOG; COG0162; -.
DR HOGENOM; HOG000242791; -.
DR KO; K01866; -.
DR OMA; GGNDQKF; -.
DR ProtClustDB; PRK05912; -.
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; 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 CHAIN 1 398 Tyrosine--tRNA ligase.
FT /FTId=PRO_0000236690.
FT DOMAIN 334 398 S4 RNA-binding.
FT MOTIF 48 57 "HIGH" region.
FT MOTIF 235 239 "KMSKS" region.
FT BINDING 238 238 ATP (By similarity).
SQ SEQUENCE 398 AA; 44447 MW; 85E4BC864466B926 CRC64;
MAENFSWLHR GIAEVFPQPT DAESDIESLE KRLATTDRPL RVKYGIDPTG ADIHLGHSIP
MRKLRGFQDA GHTAVLIIGD FTARIGDPTG KSEMRRQLTE EDVKQNAQTY LDQVRPILDF
DTPGRLEVRY NSEWLSRLDL GKITELLATM TVGQMLAKEG FADRYKKENP IFLHEFLYPL
MQGYDSVAIE ADVELGGTDQ KFNIAVGRDL QRHFGQKPQF GVLLPILIGT DGVQKMSKSL
GNYVSLSEHP GQKYQKLQGV PDQMLEQYFE LLTDLPIDKL PANPRDRQML LAWEIVKQYH
GEQAAQEAKE AAQSGGKEGA VPEFSLAGVP QFPVKLAYLL GATGLCKSTG EGKRKIQEGG
VRLDGDRISD ADTIFQQPDE LQGRVLQVGK NKFVRLVL
//
