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Database: UniProt/TrEMBL
Entry: F9ZJ56_9PROT
LinkDB: F9ZJ56_9PROT
Original site: F9ZJ56_9PROT 
ID   F9ZJ56_9PROT            Unreviewed;       400 AA.
AC   F9ZJ56;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   19-FEB-2014, entry version 16.
DE   RecName: Full=Tyrosine--tRNA ligase;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
GN   Name=tyrS; ORFNames=NAL212_2811;
OS   Nitrosomonas sp. AL212.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=153948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AL212;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
RA   Suwa Y., Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J.,
RA   Arp D.J., Norton J.M., Woyke T.;
RT   "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL   Submitted (FEB-2011) 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.
CC   -!- SIMILARITY: Contains S4 RNA-binding domain.
CC   -!- SIMILARITY: Contains SRNA-binding domain.
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DR   EMBL; CP002552; ADZ27598.1; -; Genomic_DNA.
DR   RefSeq; YP_004295760.1; NC_015222.1.
DR   EnsemblBacteria; ADZ27598; ADZ27598; NAL212_2811.
DR   GeneID; 10299352; -.
DR   KEGG; nit:NAL212_2811; -.
DR   KO; K01866; -.
DR   BioCyc; NSP153948:GHZ8-2688-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-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      338    399       S4 RNA-binding (By similarity).
FT   MOTIF        43     52       "HIGH" region (By similarity).
FT   MOTIF       227    231       "KMSKS" region (By similarity).
FT   BINDING     230    230       ATP (By similarity).
SQ   SEQUENCE   400 AA;  44795 MW;  F1F78D3EC229D59E CRC64;
     MNTSIKSQLE IIKRGSQELL VETELEAKLV SGHPLRVKAG FDPTAPDLHL GHTVLLNKLR
     QLQVMGHHIL FLIGDFTGMI GDPSGKNSTR PPLTREQVAE NAQSYTTQVF KILNPDQTEV
     VFNSTWMGKM DAADLIKLAA THTVARMLER DDFDKRYRNN QAIAIHEFLY PLIQGYDSVA
     LKADLELGGT DQKFNLLMGR ELQKHFGQAQ QCILTMPLLE GLDGVNKMSK SLNNYVGITE
     SPAEIFGKLM SVSDQLMWRY LELLSFESLQ TIQKWREEVA AGRNPRDIKV ILAQEMVTRF
     HNRTSAEDAL ADFEARFKHG ALPEEIPEKI IQAPGSEIPL VQVLKQTGLT ASTSEALRMI
     EQGAVKLNNE KITDKSIQIM RGASVVIQVG KRKFAKAIIH
//
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