ID F9ZJ56_9PROT Unreviewed; 400 AA.
AC F9ZJ56;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 29-MAY-2013, entry version 13.
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.
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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: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; Cytoplasm; Ligase;
KW 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
//
